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Conserved domains on  [gi|24797089|ref|NP_722540|]
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peroxisome biogenesis factor 10 isoform 1 [Homo sapiens]

Protein Classification

Pex2_Pex12 and RING-HC_PEX10 domain-containing protein (domain architecture ID 12057481)

Pex2_Pex12 and RING-HC_PEX10 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pex2_Pex12 pfam04757
Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of ...
18-263 5.97e-37

Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of known and predicted peroxins including Pex2, Pex10 and Pex12. This conserved region is usually associated with a C terminal ring finger (pfam00097) domain.


:

Pssm-ID: 309754  Cd Length: 203  Bit Score: 131.71  E-value: 5.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    18 DEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVT 97
Cdd:pfam04757   1 DEELESLLRPQLRYILRLLAGQRFPLNYFDELKLLLDLLYFRLTLLRGNATLGEEFYGLKRVDRDGGRLLSRRQRLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    98 LHAVLPYLLDKALlpleqelqadpdsgrplqgslgpggrgcsgaRRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRL 177
Cdd:pfam04757  81 LLVLLPYLLRKLD-------------------------------SLLESRGRRDSLKSRLKRALLKLYPFLESLYKLLNL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089   178 HVAWFYIHGVFYHLAKRLTGITYQALRPDPlrvlmsvapsalQLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLY 257
Cdd:pfam04757 130 HLFLFYLSGKYYSLSKRLLGIRYVRLTPSD------------LNGRRVGYERQLLWNAFSELLGFLLPLLLAVKFFLKFL 197

                  ....*.
gi 24797089   258 GFRQRQ 263
Cdd:pfam04757 198 EWWYSS 203
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
293-331 1.01e-24

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


:

Pssm-ID: 319441 [Multi-domain]  Cd Length: 40  Bit Score: 94.21  E-value: 1.01e-24
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16527   2 CSLCLESRRHPTATPCGHLFCWSCITEWCNEKPECPLCR 40
 
Name Accession Description Interval E-value
Pex2_Pex12 pfam04757
Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of ...
18-263 5.97e-37

Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of known and predicted peroxins including Pex2, Pex10 and Pex12. This conserved region is usually associated with a C terminal ring finger (pfam00097) domain.


Pssm-ID: 309754  Cd Length: 203  Bit Score: 131.71  E-value: 5.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    18 DEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVT 97
Cdd:pfam04757   1 DEELESLLRPQLRYILRLLAGQRFPLNYFDELKLLLDLLYFRLTLLRGNATLGEEFYGLKRVDRDGGRLLSRRQRLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    98 LHAVLPYLLDKALlpleqelqadpdsgrplqgslgpggrgcsgaRRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRL 177
Cdd:pfam04757  81 LLVLLPYLLRKLD-------------------------------SLLESRGRRDSLKSRLKRALLKLYPFLESLYKLLNL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089   178 HVAWFYIHGVFYHLAKRLTGITYQALRPDPlrvlmsvapsalQLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLY 257
Cdd:pfam04757 130 HLFLFYLSGKYYSLSKRLLGIRYVRLTPSD------------LNGRRVGYERQLLWNAFSELLGFLLPLLLAVKFFLKFL 197

                  ....*.
gi 24797089   258 GFRQRQ 263
Cdd:pfam04757 198 EWWYSS 203
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
293-331 1.01e-24

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 319441 [Multi-domain]  Cd Length: 40  Bit Score: 94.21  E-value: 1.01e-24
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16527   2 CSLCLESRRHPTATPCGHLFCWSCITEWCNEKPECPLCR 40
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
289-343 1.01e-14

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 73.00  E-value: 1.01e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24797089 289 RNPLCTLCLEERRHPTATPCGHLFCWECI-TAWCSSKAE-CPLCREKFPPQKLIYLR 343
Cdd:COG5574 214 ADYKCFLCLEEPEVPSCTPCGHLFCLSCLlISWTKKKYEfCPLCRAKVYPKKVIILR 270
zf-RING_2 pfam13639
Ring finger domain;
293-331 1.82e-11

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 58.17  E-value: 1.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 24797089   293 CTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:pfam13639   3 CPICLEEfeeGDKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
293-330 7.04e-10

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 53.67  E-value: 7.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 24797089    293 CTLCLEER-RHPTATPCGHLFCWECITAWCSSK-AECPLC 330
Cdd:smart00184   1 CPICLEEYlKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
208-331 3.29e-08

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 54.59  E-value: 3.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089 208 LRVLMSVAPS--ALQLRVRSLPGE----DLRARVSY----RLLGVISLLHLVLSMGLQLYGFRQR--------QRARKEW 269
Cdd:COG5243 183 LLNLTSEANKlcVYNYEARDDDDErstyLFRLEVCYdgltLLAYSLLFMYQFPYVRVPIYLIRQMytcfyalfRRIREHA 262
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24797089 270 RLHRGLSHRRASL----EERAVSRNPLCTLCLEERRH-------------PTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:COG5243 263 RFRRATKDLNAMYptatEEQLTNSDRTCTICMDEMFHpdheplprgldmtPKRLPCGHILHLHCLKNWLERQQTCPICR 341
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
293-340 7.18e-07

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747  Cd Length: 193  Bit Score: 48.93  E-value: 7.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24797089  293 CTLCLEERRHPTATPCGHLFCWECITAWCSSK----------------AECPLCREKFPPQKLI 340
Cdd:PLN03208  21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASnnsrqrvdqydhkrepPKCPVCKSDVSEATLV 84
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
293-339 1.12e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 49.62  E-value: 1.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 24797089   293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKL 339
Cdd:TIGR00599  29 CHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESKL 75
 
Name Accession Description Interval E-value
Pex2_Pex12 pfam04757
Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of ...
18-263 5.97e-37

Pex2 / Pex12 amino terminal region; This region is found at the N terminal of a number of known and predicted peroxins including Pex2, Pex10 and Pex12. This conserved region is usually associated with a C terminal ring finger (pfam00097) domain.


Pssm-ID: 309754  Cd Length: 203  Bit Score: 131.71  E-value: 5.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    18 DEYYRGGLRSAAGGALHSLAGARKWLEWRKEVELLSDVAYFGLTTLAGYQTLGEEYVSIIQVDPSRIHVPSSLRRGVLVT 97
Cdd:pfam04757   1 DEELESLLRPQLRYILRLLAGQRFPLNYFDELKLLLDLLYFRLTLLRGNATLGEEFYGLKRVDRDGGRLLSRRQRLLSLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089    98 LHAVLPYLLDKALlpleqelqadpdsgrplqgslgpggrgcsgaRRWMRHHTATLTEQQRRALLRAVFVLRQGLACLQRL 177
Cdd:pfam04757  81 LLVLLPYLLRKLD-------------------------------SLLESRGRRDSLKSRLKRALLKLYPFLESLYKLLNL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089   178 HVAWFYIHGVFYHLAKRLTGITYQALRPDPlrvlmsvapsalQLRVRSLPGEDLRARVSYRLLGVISLLHLVLSMGLQLY 257
Cdd:pfam04757 130 HLFLFYLSGKYYSLSKRLLGIRYVRLTPSD------------LNGRRVGYERQLLWNAFSELLGFLLPLLLAVKFFLKFL 197

                  ....*.
gi 24797089   258 GFRQRQ 263
Cdd:pfam04757 198 EWWYSS 203
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
293-331 1.01e-24

RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known as peroxisome biogenesis factor 10, peroxisomal biogenesis factor 10, peroxisome assembly protein 10, or RING finger protein 69 (RNF69), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It plays an essential role in peroxisome assembly, import of target substrates, and recycling or degradation of protein complexes and amino acids. It is an essential component of the spinal locomotor circuit, and thus its mutations may be involved in peroxisomal biogenesis disorders (PBD). Mutations in human PEX10 also result in autosomal recessive ataxia. Moreover, PEX10 functions as an E3-ubiquitin ligase with an E2, UBCH5C. It mono- or poly-ubiquitinates PEX5, a key player in peroxisomal matrix protein import, in a UBC4-dependent manner, to control PEX5 receptor recycling or degradation. It also links the E2 ubiquitin conjugating enzyme PEX4 to the protein import machinery of the peroxisome.


Pssm-ID: 319441 [Multi-domain]  Cd Length: 40  Bit Score: 94.21  E-value: 1.01e-24
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16527   2 CSLCLESRRHPTATPCGHLFCWSCITEWCNEKPECPLCR 40
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
289-343 1.01e-14

RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227861 [Multi-domain]  Cd Length: 271  Bit Score: 73.00  E-value: 1.01e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24797089 289 RNPLCTLCLEERRHPTATPCGHLFCWECI-TAWCSSKAE-CPLCREKFPPQKLIYLR 343
Cdd:COG5574 214 ADYKCFLCLEEPEVPSCTPCGHLFCLSCLlISWTKKKYEfCPLCRAKVYPKKVIILR 270
RING-HC_AtRMA_like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
293-331 1.24e-11

RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) and similar proteins; AtRMAs, including AtRma1, AtRma2, and AtRma3, are endoplasmic reticulum (ER)-localized Arabidopsis homologs of human outer membrane of the ER-anchor E3 ubiquitin-protein ligase, RING finger protein 5 (RNF5). AtRMAs possess E3 ubiquitin ligase activity, and may play a role in the growth and development of Arabidopsis. The AtRMA1 and AtRMA3 genes are predominantly expressed in major tissues, such as cotyledons, leaves, shoot-root junction, roots, and anthers, while AtRMA2 expression is restricted to the root tips and leaf hydathodes. AtRma1 probably functions with the Ubc4/5 subfamily of E2. AtRma2 is likely involved in the cellular regulation of ABP1 expression levels through interacting with auxin binding protein 1 (ABP1). AtRMA proteins contain an N-terminal C3HC4-type RING-HC finger and a trans-membrane-anchoring domain in their extreme C-terminal region.


Pssm-ID: 319659 [Multi-domain]  Cd Length: 45  Bit Score: 58.47  E-value: 1.24e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWC---SSKAECPLCR 331
Cdd:cd16745   3 CNICLDLASDPVVTLCGHLFCWPCLYRWLqrhSENRECPVCK 44
zf-RING_2 pfam13639
Ring finger domain;
293-331 1.82e-11

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 58.17  E-value: 1.82e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 24797089   293 CTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:pfam13639   3 CPICLEEfeeGDKVVILPCGHHFHRECLDKWLRSSNTCPLCR 44
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
293-332 2.39e-11

RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar proteins; TRIM40, also known as probable E3 NEDD8-protein ligase or RING finger protein 35 (RNF35), is highly expressed in the gastrointestinal tract including the stomach, small intestine, and large intestine. It enhances neddylation of inhibitor of nuclear factor kappaB kinase subunit gamma (IKKgamma), inhibits the activity of nuclear factor-kappaB (NF-kappaB)-mediated transcription, and thus prevents inflammation-associated carcinogenesis in the gastrointestinal tract. TRIM40 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region , as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319497 [Multi-domain]  Cd Length: 46  Bit Score: 57.98  E-value: 2.39e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAW-----CSSKAECPLCRE 332
Cdd:cd16583   2 CPICLDPLKEPVSTTCGHVFCRGCIAQHlekasVSGVLCCPVCRK 46
RING-HC_RNF5_like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
293-331 6.30e-11

RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 and RNF185 are E3 ubiquitin-protein ligases that are anchored to the outer membrane of the endoplasmic reticulum (ER). RNF5 acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis, and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. RNF185 controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical endoplasmic reticulum-associated degradation (ERAD) model substrates. Moreover, both RNF5 and RNF185 play important roles in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) are also included in this family. They possess E3 ubiquitin-protein ligase activity and may play a role in the growth and development of Arabidopsis. All members in this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 319448 [Multi-domain]  Cd Length: 43  Bit Score: 56.67  E-value: 6.30e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE---CPLCR 331
Cdd:cd16534   2 CNICLDTAKDAVVSMCGHLFCWPCLHQWLETRPDrptCPVCK 43
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
293-330 1.08e-10

HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to HC subclass of RING (RING-HC) finger proteins that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319363 [Multi-domain]  Cd Length: 39  Bit Score: 55.94  E-value: 1.08e-10
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSS-KAECPLC 330
Cdd:cd16449   1 CPICLELLKDPVLLPCGHTFCRSCLRRLLKEgKKKCPIC 39
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
292-331 2.33e-10

RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and similar proteins; COP1, also known as RING finger and WD repeat domain protein 2 (RFWD2) or RING finger protein 200 (RNF200), was defined as a central regulator of photomorphogenic development in plants, which targets key transcription factors for proteasome-dependent degradation. It is localized predominantly in the nucleus, but may also be present in the cytosol. Mammalian COP1 functions as an E3 ubiquitin-protein ligase that interacts with Jun transcription factors and modulates their transcriptional activity. It also interacts with and negatively regulates the tumor-suppressor protein p53. Moreover, COP1 associates with COP9 signalosome subunit 6 (CSN6), and is involved in 14-3-3 delta ubiquitin-mediated degradation. The CSN6-COP1 link enhances ubiquitin-mediated degradation of p27(Kip1), a critical CDK inhibitor involved in cell cycle regulation, to promote cancer cell growth. Furthermore, COP1 functions as the negative regulator of ETV1 and influences prognosis in triple-negative breast cancer. COP1 contains an N-terminal extension, a C3HC4-type RING-HC finger, a coiled coil domain, and seven WD40 repeats. In human COP1, a classic leucine-rich NES, and a novel bipartite NLS is bridged by the RING-HC finger.


Pssm-ID: 319418 [Multi-domain]  Cd Length: 46  Bit Score: 54.96  E-value: 2.33e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16504   4 ICPICFDIIEEAYMTKCGHSFCYKCIRTSLEQSNRCPKCN 43
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
293-330 7.04e-10

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 53.67  E-value: 7.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 24797089    293 CTLCLEER-RHPTATPCGHLFCWECITAWCSSK-AECPLC 330
Cdd:smart00184   1 CPICLEEYlKDPVILPCGHTFCRSCIRKWLESGnNTCPIC 40
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
293-331 9.11e-10

RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar proteins; HLTF, also known as DNA-binding protein/plasminogen activator inhibitor 1 regulator, or HIP116, or RING finger protein 80, or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3, or sucrose nonfermenting protein 2-like 3, is a yeast RAD5 homolog found in mammals. It has both E3 ubiquitin ligase and DNA helicase activities, and plays a pivotal role in the template-switching pathway of DNA damage tolerance. It is involved in Lys-63-linked poly-ubiquitination of proliferating cell nuclear antigen (PCNA) at Lys-164 and in the regulation of DNA damage tolerance. It shows double-stranded DNA translocase activity with 3'-5' polarity, thereby facilitating regression of the replication fork. HLTF contains an N-terminal HIRAN (HIP116 and RAD5 N-terminal) domain, a SWI/SNF helicase domain that is divided into N- and C-terminal parts by an insertion of a C3HC4-type RING-HC finger involved in the poly-ubiquitination of PCNA.


Pssm-ID: 319423 [Multi-domain]  Cd Length: 43  Bit Score: 53.46  E-value: 9.11e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSK--AECPLCR 331
Cdd:cd16509   3 CPICLDSLKDPVITPCAHVFCRGCIEQVIQREpnAKCPLCR 43
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
293-331 3.06e-09

RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319657 [Multi-domain]  Cd Length: 46  Bit Score: 51.87  E-value: 3.06e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSS---KAECPLCR 331
Cdd:cd16743   3 CNICLETAREAVVSLCGHLYCWPCLHQWLETrpeRQECPVCK 44
RING-HC_LNX3_like cd16512
RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; ...
293-331 6.47e-09

RING finger, HC subclass, found in ligand of Numb protein LNX3, LNX4, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4, or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX3/LNX4-like proteins, which contains a typical C3HC4-type RING-HC finger and two PDZ domains.


Pssm-ID: 319426 [Multi-domain]  Cd Length: 41  Bit Score: 50.98  E-value: 6.47e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPL-CR 331
Cdd:cd16512   2 CSICLEVLEDPLTTPCGHVFCSGCILPWLVQNGSCPVkCR 41
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
292-333 7.12e-09

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 339001 [Multi-domain]  Cd Length: 48  Bit Score: 50.84  E-value: 7.12e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24797089   292 LCTLCLEERRHPTATPCGHL-FCWECITAWCSSKAECPLCREK 333
Cdd:pfam13920   4 LCVICLDRPRNVVLLPCGHLcLCEECAERLRKKKKKCPICRQP 46
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
293-331 9.75e-09

RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; RNF219 may function as a modulator of late-onset Alzheimer"s disease (LOAD) associated amyloid beta A4 precursor protein (APP) endocytosis and metabolism. It genetically interacts with apolipoprotein E epsilon4 allele (APOE4). Thus a genetic variant within RNF219 was found to affect amyloid deposition in human brain and LOAD age-of-onset. Moreover, common genetic variants at the RNF219 locus had been associated with alternations in lipid metabolism, cognitive performance and central nervous system ventricle volume. RNF219 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319476 [Multi-domain]  Cd Length: 42  Bit Score: 50.45  E-value: 9.75e-09
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16562   4 CHICLGKVKQPVICPNNHVFCSSCMDLWLKRNNQCPACR 42
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
292-331 1.35e-08

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319655 [Multi-domain]  Cd Length: 40  Bit Score: 49.93  E-value: 1.35e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16741   1 ICPICQAEFQKPILLICQHIFCEECISLWFNREKTCPLCR 40
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
292-331 2.66e-08

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, also known as Casitas B-lineage lymphoma proto-oncogene, proto-oncogene c-Cbl, RING finger protein 55 (RNF55), or signal transduction protein Cbl, is a multi-domain protein that acts as a key negative regulator of various receptor and non-receptor tyrosine kinases signaling. It contains a tyrosine kinase-binding domaina (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB is responsible for the interactions with many tyrosine kinases, such as the colony-stimulating factor-1 (CSF-1) receptor, Syk/ZAP-70, and Src-family of protein tyrosine kinases. The proline-rich domain can recruit proteins with a SH3 domain. Moreover, Cbl functions as an E3 ubiquitin ligase that can bind ubiquitin-conjugating enzymes (E2s) through the RING-HC finger.


Pssm-ID: 319622  Cd Length: 57  Bit Score: 49.66  E-value: 2.66e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-CPLCR 331
Cdd:cd16708   3 LCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQgCPFCR 43
RING-HC_RNFT1_like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
292-331 2.66e-08

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 319446 [Multi-domain]  Cd Length: 40  Bit Score: 49.20  E-value: 2.66e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16532   1 LCPICQDEFKDPIKLRCKHIFCEDCVSEWFDRERTCPLCR 40
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
208-331 3.29e-08

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 54.59  E-value: 3.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089 208 LRVLMSVAPS--ALQLRVRSLPGE----DLRARVSY----RLLGVISLLHLVLSMGLQLYGFRQR--------QRARKEW 269
Cdd:COG5243 183 LLNLTSEANKlcVYNYEARDDDDErstyLFRLEVCYdgltLLAYSLLFMYQFPYVRVPIYLIRQMytcfyalfRRIREHA 262
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24797089 270 RLHRGLSHRRASL----EERAVSRNPLCTLCLEERRH-------------PTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:COG5243 263 RFRRATKDLNAMYptatEEQLTNSDRTCTICMDEMFHpdheplprgldmtPKRLPCGHILHLHCLKNWLERQQTCPICR 341
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
293-330 4.55e-08

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 333836 [Multi-domain]  Cd Length: 40  Bit Score: 48.51  E-value: 4.55e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 24797089   293 CTLCLEE-RRHPTATPCGHLFCWECITAWCSSKAE-CPLC 330
Cdd:pfam00097   1 CPICLEEpKDPVTILPCGHLFCSKCILSWLESGNVtCPLC 40
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
293-330 5.30e-08

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316445 [Multi-domain]  Cd Length: 40  Bit Score: 48.19  E-value: 5.30e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24797089   293 CTLCLEERRHP-TATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:pfam13923   2 CPICLDMLKDPsTTTPCGHVFCQKCILRALRSGNECPLC 40
RING-HC_Cbl-b cd16709
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; ...
292-331 5.45e-08

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; Cbl-b, also known as Casitas B-lineage lymphoma proto-oncogene b, RING finger protein 56 (RNF56), SH3-binding protein Cbl-b, or signal transduction protein Cbl-b, has been identified as a regulator of antigen-specific, T cell-intrinsic, peripheral immune tolerance, a state also known as clonal anergy. It may inhibit activation of the p85 subunit of phosphoinositide 3-kinase (PI3K), protein kinase C-theta (PKC-theta), and phospholipase C-gamma1 (PLC-gamma1) and negatively regulates T-cell receptor-induced transcription factor nuclear factor kappaB (NF-kappaB) activation. In addition, Cbl-b may target multiple signaling molecules involved in transforming growth factor (TGF)-beta-mediated transactivation pathways. Cbl-b contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a proline rich domain, a nuclear localization signal, a C3HC4-type RING-HC finger and an ubiquitin-associated (UBA) domain.


Pssm-ID: 319623  Cd Length: 66  Bit Score: 48.94  E-value: 5.45e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-CPLCR 331
Cdd:cd16709  19 LCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQgCPFCR 59
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
292-331 8.84e-08

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor proteins family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating the activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this family consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 319416 [Multi-domain]  Cd Length: 43  Bit Score: 47.73  E-value: 8.84e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAW-CSSKAECPLCR 331
Cdd:cd16502   3 LCKICAENDKDVRIEPCGHLLCTPCLTSWqDSDGQTCPFCR 43
mRING-HC-C3HC3D_LNX1_like cd16637
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, ...
293-331 8.91e-08

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of Numb protein LNX1, LNX2, and similar proteins; The ligand of Numb protein X (LNX) family, also known as PDZ and RING (PDZRN) family, includes LNX1-5, which can interact with Numb, a key regulator of neurogenesis and neuronal differentiation. LNX5 (also known as PDZK4 or PDZRN4L) shows high sequence homology to LNX3 and LNX4, but it lacks the RING domain. LNX1-4 proteins function as E3 ubiquitin ligases and have a unique domain architecture consisting of an N-terminal RING-HC finger for E3 ubiquitin ligase activity and either two or four PDZ domains necessary for the substrate-binding. This family corresponds to LNX1/LNX2-like proteins, which contains a modified C3HC3D-type RING-HC finger and four PDZ domains.


Pssm-ID: 319551 [Multi-domain]  Cd Length: 42  Bit Score: 47.72  E-value: 8.91e-08
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16637   4 CHICLQPLVDPLDTPCGHTFCSRCLKNYLKVQKFCPIDR 42
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
293-331 1.14e-07

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141 corresponding ZNF230 gene mutation may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 319459 [Multi-domain]  Cd Length: 39  Bit Score: 47.40  E-value: 1.14e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEeRRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16545   2 CCICMD-RKPDTILPCAHSFCQKCIDKWSVRHRTCPICR 39
RING2-HC_LONFs cd16514
RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
293-331 1.47e-07

RING finger 2, HC subclass, found in the LON peptidase N-terminal domain and RING finger proteins family; The LON peptidase N-terminal domain and RING finger proteins family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192 or RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and one N-terminal domain of the ATP-dependent protease La (LON) domain at the C-terminus. Their biological function remain unclear. This family corresponds to the second RING-HC finger.


Pssm-ID: 319428 [Multi-domain]  Cd Length: 42  Bit Score: 46.93  E-value: 1.47e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16514   4 CSLCMRLLYEPVTTPCGHTFCKKCLERCLDHSPKCPLCK 42
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
293-331 3.00e-07

RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319658 [Multi-domain]  Cd Length: 43  Bit Score: 46.05  E-value: 3.00e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSK---AECPLCR 331
Cdd:cd16744   2 CNICLDTAKDAVVSLCGHLFCWPCLHQWLETRpnrQVCPVCK 43
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
293-331 3.71e-07

H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. This family corresponds to H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319362 [Multi-domain]  Cd Length: 44  Bit Score: 45.91  E-value: 3.71e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 293 CTLCLEE----RRHPTATPCGHLFCWECITAWCSS-KAECPLCR 331
Cdd:cd16448   1 CAICLEEfeegDCPVRLLPCGHVFHKSCIDKWLESgNRTCPLCR 44
RING-HC_RNF146 cd16546
RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; ...
293-331 3.76e-07

RING finger, HC subclass, found in RING finger protein 146 (RNF146) and similar proteins; RNF146, also known as dactylidin, or iduna, is a cytoplasmic E3 ubiquitin-protein ligase that is responsible for PARylation-dependent ubiquitination (PARdU). It displays neuroprotective property due to its inhibition of Parthanatos, a PAR dependent cell death, via binding with Poly(ADP-ribose) (PAR). It also modulates PAR polymerase-1 (PARP-1)-mediated oxidative cell injury in cardiac myocytes. Moreover, RNF146 mediates tankyrase-dependent degradation of axin, thereby positively regulates Wnt signaling. It also facilitates DNA repair and protects against cell death induced by DNA damaging agents or gamma-irradiation through translocating to the nucleus after cellular injury and promoting the ubiquitination and degradation of various nuclear proteins involved in DNA damage repair. Furthermore, RNF146 is implicated in neurodegenerative disease and cancer development. It regulates the development and progression of non-small cell lung cancer (NSCLC) by enhancing cell growth, invasion, and survival. RNF146 contains an N-terminal C3HC4-type RING-HC finger followed by a WWE domain with a poly(ADP-ribose) (PAR) binding motif at the tail.


Pssm-ID: 319460 [Multi-domain]  Cd Length: 40  Bit Score: 45.84  E-value: 3.76e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16546   2 CAICLQTCVHPVRLPCGHIFCYLCVKGVAWQSKRCALCR 40
RING-HC_TRIM26_C-IV cd16598
RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar ...
293-331 3.95e-07

RING finger, HC subclass, found in tripartite motif-containing protein 26 (TRIM26) and similar proteins; TRIM26, also known as acid finger protein (AFP), RING finger protein 95 (RNF95), or zinc finger protein 173 (ZNF173), is an E3 ubiquitin-protein ligase that negatively regulates interferon-beta production and antiviral response through polyubiquitination and degradation of nuclear transcription factor IRF3. It functions as an important regulator for RNA virus-triggered innate immune response by bridging TBK1 to NEMO (NF-kappaB essential modulator, also known as IKKgamma) and mediating TBK1 activation. It also acts as a novel tumor suppressor of hepatocellular carcinoma by regulating cancer cell proliferation, colony forming ability, migration, and invasion. TRIM26 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319512 [Multi-domain]  Cd Length: 45  Bit Score: 46.03  E-value: 3.95e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE---CPLCR 331
Cdd:cd16598   4 CSICLDYLRDPVTIDCGHVFCRSCTTDIRPISGNrpvCPLCK 45
RAD18 COG5432
RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];
292-334 4.91e-07

RING-finger-containing E3 ubiquitin ligase [Signal transduction mechanisms];


Pssm-ID: 227719 [Multi-domain]  Cd Length: 391  Bit Score: 50.86  E-value: 4.91e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKF 334
Cdd:COG5432  27 RCRICDCRISIPCETTCGHTFCSLCIRRHLGTQPFCPVCREDP 69
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
292-331 5.56e-07

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 319656 [Multi-domain]  Cd Length: 41  Bit Score: 45.58  E-value: 5.56e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16742   2 ICAICQAEFREPLILICQHVFCEECLCLWFDRERTCPLCR 41
RING-HC_RNF170 cd16553
RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; ...
293-331 6.80e-07

RING finger, HC subclass, found in RING finger protein 170 (RNF170) and similar proteins; RNF170, also known as putative LAG1-interacting protein, is an endoplasmic reticulum (ER) membrane-bound E3 ubiquitin-protein ligase that mediates ubiquitination-dependent degradation of type-I inositol 1,4,5-trisphosphate (IP3) receptors (ITPR1) via the endoplasmic-reticulum-associated protein degradation (ERAD) pathway. A point mutation (arginine to cysteine at position 199) of RNF170 gene is linked with autosomal-dominant sensory ataxia (ADSA), a disease characterized by neurodegeneration in the posterior columns of the spinal cord. RNF170 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319467 [Multi-domain]  Cd Length: 44  Bit Score: 45.36  E-value: 6.80e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-----CPLCR 331
Cdd:cd16553   1 CPICLGDASYPVETNCGHIFCGNCIITYWRHGRWlgaisCPMCR 44
RING-HC_RNF4 cd16533
RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, ...
293-333 7.09e-07

RING finger, HC subclass, found in RING finger protein 4 (RNF4) and similar proteins; RNF4, also known as small nuclear ring finger protein (SNURF), is a SUMO-targeted E3 ubiquitin-protein ligase with a pivotal function in the DNA damage response (DDR) through interacting with the deubiquitinating enzyme ubiquitin-specific protease 11 (USP11), a known DDR-component, and further facilitating DNA repair. It plays a novel role in preventing the loss of intact chromosomes and ensures the maintenance of chromosome integrity. Moreover, RNF4 is responsible for the UbcH5A-catalyzed formation of K48 chains that target SUMO-modified promyelocytic leukemia (PML) protein for proteasomal degradation in response to arsenic treatment. It also interacts with telomeric repeat binding factor 2 (TRF2) in a small ubiquitin-like modifiers (SUMO)-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination through SUMO-interacting motifs (SIMs). Furthermore, RNF4 can form a complex with a Ubc13-ubiquitin conjugate and Ube2V2. It catalyzes K63-linked polyubiquitination by the Ube2V2-Ubc13 (ubiquitin-loaded) complex. Meanwhile, RNF4 negatively regulates nuclear factor kappa B (NF-kappaB) signaling by down-regulating transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1)-TAK1-binding protein2 (TAB2). RNF4 contains four SIMs followed by a C3HC4-type RING-HC finger at the C-terminus.


Pssm-ID: 319447 [Multi-domain]  Cd Length: 54  Bit Score: 45.53  E-value: 7.09e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24797089 293 CTLCLEE-------RRHPTATPCGHLFCWECITAWCSSKAECPLCREK 333
Cdd:cd16533   6 CPICMDGyseivqsGRLLVSTICGHVFCSQCIRDSIKNAHTCPTCRKK 53
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
293-340 7.18e-07

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747  Cd Length: 193  Bit Score: 48.93  E-value: 7.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24797089  293 CTLCLEERRHPTATPCGHLFCWECITAWCSSK----------------AECPLCREKFPPQKLI 340
Cdd:PLN03208  21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASnnsrqrvdqydhkrepPKCPVCKSDVSEATLV 84
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
293-331 7.32e-07

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5 enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319523 [Multi-domain]  Cd Length: 47  Bit Score: 45.17  E-value: 7.32e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE------CPLCR 331
Cdd:cd16609   3 CSICLELFTDPVTLPCGHNFCGECIRDHWDKCELikkgysCPQCR 47
RING_Ubox cd00162
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
293-330 7.41e-07

The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized as two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have different Cys/His pattern. Some lack a single Cys or His residues at typical Zn ligand positions. Especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well. C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC finger. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are close to RING-H2 finger. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerated RING fingers from Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 319361 [Multi-domain]  Cd Length: 40  Bit Score: 45.15  E-value: 7.41e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPT-ATPCGHLFCWECITAWC-SSKAECPLC 330
Cdd:cd00162   1 CPICRELMKDPVvLPSCGHTFCYSCIARWLeSSDQTCPFC 40
RING-HC_LNX3 cd16718
RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ ...
293-331 7.51e-07

RING finger, HC subclass, found in ligand of numb protein X 3 (LNX3); LNX3, also known as PDZ domain-containing RING finger protein 3 (PDZRN3), or Semaphorin cytoplasmic domain-associated protein 3 (SEMACAP3), is an E3 ubiquitin-protein ligase that was first identified as a Semaphorin-binding partner. It is also responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX3 acts as a negative regulator of osteoblast differentiation by inhibiting Wnt-beta-catenin signaling. LNX3 also plays an important role in neuromuscular junction formation. It interacts with and ubiquitinates the muscle specific tyrosine kinase (MuSK), thus promoting its endocytosis and negatively regulating the cell surface expression of this key regulator of postsynaptic assembly. LNX3 contains an N-terminal typical C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 319632 [Multi-domain]  Cd Length: 42  Bit Score: 44.98  E-value: 7.51e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPL-CR 331
Cdd:cd16718   2 CNLCNKVLEDPLTTPCGHVFCAGCVLPWVVQQGSCPVkCQ 41
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
293-331 8.77e-07

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319449 [Multi-domain]  Cd Length: 42  Bit Score: 44.72  E-value: 8.77e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16535   4 CSICSELFIEAVTLNCSHSFCSYCITEWMKRKKECPICR 42
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
293-339 1.12e-06

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 49.62  E-value: 1.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 24797089   293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKFPPQKL 339
Cdd:TIGR00599  29 CHICKDFFDVPVLTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESKL 75
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
293-331 1.12e-06

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 319488 [Multi-domain]  Cd Length: 40  Bit Score: 44.55  E-value: 1.12e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATP-CGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16574   1 CPICLGEFENKSFLDsCFHSFCFGCILEWSKVKAECPLCK 40
RING-HC_TRIM7_C-IV cd16592
RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar ...
293-331 1.44e-06

RING finger, HC subclass, found in tripartite motif-containing protein 7 (TRIM7) and similar proteins; TRIM7, also known as glycogenin-interacting protein (GNIP) or RING finger protein 90 (RNF90), is an E3 ubiquitin-protein ligase that mediates c-Jun/AP-1 activation by Ras signalling. Its phosphorylation and activation by MSK1 in response to direct activation by the Ras-Raf-MEK-ERK pathway can stimulate TRIM7 E3 ubiquitin ligase activity in mediating Lys63-linked ubiquitination of the AP-1 coactivator RACO-1, leading to RACO-1 protein stabilization. Moreover, TRIM7 binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. TRIM7 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319506 [Multi-domain]  Cd Length: 45  Bit Score: 44.39  E-value: 1.44e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAwCSSKAE----CPLCR 331
Cdd:cd16592   4 CSICLDLFRDPVSIPCGHNFCRACIRR-CWELQGstfsCPQCR 45
zf-RING_5 pfam14634
zinc-RING finger domain;
293-331 1.50e-06

zinc-RING finger domain;


Pssm-ID: 339304 [Multi-domain]  Cd Length: 43  Bit Score: 44.34  E-value: 1.50e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24797089   293 CTLCLEERRHPTATPCGHLFCWECITAwCSSKAECPLCR 331
Cdd:pfam14634   5 CFKPLSKTRPFYLTSCGHIFCEECLTK-LLKERQCPICR 42
RING-HC_malin cd16516
RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in ...
292-331 1.86e-06

RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in French), also known as NHL repeat-containing protein 1 (NHLRC1), or EPM2B, is a nuclear E3 ubiquitin-protein ligase that ubiquitinates and promotes the degradation of laforin (EPM2A encoding protein phosphatase). Malin and laforin operate as a functional complex that play key roles in regulating cellular functions such as glycogen metabolism, unfolded cellular stress response, and proteolytic processes. They act as pro-survival factors that negatively regulate the Hipk2-p53 cell death pathway. They also negatively regulate cellular glucose uptake by preventing plasma membrane targeting of glucose transporters. Moreover, they degrade polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase. Furthermore, they, together with Hsp70, form a new functional complex that suppress the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Defects in either malin or laforin may cause Lafora disease (LD), a fatal form of teenage-onset autosomal recessive progressive myoclonus epilepsy. In addition, malin may have function independent of laforin in lysosomal biogenesis and/or lysosomal glycogen disposal. Malin contains six NHL-repeat protein-protein interaction domains and a C3HC4-type RING-HC finger.


Pssm-ID: 319430 [Multi-domain]  Cd Length: 48  Bit Score: 44.05  E-value: 1.86e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24797089 292 LCTLCLE-----ERRHPTATPCGHLFCWECITAWC---SSKAECPLCR 331
Cdd:cd16516   1 ECKVCFEkfstqQQHRPRNLPCGHVLCQECVLALChpnVSKLECPFCR 48
RING-HC_PEX2 cd16526
RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as ...
293-331 2.08e-06

RING finger, HC subclass, found in peroxin-2 (PEX2) and similar proteins; PEX2, also known as peroxisome biogenesis factor 2, 35 kDa peroxisomal membrane protein, peroxisomal membrane protein 3, peroxisome assembly factor 1 (PAF-1), or RING finger protein 72 (RNF72), is an integral peroxisomal membrane protein with two transmembrane regions and a C3HC4-type RING-HC finger within its cytoplasmically exposed C-terminus. It may be involved in the biogenesis of peroxisomes, as well as in peroxisomal matrix protein import. Mutations in the PEX2 gene are the primary defect in a subset of patients with Zellweger syndrome and related peroxisome biogenesis disorders. Moreover, PEX2 functions as an E3-ubiquitin ligase that mediates the UBC4-dependent polyubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation.


Pssm-ID: 319440 [Multi-domain]  Cd Length: 43  Bit Score: 43.91  E-value: 2.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRH-PTATPCGHLFCWECITAWC--SSKAECPLCR 331
Cdd:cd16526   2 CAICGEWPTNnPHAIGCGHVFCYYCIKSNLlaDASFTCPRCG 43
PHA02929 PHA02929
N1R/p28-like protein; Provisional
308-334 2.55e-06

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 47.85  E-value: 2.55e-06
                         10        20
                 ....*....|....*....|....*..
gi 24797089  308 CGHLFCWECITAWCSSKAECPLCREKF 334
Cdd:PHA02929 200 CNHVFCIECIDIWKKEKNTCPVCRTPF 226
mRING-HC-C3HC3D_LNX2 cd16780
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); ...
292-332 2.95e-06

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 2 (LNX2); LNX2, also known as numb-binding protein 2, or PDZ domain-containing RING finger protein 1 (PDZRN1), is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. It interacts with contactin-associated protein 4 (Caspr4, also known as CNTNAP4) in a PDZ domain-dependent manner, which modulates the proliferation and neuronal differentiation of neural progenitor cells (NPCs). LNX2 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAF motif for Numb/ Numblike-LNX interaction, and four PDZ domains necessary for the binding of substrates, including ErbB2, RhoC, the presynaptic protein CAST, the melanoma/cancer-testis antigen MAGEB18 and several proteins associated with cell junctions, such as JAM4 and the Coxsackievirus and adenovirus receptor (CAR).


Pssm-ID: 319694 [Multi-domain]  Cd Length: 45  Bit Score: 43.33  E-value: 2.95e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16780   5 VCHICLQPLLQPLDTPCGHTFCFKCLRNFLQEKDFCPLDRK 45
RING-HC_RAD16_like cd16567
RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, ...
292-330 3.36e-06

RING finger, HC subclass, found in Saccharomyces cerevisiae DNA repair protein RAD16, Schizosaccharomyces pombe rhp16, and similar proteins; Budding yeast RAD16, also known as ATP-dependent helicase RAD16, is encoded by a yeast excision repair gene homologous to the recombinational repair gene RAD54 and to the SNF2 gene involved in transcriptional activation. It is a component of the global genome repair (GGR) complex which promotes global genome nucleotide excision repair (GG-NER) that removes DNA damage from non-transcribing DNA. RAD16 is involved in differential repair of DNA after UV damage, and repairs preferentially the MAT-alpha locus compared with the HML-alpha locus. Fission yeast rhp16, also known as ATP-dependent helicase rhp16, is a RAD16 homolog. It is involved in GGR via nucleotide excision repair (NER), in conjunction with rhp7, after UV irradiation. Both RAD16 and rhp16 contain a C3HC4-type RING-HC finger, as well as a DEAD-like helicase domain and a helicase superfamily C-terminal domain.


Pssm-ID: 319481 [Multi-domain]  Cd Length: 47  Bit Score: 43.20  E-value: 3.36e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSS----KAECPLC 330
Cdd:cd16567   1 VCGICNDPAEDPVVSRCHHAFCRLCVTEYIESapggEVTCPRC 43
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
293-331 3.56e-06

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may associate with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can forms huge ring-shaped oligomeric complex.


Pssm-ID: 319475 [Multi-domain]  Cd Length: 41  Bit Score: 43.24  E-value: 3.56e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE--CPLCR 331
Cdd:cd16561   1 CSICLEDPKDPVSLPCDHIHCLTCLRQWFRPVGQmhCPTCR 41
zf-C3HC4_4 pfam15227
zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like ...
293-330 4.27e-06

zinc finger of C3HC4-type, RING; This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development. This domain is likely to be DNA-binding. This zinc-finger domain together with the RDM domain, pfam11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme.


Pssm-ID: 317611 [Multi-domain]  Cd Length: 42  Bit Score: 42.78  E-value: 4.27e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 24797089   293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE----CPLC 330
Cdd:pfam15227   1 CPICLDYLEKPVSIECGHNFCLSCINSLQKEPDGegflCPLC 42
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
293-331 4.56e-06

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3 which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 42.67  E-value: 4.56e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHP---TATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16454   2 CAICLEEFEDGeevRVLPCNHLFHSNCIDPWLEQHATCPLCR 43
RING-HC_BAR cd16497
RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as ...
293-334 5.04e-06

RING finger, HC subclass, found in bifunctional apoptosis regulator (BAR); BAR, also known as RING finger protein 47, was originally identified as an inhibitor of Bax-induced apoptosis. It participates in the block of apoptosis induced by TNF-family death receptors (extrinsic pathway) and mitochondria-dependent apoptosis (intrinsic pathway). BAR is predominantly expressed by neurons in the central nervous system and is involved in the regulation of neuronal survival. It is an endoplasmic reticulum (ER)-associated RING-type E3 ubiquitin ligase that interacts with BI-1 protein and post-translationally regulates its stability as well as functions in ER stress. BAR contains an N-terminal C3HC4-type RING-HC finger, a SAM domain, a coiled-coil domain, and a C-terminal transmembrane (TM) domain. This family corresponds to the RING-HC finger responsible for the binding of ubiquitin conjugating enzymes (E2s).


Pssm-ID: 319411 [Multi-domain]  Cd Length: 46  Bit Score: 42.86  E-value: 5.04e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAW--CSSKAECPLCREKF 334
Cdd:cd16497   3 CHCCYDLLVNPTTLNCGHSFCRHCLALWwlSSKKTECPECRQKW 46
RING-H2_RNF111_like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
293-332 5.39e-06

RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319388 [Multi-domain]  Cd Length: 46  Bit Score: 42.68  E-value: 5.39e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24797089 293 CTLCLEE-------RRhptaTPCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16474   3 CTICLSEfedgeevRR----LPCMHLFHQACVDQWLATNKRCPICRV 45
RING-HC_LNX4 cd16719
RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ ...
293-331 6.06e-06

RING finger, HC subclass, found in ligand of numb protein X 4 (LNX4); LNX4, also known as PDZ domain-containing RING finger protein 4 (PDZRN4), or SEMACAP3-like protein (SEMCAP3L), is an E3 ubiquitin-protein ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX4 contains an N-terminal typical C3HC4-type RING-HC finger, two PDZ domains, and a C-terminal LNX3 homology (LNX3H) domain.


Pssm-ID: 319633 [Multi-domain]  Cd Length: 42  Bit Score: 42.62  E-value: 6.06e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPL-CR 331
Cdd:cd16719   2 CKLCGKVLEEPLSTPCGHVFCAGCLLPWAVRRRRCPLqCQ 41
RING-HC_RNF10 cd16536
RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 ...
293-330 6.72e-06

RING finger, HC subclass, found in RING finger protein 10 (RNF10) and similar proteins; RNF10 is an E3 ubiquitin-protein ligase that interacts with mesenchyme Homeobox 2 (MEOX2) transcription factor, a regulator of the proliferation, differentiation and migration of vascular smooth muscle cells and cardiomyocytes, and enhances Meox2 activation of the p21 promoter. It also regulates the expression of myelin-associated glycoprotein (MAG) genes and is required for myelin production in Schwann cells of peripheral nervous system. Moreover, RNF10 regulates retinoic acid-induced neuronal differentiation and the cell cycle exit of P19 embryonic carcinoma cells. RNF10 contains a C3HC4-type RING-HC finger and three putative nuclear localization signals.


Pssm-ID: 319450 [Multi-domain]  Cd Length: 43  Bit Score: 42.17  E-value: 6.72e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKA----ECPLC 330
Cdd:cd16536   1 CPICLEPPVAPRITKCGHIFCWPCILHYLSLSEkawrKCPIC 42
mRING-HC-C3HC3D_TRAF6 cd16643
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
291-329 6.97e-06

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) and similar proteins; TRAF6, also known as interleukin-1 signal transducer or RING finger protein 85 (RNF85), is a cytoplasmic adapter protein that mediates signals induced by the tumor necrosis factor receptor (TNFR) superfamily and Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) family. It functions as a mediator involved in the activation of mitogen-activated protein kinase (MAPK), phosphoinositide 3-kinase (PI3K), and interferon regulatory factor pathways, as well as in IL-1R-mediated activation of NF-kappaB. TRAF6 is also an oncogene that plays a vital role in K-RAS-mediated oncogenesis. TRAF6 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 319557 [Multi-domain]  Cd Length: 58  Bit Score: 42.75  E-value: 6.97e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 291 PLCTLCLeerRHPTATPCGHLFCWECITAWCSSKA-ECPL 329
Cdd:cd16643   5 PICLMAL---REPVQTPCGHRFCKSCIKKSIRDAGhRCPV 41
RING-HC_TRIM58_C-IV cd16606
RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar ...
293-331 7.11e-06

RING finger, HC subclass, found in tripartite motif-containing protein TRIM58 and similar proteins; TRIM58, also known as protein BIA2, is an erythroid E3 ubiquitin-protein ligase induced during late erythropoiesis. It binds and ubiquitinates the intermediate chain of the microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the degradation of the dynein holoprotein complex. It may participate in the erythroblast enucleation process through regulation of nuclear polarization. TRIM58 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319520 [Multi-domain]  Cd Length: 51  Bit Score: 42.70  E-value: 7.11e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWC--SSKAE-----CPLCR 331
Cdd:cd16606   4 CPVCLDFLQEPVSVDCGHSFCLRCISEFCekSDSAQggvyaCPQCR 49
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
290-330 7.62e-06

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; RNF145 is an uncharacterized RING finger protein encoded by RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 42.35  E-value: 7.62e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 290 NPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16684   2 NDICSICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLC 42
RING-HC_TRIM17_C-IV cd16595
RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar ...
293-331 7.93e-06

RING finger, HC subclass, found in tripartite motif-containing protein TRIM17 and similar proteins; TRIM17, also known as RING finger protein 16 (RNF16) or testis RING finger protein (Terf), is a crucial E3 ubiquitin ligase that is necessary and sufficient for neuronal apoptosis and contributes to Mcl-1 ubiquitination in cerebellar granule neurons (CGNs). It interacts in a SUMO-dependent manner with nuclear factor of activated T cell NFATc3 transcription factor, and thus inhibits the activity of NFATc3 by preventing its nuclear localization. In contrast, it binds to and inhibits NFATc4 transcription factor in a SUMO-independent manner. Moreover, TRIM17 stimulates degradation of kinetochore protein ZW10 interacting protein (ZWINT), a known component of the kinetochore complex required for the mitotic spindle checkpoint, and negatively regulates cell proliferation. TRIM17 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319509 [Multi-domain]  Cd Length: 48  Bit Score: 42.44  E-value: 7.93e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWC------SSKAECPLCR 331
Cdd:cd16595   4 CSICLDYFKDPVILRCGHNFCRACITQFWekqgglQGKLTCPECR 48
RING-HC_TRIM56_C-V cd16584
RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar ...
293-331 8.04e-06

RING finger, HC subclass, found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may do not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319498 [Multi-domain]  Cd Length: 44  Bit Score: 42.38  E-value: 8.04e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWEC---ITAWCSSKAECPLCR 331
Cdd:cd16584   3 CPICLEHYTKPKSLPCLHTFCEDCleqLIDHNSRRFSCPICR 44
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
292-331 9.39e-06

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR) mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A through blocking of Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide Induced Construct 5 (Hic-5).


Pssm-ID: 319624  Cd Length: 53  Bit Score: 42.38  E-value: 9.39e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-CPLCR 331
Cdd:cd16710   6 LCKICAERDKDVRIEPCGHLLCSCCLAAWQHSDSQtCPFCR 46
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
293-337 9.48e-06

Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain. The architecture suggests a possible role in an RNA-processing complex.


Pssm-ID: 316929  Cd Length: 46  Bit Score: 41.96  E-value: 9.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 24797089   293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKaeCPLCREKFPPQ 337
Cdd:pfam14447   1 CVLCGRVGTVHILSPCGHLVCRDCFDGSDYSG--CPICHRRIDPD 43
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
293-331 1.06e-05

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediated intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids through interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 319461 [Multi-domain]  Cd Length: 39  Bit Score: 41.73  E-value: 1.06e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16547   1 CSICHGVLKCPYMLPCSHIFCKKCILQWLKRQETCPCCR 39
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
293-328 1.10e-05

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 338747 [Multi-domain]  Cd Length: 38  Bit Score: 41.60  E-value: 1.10e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24797089   293 CTLCLEERRHPTaTPCGHLFCWECITAWCSSKAE---CP 328
Cdd:pfam13445   1 CPICLELFTDPV-LPCGHTFCRECLEEMSLLKGGrfkCP 38
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
293-331 1.14e-05

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 319412 [Multi-domain]  Cd Length: 48  Bit Score: 42.00  E-value: 1.14e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSK---AECPLCR 331
Cdd:cd16498   7 CPICLDLMKNPVSTKCDHQFCRFCILKLLSRKkgsAPCPLCK 48
mRING-HC-C3HC3D_LNX1 cd16779
Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); ...
292-331 1.14e-05

Modified RING finger, HC subclass (C3HC3D-type), found in ligand of numb protein X 1 (LNX1); LNX1, also known as numb-binding protein 1 or PDZ domain-containing RING finger protein 2, is a PDZ domain-containing RING-type E3 ubiquitin ligase responsible for the ubiquitination and degradation of Numb, a component of the Notch signaling pathway that functions in the specification of cell fates during development and is known to control cell numbers during neurogenesis in vertebrates. LNX1 contains an N-terminal modified C3HC3D-type RING-HC finger, a NPAY motif for Numb-LNX interaction, and four PDZ domains necessary for the binding of substrates, including CAR, ErbB2, SKIP, JAM4, CAST, c-Src, Claudins, RhoC, KCNA4, PAK6, PLEKHG5, PKC-alpha1, TYK2, PDZ-binding kinase (PBK), LNX2, and itself.


Pssm-ID: 319693 [Multi-domain]  Cd Length: 42  Bit Score: 41.72  E-value: 1.14e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16779   3 ICHICLQPLIQPLDTPCGHTYCTLCLTNFLVEKDFCPVDR 42
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
292-332 1.73e-05

RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; RNF208 is an E3 ubiquitin-protein ligase whose activity can be modulated by S-nitrosylation. It contains a C3HC4-type RING-HC finger.


Pssm-ID: 319473 [Multi-domain]  Cd Length: 50  Bit Score: 41.31  E-value: 1.73e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKA-----ECPLCRE 332
Cdd:cd16559   3 ECPLCGETYNRPRILSCLHSFCEPCLQKLYESCPkykfiSCPTCKR 48
mRING_PEX12 cd16451
Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as ...
293-328 2.12e-05

Modified RING finger found in peroxin-12 (PEX12) and similar proteins; PEX12, also known as peroxisome assembly protein 12 or peroxisome assembly factor 3 (PAF-3), is a RING finger domain-containing integral membrane peroxin required for protein import into peroxisomes. Mutations in human PEX12 result in the peroxisome deficiency Zellweger syndrome of complementation group III (CG-III), a lethal neurological disorder. PEX12 also functions as an E3-ubiquitin ligase that facilitates the PEX4-dependent monoubiquitination of PEX5, a key player in peroxisomal matrix protein import, to control PEX5 receptor recycling or degradation. PEX12 contains a modified RING finger that lacks the third, fourth, and eighth zinc-binding residues of the consensus RING finger motif, suggesting PEX12 may only bind one zinc ion.


Pssm-ID: 319365 [Multi-domain]  Cd Length: 42  Bit Score: 41.02  E-value: 2.12e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 24797089 293 CTLCLEERRHPTA-TPCGHLFCWECITAWCSSKAECP 328
Cdd:cd16451   1 CPLCRKKRTNPTAlSTSGYVFCYPCIYRYVKEHGRCP 37
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
292-331 2.27e-05

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, or TPR repeat protein D, or TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It also affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. TTC3 contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 319395 [Multi-domain]  Cd Length: 42  Bit Score: 40.79  E-value: 2.27e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 292 LCTLCLEERRHPT--ATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16481   1 PCSICHEELKPGTvrKLDCGHRFHKGCIRQWLKEQSTCPTCR 42
RING-HC_TRIM10_C-IV cd16593
RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar ...
293-331 2.41e-05

RING finger, HC subclass, found in tripartite motif-containing protein 10 (TRIM10) and similar proteins; TRIM10, also known as B30-RING finger protein (RFB30), RING finger protein 9 (RNF9), or hematopoietic RING finger 1 (HERF1), is a novel hematopoiesis-specific RING finger protein required for terminal differentiation of erythroid cells. TRIM10 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319507 [Multi-domain]  Cd Length: 49  Bit Score: 41.15  E-value: 2.41e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKA-------ECPLCR 331
Cdd:cd16593   4 CPICQGTLREPVTIDCGHNFCRACLTRYCEIPGpdleeppTCPLCK 49
RING-HC_TRIM4_C-IV_like cd16590
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, ...
293-331 2.50e-05

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM4, TRIM75, tripartite motif family-like protein 1 (TRIML1) and similar proteins; TRIM4 and TRIM75, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM4, also known as RING finger protein 87 (RNF87), is a cytoplasmic E3 ubiquitin-protein ligase that it had recently evolved and is present only in higher mammals. It transiently interacts with mitochondria, induces mitochondrial aggregation and sensitizes the cells to hydrogen peroxide (H2O2) induced death. Its interaction with peroxiredoxin 1 (PRX1) is critical for the regulation of H2O2 induced cell death. Moreover, TRIM4 functions as a positive regulator of RIG-I-mediated type I interferon induction. It regulates the K63-linked ubiquitination of RIG-1 and assembly of antiviral signaling complex at mitochondria. TRIM75 mainly localizes within spindles, suggesting it may function in spindle organization and thereby affect meiosis. The family also includes TRIML1 that is identical to TRIM11 and TRIM17 except for the absence of B-box domain. TRIML1, also known as RING finger protein 209 (RNF209), is a probable E3 ubiquitin-protein ligase expressed in embryo before implantation. It plays an important role in blastocyst development. By interacting with USP5 (also known as isoT), TRIML1 may exerts its influence on debranching ubiquitin from multi-chains on the stability and activity of protein substrates in the preimplantation embryo.


Pssm-ID: 319504 [Multi-domain]  Cd Length: 45  Bit Score: 40.92  E-value: 2.50e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECIT-AW--CSSKAECPLCR 331
Cdd:cd16590   4 CSICLDYFKDPVTIECGHNFCRGCILqSWenLNTPFSCPECR 45
COG5152 COG5152
Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function ...
262-330 3.15e-05

Uncharacterized conserved protein, contains RING and CCCH-type Zn-fingers [General function prediction only];


Pssm-ID: 227481 [Multi-domain]  Cd Length: 259  Bit Score: 44.68  E-value: 3.15e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24797089 262 RQRARKEWRLHRGLShrrASLEERAVSRNP------LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:COG5152 165 RSDFKTGWKLNQEWN---AEYEEAPVISGPgekipfLCGICKKDYESPVVTECGHSFCSLCAIRKYQKGDECGVC 236
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
286-331 3.16e-05

RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control.


Pssm-ID: 315369 [Multi-domain]  Cd Length: 55  Bit Score: 40.76  E-value: 3.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24797089   286 AVSRNPLCTLCLEERRHPTAT------PCGHLFCWECITAWCSSKAECPLCR 331
Cdd:pfam12678   4 AICRNPFEEPCPECQAPGDDEcpvvwgECGHAFHLHCISRWLKTNNTCPLCR 55
RING-HC_TRIM21_C-IV cd16596
RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar ...
293-331 3.25e-05

RING finger, HC subclass, found in tripartite motif-containing protein TRIM21 and similar proteins; TRIM21, also known as 52 kDa Ro protein, 52 kDa ribonucleoprotein autoantigen Ro/SS-A, Ro(SS-A), RING finger protein 81 (RNF81), or Sjoegren syndrome type A antigen (SS-A), is a ubiquitously expressed E3 ubiquitin-protein ligase and a high affinity antibody receptor uniquely expressed in the cytosol of mammalian cells. As a cytosolic Fc receptor, TRIM21 binds the Fc of virus-associated antibodies and targets the complex in the cytosol for proteasomal degradation in a process known as antibody-dependent intracellular neutralization (ADIN), and provides an intracellular immune response to protect host defense against pathogen infection. It shows remarkably broad isotype specificity as it does not only bind IgG, but also IgM and IgA. Moreover, TRIM21 promotes the cytosolic DNA sensor cGAS and the cytosolic RNA sensor RIG-I sensing of viral genomes during infection by antibody-opsonized virus. It stimulates inflammatory signaling and activates innate transcription factors, such as nuclear factor-kappaB (NF-kappaB). TRIM21 also plays an essential role in p62-regulated redox homeostasis, suggesting a viable target for treating pathological conditions resulting from oxidative damage. Furthermore, TRIM21 may have implications for various autoimmune diseases associated uncontrolled antiviral signaling through the regulation of Nmi-IFI35 complex-mediated inhibition of innate antiviral response. TRIM21 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319510 [Multi-domain]  Cd Length: 44  Bit Score: 40.63  E-value: 3.25e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITA----WCSSkaeCPLCR 331
Cdd:cd16596   5 CSICLDPFVEPMSIECGHSFCQECISEvgkyGGSV---CPVCR 44
RING-HC_TRIM11_like_C-IV cd16594
RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, ...
293-331 3.31e-05

RING finger, HC subclass, found in tripartite motif-containing proteins, TRIM11 and TRIM27, and similar proteins; TRIM11 and TRIM27, two closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain. TRIM11, also known as protein BIA1, or RING finger protein 92 (RNF92), is an E3 ubiquitin-protein ligase involved in the development of the central nervous system. It is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth. TRIM11 acts as a potential therapeutic target for congenital central hypoventilation syndrome (CCHS) through mediating the degradation of congenital central hypoventilation syndrome-associated polyalanine-expanded Phox2b. Trim11 modulates the function of neurogenic transcription factor Pax6 through ubiquitin-proteosome system, and thus plays an essential role for the Pax6-dependent neurogenesis. It also binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105), humanin, a neuroprotective peptide against Alzheimer"s disease-relevant insults, through the ubiquitin-proteasome system, and further regulates ARC105 function in transforming growth factor beta (TGFbeta) signaling. Moreover, TRIM11 negatively regulates retinoic acid-inducible gene-I (RIG-I)-mediated interferon-beta (IFNbeta) production and antiviral activity by targeting TANK-binding kinase-1 (TBK1). It may contribute to the endogenous restriction of retroviruses in cells. It enhances N-tropic murine leukemia virus (N-MLV) entry by interfering with Ref1 restriction. It also suppresses the early steps of human immunodeficiency virus HIV-1 transduction, resulting in decreased reverse transcripts. TRIM27, also known as RING finger protein 76 (RNF76), RET finger protein (RFP), or zinc finger protein RFP, is a nuclear E3 ubiquitin-protein ligase that is highly expressed in testis and in various tumor cell lines. Expression of TRIM27 is associated with prognosis of colon and endometrial cancers. TRIM27 was first identified as a fusion partner of the RET receptor tyrosine kinase. It functions as a transcriptional repressor and associates with several proteins involved in transcriptional activity, such as enhancer of polycomb 1 (Epc1), a member of the Polycomb group proteins, and Mi-2beta, a main component of the nucleosome remodeling and deacetylase (NuRD) complex, and the cell cycle regulator retinoblastoma protein (RB1). It also interacts with HDAC1, leading to downregulation of thioredoxin binding protein 2 (TBP-2), which inhibits the function of thioredoxin. Moreover, TRIM27 mediates Pax7-induced ubiquitination of MyoD in skeletal muscle atrophy. In addition, it inhibits muscle differentiation by modulating serum response factor (SRF) and Epc1. Furthermore, TRIM27 promote a non-canonical polyubiquitinations of PTEN, a lipid phosphatase that catalyzes PtdIns(3,4,5)P3 (PIP3) to PtdIns(4,5)P2 (PIP2). It is an IKKepsilon-interacting protein that regulates IkappaB kinase (IKK) function and negatively regulates signaling involved in the antiviral response and inflammation. In addition, TRIM27 forms a protein complex with MBD4 or MBD2 or MBD3, and thus plays an important role in the enhancement of transcriptional repression through MBD proteins in tumorigenesis, spermatogenesis, and embryogenesis. It is also a component of an estrogen receptor 1 (ESR1) regulatory complex, and is involved in estrogen receptor-mediated transcription in MCF-7 cells. Meanwhile, TRIM27 interacts with the hinge region of chromosome 3 protein (SMC3), a component of the multimeric cohesin complex that holds sister chromatids together and prevents their premature separation during mitosis.


Pssm-ID: 319508 [Multi-domain]  Cd Length: 45  Bit Score: 40.53  E-value: 3.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE---CPLCR 331
Cdd:cd16594   4 CPVCLEYFTDPVILDCGHNFCRACILRCWETRATpvsCPQCR 45
mRING-HC-C3HC3D_PHRF1 cd16635
Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger ...
293-331 3.83e-05

Modified RING finger, HC subclass (C3HC3D-type), found in PHD and RING finger domain-containing protein 1(PHRF1) and similar proteins; PHRF1, also known as KIAA1542, or CTD-binding SR-like protein rA9, is a ubiquitin ligase which induces the ubiquitination of TGIF (TG-interacting factor) at lysine 130. It acts as a tumor suppressor that promotes the transforming growth factor (TGF)-beta cytostatic program through selective release of TGIF-driven promyelocytic leukemia protein (PML) inactivation. PHRF1 contains a plant homeodomain (PHD) finger and a modified C3HC3D-type RING-HC finger.


Pssm-ID: 319549 [Multi-domain]  Cd Length: 44  Bit Score: 40.11  E-value: 3.83e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEE-RRHPTATP--CGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16635   3 CPICLNEfTDQAVGTPesCDHYFCLDCILEWSKNVNTCPVDR 44
RING-HC_TRIM25_C-IV cd16597
RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar ...
293-331 3.90e-05

RING finger, HC subclass, found in tripartite motif-containing protein TRIM25 and similar proteins; TRIM25, also known as estrogen-responsive finger protein (EFP), RING finger protein 147 (RNF147), or RING-type E3 ubiquitin transferase, is an E3 ubiquitin/ISG15 ligase that is induced by estrogen and is therefore particularly abundant in placenta and uterus. TRIM25 regulates various cellular processes through E3 ubiquitin ligase activity, transferring ubiquitin and ISG15 to target proteins. It mediates K63-linked polyubiquitination of retinoic acid inducible gene I (RIG-I) that is crucial for downstream antiviral interferon signaling. It is also required for melanoma differentiation-associated gene 5 (MDA5) and mitochondrial antiviral signaling (MAVS, also known as IPS-1, VISA, Cardiff) mediated activation of nuclear factor-kappaB (NF-kappaB) and interferon production. Upon UV irradiation, TRIM25 interacts with mono-ubiquitinated PCNA and promotes its ISG15 modification (ISGylation), suggesting a crucial role in termination of error-prone translesion DNA synthesis. TRIM25 also functions as a novel regulator of p53 and Mdm2. It enhances p53 and Mdm2 abundance by inhibiting their ubiquitination and degradation in 26S proteasomes. Meanwhile, it inhibits p53's transcriptional activity and dampens the response to DNA damage, and is essential for medaka development and this dependence is rescued by silencing of p53. Moreover, TRIM25 is involved in the host cellular innate immune response against retroviral infection. It interferes with the late stage of feline leukemia virus (FeLV) replication. Furthermore, TRIM25 acts as an oncogene in gastric cancer. Its blockade by RNA interference inhibits migration and invasion of gastric cancer cells through transforming growth factor-beta (TGF-beta) signaling, suggesting it presents a novel target for the detection and treatment of gastric cancer. In addition, TRIM25 acts as an RNA-specific activator for Lin28a/TuT4-mediated uridylation. TRIM25 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319511 [Multi-domain]  Cd Length: 44  Bit Score: 40.25  E-value: 3.90e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECIT-AWCS--SKAECPLCR 331
Cdd:cd16597   3 CSICLCLFDNPVTLPCGHNFCANCLEeTWADqiSSLFCPQCR 44
RING-HC_MEX3B cd16721
RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger ...
293-331 4.13e-05

RING finger, HC subclass, found in RNA-binding protein MEX3B; MEX3B, also known as RING finger and KH domain-containing protein 3 (RKHD3), or RING finger protein 195 (RNF195), is a RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It regulates the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions. It has a 3' long conserved untranslated region (3'LCU)-mediated fine-tuning system for mRNA regulation in early vertebrate development such as anteroposterior (AP) patterning and signal transduction. MEX3B contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3B shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319635  Cd Length: 43  Bit Score: 40.25  E-value: 4.13e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGH-LFCWECITAWCS-SKAECPLCR 331
Cdd:cd16721   3 CSVCFESEVIAALVPCGHnLFCMECANRICEkSEPECPVCH 43
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
293-334 4.17e-05

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; The family includes two highly similar E3 ubiquitin-protein ligases Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Furthermore, Praja-1 regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of the Dlx/Msx-interacting MAGE/Necdin family protein, Dlxin-1, via an ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, or NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP) dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Moreover, Praja-2, together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Furthermore, Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 319379 [Multi-domain]  Cd Length: 46  Bit Score: 40.06  E-value: 4.17e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLCREKF 334
Cdd:cd16465   2 CPICCCEyvkDEIATELPCHHLFHKLCITAWLQKSGTCPVCRHVL 46
RING-HC_TRIM5_like-C-IV cd16591
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, ...
293-331 4.57e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM5, TRIM6, TRIM22, TRIM34 and similar proteins; TRIM5, TRIM6, TRIM22, and TRIM34, four closely related tripartite motif-containing proteins, belong to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. TRIM5, also known as RING finger protein 88 (RNF88), is a capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. Its retroviral restriction activity correlates with the ability to activate TAK1-dependent innate immune signaling. TRIM5 also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Moreover, TRIM5 plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. It also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction. TRIM6, also known as RING finger protein 89 (RNF89), is an E3-ubiquitin ligase that cooperates with the E2-ubiquitin conjugase UbE2K to catalyze the synthesis of unanchored K48-linked polyubiquitin chains, and further stimulates the interferon-I kappa B kinase epsilon (IKKepsilon) kinase-mediated antiviral response. It also regulates the transcriptional activity of Myc during the maintenance of embryonic stem (ES) cell pluripotency, and may act as a novel regulator for Myc-mediated transcription in ES cells. TRIM22, also known as 50 kDa-stimulated trans-acting factor (Staf-50) or RING finger protein 94 (RNF94), is an E3 ubiquitin-protein ligase that plays an integral role in the host innate immune response to viruses. It has been shown to inhibit the replication of a number of viruses, including HIV-1, hepatitis B, and influenza A. TRIM22 acts as a suppressor of basal HIV-1 long terminal repeat (LTR)-driven transcription by preventing the transcription factor specificity protein 1 (Sp1) binding to the HIV-1 promoter. It also controls FoxO4 activity and cell survival by directing Toll-like receptor 3 (TLR3)-stimulated cells toward type I interferon (IFN) type I gene induction or apoptosis. Moreover, TRIM22 can activate the noncanonical nuclear factor-kappaB (NF-kappaB) pathway by activating I kappa B kinase alpha (IKKalpha). It also regulates nucleotide binding oligomerization domain containing 2 (NOD2)-dependent activation of interferon-beta signaling and nuclear factor-kappaB. TRIM34, also known as interferon-responsive finger protein 1 or RING finger protein 21 (RNF21), may function as antiviral protein that contribute to the defense against retroviral infections.


Pssm-ID: 319505 [Multi-domain]  Cd Length: 49  Bit Score: 40.16  E-value: 4.57e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSS------KAECPLCR 331
Cdd:cd16591   4 CPICLELLTEPLSLDCGHSFCRACITANHKEsvltdgESSCPVCR 48
RING-HC_TRIM47_C-IV cd16604
RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar ...
293-331 4.59e-05

RING finger, HC subclass, found in tripartite motif-containing protein 47 (TRIM47) and similar proteins; TRIM47, also known as gene overexpressed in astrocytoma protein (GOA) or RING finger protein 100 (RNF100), belongs a subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. It plays an important role in the process of dedifferentiation that is associated with astrocytoma tumorigenesis.


Pssm-ID: 319518 [Multi-domain]  Cd Length: 47  Bit Score: 40.19  E-value: 4.59e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAW------CSSKAECPLCR 331
Cdd:cd16604   3 CPICLDALRDPVTLPCGHNYCLACLQHLwekngsRGGAYRCPECQ 47
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
291-331 5.05e-05

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 319583 [Multi-domain]  Cd Length: 46  Bit Score: 40.05  E-value: 5.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 291 PLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16669   3 PVCLLEFEEGEEVKEMPCKHSFHSGCILPWLKKTNSCPLCR 43
RING-H2_EL5_like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
293-331 6.12e-05

RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.


Pssm-ID: 319375 [Multi-domain]  Cd Length: 43  Bit Score: 39.60  E-value: 6.12e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEE------RRHPtatPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16461   2 CPICLEDfedgelVRLL---KCGHVFHKECIDLWLRSHSTCPLCR 43
COG5222 COG5222
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
258-333 6.75e-05

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227547 [Multi-domain]  Cd Length: 427  Bit Score: 44.35  E-value: 6.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24797089 258 GFRQRQRARKEWRLHRGLSHRRASLEERAVSRNPL-----CTLCLEERRHPTATP-CGHLFCWECI-TAWCSSKAECPLC 330
Cdd:COG5222 237 GYVVAQPDVQSWEKYQQRTKAVAEIPDQVYKMQPPnislkCPLCHCLLRNPMKTPcCGHTFCDECIgTALLDSDFKCPNC 316

                ...
gi 24797089 331 REK 333
Cdd:COG5222 317 SRK 319
RING-HC_TRIM60_like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and ...
293-331 7.21e-05

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and similar proteins; TRIM60 and TRIM61 are two closely related tripartite motif-containing proteins. TRIM60, also known as RING finger protein 129 (RNF129) or RING finger protein 33 (RNF33), is a cytoplasmic protein expressed in the testis. It may play an important role in the spermatogenesis process, the development of the preimplantation embryo, and in testicular functions. RNF33 interacts with the cytoplasmic kinesin motor proteins KIF3A and KIF3B suggesting possible contribution to cargo movement along the microtubule in the expressed sites. It is also involved in spermatogenesis in Sertoli cells under the regulation of nuclear factor-kappaB (NF-kappaB). TRIM60 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast to TRIM60, TRIM61 belongs to the C-V subclass of TRIM family that contains RBCC domains only. Its biological function remains unclear.


Pssm-ID: 319521 [Multi-domain]  Cd Length: 47  Bit Score: 39.58  E-value: 7.21e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECIT-AW--CSSKAECPLCR 331
Cdd:cd16607   4 CPICLEYLKDPVTINCGHNFCRSCLIvSWkdLDDTFPCPVCR 45
RING-H2_RNF24_like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
292-330 7.52e-05

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; The family includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, ?3, ?4, ?5, ?6, and ?7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergoes degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319383 [Multi-domain]  Cd Length: 47  Bit Score: 39.36  E-value: 7.52e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 292 LCTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16469   2 TCAVCLEDfkkKEELGVCPCGHAFHRKCLLKWLEVRNVCPMC 43
SP-RING_like cd16452
A group of variants of RING finger including SP-RING finger, SPL-RING finger, dRING finger, ...
292-331 8.51e-05

A group of variants of RING finger including SP-RING finger, SPL-RING finger, dRING finger, and RING-like Rtf2 domain; The family corresponds to a group of proteins with variants of RING fingers that are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues compared with the classic C3H2C3-/C3HC4-type RING fingers. They include SP-RING finger found in the Siz/PIAS RING (SP-RING) family of SUMO E3 ligases, SPL-RING finger found in E3 SUMO-protein ligase NSE2, degenerated RING (dRING) finger found in Saccharomyces cerevisiae required for meiotic nuclear division protein 5 (Rmd5p) and homologs, and RING-like Rtf2 domain found in the replication termination factor 2 (Rtf2) protein family. The SP-RING family includes PIAS (protein inhibitor of activated STAT) proteins, Zmiz proteins, and Siz proteins from plants and fungi. The PIAS (protein inhibitor of activated STAT) protein family modulates the activity of several transcription factors and acts as an E3 ubiquitin ligase in the sumoylation pathway. NSE2, also known as MMS21 homolog (MMS21) or non-structural maintenance of chromosomes element 2 homolog (Non-SMC element 2 homolog, NSMCE2), is an autosumoylating small ubiquitin-like modifier (SUMO) ligase required for the response to DNA damage. It regulates sumoylation and nuclear-to-cytoplasmic translocation of skeletal and heart muscle-specific variant of the alpha subunit of nascent polypeptide associated complex (skNAC)-Smyd1 in myogenesis. It is also required for resisting extrinsically induced genotoxic stress. Rmd5p, also known as glucose-induced degradation protein 2 (Gid2) or sporulation protein RMD5, is an E3 ubiquitin ligase that forms the heterodimeric E3 ligase unit of the glucose induced degradation deficient (GID) complex with Gid9 (also known as Fyv10), which has a degenerated RING finger as well. The GID complex triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1, 6-bisphosphate by fructose-1, 6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase (PEPCK), and cytoplasmic malate dehydrogenase (c-MDH). The Rtf2 protein family includes a group of conserved proteins found in eukaryotes ranging from fission yeast to humans. The defining member of the family is Schizosaccharomyces pombe Rtf2 (SpRtf2), which is a proliferating cell nuclear antigen-interacting protein that functions as a key requirement for efficient replication termination at the site-specific replication barrier RTS1. It promotes termination at RTS1 by preventing replication restart. The RING-like Rtf2 domain in fission yeast is required to stabilize a paused DNA replication fork during imprinting at the mating type locus, possibly by facilitating sumoylation of PCNA. The family also includes Arabidopsis RTF2 (AtRTF2), an essential nuclear protein required for both normal embryo development and for proper expression of the GFP reporter gene. It plays a critical role in splicing the GFP pre-mRNA, and may also have a more transient regulatory role during the spliceosome cycle. The biological function of Rtf2 homologs found in eumetazoa remains unclear.


Pssm-ID: 319366 [Multi-domain]  Cd Length: 42  Bit Score: 39.25  E-value: 8.51e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-CPLCR 331
Cdd:cd16452   2 ICPITLELMDPPVITPCGHTFSRAAILEWLTKKKRkCPTCR 42
mRING-H2-C3H2C2D_RBX1 cd16485
modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and ...
286-330 8.79e-05

modified RING finger, H2 subclass (C3H2C2D-type), found in RING-box protein 1 (RBX1) and similar proteins; RBX1, also known as Hrt1, protein ZYP, RING finger protein 75 (RNF75), or regulator of cullins 1 (ROC1), is an E3 ubiquitin-protein ligase necessary for ubiquitin ligation activity of the multimeric cullin (Cul)-RING E3 ligases (CRLs). RBX1-containing CRLs are involved in NEDD8 pathway and RBX1 specifically regulate NEDD8ylation of Cul1-4. It can also bind and activate HIV-1 Vif-Cullin5 E3 ligase complex in vitro. Moreover, RBX1 is an essential element of Skp1/Cullins/F-box (SCF) E3-ubiquitin ligase complex that targets diverse proteins for proteasome-mediated degradation. It is a direct functional target of miR-194 and plays an important role in proliferation and migration of gastric cancer (GC) cells. RBX1 is also an essential component of KEAP1/CUL3/RBX1 E3-ubiquitin ligase complex that functions as a regulator of NFE2-related factor 2 (NRF2) and plays a key role in NRF2 pathway deregulation in multiple tumor types, including ovarian carcinomas (OVCA) and papillary thyroid carcinoma (PTC). Furthermore, RBX1 associates with DDB1, Cul4A, and Fbxw5 to form the Fbxw5-DDB1-Cul4A-Rbx1 complex that may function as a dual SUMO/ubiquitin ligase suppressing c-Myb activity through sumoylation or ubiquitination. RBX1 contains a C-terminal modified RING-H2 finger that is C3H2C2D-type, rather than the canonical C3H2C3-type. The modified RING-H2 finger is essential for its ligase activity.


Pssm-ID: 319399 [Multi-domain]  Cd Length: 62  Bit Score: 39.66  E-value: 8.79e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24797089 286 AVSRNPLCTLCLEERRHPTATP----------CGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16485   4 AICRNHIMDLCIECQANQASATseectvawgvCNHAFHFHCISRWLKTRQVCPLD 58
RING-HC_TRIM69_C-IV cd16611
RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar ...
293-331 9.34e-05

RING finger, HC subclass, found in tripartite motif-containing protein 69 (TRIM69) and similar proteins; TRIM69, also known as RFP-like domain-containing protein trimless or RING finger protein 36 (RNF36), is a testis E3 ubiquitin-protein ligase that plays a specific role in apoptosis and may also play an important role in germ cell homeostasis during spermatogenesis. TRIM69 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319525 [Multi-domain]  Cd Length: 44  Bit Score: 39.36  E-value: 9.34e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECIT-AW-CSSKAECPLCR 331
Cdd:cd16611   4 CPLCVEWFKDPVMLPCGHNFCRACIEdVWeGQSSFACPECR 44
RING-HC_TRIM31_C-V cd16582
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar ...
293-330 9.49e-05

RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins; TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.


Pssm-ID: 319496 [Multi-domain]  Cd Length: 41  Bit Score: 38.99  E-value: 9.49e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16582   4 CPICLDILQKPVTIDCGHTFCLKCITQIKEGFFKCPLC 41
RING-HC_MEX3 cd16518
RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 ...
293-331 9.77e-05

RING finger, HC subclass, found in RNA-binding proteins of the evolutionarily-conserved MEX-3 family; The family includes MEX-3 family phosphoproteins have been found in vertebrates. They are mediators of post-transcriptional regulation in different organisms, and have been implicated in many core biological processes, including embryonic development, epithelial homeostasis, immune responses, metabolism, and cancer. They contain two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. They shuttle between the nucleus and the cytoplasm via the CRM1-dependent export pathway. The RNA-binding protein MEX-3 from nematode Caenorhabditis elegans is the founding member of the MEX-3 family. Due to the lack of RING-HC finger, it is not included here.


Pssm-ID: 319432  Cd Length: 41  Bit Score: 38.89  E-value: 9.77e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGH-LFCWECITAWC-SSKAECPLCR 331
Cdd:cd16518   1 CVVCFESEVVAALVPCGHnLFCMECANRICeKSDAECPVCH 41
RING-HC_RAD18 cd16529
RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; ...
293-331 9.82e-05

RING finger, HC subclass, found in postreplication repair protein RAD18 and similar proteins; RAD18, also known as HR18 or RING finger protein 73 (RNF73), is an E3 ubiquitin-protein ligase involved in post replication repair of UV-damaged DNA via its recruitment to stalled replication forks. It associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on K164. It also interacts with another E2 ubiquitin conjugating enzyme RAD6 to form a complex that monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Moreover, Rad18 is a key factor in double-strand break DNA damage response (DDR) pathways via its association with K63-linked polyubiquitylated chromatin proteins. It can function as a mediator for DNA damage response signals to activate the G2/M checkpoint in order to maintain genome integrity and cell survival after ionizing radiation (IR) exposure. RAD18 contains a C3HC4-type RING-HC finger, a ubiquitin-binding zinc finger domain (UBZ), a SAP (SAF-A/B, Acinus and PIAS) domain, and a RAD6-binding domain (R6BD).


Pssm-ID: 319443 [Multi-domain]  Cd Length: 42  Bit Score: 39.17  E-value: 9.82e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRH-PTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16529   3 CPICFDYFDTaPMITPCSHNFCSLCIRRHLSYKTQCPTCR 42
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
290-331 1.13e-04

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated- (FHA) and a C3HC4-type RING-HC finger.


Pssm-ID: 319417 [Multi-domain]  Cd Length: 44  Bit Score: 38.93  E-value: 1.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 290 NPLCTLCLEERRHP-TATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16503   2 TLLCSICQDLLHDCvSLQPCMHNFCAGCYSEWMERSSLCPQCR 44
APC11 COG5194
Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational ...
286-338 1.34e-04

Component of SCF ubiquitin ligase and anaphase-promoting complex [Posttranslational modification, protein turnover, chaperones / Cell division and chromosome partitioning];


Pssm-ID: 227521 [Multi-domain]  Cd Length: 88  Bit Score: 40.20  E-value: 1.34e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24797089 286 AVSRNPLCTLCLEERrhPTATP----------CGHLFCWECITAWCSSKAECPLCREKFPPQK 338
Cdd:COG5194  24 AICRNHIMGTCPECQ--FGMTPgdecpvvwgvCNHAFHDHCIYRWLDTKGVCPLDRQTWVLAD 84
RING-HC_RNF180 cd16554
RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; ...
293-331 1.35e-04

RING finger, HC subclass, found in RING finger protein 180 (RNF180) and similar proteins; RNF180, also known as Rines, is a membrane-bound E3 ubiquitin-protein ligase well conserved among vertebrates. It is a critical regulator of the monoaminergic system, as well as emotional and social behavior. It interacts with brain monoamine oxidase A (MAO-A) and targets it for ubiquitination and degradation. It also functions as a novel tumor suppressor in gastric carcinogenesis. The hypermethylated CpG site count of RNF180 DNA promoter can be used to predict the survival of gastric cancer. RNF180 contains a novel conserved dual specificity protein phosphatase Rines conserved (DSPRC) domain, a basic coiled-coil domain, a C3HC4-type RING-HC finger, and a C-terminal hydrophobic region that is predicted to be a transmembrane domain.


Pssm-ID: 319468 [Multi-domain]  Cd Length: 44  Bit Score: 38.88  E-value: 1.35e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRHP-TATPCGHLFCWEC---ITAWCSSKAECPLCR 331
Cdd:cd16554   2 CPVCLDLYYDPyMCYPCGHIFCEPClrqLAKSSPKNTPCPLCR 44
RING-HC_RNF166 cd16549
RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; ...
293-334 1.37e-04

RING finger, HC subclass, found in RING finger protein 166 (RNF166) and similar proteins; RNF166 is encoded by gene RNF166 targeted by thyroid hormone receptor alpha1 (TRalpha1), which is important in brain development. It plays an important role in RNA virus-induced interferon-beta production by enhancing the ubiquitination of TRAF3 and TRAF6. RNF166, together with three closely related proteins: RNF114, RNF125 and RNF138, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 319463 [Multi-domain]  Cd Length: 47  Bit Score: 38.66  E-value: 1.37e-04
                        10        20        30        40
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gi 24797089 293 CTLCLEERRHPTA-TPCGHLFCWECITAWCSSKA-ECPLCREKF 334
Cdd:cd16549   4 CPICLEVYHKPVSiASCGHTFCGECLQPCLQVPSpLCPLCRMPF 47
RING-HC_RNF135_like cd16543
RING finger, HC subclass, found in RING finger protein 135 (RNF135), tripartite ...
293-331 1.45e-04

RING finger, HC subclass, found in RING finger protein 135 (RNF135), tripartite motif-containing protein 15 (TRIM15) and similar proteins; RNF135, also known as RIG-I E3 ubiquitin ligase (REUL) or Riplet, is a widely expressed E3 ubiquitin-protein ligase that consists of an N-terminal C3HC4-type RING-HC finger and C-terminal B30.2/SPRY and PRY motifs, but lacks the B-box and coiled-coil domains that are also typically present in TRIM proteins. RNF135 serves as a specific retinoic acid-inducible gene-I (RIG-I)-interacting protein that ubiquitinates RIG-I and specifically stimulates RIG-I-mediated innate antiviral activity to produce antiviral type-I interferon (IFN) during the early phase of viral infection. It also has been identified as a bio-marker and therapy target of glioblastoma. It associates with the ERK signal transduction pathway and plays a role in glioblastoma cell proliferation, migration and cell cycle. TRIM15, also known as RING finger protein 93 (RNF93), zinc finger protein 178 (ZNF178), or zinc finger protein B7 (ZNFB7), is a focal adhesion protein that regulates focal adhesion disassembly. It localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. TRIM15 can also associate with coronin 1B, cortactin, filamin binding LIM protein1, and vasodilator-stimulated phosphoprotein, which are involved in actin cytoskeleton dynamics. As an additional component of the integrin adhesome, it regulates focal adhesion turnover and cell migration. TRIM15 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a SPRY/B30.2 domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319457 [Multi-domain]  Cd Length: 37  Bit Score: 38.59  E-value: 1.45e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKaeCPLCR 331
Cdd:cd16543   1 CILCQGLLFDPVTIPCGHTFCRRCLERLPSKL--CPTCR 37
RING-HC_TRIM3 cd16768
RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also ...
292-331 1.50e-04

RING finger, HC subclass, found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in glioblastoma. It binds to the cdk inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclin D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of postsynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendritic spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319682 [Multi-domain]  Cd Length: 45  Bit Score: 38.83  E-value: 1.50e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKA---ECPLCR 331
Cdd:cd16768   3 VCSICLDRYHNPKVLPCLHTFCERCLQNYIPPQSltlSCPVCR 45
RING-H2_RNF126_like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
293-331 1.80e-04

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; The family includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319581 [Multi-domain]  Cd Length: 43  Bit Score: 38.45  E-value: 1.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEE-RRHPTA--TPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16667   2 CAVCKEDfKVGEKVrqLPCNHVFHPDCIVPWLEQHNTCPVCR 43
RING-HC_DTX3 cd16711
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar ...
293-331 1.88e-04

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3) and similar proteins; DTX3, also known as RING finger protein 154 (RNF154), is an E3 ubiquitin-protein ligase that belongs to the Deltex (DTX) family. In contrast to other DTXs, DTX3 does not contain N-terminal two Notch-binding WWE domains, but a short unique N-terminal domain, suggesting it does not interact with intracellular domain of Notch. Its C-terminal region includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain.


Pssm-ID: 319625 [Multi-domain]  Cd Length: 41  Bit Score: 38.18  E-value: 1.88e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEE-RRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16711   2 CPICLGEiQNKKTLDKCKHSFCEDCITRALQVKKACPMCG 41
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
293-331 1.94e-04

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. Moreover, RNF111 regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 319595 [Multi-domain]  Cd Length: 46  Bit Score: 38.52  E-value: 1.94e-04
                        10        20        30        40
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gi 24797089 293 CTLCL---EERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16681   3 CTICLsilEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICR 44
RING-HC_LRSAM1 cd16515
RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing ...
292-331 2.07e-04

RING finger, HC subclass, found in leucine-rich repeat and sterile alpha motif-containing protein 1 (LRSAM1) and similar proteins; LRSAM1, also known as Tsg101-associated ligase (TAL), or RIFLE, is an E3 ubiquitin-protein ligase that physically associates with, and selectively ubiquitylates, Tsg101, an E2-like molecule that regulates vesicular trafficking processes in yeast and mammals. It regulates a Tsg101-associated complex responsible for the sorting of cargo into cytoplasm-containing vesicles that bud at the multivesicular body and at the plasma membrane. LRSAM1 is a multidomain protein containing an N-terminal leucine-rich repeat (LRR), followed by several recognizable motifs, including an ezrin-radixin-moezin (ERM) domain, a coiled-coil (CC) region, a SAM domain, and a C-terminal C3HC4-type RING-HC finger domain.


Pssm-ID: 319429  Cd Length: 40  Bit Score: 38.04  E-value: 2.07e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCweCITawCSSK-AECPLCR 331
Cdd:cd16515   1 ECVICLEQESQMIFLPCGHVCC--CQT--CSAPlQSCPLCR 37
RING-HC_RNF114 cd16540
RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; ...
293-331 2.10e-04

RING finger, HC subclass, found in RING finger protein 114 (RNF114) and similar proteins; RNF114, also known as zinc finger protein 228 (ZNF228) or zinc finger protein 313 (ZNF313), is a p21(WAF1)-targeting ubiquitin E3 ligase that interacts with X-linked inhibitor of apoptosis (XIAP)-associated factor 1 (XAF1) and may play a role in p53-mediated cell-fate decisions. It is involved in immune response to double-stranded RNA in disease pathogenesis. Moreover, RNF114 interacts with A20 and modulates its ubiquitylation. It negatively regulates nuclear factor-kappaB (NF-kappaB)-dependent transcription and positively regulates T-cell activation. RNF114 may play a putative role in the regulation of immune responses, since it corresponds to a novel psoriasis susceptibility gene, ZNF313. RNF114, together with three closely related proteins: RNF125, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 319454 [Multi-domain]  Cd Length: 42  Bit Score: 38.28  E-value: 2.10e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-CPLCR 331
Cdd:cd16540   3 CPVCLEVFEKPVRVPCGHVFCSACLQECLKPKKPvCGVCR 42
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
293-332 2.40e-04

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity through modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. Furthermore, RNF6 acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana.


Pssm-ID: 319587 [Multi-domain]  Cd Length: 45  Bit Score: 38.08  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24797089 293 CTLCLEE-------RRhptaTPCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16673   3 CSVCINEyatgnklRR----LPCAHEFHIHCIDRWLSENSTCPICRQ 45
RING-HC_TRIM39_C-IV cd16601
RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar ...
293-330 2.44e-04

RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins; TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcriptions, which is induced by inflammatory stimulants such as tumor necrosis factor alpha (TNFalpha). Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319515 [Multi-domain]  Cd Length: 44  Bit Score: 38.11  E-value: 2.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAW---CSSKAECPLC 330
Cdd:cd16601   4 CSVCLEYLKEPVIIECGHNFCKACITRWwedLERDFPCPVC 44
RING-HC_TRIM68_C-IV cd16610
RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar ...
293-331 2.59e-04

RING finger, HC subclass, found in tripartite motif-containing protein 68 (TRIM68) and similar proteins; TRIM68, also known as RING finger protein 137 (RNF137) or SSA protein SS-56 (SS-56), is an E3 ubiquitin-protein ligase that negatively regulates Toll-like receptor (TLR)- and RIG-I-like receptor (RLR)-driven type I interferon production by degrading TRK fused gene (TFG), a novel driver of IFN-beta downstream of anti-viral detection systems. It also functions as a cofactor for androgen receptor-mediated transcription through regulating ligand-dependent transcription of androgen receptor in prostate cancer cells. Moreover, TRIM68 is a cellular target of autoantibody responses in Sjogren"s syndrome (SS), as well as systemic lupus erythematosus (SLE). It is also an auto-antigen for T cells in SS and SLE. TRIM68 belongs the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, a B-box, and two coiled coil domains, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319524 [Multi-domain]  Cd Length: 49  Bit Score: 37.99  E-value: 2.59e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-------CPLCR 331
Cdd:cd16610   4 CPICMTFLREPVSIDCGHSFCHSCLSGLWEVPGEsqnwgytCPLCR 49
RING-HC_RNF112 cd16538
RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; ...
291-332 2.69e-04

RING finger, HC subclass, found in RING finger protein 112 (RNF112) and similar proteins; RNF112, also known as brain finger protein (BFP), zinc finger protein 179 (ZNF179), or neurolastin, is a peripheral membrane protein that is predominantly expressed in the central nervous system and localizes to endosomes. It contains functional GTPase and C3HC4-type RING-HC finger domains and has been identified as a brain-specific dynamin family GTPase that affects endosome size and spine density. Moreover, RNF112 acts as a downstream target of sigma-1 receptor (Sig-1R) regulation and may play a novel role in neuroprotection by mediating the neuroprotective effects of dehydroepiandrosterone (DHEA) and its sulfated analog (DHEAS).


Pssm-ID: 319452 [Multi-domain]  Cd Length: 48  Bit Score: 38.03  E-value: 2.69e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 291 PLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16538   1 PTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPE 42
RING-HC_TRIM35_C-IV cd16599
RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar ...
292-332 2.81e-04

RING finger, HC subclass, found in tripartite motif-containing protein 35 (TRIM35) and similar proteins; TRIM35, also known as hemopoietic lineage switch protein 5 (HLS5), is a putative hepatocellular carcinoma (HCC) suppressor that inhibits phosphorylation of pyruvate kinase isoform M2 (PKM2), which is involved in aerobic glycolysis of cancer cells and further suppresses the Warburg effect and tumorigenicity in HCC. It also negatively regulates Toll-like receptor 7 (TLR7)- and TLR9-mediated type I interferon production by suppressing the stability of interferon regulatory factor 7 (IRF7). Moreover, TRIM35 regulates erythroid differentiation by modulating globin transcription factor 1 (GATA-1) activity. TRIM35 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319513 [Multi-domain]  Cd Length: 44  Bit Score: 37.99  E-value: 2.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECIT-AWCSSKAECPLCRE 332
Cdd:cd16599   3 LCPICYDPFREAVTLRCGHNFCKGCVSrSWEVRSHTCPVCKE 44
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
293-331 2.90e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 319495 [Multi-domain]  Cd Length: 45  Bit Score: 37.82  E-value: 2.90e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWC--SSKAECPLCR 331
Cdd:cd16581   5 CSICLDIFNDPRVLPCLHTFCKNCLEGRAaeSGPLKCPTCR 45
RING-HC_MEX3D cd16723
RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger ...
293-331 3.02e-04

RING finger, HC subclass, found in RNA-binding protein MEX3D; MEX3D, also known as RING finger and KH domain-containing protein 1 (RKHD1), RING finger protein 193 (RNF193), or TINO, is a RNA-binding phosphoprotein that controls the stability of the transcripts coding for the anti-apoptotic protein BCL-2, and negatively regulates BCL-2 in HeLa cells. MEX3D contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3D shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319637  Cd Length: 45  Bit Score: 37.95  E-value: 3.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGH-LFCWECITAWC-SSKAECPLCR 331
Cdd:cd16723   3 CVVCFESEVIAALVPCGHnLFCMECAIRICeKSEPECPACH 43
RING-HC_MEX3A cd16720
RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger ...
293-330 3.02e-04

RING finger, HC subclass, found in RNA-binding protein MEX3A; MEX3A, also known as RING finger and KH domain-containing protein 4 (RKHD4), is a RNA-binding phosphoprotein that localizes in P-bodies and stress granules, which are two structures involved in the storage and turnover of mRNAs. It has been implicated in the regulation of tumorigenesis. It controls the polarity and stemness of intestinal epithelial cells through the post-transcriptional regulation of the homeobox transcription factor CDX2, which plays a crucial role in intestinal cell fate specification, both during normal development and in tumorigenic processes involving intestinal reprogramming. Moreover, it exhibits a transforming activity when overexpressed in gastric epithelial cells. MEX3A contains two K homology (KH) domains that provide RNA-binding capacity, and a C-terminal C3HC4-type RING-HC finger. Like other MEX-3 family proteins, MEX3A shuttles between the nucleus and the cytoplasm via the CRM1-dependent export pathway.


Pssm-ID: 319634  Cd Length: 43  Bit Score: 37.57  E-value: 3.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGH-LFCWECITAWC-SSKAECPLC 330
Cdd:cd16720   3 CMVCFESEVTAALVPCGHnLFCMECAVRICeRNEPECPVC 42
mRING-HC-C4C4_TRIM37_C-VIII cd16619
Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 ...
293-331 3.05e-04

Modified RING finger, HC subclass (C4C4-type), found in tripartite motif-containing protein 37 (TRIM37) and similar proteins; TRIM37, also known as mulibrey nanism protein, or MUL, is a peroxisomal E3 ubiquitin-protein ligase that is involved in the tumorigenesis of several cancer types, including pancreatic ductal adenocarcinoma (PDAC), hepatocellular carcinoma (HCC), breast cancer, and sporadic fibrothecoma. It mono-ubiquitinates histone H2A, a chromatin modification associated with transcriptional repression. Moreover, TRIM37 possesses anti-HIV-1 activity, and interferes with viral DNA synthesis. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction, and hepatomegaly. TRIM37 belongs to the C-VIII subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a MATH (meprin and TRAF-C homology) domain positioned C-terminal to the RBCC domain. Its MATH domain has been shown to interact with the TRAF (TNF-Receptor-Associated Factor) domain of six known TRAFs in vitro.


Pssm-ID: 319533 [Multi-domain]  Cd Length: 43  Bit Score: 37.71  E-value: 3.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATP-CGHLFCWECITAW-CSSKAECPLCR 331
Cdd:cd16619   3 CFICMEKLRDARLCPhCSKLCCFSCIRRWlTEQRSQCPHCR 43
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
292-332 3.27e-04

RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM2 also plays a role in mediating the p42/p44 MAPK-dependent ubiquitination of the cell death-promoting protein Bcl-2-interacting mediator of cell death (Bim) in rapid ischemic tolerance. TRIM2 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319681 [Multi-domain]  Cd Length: 46  Bit Score: 37.71  E-value: 3.27e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKA---ECPLCRE 332
Cdd:cd16767   3 ICSICLDRYKNPKVLPCLHTFCERCLQNYIPAHSltlSCPVCRQ 46
RING-HC_TRIM72_C-IV cd16612
RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar ...
293-331 3.58e-04

RING finger, HC subclass, found in tripartite motif-containing protein 72 (TRIM72) and similar proteins; TRIM72, also known as Mitsugumin-53 (MG53), is a muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at muscle injury sites. It is required in repair of alveolar epithelial cells under plasma membrane stress failure. It interacts with dysferlin to regulate sarcolemmal repair. Upregulation of TRIM72 develops obesity, systemic insulin resistance, dyslipidemia, and hyperglycemia, as well as induces diabetic cardiomyopathy through transcriptional activation of peroxisome proliferation-activated receptor alpha (PPAR-alpha) signaling pathway. Compensation for the absence of AKT signaling by ERK signaling during TRIM72 overexpression leads to pathological hypertrophy. Moreover, TRIM72 functions as a novel negative feedback regulator of myogenesis via targeting insulin receptor substrate-1 (IRS-1). It is transcriptionally activated by the synergism of myogenin (MyoD) and myocyte enhancer factor 2 (MEF2). TRIM72 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319526 [Multi-domain]  Cd Length: 47  Bit Score: 37.55  E-value: 3.58e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE-----CPLCR 331
Cdd:cd16612   4 CPLCLELFRAPVTPECGHTFCQACLTRVAKEQDQngttpCPTCQ 47
RING-HC_RNF113A_B cd16539
RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; ...
293-330 4.09e-04

RING finger, HC subclass, found in RING finger proteins RNF113A, RNF113B, and similar proteins; RNF113A, also known as zinc finger protein 183 (ZNF183), is an E3 ubiquitin-protein ligase that physically interacts with the E2 protein, UBE2U. A nonsense mutation in RNF113A is associated with an X-linked trichothiodystrophy (TTD). Its yeast ortholog Cwc24p is predicted to have a spliceosome function and acts in a complex with Cef1p to participate in pre-U3 snoRNA splicing, indirectly affecting pre-rRNA processing. It is also important for the U2 snRNP binding to primary transcripts and co-migrates with spliceosomes. Moreover, the ortholog of RNF113A in fruit flies may also act as a spliceosome and is hypothesized to be involved in splicing, namely within the central nervous system. The ortholog in Caenorhabditis elegans is involved in DNA repair of inter-strand crosslinks. RNF113B, also known as zinc finger protein 183-like 1, shows high sequence similarity with RNF113A. Both RNF113A and RNF113B contain a CCCH-type zinc finger, which is commonly found in RNA-binding proteins involved in splicing, and a C3HC4-type RING-HC finger, which is frequently found in E3 ubiquitin ligases.


Pssm-ID: 319453 [Multi-domain]  Cd Length: 41  Bit Score: 37.21  E-value: 4.09e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16539   3 CFICRKPFKNPVVTKCGHYFCEKCALKHYRKSKRCFVC 40
RING-HC_RNF20_like cd16704
RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; ...
293-334 4.15e-04

RING finger, HC subclass, found in RING finger protein RNF20, RNF40, and similar proteins; RNF20, also known as BRE1A, and RNF40, also known as BRE1B, are E3 ubiquitin-protein ligases that work together to form a heterodimeric complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. RNF20 regulates the cell cycle and differentiation of neural precursor cells (NPCs) and links histone H2B ubiquitylation with inflammation and inflammation-associated cancer. RNF40, also known as 95 kDa retinoblastoma-associated protein (RBP95), was identified as a novel leucine zipper retinoblastoma protein (pRb)-associated protein that may function as a regulation factor in the process of RNA polymerase II-mediated transcription and/or transcriptional processing. All family members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319618 [Multi-domain]  Cd Length: 46  Bit Score: 37.51  E-value: 4.15e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECI-TAWCSSKAECPLCREKF 334
Cdd:cd16704   3 CPCCNTRRKDAVLTKCFHVFCFECLkTRYETRQRKCPKCNAAF 45
RING-H2_RNF121_like cd16475
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ...
307-333 4.35e-04

RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; The family includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damages. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a novel positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All family members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity.


Pssm-ID: 319389 [Multi-domain]  Cd Length: 55  Bit Score: 37.65  E-value: 4.35e-04
                        10        20
                ....*....|....*....|....*....
gi 24797089 307 PCGHLFCWECITAWC--SSKAECPLCREK 333
Cdd:cd16475  27 SCGHVFHEFCIRGWCivGKKQTCPYCKEK 55
RING-HC_MYLIP cd16523
RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) ...
292-331 4.41e-04

RING finger, HC subclass, found in myosin regulatory light chain interacting protein (MYLIP) and similar proteins; MYLIP, also known as inducible degrader of the low-density lipoprotein (LDL)-receptor (IDOL), or MIR, is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR, and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains an ERM-homology domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319437  Cd Length: 38  Bit Score: 37.11  E-value: 4.41e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSkaeCPLCR 331
Cdd:cd16523   1 LCMVCCEEEINSAFCPCGHMVCCESCAAQLQS---CPVCR 37
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
293-332 4.61e-04

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 319480 [Multi-domain]  Cd Length: 41  Bit Score: 37.34  E-value: 4.61e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHL-FCWECitawCSSKAECPLCRE 332
Cdd:cd16566   3 CTLCFDKVADTTLRPCGHSgFCMDC----ALQLETCPLCRQ 39
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
293-331 4.68e-04

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting the crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, Synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, Synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of Synoviolin may represent a protective response against neurodegeneration in Parkinson"s disease (PD). In addition, Synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 319393 [Multi-domain]  Cd Length: 43  Bit Score: 37.28  E-value: 4.68e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEE-RRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16479   4 CIICREEmVSGAKKLPCGHIFHLSCLRSWLQRQQTCPTCR 43
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
293-334 5.28e-04

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 319369 [Multi-domain]  Cd Length: 44  Bit Score: 36.96  E-value: 5.28e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCREKF 334
Cdd:cd16455   3 CAICWESMQTARKLPCGHLFHNSCLRSWLEQDTSCPTCRRSL 44
RING-HC_DTX3L cd16712
RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, ...
293-330 5.98e-04

RING finger, HC subclass, found in protein Deltex-3-like (DTX3L) and similar proteins; DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), is a RING-domain E3 ubiquitin-protein ligase that regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. DTX3L has a unique N-terminus, but lacks the highly basic N-terminal motif and the central proline-rich motif present in other Deltex (DTX) family members, such as DTX1, DTX2, and DTX4. Moreover, its C-terminal region is highly homologous to DTX3. It includes a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N-terminus and further enhance self-ubiquitination.


Pssm-ID: 319626 [Multi-domain]  Cd Length: 41  Bit Score: 36.66  E-value: 5.98e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATP-CGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16712   2 CPICMDKVSDPKVLPkCKHVFCAACIDEAFKHKPVCPVC 40
RING-HC_TRIM62_C-IV cd16608
RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar ...
292-331 6.29e-04

RING finger, HC subclass, found in tripartite motif-containing protein 62 (TRIM62) and similar proteins; TRIM62, also known as Ductal Epithelium Associated Ring Chromosome 1 (DEAR1), is a cytoplasmic E3 ubiquitin-protein ligase that was identified as a dominant regulator of acinar morphogenesis in the mammary gland. It is implicated in the inflammatory response of immune cells by regulating the Toll-like receptor 4 (TLR4) signaling pathway, leading to increased activity of the activator protein 1 (AP-1) transcription factor in primary macrophages. It is also involved in muscular protein homeostasis, especially during inflammation-induced atrophy, and may play a role in the pathogenesis of ICU-acquired weakness (ICUAW) by activating and maintaining inflammation in myocytes. Moreover, TRIM62 facilitates K27-linked poly-ubiquitination of CARD9 and also regulates CARD9-mediated anti-fungal immunity and intestinal inflammation. Furthermore, TRIM62 is involved in the regulation of apical-basal polarity and acinar morphogenesis. It also functions as a chromosome 1p35 tumor suppressor and negatively regulates transforming growth factor beta (TGFbeta)-driven epithelial-mesenchymal transition (EMT) through binding to and promoting the ubiquitination of SMAD3, a major effector of TGFbeta-mediated EMT. TRIM62 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319522 [Multi-domain]  Cd Length: 50  Bit Score: 36.96  E-value: 6.29e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITA-WCSSKA----ECPLCR 331
Cdd:cd16608   5 LCSICLSIYQDPVSFGCEHYFCRKCITEhWSRQEHqgtrDCPECR 49
RING-HC_MID_C-I cd16575
RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; ...
293-332 7.03e-04

RING finger, HC subclass, found in midline-1 (MID1), midline-2 (MID2) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is highly related to MID1. It associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. They also play a central role in the regulation of granule exocytosis and the functional redundancy exists between MID1 and MID2 in cytotoxic lymphocytes (CTL). Both MID1 and MID2 belong to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319489 [Multi-domain]  Cd Length: 52  Bit Score: 37.13  E-value: 7.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKAE------------CPLCRE 332
Cdd:cd16575   1 CPICLELFEDPILLPCSHNLCKSCAERLVVSHCGsgesgetresfrCPTCRT 52
RING-HC_RING1 cd16739
RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar ...
292-333 7.13e-04

RING finger, HC subclass, found in really interesting new gene 1 protein (RING1) and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. It is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase that transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING1 interacts with multiple PcG proteins and displays tumorigenic activity. It also shows zinc-dependent DNA binding activity. Moreover, RING1 inhibits transactivation of the DNA-binding protein recombination signal binding protein-Jkappa (RBP-J) by Notch through interaction with the LIM domains of KyoT2. RING1 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319653  Cd Length: 44  Bit Score: 36.64  E-value: 7.13e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 292 LCTLCLEERRHPTATP-CGHLFCWECI-TAWCSSKAECPLCREK 333
Cdd:cd16739   1 MCPICLDMLKNTMTTKeCLHRFCSDCIvTALRSGNKECPTCRKK 44
RING-HC_MKRN1_3 cd16730
RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; ...
292-331 7.56e-04

RING finger, HC subclass, found in makorin-1 (MKRN1), makorin-3 (MKRN3), and similar proteins; MKRN1, also known as makorin RING finger protein 1 or RING finger protein 61 (RNF61), is an E3 ubiquitin-protein ligase targeting the telomerase catalytic subunit (TERT) for proteasome processing. It regulates the ubiquitination and degradation of peroxisome-proliferator-activated receptor gamma (PPARgamma), a nuclear receptor that is linked to obesity and metabolic diseases. It also mediates the posttranslational regulation of p14ARF, and thus potentially regulates cellular senescence and tumorigenesis in gastric cancer. Moreover, MKRN1 functions as a differentially negative regulator of p53 and p21, and controls cell cycle arrest and apoptosis. It induces degradation of West Nile virus (WNV) capsid protein to protect cells from WNV. Furthermore, MKRN1 may represent a nuclear protein with multiple nuclear functions, including regulating RNA polymerase II-catalyzed transcription. It is a RNA-binding protein involved in the modulation of cellular stress and apoptosis. It predominantly associates with proteins involved in mRNA metabolism including regulators of mRNA turnover, transport, and/or translation, and acts as a component of a ribonucleoprotein complex in embryonic stem cells (ESCs) that is recruited to stress granules upon exposure to environmental stress. Meanwhile, MKRN1 interacts with poly(A)-binding protein (PABP), a key component of different ribonucleoprotein complexes, in an RNA-independent manner, and stimulates translation in nerve cells. In addition, MKRN1 is a novel SEREX (serological identification of antigens by recombinant cDNA expression cloning) antigen of esophageal squamous cell carcinoma (SCC). It may be involved in carcinogenesis of the well-differentiated type of tumors possibly via ubiquitination of filamin A interacting protein 1 (L-FILIP). Human MKRN1 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. MKRN3, also known as makorin RING finger protein 3, RING finger protein 63 (RNF63), or zinc finger protein 127 (ZNF127), is a therian mammal-specific retrocopy of MKRN1. It acts as a putative E3 ubiquitin-protein ligase involved in ubiquitination and cell signaling. MKRN3 shows a potential inhibitory effect on hypothalamic gonadotropin-releasing hormone (GnRH) secretion. Its defects represent the most frequent known genetic cause of familial central precocious puberty (CPP). In contrast to human MKRN1, human MKRN3 lacks the second C3H1-type zinc finger at the N-terminal region. The RING-HC finger of mammalian MKRN4 shows high sequence similarity with that of MKRN3, and is also included in this subfamily.


Pssm-ID: 319644 [Multi-domain]  Cd Length: 61  Bit Score: 37.09  E-value: 7.56e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24797089 292 LCTLCLE---------ERRHPTATPCGHLFCWECITAWCSSKA-------ECPLCR 331
Cdd:cd16730   3 VCGICMEvvyekanpsERRFGILSNCNHTYCLKCIRKWRSAKQfenkiikSCPECR 58
RING-HC_UHRF cd16613
RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing ...
292-332 7.88e-04

RING finger, HC subclass, found in ubiquitin-like PHD and RING finger domain-containing proteins, UHRF1 and UHRF2, and similar proteins; UHRF1 is a unique chromatin effector protein that integrates the recognition of both histone PTMs and DNA methylation. It is essential for cell proliferation and plays a critical role in the development and progression of many human carcinomas, such as laryngeal squamous cell carcinoma (LSCC), gastric cancer (GC), esophageal squamous cell carcinoma (ESCC), colorectal cancer, prostate cancer, and breast cancer. UHRF1 acts as a transcriptional repressor through its binding to histone H3 when it is unmodified at Arg2. Its overexpression in human lung fibroblasts results in downregulation of expression of the tumor suppressor pRB. It also plays a role in transcriptional repression of the cell cycle regulator p21. Moreover, UHRF1-dependent repression of transcription factors can facilitate the G1-S transition. It interacts with Tat-interacting protein of 60 kDa (TIP60) and induces degradation-independent ubiquitination of TIP60. It is also an N-methylpurine DNA glycosylase (MPG)-interacting protein that binds MPG in a p53 status-independent manner in the DNA base excision repair (BER) pathway. In addition, UHRF1 functions as an epigenetic regulator that is important for multiple aspects of epigenetic regulation, including maintenance of DNA methylation patterns and recognition of various histone modifications. UHRF2 was originally identified as a ubiquitin ligase acting as a small ubiquitin-like modifier (SUMO) E3 ligase that enhances zinc finger protein 131 (ZNF131) SUMOylation, but does not enhance ZNF131 ubiquitination. It also ubiquitinates PCNP, a PEST-containing nuclear protein. Moreover, UHRF2 functions as a nuclear protein involved in cell-cycle regulation and has been implicated in tumorigenesis. It interacts with cyclins, CDKs, p53, pRB, PCNA, HDAC1, DNMTs, G9a, methylated histone H3 lysine 9, and methylated DNA. It interacts with the cyclin E-CDK2 complex, ubiquitinates cyclins D1 and E1, induces G1 arrest, and is involved in the G1/S transition regulation. Furthermore, UHRF2 is a direct transcriptional target of the transcription factor E2F-1 in the induction of apoptosis. It recruits HDAC1 and binds to methyl-CpG. UHRF2 also participates in the maturation of Hepatitis B virus (HBV) by interacting with the HBV core protein and promoting its degradation. Both UHRF1 and UHRF2 contain an N-terminal ubiquitin-like domain (UBL), a tandem Tudor domain (TTD), a plant homeodomain (PHD) finger, a SET- and RING-associated (SRA) domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319527 [Multi-domain]  Cd Length: 46  Bit Score: 36.61  E-value: 7.88e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAwcSSKAE---CPLCRE 332
Cdd:cd16613   2 TCICCQEVVYQPITTPCQHNVCKGCLQR--SFKAEvysCPACRH 43
RING-HC_TRIM41_like_C-IV cd16602
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and ...
293-332 8.22e-04

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM41, TRIM52 and similar proteins; TRIM41 and TRIM52, two closely related tripartite motif-containing proteins, have dramatically expanded RING domains compared with the rest of the TRIM family proteins. TRIM41 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. In contrast, TRIM52 lacks the putative viral recognition SPRY/B30.2 domain, and thus has been classified to the C-V subclass of TRIM family that contains only RBCC domains. TRIM41, also known as RING finger-interacting protein with C kinase (RINCK), is an E3 ubiquitin-protein ligase that promotes the ubiquitination of protein kinase C (PKC) isozymes in cells. It specifically recognizes the C1 domain of PKC isozymes. It controls the amplitude of PKC signaling by controlling the amount of PKC in the cell. TRIM52, also known as RING finger protein 102 (RNF102), is encoded by a novel, noncanonical antiviral TRIM52 gene in primate genomes with unique specificity determined by the rapidly evolving RING domain.


Pssm-ID: 319516 [Multi-domain]  Cd Length: 41  Bit Score: 36.38  E-value: 8.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITA-WCSskaeCPLCRE 332
Cdd:cd16602   5 CAICLDYFRDPVSIGCGHNFCRVCVTQlWFT----CPQCRK 41
RING-HC_RNF125 cd16542
RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as ...
293-331 8.34e-04

RING finger, HC subclass, found in RING finger protein 125 (RNF125); RNF125, also known as T-cell RING activation protein 1 (TRAC-1), is an E3 ubiquitin-protein ligase that is predominantly expressed in lymphoid cells, and functions as a positive regulator of T cell activation. It also down-modulates HIV replication and inhibits pathogen-induced cytokine production. It negatively regulates type I interferon signaling, which conjugates Lys(48)-linked ubiquitination to retinoic acid-inducible gene-I (RIG-I) and subsequently leads to the proteasome-dependent degradation of RIG-I. Further, RNF125 conjugates ubiquitin to melanoma differentiation-associated gene 5 (MDA5), a family protein of RIG-I. It thus acts as a negative regulator of RIG-I signaling, and is a direct target of miR-15b in the context of Japanese encephalitis virus (JEV) infection. Moreover, RNF125 binds to and ubiquitinates JAK1, prompting its degradation and inhibition of receptor tyrosine kinase (RTK) expression. It also negatively regulates p53 function through physical interaction and ubiquitin-mediated proteasome degradation. Mutations in RNF125 may lead to overgrowth syndromes (OGS). RNF125, together with three closely related proteins: RNF114, RNF138 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM). The UIM of RNF125 binds K48-linked poly-ubiquitin chains and is, together with the RING domain, required for auto-ubiquitination.


Pssm-ID: 319456 [Multi-domain]  Cd Length: 42  Bit Score: 36.31  E-value: 8.34e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECI-TAWCSSKAECPLCR 331
Cdd:cd16542   3 CAICLEVLHQPVRTRCGHVFCRTCIiTSLKNNTWTCPYCR 42
RING-HC_MID2 cd16754
RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as ...
293-331 8.37e-04

RING finger, HC subclass, found in midline-2 (MID2) and similar proteins; MID2, also known as midin-2, midline defect 2, RING finger protein 60 (RNF60), or tripartite motif-containing protein 1 (TRIM1), is a probable E3 ubiquitin-protein ligase that is highly related to MID1 that associate with cytoplasmic microtubules along their length and throughout the cell cycle. Like MID1, MID2 associates with the microtubule network and may at least partially compensate for the loss of MID1. Both MID1 and MID2 interacts with Alpha 4, which is a regulatory subunit of PP2-type phosphatases, such as PP2A, and an integral component of the rapamycin-sensitive signaling pathway. MID2 can also substitute for MID1 to control exocytosis of lytic granules in cytotoxic T cells. Loss-of-function mutations in MID2 lead to the human X-linked intellectual disability (XLID). MID2 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxy-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID2 hetero-dimerizes in vitro with its paralog MID1.


Pssm-ID: 319668 [Multi-domain]  Cd Length: 53  Bit Score: 36.94  E-value: 8.37e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWEC----ITAWCSSKA--------ECPLCR 331
Cdd:cd16754   1 CPICLELFEDPLLLPCAHSLCFSCahriLTSGCSSGEsiepvaafQCPTCR 51
RING-H2_RNF139_like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
292-330 8.49e-04

RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. The mutation of RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319390 [Multi-domain]  Cd Length: 41  Bit Score: 36.29  E-value: 8.49e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16476   2 VCAICYQEMKNARITPCQHYFHGVCLRKWLYVQDRCPLC 40
mRING-HC-C3HC3D_SCAF11 cd16636
Modified RING finger, HC subclass (C3HC3D-type), found in SR-related and CTD-associated factor ...
289-331 8.79e-04

Modified RING finger, HC subclass (C3HC3D-type), found in SR-related and CTD-associated factor 11 (SCAF11) and similar proteins; SCAF11, also known as CTD-associated SR protein 11 (CASP11), renal carcinoma antigen NY-REN-40, SC35-interacting protein 1 (Sip1), Serine/arginine-rich splicing factor 2 (SRSF2)-interacting protein, or splicing regulatory protein 129 (SRrp129), is a novel arginine-serine-rich (RS) domain-containing protein essential for pre-mRNA splicing. It functions as an auxiliary splice factor interacting with spliceosomal component SC35 promoting RNAPII elongation. In addition to SR proteins, such as SC35, ASF/SF2, SRp75, and SRp20, SCAF11 also associates with U1-70K and U2AF65, proteins associated with 5' and 3' splice sites, respectively. SCAF11 contains an N-terminal modified C3HC3D-type RING-HC finger, an internal serine-arginine rich domain (SR domain), and a C-terminal SRI domain.


Pssm-ID: 319550  Cd Length: 43  Bit Score: 36.31  E-value: 8.79e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 289 RNPLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16636   1 RCPICLNCLLEQEVAFPENCSHVFCLTCILKWAETLTSCPVDR 43
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
307-332 8.89e-04

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319715 [Multi-domain]  Cd Length: 44  Bit Score: 36.46  E-value: 8.89e-04
                        10        20
                ....*....|....*....|....*.
gi 24797089 307 PCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16801  19 PCNHLFHNDCIVPWLEQHDTCPVCRK 44
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
293-331 9.14e-04

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 36.49  E-value: 9.14e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTAT---PCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16803   3 CAVCIEGYKQNDVVrilPCKHVFHKSCVDPWLNEHCTCPMCK 44
RING-HC_RING2 cd16740
RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar ...
292-333 9.43e-04

RING finger, HC subclass, found in really interesting new gene 2 protein (RING2) and similar proteins; RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. RING2 is a core component of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. The enzymatic activity of RING2 is enhanced by the interaction with BMI1/PCGF4, and it is dispensable for early embryonic development and much of the gene repression activity of PRC1. Moreover, RING2 plays a key role in terminating neural precursor cell (NPC)-mediated production of subcerebral projection neurons (SCPNs) during neocortical development. It also plays a critical role in nonhomologous end-joining (NHEJ)-mediated end-to-end chromosome fusions. Furthermore, RING2 is essential for expansion of hepatic stem/progenitor cells. It promotes hepatic stem/progenitor cell expansion through simultaneous suppression of cyclin-dependent kinase inhibitors (CDKIs) Cdkn1a and Cdkn2a, known negative regulators of cell proliferation. RING2 also negatively regulates p53 expression through directly binding with both p53 and MDM2 and promoting MDM2-mediated p53 ubiquitination in selective cancer cell types to stimulate tumor development. RING2 contains a C3HC4-type RING-HC finger.


Pssm-ID: 319654  Cd Length: 47  Bit Score: 36.58  E-value: 9.43e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 292 LCTLCLEERRHPTATP-CGHLFCWECI-TAWCSSKAECPLCREK 333
Cdd:cd16740   4 MCPICLDMLKNTMTTKeCLHRFCADCIiTALRSGNKECPTCRKK 47
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
293-331 1.13e-03

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 319364 [Multi-domain]  Cd Length: 49  Bit Score: 36.10  E-value: 1.13e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEE----RRHPTAT-PCGHLFCWECITAWCSSK-AECPLCR 331
Cdd:cd16450   5 CPICFEPwtnsGSHRLCSlKCGHLFGRSCIEKWLKGQgGKCPQCN 49
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
293-332 1.25e-03

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319714 [Multi-domain]  Cd Length: 47  Bit Score: 36.12  E-value: 1.25e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLCRE 332
Cdd:cd16800   3 CPVCKEDytvEEQVRQLPCNHFFHSDCIVPWLELHDTCPVCRK 45
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
292-332 1.29e-03

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 36.18  E-value: 1.29e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 292 LCTLCLEERRHPT---ATPCGHLFCWECITAWCS-SKAECPLCRE 332
Cdd:cd16797   2 VCAICLDEYEEGDklrVLPCSHAYHSKCVDPWLTqTKKTCPVCKQ 46
mRING-HC-C3HC3D_Nrdp1 cd16634
Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation ...
291-331 1.38e-03

Modified RING finger, HC subclass (C3HC3D-type), found in neuregulin receptor degradation protein-1 (Nrdp1) and similar proteins; Nrdp1 (referred to as FLRF in mice), also known as RING finger protein 41 (RNF41), is an E3 ubiquitin-protein ligase that plays a critical role in the regulation of cell growth and apoptosis, inflammation and production of reactive oxygen species (ROS), as well as in doxorubicin (DOX)-induced cardiac injury. It promoten and degradation of the epidermal growth factor receptor (EGFR/ErbB) family member, ErbB3, which is independent of growth factor stimulation. It also promotes M2 macrophage polarization by ubiquitinating and activating transcription factor CCAAT/enhancer-binding Protein beta (C/EBPbeta) via Lys-63-linked ubiquitination. Moreover, Nrdp1 interacts with and modulates activity of Parkin, a causative protein for early onset recessive juvenile parkinsonism (AR-JP). It also interacts with ubiquitin-specific protease 8 (USP8), which is involved in trafficking of various transmembrane proteins. Furthermore, Nrdp1 inhibits basal lysosomal degradation and enhances ectodomain shedding of JAK2-associated cytokine receptors. Its phosphorylation by the kinase Par-1b (also known as MARK2) is required for epithelial cell polarity. Nrdp1 contains an N-terminal modified C3HC3D-type RING-HC finger required for enhancing ErbB3 degradation, a B-box, a coiled-coil domain responsible for Nrdp1 oligomerization, and a C-terminal ErbB3-binding domain.


Pssm-ID: 319548 [Multi-domain]  Cd Length: 43  Bit Score: 35.86  E-value: 1.38e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 291 PLCTLCLEErrhPTATP-CGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16634   5 PICSGVLEE---PLQAPhCEHAFCNACITEWLSRQQTCPVDR 43
RING-HC_RNF138 cd16544
RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; ...
292-331 1.41e-03

RING finger, HC subclass, found in RING finger protein 138 (RNF138) and similar proteins; RNF138, also known as Nemo-like kinase-associated RING finger protein (NARF) or NLK-associated RING finger protein, is an E3 ubiquitin-protein ligase that plays an important role in glioma cell proliferation, apoptosis, and cell cycle. It specifically cooperates with the E2 conjugating enzyme E2-25K (Hip-2/UbcH1), regulates the ubiquitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF), and further suppresses Wnt-beta-catenin signaling. RNF138, together with three closely related proteins: RNF114, RNF125 and RNF166, forms a novel family of ubiquitin ligases with a C3HC4-type RING-HC finger, a C2HC-, and two C2H2-type zinc fingers, as well as a ubiquitin interacting motif (UIM).


Pssm-ID: 319458 [Multi-domain]  Cd Length: 46  Bit Score: 35.93  E-value: 1.41e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 292 LCTLCLEERRHPTAT-PCGHLFCWECI-TAWCSSKAECPLCR 331
Cdd:cd16544   4 SCPVCQEVLQTPIRTkKCRHVFCRKCFlLAMRRSGAHCPLCR 45
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
291-332 1.43e-03

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 319371 [Multi-domain]  Cd Length: 44  Bit Score: 35.72  E-value: 1.43e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 24797089 291 PLCTLCLEERRHPTA----TPCGHLFCWECITAWCSSKaeCPLCRE 332
Cdd:cd16457   1 PTCPVCLERMDESVSgiltILCNHSFHCDCLKRWGDST--CPVCRY 44
RING-HC_CblA_like cd16501
RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and ...
292-331 1.44e-03

RING finger, HC subclass, found in Dictyostelium discoideum Cbl-like protein A (CblA) and similar proteins; CblA is a Dictyostelium homolog of the Cbl proteins which are multi-domain proteins acting as key negative regulators of various receptor and non-receptor tyrosine kinases signaling. CblA upregulates STATc tyrosine phosphorylation by downregulating PTP3, the protein tyrosine phosphatase responsible for dephosphorylating STATc. STATc is a signal transducer and activator of transcription protein. Like other Cbl proteins, CblA contains a tyrosine-kinase-binding domain (TKB), a proline-rich domain, a C3HC4-type RING-HC finger, and an ubiquitin-associated (UBA) domain. TKB, also known as a phosphotyrosine binding PTB domain, is composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain. This family also includes Drosophila melanogaster defense repressor 1 (Dnr1) that was identified as an inhibitor of Dredd activity in the absence of a microbial insult in Drosophila S2 cells. It inhibits the Drosophila initiator caspases Dredd and Dronc. Moreover, Dnr1 acts as a negative regulator of the Imd (immune deficiency) innate immune-response pathway. Its mutations cause neurodegeneration in Drosophila by activating the innate immune response in the brain. Dnr1 contains a FERM N-terminal domain followed by a region rich in glutamine and serine residues, a central FERM domain, and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 319415  Cd Length: 37  Bit Score: 35.54  E-value: 1.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCweciTAWCSSK-AECPLCR 331
Cdd:cd16501   1 LCKVCMDNEINTVFLPCGHVIC----CSECAARlSKCPICR 37
RING-HC_RING1_like cd16531
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and ...
293-331 1.44e-03

RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins; RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), was identified as a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members in this family contain a C3HC4-type RING-HC finger.


Pssm-ID: 319445 [Multi-domain]  Cd Length: 41  Bit Score: 35.87  E-value: 1.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHP-TATPCGHLFCWECIT-AWCSSKAECPLCR 331
Cdd:cd16531   1 CPICLDIIKNTmTTKECLHRFCAECITtALRSGNKECPTCR 41
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
291-330 1.49e-03

RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating Frizzled receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3?-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control potentially through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region.


Pssm-ID: 319712 [Multi-domain]  Cd Length: 47  Bit Score: 36.07  E-value: 1.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 291 PLCTLCLEE---RRHPTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16798   1 PICAICLEEfseGQELRIISCAHEFHRECVDPWLHQHRTCPLC 43
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
293-331 1.65e-03

RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; RNF165, also known as Arkadia-like 2, or Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It thus acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, a NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord.


Pssm-ID: 319596 [Multi-domain]  Cd Length: 51  Bit Score: 35.83  E-value: 1.65e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCL---EERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16682   3 CTICLsmlEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICR 44
RING-HC_NHL-1_like cd16524
RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and ...
293-331 1.76e-03

RING finger, HC subclass, found in Caenorhabditis elegans RING finger protein NHL-1 and similar proteins; NHL-1 functions as an E3 ubiquitin-protein ligase in the presence of both UBC-13 and UBC-1 within the ubiquitin pathway of Caenorhabditis elegans. It acts in chemosensory neurons to promote stress resistance in distal tissues by the transcription factor DAF-16 activation but is dispensable for the activation of heat shock factor 1 (HSF-1). NHL-1 belongs to the TRIM (tripartite motif)-NHL family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319438 [Multi-domain]  Cd Length: 45  Bit Score: 35.49  E-value: 1.76e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWE-CITA---WCSSKAECPLCR 331
Cdd:cd16524   3 CAICLDRYRRPKLLPCQHTFCQSpCLEGlvdYVNRKLKCPECR 45
RING-HC_TRIM50_like_C-IV cd16605
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 ...
292-332 1.88e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins; TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with the histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The family also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins and may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by an N-terminal RBCC domains only.


Pssm-ID: 319519 [Multi-domain]  Cd Length: 45  Bit Score: 35.57  E-value: 1.88e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECITAW-CSSKAE--CPLCRE 332
Cdd:cd16605   2 LCPICLEVFKEPLMLQCGHSYCKSCLVSLsCELDGQllCPVCRQ 45
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
283-333 2.05e-03

RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar proteins; The cellular inhibitor of apoptosis protein c-IAPs function as ubiquitin E3 ligases that mediate the ubiquitination of the substrates involved in apoptosis, nuclear factor-kappaB (NF-kappaB) signaling, and oncogenesis. Unlike other apoptosis proteins (IAPs), such as XIAP, c-IAPs exhibit minimal binding to caspases and may not play an important role in the inhibition of these proteases. c-IAP1, also known as baculoviral IAP repeat-containing protein BIRC2, IAP-2, RING finger protein 48, or TNFR2-TRAF-signaling complex protein 2, is a potent regulator of the tumor necrosis factor (TNF) receptor family and NF-kappaB signaling pathways in the cytoplasm. It can also regulate E2F1 transcription factor-mediated control of cyclin transcription in the nucleus. c-IAP2, also known as BIRC3, IAP-1, apoptosis inhibitor 2 (API2), or IAP homolog C, also influences ubiquitin-dependent pathways that modulate innate immune signalling by activation of NF-kappaB. c-IAPs contain three N-terminal baculoviral IAP repeat (BIR) domains that enable interactions with proteins, a ubiquitin-association (UBA) domain that is responsible for the binding of binds polyubiquitin (polyUb), a caspase activation and recruitment domain (CARD) that serves as a protein interaction surface, and a C3HC4-type RING-HC finger at the carboxyl terminus that is required for ubiquitin ligase activity. Livin, also known as baculoviral IAP repeat-containing protein 7 (BIRC7), or kidney inhibitor of apoptosis protein (KIAP), or melanoma inhibitor of apoptosis protein (ML-IAP), or RING finger protein 50, was identified as the melanoma IAP. It plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is regulated by the inhibition of caspase-3, -7, and -9. Its E3 ubiquitin-ligase-like activity promotes degradation of Smac/DIABLO, a critical endogenous regulator of all IAPs. Unlike other family members, mammalian livin contains a single BIR domain and a C3HC4-type RING-HC finger. The UBA domain can be detected in non-mammalian homologs of livin.


Pssm-ID: 319627 [Multi-domain]  Cd Length: 54  Bit Score: 35.52  E-value: 2.05e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 24797089 283 EERavsrnpLCTLCLEERRHPTATPCGHL-FCWECitawCSSKAECPLCREK 333
Cdd:cd16713   3 EER------TCKVCMDKEVSIVFVPCGHLaVCQEC----APSLRKCPICRAK 44
RING-HC_TRIM8_C-V cd16580
RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar ...
292-330 2.06e-03

RING finger, HC subclass, found in tripartite motif-containing protein 8 (TRIM8) and similar proteins; TRIM8, also known as glioblastoma-expressed RING finger protein (GERP) or RING finger protein 27 (RNF27), is a probable E3 ubiquitin-protein ligase that may promote proteasomal degradation of suppressor of cytokine signaling 1 (SOCS1) and further regulate interferon-gamma signaling. It functions as a new p53 modulator that stabilizes p53 impairing its association with MDM2 and inducing the reduction of cell proliferation. TRIM8 deficit dramatically impairs p53 stabilization and activation in response to chemotherapeutic drugs. TRIM8 also modulates tumor necrosis factor-alpha (TNFalpha) and interleukin-1beta (IL-1beta)-triggered nuclear factor-kappaB (NF- kappa B) activation by targeting transforming growth factor beta (TGFbeta) activated kinase 1 (TAK1) for K63-linked polyubiquitination. Moreover, TRIM8 modulates translocation of phosphorylated STAT3 into the nucleus through interaction with Hsp90beta and consequently regulates transcription of Nanog in embryonic stem cells. It also interacts with protein inhibitor of activated STAT3 (PIAS3), which inhibits IL-6-dependent activation of STAT3. TRIM8 belongs to the C-V subclass of nuclear TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The coiled coil domain is required for homodimerization and the region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.


Pssm-ID: 319494 [Multi-domain]  Cd Length: 44  Bit Score: 35.32  E-value: 2.06e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 292 LCTLCLEERRHPTATPCGHLFCWECIT-AWC--SSKAECPLC 330
Cdd:cd16580   2 ICPICLHVFVEPVQLPCKHNFCRGCIGeAWAkeAGLVRCPEC 43
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
293-331 2.16e-03

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatoric component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 319374 [Multi-domain]  Cd Length: 43  Bit Score: 35.39  E-value: 2.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEE--RRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16460   3 CVICHENlsPENLSVLPCAHKFHSQCIRPWLMQQRTCPTCR 43
RING-H2_GRAIL cd16668
RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL ...
293-331 2.31e-03

RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL transmembrane proteins family includes RING finger proteins RNF128 (also known as GRAIL), RNF130, RNF133, RNF148, RNF149, and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF128 is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression regulated by histone deacetylases. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. The family also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the funding members of the family. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 319582 [Multi-domain]  Cd Length: 48  Bit Score: 35.40  E-value: 2.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 293 CTLCLEERRhPTAT----PCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16668   2 CAVCIEPYK-PGDVvrilPCKHIFHKSCVDPWLLEHRTCPMCK 43
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
293-331 2.31e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain.


Pssm-ID: 319500 [Multi-domain]  Cd Length: 45  Bit Score: 35.47  E-value: 2.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKA---ECPLCR 331
Cdd:cd16586   4 CGICLERYKNPKVLPCLHTFCERCLQNYIPAESlslSCPVCR 45
RING-HC_RNF212_like cd16560
RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; ...
293-330 2.42e-03

RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; The family includes RING finger protein RNF212, RNF212B, and their homologs. RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for small ubiquitin-related modifier (SUMO) modification. RNF212B shows high sequence similarity with RNF212, but its biological function remains unclear. Members in this family contain an N-terminal C3HC4-type RING-HC finger. The family also includes two homologs of RNF212, meiotic procrossover factors Zip3 and ZHP-3, which have been identified in Saccharomyces cerevisiae and Caenorhabditis elegans, respectively. Budding yeast Zip3 is a small ubiquitin-related modifier (SUMO) E3 ligase implicated in the SUMO pathway of post-translational modification. It sumoylates chromosome axis proteins, thus promoting synaptonemal complex polymerization. It also acts as a Smt3 E3 ligase. Zip3 includes a SUMO Interacting Motif (SIM) and a modified C3HCHC2-type RING-HC finger that are important for Zip3 in vitro E3 ligase activity and necessary for SC polymerization and correct sporulation. ZHP-3 acts at crossovers to couple meiotic recombination with synaptonemal complex disassembly and chiasma formation in Caenorhabditis elegans. It possess a C3HC4-type RING-HC finger.


Pssm-ID: 319474  Cd Length: 41  Bit Score: 35.16  E-value: 2.42e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTA---TPCGHLFCWECITAwcSSKAECPLC 330
Cdd:cd16560   2 CNRCFQEPIRNDCfsiTSCGHIFCDKCAGK--GKKNECLIC 40
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
292-331 2.67e-03

RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the body in human, especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. Moreover, RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomous by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals.


Pssm-ID: 319593 [Multi-domain]  Cd Length: 49  Bit Score: 35.42  E-value: 2.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCL---EERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16679   4 LCVVCMcdfESRQLLRVLPCNHEFHAKCVDKWLKANRTCPICR 46
RING-H2_RNF38_like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
292-331 2.70e-03

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; The family includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 319386 [Multi-domain]  Cd Length: 45  Bit Score: 35.15  E-value: 2.70e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCL---EERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16472   3 SCVVCMcdfEARQLLRVLPCSHEFHAKCVDKWLKTNRTCPICR 45
RING-HC_MKRN cd16521
RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family ...
293-331 3.37e-03

RING finger, HC subclass, found in the makorin (MKRN) protein family; The MKRN protein family includes the ribonucleoproteins that are characterized by a variety of zinc-finger motifs, including typical arrays of one to four C3H1-type zinc fingers and a C3HC4-type RING-HC finger. Another motif rich in Cys and His residues (CH), with so far unknown function, is also generally present in MKRN proteins. MKRN proteins may have E3 ubiquitin ligase activity.


Pssm-ID: 319435 [Multi-domain]  Cd Length: 51  Bit Score: 34.99  E-value: 3.37e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLE-----ERRHPTATPCGHLFCWECITAWCSSKAE-------CPLCR 331
Cdd:cd16521   1 CGICLEvvlpsERRFGILPNCDHPFCLACIRDWRGSKDQektvvraCPICR 51
PHA02926 PHA02926
zinc finger-like protein; Provisional
287-334 3.42e-03

zinc finger-like protein; Provisional


Pssm-ID: 165237 [Multi-domain]  Cd Length: 242  Bit Score: 38.50  E-value: 3.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24797089  287 VSRNPLCTLCLE---------ERRHPTATPCGHLFCWECITAWCSSKAE------CPLCREKF 334
Cdd:PHA02926 167 VSKEKECGICYEvvyskrlenDRYFGLLDSCNHIFCITCINIWHRTRREtgasdnCPICRTRF 229
RING-HC_GEFO_like cd16507
RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange ...
293-330 3.66e-03

RING finger, HC subclass, found in Dictyostelium discoideum Ras guanine nucleotide exchange factor O (RasGEFO) and similar proteins; RasGEFO, also known as RasGEF domain-containing protein O, is one of the Ras guanine-nucleotide exchange factors (RasGEFs), which are the proteins that activate Ras through catalyzing the replacement of GDP with GTP. They are particularly important for signaling in development and chemotaxis in many organisms, including Dictyostelium. RasGEFO contain a C3HC4-type RING-HC finger that may be responsible for the E3 ubiquitin ligase activity.


Pssm-ID: 319421  Cd Length: 40  Bit Score: 34.49  E-value: 3.66e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHP-TATPCGHLFCWECITAwCSSKAECPLC 330
Cdd:cd16507   2 CLQCMQLFKEPmTLIPCGHTFCAACLAK-CGSSIACNMC 39
RING-H2_RNF43_like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
292-331 4.07e-03

RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligases family, which has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger domain followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling through interacting with complexes of frizzled receptors (FZD) and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of Frizzled receptors (FZD) and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block Frizzled ubiquitination and enhances Wnt signaling.


Pssm-ID: 319580 [Multi-domain]  Cd Length: 45  Bit Score: 34.72  E-value: 4.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCLEERRHPT---ATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16666   1 VCAICLEEFKDGQelrVLPCSHEFHRHCVDPWLLQNRTCPLCL 43
mRING-HC-C3HC5_MGRN1_like---blasttree cd16789
Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 ...
292-331 4.95e-03

Modified RING finger, HC subclass (C3HC5-type), found in mahogunin RING finger protein 1 (MGRN1), RING finger protein 157 (RNF157) and similar proteins; MGRN1, also known as RING finger protein 156 (RNF156), is a cytosolic E3 ubiquitin-protein ligase that inhibits signaling through the G protein-coupled melanocortin receptors-1 (MC1R), -2 (MC2R) and -4 (MC4R) via ubiquitylation-dependent and -independent processes. It suppresses chaperone-associated misfolded protein aggregation and toxicity. MGRN1 interacts with cytosolic prion proteins (PrPs) that are linked with neurodegeneration. It also interacts with expanded polyglutamine proteins, and suppresses misfolded polyglutamine aggregation and cytotoxicity. Moreover, MGRN1 inhibits melanocortin receptor signaling by competition with Galphas, suggesting a novel pathway for melanocortin signaling from the cell surface to the nucleus. Furthermore, MGRN1 interacts with and ubiquitylates TSG101, a key component of the endosomal sorting complex required for transport (ESCRT)-I, and regulates endosomal trafficking. A null mutation in the gene encoding MGRN1 causes spongiform neurodegeneration, suggesting a link between dysregulation of endosomal trafficking and spongiform neurodegeneration. RNF157 is a cytoplasmic E3 ubiquitin ligase predominantly expressed in brain. It is a homolog of the E3 ligase mahogunin ring finger-1 (MGRN1). In cultured neurons, it promotes neuronal survival in an E3 ligase-dependent manner. In contrast, it supports growth and maintenance of dendrites independent of its E3 ligase activity. RNF157 interacts with and ubiquitinates the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65), which regulates neuronal survival, but not dendritic growth downstream of RNF157. The nuclear localization of APBB1 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. Both MGRN1 and RNF157 contain a modified C3HC5-type RING-HC finger, and a functionally uncharacterized region, known as domain associated with RING2 (DAR2), N-terminal to the RING finger. The C3HC5-type RING-HC finger is distinguished from typical C3HC4 RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 319703  Cd Length: 41  Bit Score: 34.24  E-value: 4.95e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 292 LCTLCLEERRHPTATPCGHL-FCWECITAWCSSKAECPLCR 331
Cdd:cd16789   1 ECVICLSDPRDTTVLPCRHLcLCSECAEVLRYQSNKCPICR 41
RING-HC_RNF220 cd16563
RING finger, HC subclass, found in RING finger protein 220 (RNF220) and similar proteins; ...
293-330 5.27e-03

RING finger, HC subclass, found in RING finger protein 220 (RNF220) and similar proteins; RNF220 is an E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of Sin3B, a scaffold protein of the Sin3/HDAC (histone deacetylase) corepressor complex. It can also bind E2 and mediate auto-ubiquitination of itself. Moreover, RNF220 specifically interacts with beta-catenin, and enhances canonical Wnt signaling through ubiquitin-specific protease 7 (USP7)-mediated deubiquitination and stabilization of beta-catenin, which is independent of its E3 ligase activity. RNF220 contains a characteristic C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319477 [Multi-domain]  Cd Length: 41  Bit Score: 34.31  E-value: 5.27e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHP-TATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16563   2 CLICMDPYTNPlVSIQCWHVHCEECWLRTLGAKKLCPQC 40
mRING-HC-C3HC3D_TRAF5 cd16642
Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) ...
291-329 5.28e-03

Modified RING finger, HC subclass (C3HC3D-type), found in tumor necrosis factor (TNF) receptor-associated factor 5 (TRAF5) and similar proteins; TRAF5, also known as RING finger protein 84 (RNF84), is an important signal transducer for a wide range of TNF receptor superfamily members, including tumor necrosis factor receptor 1 (TNFR1), tumor necrosis factor receptor 2 (TNFR2), CD40, and other lymphocyte costimulatory receptors, RANK/TRANCE-R, ectodysplasin-A Receptor (EDAR), lymphotoxin-beta receptor (LT-betaR), latent membrane protein 1 (LMP1), and IRE1. It functions as an activator of NF-kappaB, MAPK, and JNK, and is involved in both RANKL- and TNFalpha-induced osteoclastogenesis. It mediates CD40 signaling through associating with the cytoplasmic tail of CD40. It also negatively regulates Toll-like receptor (TLR) signaling and functions as a negative regulator of the interleukin 6 (IL-6) receptor signaling pathway that limits the differentiation of inflammatory CD4(+) T cells. TRAF5 contains an N-terminal domain with a modified C3HC3D-type RING-HC finger and several zinc fingers, and a C-terminal TRAF domain that comprises a coiled coil domain and a conserved TRAF-C domain.


Pssm-ID: 319556 [Multi-domain]  Cd Length: 43  Bit Score: 34.35  E-value: 5.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 291 PLCTLCLeerRHPTATPCGHLFCWECITAWCSSK--AECPL 329
Cdd:cd16642   4 ATCHFVL---HNPHQTGCGHRFCEHCILVLLELNptPACPI 41
RING-HC_UNK cd16771
RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, ...
293-330 5.33e-03

RING finger, HC subclass, found in RING finger protein unkempt (UNK) and similar proteins; UNK, also known as zinc finger CCCH domain-containing protein 5, is a metazoan-specific zinc finger protein enriched in embryonic brains. It may play a broad regulatory role during the formation of the central nervous system (CNS). It is a sequence-specific RNA-binding protein required for the early neuronal morphology. UNK is a neurogenic component of the mTOR pathway, and functions as a negative regulator of the timing of photoreceptor differentiation. It also specifically binds to Brg/Brm-associated factor BAF60b and promotes its ubiquitination in a Rac1-dependent manner. UNK contains six tandem CCCH-type zinc fingers at the N-terminus, and a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319685  Cd Length: 37  Bit Score: 34.00  E-value: 5.33e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24797089 293 CTLCLEERRHPTATPCGHL-FCWECITAWCsskaECPLC 330
Cdd:cd16771   2 CMKCQERNRSVTVLPCQHLvLCETCAEAVT----ECPYC 36
RING-HC_DTX3_like cd16506
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like ...
293-331 5.44e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Deltex3 (DTX3), Deltex-3-like (DTX3L) and similar proteins; The family contains Deltex3 (DTX3) and Deltex-3-like (DTX3L), both of which are E3 ubiquitin-protein ligases belonging to the Deltex (DTX) family. DTX3, also known as RING finger protein 154 (RNF154), has a biological function that remains unclear. DTX3L, also known as B-lymphoma- and BAL-associated protein (BBAP) or Rhysin-2 (Rhysin2), regulates endosomal sorting of the G protein-coupled receptor CXCR4 from endosomes to lysosomes. It also regulates subcellular localization of its partner protein, B aggressive lymphoma (BAL), by a dynamic nucleocytoplasmic trafficking mechanism. In contrast to other DTXs, both DTX3 and DTX3L contain a C3HC4-type RING-HC finger, and a previously unidentified C-terminal domain. DTX3L can associate with DTX1 through its unique N termini and further enhance self-ubiquitination.


Pssm-ID: 319420 [Multi-domain]  Cd Length: 41  Bit Score: 34.03  E-value: 5.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATP-CGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16506   2 CPICLDTISNKKVLLkCKHSFCAPCINKALTVKPICPICQ 41
RING1-HC_LONFs cd16513
RING finger 1, HC subclass, found in the LON peptidase N-terminal domain and RING finger ...
291-331 5.50e-03

RING finger 1, HC subclass, found in the LON peptidase N-terminal domain and RING finger proteins family; The LON peptidase N-terminal domain and RING finger proteins family includes LONRF1 (also known as RING finger protein 191 or RNF191), LONRF2 (also known as RING finger protein 192 or RNF192, or neuroblastoma apoptosis-related protease), LONRF3 (also known as RING finger protein 127 or RNF127), which are characterized by containing two C3HC4-type RING-HC fingers, four tetratricopeptide (TPR) repeats, and one N-terminal domain of the ATP-dependent protease La (LON) domain at the C-terminus. Their biological function remain unclear. This family corresponds to the first RING-HC finger.


Pssm-ID: 319427  Cd Length: 42  Bit Score: 34.35  E-value: 5.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 291 PLCTLCLEERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16513   2 PSCNGFLYETPLPVTSPCGHTYCKRCLEKFYASDSRCLVCR 42
RING-HC_ScPSH1_like cd16568
RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated ...
293-331 6.15e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae POB3/SPT16 histone-associated protein 1 (ScPSH1), Arabidopsis thaliana Protein KEEP ON GOING (AtKEG) and similar proteins; ScPSH1 is a Cse4-specific E3 ubiquitin ligase that interacts with the kinetochore protein Pat1 and targets the degradation of budding yeast centromeric histone H3 variant, CENP-ACse4, which is essential for faithful chromosome segregation. ScPSH1 contains a C3HC4-type RING-HC finger and a DNA directed RNA polymerase domain. AtKEG is an E3 ubiquitin ligase essential for Arabidopsis growth and development. It maintains low levels of ABSCISIC ACID-INSENSITIVE5 (ABI5) in the absence of stress and thus functions as a negative regulator of abscisic acid (ABA) signaling. AtKEG is a multidomain protein that includes a C3HC4-type RING-HC finger, a kinase domain, ankyrin repeats, and 12 HERC2-like (for HECT and RCC1-like) repeats.


Pssm-ID: 319482 [Multi-domain]  Cd Length: 45  Bit Score: 34.01  E-value: 6.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24797089 293 CTLCLEE-RRHPTATPCGHLFCWECITAWCSSKAE----CPLCR 331
Cdd:cd16568   2 CSVCHDRlNEVPMMLPCGHGFCKKCLNKMFSTSSDkrlaCPTCR 45
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
292-331 6.23e-03

RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger.


Pssm-ID: 319594 [Multi-domain]  Cd Length: 45  Bit Score: 34.26  E-value: 6.23e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24797089 292 LCTLCL---EERRHPTATPCGHLFCWECITAWCSSKAECPLCR 331
Cdd:cd16680   3 LCVVCFsdfESRQLLRVLPCNHEFHTKCVDKWLKTNRTCPICR 45
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
293-336 6.27e-03

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 38.05  E-value: 6.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24797089 293 CTLCLE---ERRHPTATPCGHLFCWECITAWCSS-KAECPLCREKFPP 336
Cdd:COG5540 326 CAICMSnfiKNDRLRVLPCDHRFHVGCVDKWLLGySNKCPVCRTAIPP 373
RING-HC_MKRN2 cd16731
RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known ...
292-331 7.43e-03

RING finger, HC subclass, found in makorin-2 (MKRN2) and similar proteins; MKRN2, also known as makorin RING finger protein 2, RING finger protein 62 (RNF62), or HSPC070, is a putative ribonucleoprotein that acts as a neurogenesis inhibitor acting upstream of glycogen synthase kinase-3beta (GSK-3beta) in the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. It also functions on promoting cell proliferation of primary CD34+ progenitor cells and K562 cells, indicating its possible involvement in normal and malignant hematopoiesis. Mammalian MKRN2 contains three N-terminal C3H1-type zinc fingers, a motif rich in Cys and His residues (CH), a C3HC4-type RING-HC finger, and another C3H1-type zinc finger at the C-terminus. The third C3H1-type zinc finger, the CH motif, as well as the RING zinc finger are necessary for its anti-neurogenic activity.


Pssm-ID: 319645 [Multi-domain]  Cd Length: 58  Bit Score: 34.11  E-value: 7.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24797089 292 LCTLCLE---------ERRHPTATPCGHLFCWECITAW-CSSKAE------CPLCR 331
Cdd:cd16731   3 VCSICMEvvyekasasERRFGILSNCNHTYCLSCIRQWrCAKQFEnpiiksCPECR 58
RING-HC_BRE1_like cd16499
RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ...
293-331 7.69e-03

RING finger, HC subclass, found in yeast Bre1 and its homologs from eukaryotes; Bre1 is an E3 ubiquitin-protein ligase that catalyzes monoubiquitination of histone H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The Rad6-Bre1-mediated histone H2B ubiquitylation modulates the formation of double-strand breaks (DSBs) during meiosis in yeast. it is also required, indirectly, for the methylation of histone 3 on lysine 4 (H3K4) and 79. RNF20, also known as BRE1A and RNF40, also known as BRE1B, are the mammalian homologs of Bre1. They work together to form a heterodimeric Bre1 complex that facilitate the K120 monoubiquitination of histone H2B (H2Bub1), a DNA damage-induced histone modification that is crucial for recruitment of the chromatin remodeler SNF2h to DNA double-strand break (DSB) damage sites. Moreover, Bre1 complex acts as a tumor suppressor, augmenting expression of select tumor suppressor genes and suppressing select oncogenes. Deficiency in the mammalian histone H2B ubiquitin ligase Bre1 leads to replication stress and chromosomal instability. All family members contain a C3HC4-type RING-HC finger at its C-terminus.


Pssm-ID: 319413 [Multi-domain]  Cd Length: 42  Bit Score: 33.72  E-value: 7.69e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAWCSSKA-ECPLCR 331
Cdd:cd16499   3 CSVCNDRQKDVILTKCGHVFCKECIQERLETRQrKCPSCN 42
RING-HC_RBR_TRIAD1_like cd16623
RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 ...
293-330 8.02e-03

RING finger, HC subclass, found in two RING fingers and DRIL [double RING finger linked] 1 (TRIAD1), ankyrin repeat and IBR domain-containing protein 1 (ANKIB1) and similar proteins; TRIAD1, also known as ariadne-2 (ARI-2), protein ariadne-2 homolog, Ariadne RBR E3 ubiquitin protein ligase 2 (ARIH2), or UbcM4-interacting protein 48, is a RBR-type E3 ubiquitin-protein ligase that catalyzes the formation of polyubiquitin chains linked via lysine-48 as well as lysine-63 residues. Its auto-ubiquitylation can be catalyzed by the E2 conjugating enzyme UBCH7. TRIAD1 has been implicated in hematopoiesis, specifically in myelopoiesis, as well as in embryogenesis. ANKIB1 is a RBR-type E3 ubiquitin-protein ligase that may function as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates. Both TRIAD1 and ANKIB1 contain a RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain use an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This family corresponds to the RING domain, a C3HC4-type RING-HC finger required for RBR-mediated ubiquitination. In contrast to TRIAD1, ANKIB1 harbors an extra N-terminal ankyrin repeats domain.


Pssm-ID: 319537  Cd Length: 50  Bit Score: 33.85  E-value: 8.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24797089 293 CTLCLEERRH--PTATPCGHLFCWECITAWCSSKAECPLC 330
Cdd:cd16623   1 CGICCDDIPPdeMVLLPCGHYFCRTCWTGYLTSKIKEGGC 40
RING-HC_MID1 cd16753
RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as ...
293-331 8.10e-03

RING finger, HC subclass, found in midline-1 (MID1) and similar proteins; MID1, also known as midin, midline 1 RING finger protein, putative transcription factor XPRF, RING finger protein 59 (RNF59), or tripartite motif-containing protein 18 (TRIM18), is a microtubule-associated E3 ubiquitin-protein ligase implicated in epithelial-mesenchymal differentiation, cell migration and adhesion, and programmed cell death along specific regions of the ventral midline during embryogenesis. It monoubiquinates the alpha4 subunit of protein phosphatase 2A (PP2A), promoting proteosomal degradation of the catalytic subunit of PP2A (PP2Ac) and preventing the A and B subunits from forming an active complex. It promotes allergen and rhinovirus-induced asthma through the inhibition of PP2A activity. It is strongly upregulated in cytotoxic lymphocytes (CTLs) and directs lytic granule exocytosis and cytotoxicity of killer T cells. Loss-of-function mutations in MID1 lead to the human X-linked Opitz G/BBB (XLOS) syndrome characterized by defective midline development during embryogenesis. MID1 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. MID1 hetero-dimerizes in vitro with its paralog MID2.


Pssm-ID: 319667 [Multi-domain]  Cd Length: 54  Bit Score: 34.26  E-value: 8.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWEC----ITAWCSSKA--------ECPLCR 331
Cdd:cd16753   3 CPICLELFEDPLLLPCAHSLCFNCahriLVSHCASNEsvesitafQCPTCR 53
RING-HC_RNF168 cd16550
RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; ...
293-331 8.58e-03

RING finger, HC subclass, found in RING finger protein 168 (RNF168) and similar proteins; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates, such as H2A and H2AX with H2AK13/15 ubiquitylation, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin.


Pssm-ID: 319464 [Multi-domain]  Cd Length: 42  Bit Score: 33.42  E-value: 8.58e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24797089 293 CTLCLEERRHPTATPCGHLFCWECITAwCSSKA--ECPLCR 331
Cdd:cd16550   1 CPICLEILVEPVTLPCKHELCLPCFQQ-TVEKAnlCCPLCR 40
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
293-333 8.85e-03

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1, or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway through interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 319387 [Multi-domain]  Cd Length: 46  Bit Score: 33.81  E-value: 8.85e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24797089 293 CTLCLEERR---HPTATPCGHLFCWECITAWCSS-KAECPLCREK 333
Cdd:cd16473   2 CVICLENYEegcLLCGLPCGHVFHQNCIDVWLTRdNHCCPVCRWP 46
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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