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Conserved domains on  [gi|530416087|ref|XP_005258753.1|]
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PREDICTED: E3 ubiquitin-protein ligase CBL-C isoform X3 [Homo sapiens]

Protein Classification

Cbl_N and SH2_Cbl-b_TKB domain-containing protein (domain architecture ID 12033534)

protein containing domains Cbl_N, Cbl_N2, SH2_Cbl-b_TKB, and RING-HC_Cbl-c

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SH2_Cbl-b_TKB cd09920
Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. ...
226-322 2.09e-60

Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. The Cbl (for Casitas B-lineage lymphoma) family of E3 ubiquitin ligases contains three members Cbl, Cbl-b and Cbl-c. The founding member Cbl was discovered first as the oncogenic protein v-Cbl, a Gag-fusion transforming protein of Cas NS-1 retrovirus, which causes pre- and pro-B lymphomas in mice. The N-terminus of the Cbl proteins is composed of a tyrosine kinase-binding (TKB) domain, also called phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. In addition, Cbl and Cbl-b contain a leucine zipper motif and a proline-rich domain in the C-terminus. The TKB domain consists of a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Cbl-b plays a role in early hematopoietic development and is a negative regulator of T-cell receptor, B-cell receptor and high affinity immunoglobulin epsilon receptor signal transduction pathways. It also negatively regulates insulin-like growth factor 1 signaling during muscle atrophy caused by unloading and is involved in EGFR ubiquitination and internalization. Diseases associated with defects in Cbl-b include: multiple sclerosis, autoimmune diseases, including type 1 diabetes, and a craniofacial phenotype. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


:

Pssm-ID: 198176  Cd Length: 97  Bit Score: 194.58  E-value: 2.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 226 KNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDG 305
Cdd:cd09920    1 RNWQVLAVTHPGYMAFLTYDEVKARLQKFRDKPGSYVFRLSCTRLGQWAIGYVTADGKILQTIPQNKSLCQALIDGSREG 80
                         90
                 ....*....|....*..
gi 530416087 306 FYLYPDGKTHNPDLTEL 322
Cdd:cd09920   81 FYLYPDGRLDNPDLSGA 97
Cbl_N pfam02262
CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or ...
16-145 3.82e-55

CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. Cbl_N is comprised of 3 structural domains of which this is the first - a four helix bundle.


:

Pssm-ID: 308077  Cd Length: 122  Bit Score: 181.60  E-value: 3.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087   16 RALGRAVRMLQRLEEQCVDPRLSV--SPPSLRDLLPRTAQLLREVAHSRRAaggggPGGPGGSGDFLLIYLANLEAKSRQ 93
Cdd:pfam02262   1 KTLEKAVKLLDKLVKLCQDPRLNLknSPPYLLDLLPDTYQHLRLIASAYRG-----GLDALGENDYLRIFLANLLAKCKQ 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530416087   94 VAALLpprgrRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYC 145
Cdd:pfam02262  76 AAKLF-----KEAKEKMFDEGSEYRRQLTKLSLIFSHMLAELKALFPDGKFC 122
Cbl_N2 pfam02761
CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF ...
149-232 6.12e-46

CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the central EF hand domain.


:

Pssm-ID: 308414  Cd Length: 84  Bit Score: 156.22  E-value: 6.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087  149 YQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNW 228
Cdd:pfam02761   1 FRITKKDAAEFWKKNFGKRTIVPWSEFRQALRKVHPISSGDEAMALKSTIDLTCNDHISIFEFDVFTRLFQPWSTLLRNW 80

                  ....
gi 530416087  229 QLLA 232
Cdd:pfam02761  81 NVLA 84
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
345-397 2.10e-29

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: 109.79  E-value: 2.10e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530416087 345 DSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWE 397
Cdd:cd16710    1 NSTFELCKICAERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGRE 53
 
Name Accession Description Interval E-value
SH2_Cbl-b_TKB cd09920
Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. ...
226-322 2.09e-60

Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. The Cbl (for Casitas B-lineage lymphoma) family of E3 ubiquitin ligases contains three members Cbl, Cbl-b and Cbl-c. The founding member Cbl was discovered first as the oncogenic protein v-Cbl, a Gag-fusion transforming protein of Cas NS-1 retrovirus, which causes pre- and pro-B lymphomas in mice. The N-terminus of the Cbl proteins is composed of a tyrosine kinase-binding (TKB) domain, also called phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. In addition, Cbl and Cbl-b contain a leucine zipper motif and a proline-rich domain in the C-terminus. The TKB domain consists of a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Cbl-b plays a role in early hematopoietic development and is a negative regulator of T-cell receptor, B-cell receptor and high affinity immunoglobulin epsilon receptor signal transduction pathways. It also negatively regulates insulin-like growth factor 1 signaling during muscle atrophy caused by unloading and is involved in EGFR ubiquitination and internalization. Diseases associated with defects in Cbl-b include: multiple sclerosis, autoimmune diseases, including type 1 diabetes, and a craniofacial phenotype. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198176  Cd Length: 97  Bit Score: 194.58  E-value: 2.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 226 KNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDG 305
Cdd:cd09920    1 RNWQVLAVTHPGYMAFLTYDEVKARLQKFRDKPGSYVFRLSCTRLGQWAIGYVTADGKILQTIPQNKSLCQALIDGSREG 80
                         90
                 ....*....|....*..
gi 530416087 306 FYLYPDGKTHNPDLTEL 322
Cdd:cd09920   81 FYLYPDGRLDNPDLSGA 97
Cbl_N pfam02262
CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or ...
16-145 3.82e-55

CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. Cbl_N is comprised of 3 structural domains of which this is the first - a four helix bundle.


Pssm-ID: 308077  Cd Length: 122  Bit Score: 181.60  E-value: 3.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087   16 RALGRAVRMLQRLEEQCVDPRLSV--SPPSLRDLLPRTAQLLREVAHSRRAaggggPGGPGGSGDFLLIYLANLEAKSRQ 93
Cdd:pfam02262   1 KTLEKAVKLLDKLVKLCQDPRLNLknSPPYLLDLLPDTYQHLRLIASAYRG-----GLDALGENDYLRIFLANLLAKCKQ 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530416087   94 VAALLpprgrRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYC 145
Cdd:pfam02262  76 AAKLF-----KEAKEKMFDEGSEYRRQLTKLSLIFSHMLAELKALFPDGKFC 122
Cbl_N3 pfam02762
CBL proto-oncogene N-terminus, SH2-like domain; Cbl is an adaptor protein that binds EGF ...
235-313 5.99e-51

CBL proto-oncogene N-terminus, SH2-like domain; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the C-terminal SH2 domain.


Pssm-ID: 308415  Cd Length: 80  Bit Score: 169.39  E-value: 5.99e-51
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530416087  235 HPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGK 313
Cdd:pfam02762   1 HPGYMAFLTYDEVKAVLQKFRTKPGSYIFRLSCTRLGQWAIGYVTPDGKILQTIPQNKSLYQALIDGEREGFYLYPDGQ 79
Cbl_N2 pfam02761
CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF ...
149-232 6.12e-46

CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the central EF hand domain.


Pssm-ID: 308414  Cd Length: 84  Bit Score: 156.22  E-value: 6.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087  149 YQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNW 228
Cdd:pfam02761   1 FRITKKDAAEFWKKNFGKRTIVPWSEFRQALRKVHPISSGDEAMALKSTIDLTCNDHISIFEFDVFTRLFQPWSTLLRNW 80

                  ....
gi 530416087  229 QLLA 232
Cdd:pfam02761  81 NVLA 84
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
345-397 2.10e-29

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: 109.79  E-value: 2.10e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530416087 345 DSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWE 397
Cdd:cd16710    1 NSTFELCKICAERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGRE 53
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
351-393 2.33e-08

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: 51.59  E-value: 2.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530416087  351 CKICAESNKDVKIEPCGHLLCSCClaaWQHSDSQTCPFCRCEI 393
Cdd:pfam14447   1 CVLCGRVGTVHILSPCGHLVCRDC---FDGSDYSGCPICHRRI 40
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
351-389 2.06e-06

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  Cd Length: 40  Bit Score: 45.96  E-value: 2.06e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530416087   351 CKICAE-SNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFC 389
Cdd:smart00184   1 CPICLEeYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
351-390 4.90e-05

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


Pssm-ID: 227861  Cd Length: 271  Bit Score: 44.50  E-value: 4.90e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530416087 351 CKICAESNKDVKIEPCGHLLC-SCCLAAWQHSDSQTCPFCR 390
Cdd:COG5574  218 CFLCLEEPEVPSCTPCGHLFClSCLLISWTKKKYEFCPLCR 258
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
351-415 1.97e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747  Cd Length: 193  Bit Score: 39.30  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQT---------------CPFCRCEIKGWEAVSIYQfHGQATAEDSGN 415
Cdd:PLN03208  21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNSrqrvdqydhkreppkCPVCKSDVSEATLVPIYG-RGQKAPQSGSN 99
 
Name Accession Description Interval E-value
SH2_Cbl-b_TKB cd09920
Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. ...
226-322 2.09e-60

Src homology 2 (SH2) domain found in the Cbl-b TKB domain; SH2 found in the Cbl-b TKB domain. The Cbl (for Casitas B-lineage lymphoma) family of E3 ubiquitin ligases contains three members Cbl, Cbl-b and Cbl-c. The founding member Cbl was discovered first as the oncogenic protein v-Cbl, a Gag-fusion transforming protein of Cas NS-1 retrovirus, which causes pre- and pro-B lymphomas in mice. The N-terminus of the Cbl proteins is composed of a tyrosine kinase-binding (TKB) domain, also called phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. In addition, Cbl and Cbl-b contain a leucine zipper motif and a proline-rich domain in the C-terminus. The TKB domain consists of a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain. Cbl-b plays a role in early hematopoietic development and is a negative regulator of T-cell receptor, B-cell receptor and high affinity immunoglobulin epsilon receptor signal transduction pathways. It also negatively regulates insulin-like growth factor 1 signaling during muscle atrophy caused by unloading and is involved in EGFR ubiquitination and internalization. Diseases associated with defects in Cbl-b include: multiple sclerosis, autoimmune diseases, including type 1 diabetes, and a craniofacial phenotype. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198176  Cd Length: 97  Bit Score: 194.58  E-value: 2.09e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 226 KNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDG 305
Cdd:cd09920    1 RNWQVLAVTHPGYMAFLTYDEVKARLQKFRDKPGSYVFRLSCTRLGQWAIGYVTADGKILQTIPQNKSLCQALIDGSREG 80
                         90
                 ....*....|....*..
gi 530416087 306 FYLYPDGKTHNPDLTEL 322
Cdd:cd09920   81 FYLYPDGRLDNPDLSGA 97
Cbl_N pfam02262
CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or ...
16-145 3.82e-55

CBL proto-oncogene N-terminal domain 1; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. Cbl_N is comprised of 3 structural domains of which this is the first - a four helix bundle.


Pssm-ID: 308077  Cd Length: 122  Bit Score: 181.60  E-value: 3.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087   16 RALGRAVRMLQRLEEQCVDPRLSV--SPPSLRDLLPRTAQLLREVAHSRRAaggggPGGPGGSGDFLLIYLANLEAKSRQ 93
Cdd:pfam02262   1 KTLEKAVKLLDKLVKLCQDPRLNLknSPPYLLDLLPDTYQHLRLIASAYRG-----GLDALGENDYLRIFLANLLAKCKQ 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530416087   94 VAALLpprgrRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYC 145
Cdd:pfam02262  76 AAKLF-----KEAKEKMFDEGSEYRRQLTKLSLIFSHMLAELKALFPDGKFC 122
Cbl_N3 pfam02762
CBL proto-oncogene N-terminus, SH2-like domain; Cbl is an adaptor protein that binds EGF ...
235-313 5.99e-51

CBL proto-oncogene N-terminus, SH2-like domain; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the C-terminal SH2 domain.


Pssm-ID: 308415  Cd Length: 80  Bit Score: 169.39  E-value: 5.99e-51
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530416087  235 HPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGK 313
Cdd:pfam02762   1 HPGYMAFLTYDEVKAVLQKFRTKPGSYIFRLSCTRLGQWAIGYVTPDGKILQTIPQNKSLYQALIDGEREGFYLYPDGQ 79
Cbl_N2 pfam02761
CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF ...
149-232 6.12e-46

CBL proto-oncogene N-terminus, EF hand-like domain; Cbl is an adaptor protein that binds EGF receptors (or other tyrosine kinases) and SH3 domains, functioning as a negative regulator of many signaling pathways. The N-terminal domain is evolutionarily conserved, and is known to bind to phosphorylated tyrosine residues. The so called N-terminal domain is actually 3 structural domains, of which this is the central EF hand domain.


Pssm-ID: 308414  Cd Length: 84  Bit Score: 156.22  E-value: 6.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087  149 YQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNW 228
Cdd:pfam02761   1 FRITKKDAAEFWKKNFGKRTIVPWSEFRQALRKVHPISSGDEAMALKSTIDLTCNDHISIFEFDVFTRLFQPWSTLLRNW 80

                  ....
gi 530416087  229 QLLA 232
Cdd:pfam02761  81 NVLA 84
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
345-397 2.10e-29

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: 109.79  E-value: 2.10e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530416087 345 DSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWE 397
Cdd:cd16710    1 NSTFELCKICAERDKDVRIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGRE 53
RING-HC_Cbl-b cd16709
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-b and similar proteins; ...
333-397 8.45e-27

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: 102.86  E-value: 8.45e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530416087 333 VSEEQLQLYWAMDSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWE 397
Cdd:cd16709    2 VTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTAWQESDGQGCPFCRCEIKGTE 66
RING-HC_Cbl_like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
348-390 1.32e-25

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  Cd Length: 43  Bit Score: 98.97  E-value: 1.32e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530416087 348 FELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCR 390
Cdd:cd16502    1 FQLCKICAENDKDVRIEPCGHLLCTPCLTSWQDSDGQTCPFCR 43
RING-HC_Cbl cd16708
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl and similar proteins; Cbl, ...
348-404 6.81e-23

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: 92.03  E-value: 6.81e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530416087 348 FELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWEAVSIYQF 404
Cdd:cd16708    1 FQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPF 57
RING_Ubox cd00162
The superfamily of RING finger (Really Interesting New Gene) domain and U-box domain; RING ...
351-389 6.09e-09

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  Cd Length: 40  Bit Score: 53.24  E-value: 6.09e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAES-NKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFC 389
Cdd:cd00162    1 CPICRELmKDPVVLPSCGHTFCYSCIARWLESSDQTCPFC 40
Prok-RING_4 pfam14447
Prokaryotic RING finger family 4; RING finger family domain found sporadically in bacteria. ...
351-393 2.33e-08

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: 51.59  E-value: 2.33e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530416087  351 CKICAESNKDVKIEPCGHLLCSCClaaWQHSDSQTCPFCRCEI 393
Cdd:pfam14447   1 CVLCGRVGTVHILSPCGHLVCRDC---FDGSDYSGCPICHRRI 40
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
349-396 2.20e-07

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 316442  Cd Length: 50  Bit Score: 48.92  E-value: 2.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530416087  349 ELCKICAESNKDVKIEPCGHL-LCSCClAAWQHSDSQTCPFCRCEIKGW 396
Cdd:pfam13920   3 RLCVICLDRPRNVVLLPCGHLcLCEEC-AERLLRKKKKCPICRQPIESV 50
RING-HC_RNF5_like cd16534
RING finger, HC subclass, found in RING finger protein RNF5, RNF185 and similar proteins; RNF5 ...
351-390 8.26e-07

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  Cd Length: 43  Bit Score: 47.04  E-value: 8.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHS--DSQTCPFCR 390
Cdd:cd16534    2 CNICLDTAKDAVVSMCGHLFCWPCLHQWLETrpDRPTCPVCK 43
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
351-389 2.06e-06

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  Cd Length: 40  Bit Score: 45.96  E-value: 2.06e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 530416087   351 CKICAE-SNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFC 389
Cdd:smart00184   1 CPICLEeYLKDPVILPCGHTFCRSCIRKWLESGNNTCPIC 40
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; RING finger is a specialized type of ...
351-389 2.97e-06

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  Cd Length: 39  Bit Score: 45.54  E-value: 2.97e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFC 389
Cdd:cd16449    1 CPICLELLKDPVLLPCGHTFCRSCLRRLLKEGKKKCPIC 39
RING-HC_AtRMA_like cd16745
RING finger, HC subclass, found in Arabidopsis thaliana RING membrane-anchor proteins (AtRMAs) ...
351-390 1.40e-05

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  Cd Length: 45  Bit Score: 43.45  E-value: 1.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAW--QHSDSQTCPFCR 390
Cdd:cd16745    3 CNICLDLASDPVVTLCGHLFCWPCLYRWlqRHSENRECPVCK 44
RING-HC_BIRC2_3_7 cd16713
RING finger, HC subclass, found in apoptosis protein c-IAP1, c-IAP2, livin, and similar ...
350-395 2.81e-05

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  Cd Length: 54  Bit Score: 42.83  E-value: 2.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530416087 350 LCKICAESNKDVKIEPCGHL-LCSCCLAAWQHsdsqtCPFCRCEIKG 395
Cdd:cd16713    6 TCKVCMDKEVSIVFVPCGHLaVCQECAPSLRK-----CPICRAKIKG 47
RING-HC_TRIM40-C-V cd16583
RING finger, HC subclass, found in tripartite motif-containing protein 40 (TRIM40) and similar ...
351-390 4.69e-05

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  Cd Length: 46  Bit Score: 41.80  E-value: 4.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAW----QHSDSQTCPFCR 390
Cdd:cd16583    2 CPICLDPLKEPVSTTCGHVFCRGCIAQHlekaSVSGVLCCPVCR 45
PEX10 COG5574
RING-finger-containing E3 ubiquitin ligase [Posttranslational modification, protein turnover, ...
351-390 4.90e-05

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


Pssm-ID: 227861  Cd Length: 271  Bit Score: 44.50  E-value: 4.90e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530416087 351 CKICAESNKDVKIEPCGHLLC-SCCLAAWQHSDSQTCPFCR 390
Cdd:COG5574  218 CFLCLEEPEVPSCTPCGHLFClSCLLISWTKKKYEFCPLCR 258
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
351-389 7.60e-05

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: 306580  Cd Length: 40  Bit Score: 41.19  E-value: 7.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 530416087  351 CKICAESNKD-VKIEPCGHLLCSCCLAAWQHSDSQTCPFC 389
Cdd:pfam00097   1 CPICLEEPKDpVTLLPCGHLFCSKCIRSWLESGNVTCPLC 40
zf-RING_2 pfam13639
Ring finger domain;
351-390 9.34e-05

Ring finger domain;


Pssm-ID: 316187  Cd Length: 44  Bit Score: 41.26  E-value: 9.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530416087  351 CKIC---AESNKDVKIEPCGHLLCSCCLAAWQHSdSQTCPFCR 390
Cdd:pfam13639   3 CPICleeFEDGDEVRVLPCGHHFHRECLDKWLRS-SNTCPLCR 44
RING-HC_RNF185 cd16744
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ...
351-390 1.07e-04

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  Cd Length: 43  Bit Score: 41.05  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHS--DSQTCPFCR 390
Cdd:cd16744    2 CNICLDTAKDAVVSLCGHLFCWPCLHQWLETrpNRQVCPVCK 43
RING-HC_RNF5 cd16743
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ...
351-390 1.16e-04

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  Cd Length: 46  Bit Score: 40.70  E-value: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHS--DSQTCPFCR 390
Cdd:cd16743    3 CNICLETAREAVVSLCGHLYCWPCLHQWLETrpERQECPVCK 44
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
351-393 1.54e-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  Cd Length: 44  Bit Score: 40.43  E-value: 1.54e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSqTCPFCRCEI 393
Cdd:cd16455    3 CAICWESMQTARKLPCGHLFHNSCLRSWLEQDT-SCPTCRRSL 44
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
325-429 1.87e-04

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


Pssm-ID: 227561  Cd Length: 493  Bit Score: 43.47  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 325 AEPQQRIHVSEEQlqlywamDSTFELCKICAESNKDVKIEPCGHLLCSCC---LAAWQHSDSqtCPFCRCEikgWEAVSI 401
Cdd:COG5236   45 AEPNLTTSSADDT-------DEENMNCQICAGSTTYSARYPCGHQICHACavrLRALYMQKG--CPLCRTE---TEAVVF 112
                         90       100
                 ....*....|....*....|....*....
gi 530416087 402 yqfhgQATAEDSGNSSDQ-EGRELELGQN 429
Cdd:COG5236  113 -----TASSPADITDRRQwKGREEKVGIF 136
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
351-390 1.96e-04

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  Cd Length: 39  Bit Score: 40.08  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVkIEPCGHLLCSCCLAAWQHSDSqTCPFCR 390
Cdd:cd16545    2 CCICMDRKPDT-ILPCAHSFCQKCIDKWSVRHR-TCPICR 39
RING-HC_RNF208 cd16559
RING finger, HC subclass, found in RING finger protein 208 (RNF208) and similar proteins; ...
350-392 2.71e-04

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  Cd Length: 50  Bit Score: 39.77  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530416087 350 LCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQ----TCPFCRCE 392
Cdd:cd16559    3 ECPLCGETYNRPRILSCLHSFCEPCLQKLYESCPKykfiSCPTCKRE 49
SH2 cd00173
Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they ...
236-322 2.75e-04

Src homology 2 (SH2) domain; In general, SH2 domains are involved in signal transduction; they bind pTyr-containing polypeptide ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites. They are present in a wide array of proteins including: adaptor proteins (Nck1, Crk, Grb2), scaffolds (Slp76, Shc, Dapp1), kinases (Src, Syk, Fps, Tec), phosphatases (Shp-1, Shp-2), transcription factors (STAT1), Ras signaling molecules (Ras-Gap), ubiquitination factors (c-Cbl), cytoskeleton regulators (Tensin), signal regulators (SAP), and phospholipid second messengers (PLCgamma), amongst others.


Pssm-ID: 198173  Cd Length: 79  Bit Score: 40.13  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 236 PGYMAFLTYDEVQERLQACrdKPGSYIFRPSCTRLGQWAIGYVSSDGSIlqtipankplSQVLLEGQKDGFYLYPDGKTH 315
Cdd:cd00173    1 PWFHGSISREEAERLLRGK--PDGTFLVRESSSEPGDYVLSVRSGDGKV----------KHYLIERNEGGYYLLGGSGRT 68

                 ....*..
gi 530416087 316 NPDLTEL 322
Cdd:cd00173   69 FPSLPEL 75
RING-HC_COP1 cd16504
RING finger, HC subclass, found in constitutive photomorphogenesis protein 1 (COP1) and ...
350-393 2.77e-04

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  Cd Length: 46  Bit Score: 39.55  E-value: 2.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530416087 350 LCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSqTCPFCRCEI 393
Cdd:cd16504    4 ICPICFDIIEEAYMTKCGHSFCYKCIRTSLEQSN-RCPKCNFVL 46
RING-HC_TRIM2_like_C-VII cd16586
RING finger, HC subclass, found in tripartite motif-containing protein TRIM2, TRIM3, and ...
348-390 4.38e-04

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  Cd Length: 45  Bit Score: 38.94  E-value: 4.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530416087 348 FELCKICAESNKDVKIEPCGHLLCSCCLAAW--QHSDSQTCPFCR 390
Cdd:cd16586    1 FLSCGICLERYKNPKVLPCLHTFCERCLQNYipAESLSLSCPVCR 45
mRING-HC-C3HC5_RNF26 cd16788
Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and ...
350-393 5.67e-04

Modified RING finger, HC subclass (C3HC5-type), found in RING finger protein 26 (RNF26) and similar proteins; RNF26 is an E3 ubiquitin ligase that temporally regulates virus-triggered type I interferon induction by increasing the stability of Mediator of IRF3 activation, MITA, also known as STING, through K11-linked polyubiquitination of MITA after viral infection and promoting degradation of IRF3, another important component required for virus-triggered interferon induction. Although RNF26 substrates of ubiquitination remain unclear at present, RNF26 upregulation in gastric cancer might be implicated in carcinogenesis through dysregulation of growth regulators. RNF26 contains an N-terminal leucine zipper domain and a C-terminal modified C3HC5-type RING-HC finger, which 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: 319702  Cd Length: 48  Bit Score: 38.95  E-value: 5.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530416087 350 LCKICAESNKDVKIEPCGHL-LCSCC----LAAWQHsdSQTCPFCRCEI 393
Cdd:cd16788    2 KCVICQDQVKTVLLLPCRHMcLCRGCanilLRQPVY--QRNCPLCRSMI 48
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
349-390 1.19e-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  Cd Length: 46  Bit Score: 37.72  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530416087 349 ELCKICAESNKD---VKIEPCGHLLCSCCLAAWQHSDSQTCPFCR 390
Cdd:cd16797    1 DVCAICLDEYEEgdkLRVLPCSHAYHSKCVDPWLTQTKKTCPVCK 45
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
350-390 1.37e-03

RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain.


Pssm-ID: 319394  Cd Length: 45  Bit Score: 37.53  E-value: 1.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530416087 350 LCKICAE---SNKDVKIEPCGHLLCSCCLAAWQHS-DSQTCPFCR 390
Cdd:cd16480    1 YCTICSDffdNSRDVAAIHCGHTFHYECLLQWFETaPSRTCPQCR 45
RING-HC_TRIM60_like_C-IV cd16607
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM60, TRIM61 and ...
351-390 1.62e-03

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  Cd Length: 47  Bit Score: 37.65  E-value: 1.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 351 CKICAESNKDVKIEPCGHLLC-SCCLAAWQH-SDSQTCPFCR 390
Cdd:cd16607    4 CPICLEYLKDPVTINCGHNFCrSCLIVSWKDlDDTFPCPVCR 45
RING-HC_malin cd16516
RING finger, HC subclass, found in malin and similar proteins; Malin ("mal" for seizure in ...
350-390 1.67e-03

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  Cd Length: 48  Bit Score: 37.51  E-value: 1.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530416087 350 LCKICAE-----SNKDVKIEPCGHLLCSCCLAAWQHSDSQT--CPFCR 390
Cdd:cd16516    1 ECKVCFEkfstqQQHRPRNLPCGHVLCQECVLALCHPNVSKleCPFCR 48
PLN03208 PLN03208
E3 ubiquitin-protein ligase RMA2; Provisional
351-415 1.97e-03

E3 ubiquitin-protein ligase RMA2; Provisional


Pssm-ID: 178747  Cd Length: 193  Bit Score: 39.30  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQT---------------CPFCRCEIKGWEAVSIYQfHGQATAEDSGN 415
Cdd:PLN03208  21 CNICLDQVRDPVVTLCGHLFCWPCIHKWTYASNNSrqrvdqydhkreppkCPVCKSDVSEATLVPIYG-RGQKAPQSGSN 99
RING-H2_Pirh2 cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
351-390 1.98e-03

RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It ubiquitylates preferably the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits p73, a homolog of the tumor suppressor p53, transcriptional activity by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. In addition, Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. Pirh2 also interacts with TIP60 and the TIP60-Pirh2 association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs.


Pssm-ID: 319378  Cd Length: 45  Bit Score: 37.17  E-value: 1.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 530416087 351 CKICAE----SNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCR 390
Cdd:cd16464    2 CPVCLEdlftSREPVHVLPCGHLMHSTCFEEYLKSGNYRCPLCS 45
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
351-421 2.12e-03

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


Pssm-ID: 227568  Cd Length: 491  Bit Score: 39.95  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAES-------------NKDVKIEPCGHLLCSCCLAAWQHSdSQTCPFCRCEIKGWEA--------VSIYQFHGQAT 409
Cdd:COG5243  290 CTICMDEmfhpdheplprglDMTPKRLPCGHILHLHCLKNWLER-QQTCPICRRPVIFDQSsptpaspnVRNTQIATQVP 368
                         90
                 ....*....|...
gi 530416087 410 AEDS-GNSSDQEG 421
Cdd:COG5243  369 NPDNtPTTTAVPG 381
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
349-389 2.64e-03

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  Cd Length: 43  Bit Score: 36.96  E-value: 2.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530416087 349 ELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSdSQTCPFC 389
Cdd:cd16684    3 DICSICYQDMKSAVITPCSHFFHAGCLKKWLYV-QETCPLC 42
RING-HC_TRIM2 cd16767
RING finger, HC subclass, found in tripartite motif-containing protein 2 (TRIM2); TRIM2, also ...
348-390 2.89e-03

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  Cd Length: 46  Bit Score: 36.94  E-value: 2.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530416087 348 FELCKICAESNKDVKIEPCGHLLCSCCLAAW--QHSDSQTCPFCR 390
Cdd:cd16767    1 FLICSICLDRYKNPKVLPCLHTFCERCLQNYipAHSLTLSCPVCR 45
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
351-390 3.46e-03

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  Cd Length: 47  Bit Score: 36.31  E-value: 3.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAW-----QHSDSQTCPFCR 390
Cdd:cd16609    3 CSICLELFTDPVTLPCGHNFCGECIRDHwdkceLIKKGYSCPQCR 47
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
351-393 3.49e-03

RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; RNF150 is a RING finger protein that its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 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: 319719  Cd Length: 49  Bit Score: 36.54  E-value: 3.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530416087 351 CKICAES---NKDVKIEPCGHLLCSCCLAAWQhSDSQTCPFCRCEI 393
Cdd:cd16805    3 CAVCIEGykpNDVVRILPCRHLFHKSCVDPWL-LDHRTCPMCKMNI 47
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
350-390 3.49e-03

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  Cd Length: 44  Bit Score: 36.62  E-value: 3.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 530416087 350 LCKICAESNKD-VKIEPCGHLLCSCCLAAWQHSdSQTCPFCR 390
Cdd:cd16503    4 LCSICQDLLHDcVSLQPCMHNFCAGCYSEWMER-SSLCPQCR 44
RING-H2_RNF111_like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
349-391 3.65e-03

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  Cd Length: 46  Bit Score: 36.52  E-value: 3.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530416087 349 ELCKICA---ESNKDVKIEPCGHLLCSCCLAAWQHSDSQtCPFCRC 391
Cdd:cd16474    1 EKCTICLsefEDGEEVRRLPCMHLFHQACVDQWLATNKR-CPICRV 45
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
351-393 3.79e-03

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


Pssm-ID: 227827  Cd Length: 374  Bit Score: 39.21  E-value: 3.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530416087 351 CKICAES---NKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEI 393
Cdd:COG5540  326 CAICMSNfikNDRLRVLPCDHRFHVGCVDKWLLGYSNKCPVCRTAI 371
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
351-390 3.89e-03

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  Cd Length: 41  Bit Score: 36.31  E-value: 3.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAW-QHSDSQTCPFCR 390
Cdd:cd16561    1 CSICLEDPKDPVSLPCDHIHCLTCLRQWfRPVGQMHCPTCR 41
SH2_Jak_family cd09921
Src homology 2 (SH2) domain in the Janus kinase (Jak) family; The Janus kinases (Jak) are a ...
251-322 3.93e-03

Src homology 2 (SH2) domain in the Janus kinase (Jak) family; The Janus kinases (Jak) are a family of 4 non-receptor tyrosine kinases (Jak1, Jak2, Jak3, Tyk2) which respond to cytokine or growth factor receptor activation. To transduce cytokine signaling, a series of conformational changes occur in the receptor-Jak complex upon extracellular ligand binding. This results in trans-activation of the receptor-associated Jaks followed by phosphorylation of receptor tail tyrosine sites. The Signal Transducers and Activators of Transcription (STAT) are then recruited to the receptor tail, become phosphorylated and translocate to the nucleus to regulate transcription. Jaks have four domains: the pseudokinase domain, the catalytic tyrosine kinase domain, the FERM (band four-point-one, ezrin, radixin, and moesin) domain, and the SH2 (Src Homology-2) domain. The Jak kinases are regulated by several enzymatic and non-enzymatic mechanisms. First, the Jak kinase domain is regulated by phosphorylation of the activation loop which is associated with the catalytically competent kinase conformation and is distinct from the inactive kinase conformation. Second, the pseudokinase domain directly modulates Jak catalytic activity with the FERM domain maintaining an active state. Third, the suppressor of cytokine signaling (SOCS) family and tyrosine phosphatases directly regulate Jak activity. Dysregulation of Jak activity can manifest as either a reduction or an increase in kinase activity resulting in immunodeficiency, inflammatory diseases, hematological defects, autoimmune and myeloproliferative disorders, and susceptibility to infection. Altered Jak regulation occurs by many mechanisms, including: gene translocations, somatic or inherited point mutations, receptor mutations, and alterations in the activity of Jak regulators such as SOCS or phosphatases. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites.


Pssm-ID: 198177  Cd Length: 97  Bit Score: 36.49  E-value: 3.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530416087 251 LQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTipankplSQVLLEGQKDGFYLYPDGKTHNPDLTEL 322
Cdd:cd09921   28 LKERGNKPGSYILRESETEYDTYYIDVCVKDGSRFQT-------KTFKIEKKEGGVFFLDGDSREYPSLRDL 92
RING-HC_RNF169 cd16551
RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; ...
351-390 4.03e-03

RING finger, HC subclass, found in RING finger protein 169 (RNF169) and similar proteins; RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to regulation of the DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU (motif interacting with ubiquitin) domain.


Pssm-ID: 319465  Cd Length: 41  Bit Score: 36.34  E-value: 4.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCR 390
Cdd:cd16551    2 CAGCMEMPGEAIALPCGHSLCRGCAKSYFTINGPSCPRCR 41
RING-HC_PEX10 cd16527
RING finger, HC subclass, found in peroxin-10 (PEX10) and similar proteins; PEX10, also known ...
351-390 4.08e-03

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  Cd Length: 40  Bit Score: 36.04  E-value: 4.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQtCPFCR 390
Cdd:cd16527    2 CSLCLESRRHPTATPCGHLFCWSCITEWCNEKPE-CPLCR 40
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
351-393 5.00e-03

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  Cd Length: 49  Bit Score: 36.10  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530416087 351 CKICAES---NKDVKIEPCGHLLCSCCLAAWQhSDSQTCPFCRCEI 393
Cdd:cd16803    3 CAVCIEGykqNDVVRILPCKHVFHKSCVDPWL-NEHCTCPMCKLNI 47
RING-H2_GRAIL cd16668
RING finger, H2 subclass, found in the GRAIL transmembrane proteins family; The GRAIL ...
351-393 5.29e-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  Cd Length: 48  Bit Score: 35.78  E-value: 5.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 530416087 351 CKICAESNKD---VKIEPCGHLLCSCCLAAWQHsDSQTCPFCRCEI 393
Cdd:cd16668    2 CAVCIEPYKPgdvVRILPCKHIFHKSCVDPWLL-EHRTCPMCKLDI 46
RING-HC_RNF219 cd16562
RING finger, HC subclass, found in RING finger protein 219 (RNF219) and similar proteins; ...
351-390 7.00e-03

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  Cd Length: 42  Bit Score: 35.43  E-value: 7.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 530416087 351 CKICAESNKDVKIEPCGHLLCSCCLAAWQhSDSQTCPFCR 390
Cdd:cd16562    4 CHICLGKVKQPVICPNNHVFCSSCMDLWL-KRNNQCPACR 42
PHA02929 PHA02929
N1R/p28-like protein; Provisional
345-390 7.52e-03

N1R/p28-like protein; Provisional


Pssm-ID: 222944  Cd Length: 238  Bit Score: 37.84  E-value: 7.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530416087 345 DSTFELCKICAES--NKDVK------IEPCGHLLCSCCLAAWQHSDSqTCPFCR 390
Cdd:PHA02929 171 RSKDKECAICMEKvyDKEIKnmyfgiLSNCNHVFCIECIDIWKKEKN-TCPVCR 223
RING-HC_HLTF cd16509
RING finger, HC subclass, found in helicase-like transcription factor (HLTF) and similar ...
349-390 8.01e-03

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  Cd Length: 43  Bit Score: 35.35  E-value: 8.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 530416087 349 ELCKICAESNKDVKIEPCGHLLCSCCLAAW-QHSDSQTCPFCR 390
Cdd:cd16509    1 EECPICLDSLKDPVITPCAHVFCRGCIEQViQREPNAKCPLCR 43
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
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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