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Conserved domains on  [gi|131129|sp|P09108|]
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RecName: Full=43 kDa receptor-associated protein of the synapse; Short=RAPsyn; AltName: Full=43 kDa postsynaptic protein; AltName: Full=Acetylcholine receptor-associated 43 kDa protein

Protein Classification

TPR and RING-H2_Rapsyn domain-containing protein (domain architecture ID 11721572)

protein containing domains SNAP, TPR, and RING-H2_Rapsyn

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SNAP super family cl24038
Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the ...
1-80 4.98e-31

Soluble N-ethylmaleimide-sensitive factor (NSF) Attachment Protein family; Members of the soluble NSF attachment protein (SNAP) family are involved in intracellular membrane trafficking, including vesicular transport between the endoplasmic reticulum and Golgi apparatus. Higher eukaryotes contain three isoforms of SNAPs: alpha, beta, and gamma. Alpha-SNAP is universally present in eukaryotes and acts as an adaptor protein between SNARE (integral membrane SNAP receptor) and NSF for recruitment to the 20S complex. Beta-SNAP is brain-specific and shares high sequence identity (about 85%) with alpha-SNAP. Gamma-SNAP is weakly related (about 20-25% identity) to the two other isoforms, and is ubiquitous. It may help regulate the activity of the 20S complex. The X-ray structures of vertebrate gamma-SNAP and yeast Sec17, a SNAP family member, show similar all-helical structures consisting of an N-terminal extended twisted sheet of four Tetratricopeptide repeat (TPR)-like helical hairpins and a C-terminal helical bundle.


The actual alignment was detected with superfamily member pfam10579:

Pssm-ID: 329252  Cd Length: 80  Bit Score: 113.46  E-value: 4.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129       1 MGQDQTKQQIEKGLQLYQANETGKALEIWQQVVERSTELPGRFRALGCLITAHSEMGKYEDMLRFAVAQSEAARQMGDPE 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 5.03e-21

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


:

Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 85.18  E-value: 5.03e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 131129   360 ELYCGLCGESIGDQNSQLQALPCSHLFHLKCLQTN--GNRGCPNCKR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-242 4.52e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


:

Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.00  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129     9 QIEKGLQLYQANETGKALEIWQQVVERStELPGRFRALGCLITAHSEMGKYEDmlrfAVAQSEAARQMGDPERVTEAYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELE-LLPNLAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129    89 LArGHEKLCEFSEAVAYCRTCLGAEGGPLRLqfnGQVCLSMGNAFLGLSAFQKALECFEKALRYAHGNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131129   169 LGAFYVQLKDYEKALFFPCKSAELVADYgrgwslkykAMSRYHMAAAYRKLGRMDDAMECCEESMKIALQHQDR 242
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDLYNL 272
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 4.98e-31

Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies upon the clustering of acetylcholine receptors and other proteins in the muscle membrane. Rapsyn is a peripheral membrane protein that is selectively concentrated at the neuromuscular junction and is essential for the formation of synaptic acetylcholine receptor aggregates. Acetylcholine receptors fail to aggregate beneath nerve terminals in mice where rapsyn has been knocked out. The N-terminal six amino acids of rapsyn are its myristoylation site, and myristoylation is necessary for the targeting of the protein to the membrane.


Pssm-ID: 313739  Cd Length: 80  Bit Score: 113.46  E-value: 4.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129       1 MGQDQTKQQIEKGLQLYQANETGKALEIWQQVVERSTELPGRFRALGCLITAHSEMGKYEDMLRFAVAQSEAARQMGDPE 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 5.03e-21

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 85.18  E-value: 5.03e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 131129   360 ELYCGLCGESIGDQNSQLQALPCSHLFHLKCLQTN--GNRGCPNCKR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-242 4.52e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.00  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129     9 QIEKGLQLYQANETGKALEIWQQVVERStELPGRFRALGCLITAHSEMGKYEDmlrfAVAQSEAARQMGDPERVTEAYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELE-LLPNLAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129    89 LArGHEKLCEFSEAVAYCRTCLGAEGGPLRLqfnGQVCLSMGNAFLGLSAFQKALECFEKALRYAHGNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131129   169 LGAFYVQLKDYEKALFFPCKSAELVADYgrgwslkykAMSRYHMAAAYRKLGRMDDAMECCEESMKIALQHQDR 242
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDLYNL 272
TPR_12 pfam13424
Tetratricopeptide repeat;
206-278 4.07e-06

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 44.30  E-value: 4.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 131129     206 AMSRYHMAAAYRKLGRMDDAMECCEESMKIA--LQHQDRPLQALCLLCFADIHRHRSDIGKALPRYESSLNIMTE 278
Cdd:pfam13424   3 ATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-409 1.74e-03

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 39.98  E-value: 1.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 131129   363 CGLCGESIgDQNSQLQALPCSHLFHLKCLQT--NGNR-GCPNCkRSSVKP 409
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVC-RTAIPP 373
zf-RING_2 pfam13639
Ring finger domain;
363-403 6.53e-03

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 34.29  E-value: 6.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 131129     363 CGLCGESIGDQNSqLQALPCSHLFHLKCLQ---TNGNRgCPNCK 403
Cdd:pfam13639   3 CPICLEEFEEGDK-VVILPCGHHFHRECLDkwlRSSNT-CPLCR 44
 
Name Accession Description Interval E-value
Rapsyn_N pfam10579
Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies ...
1-80 4.98e-31

Rapsyn N-terminal myristoylation and linker region; Neuromuscular junction formation relies upon the clustering of acetylcholine receptors and other proteins in the muscle membrane. Rapsyn is a peripheral membrane protein that is selectively concentrated at the neuromuscular junction and is essential for the formation of synaptic acetylcholine receptor aggregates. Acetylcholine receptors fail to aggregate beneath nerve terminals in mice where rapsyn has been knocked out. The N-terminal six amino acids of rapsyn are its myristoylation site, and myristoylation is necessary for the targeting of the protein to the membrane.


Pssm-ID: 313739  Cd Length: 80  Bit Score: 113.46  E-value: 4.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129       1 MGQDQTKQQIEKGLQLYQANETGKALEIWQQVVERSTELPGRFRALGCLITAHSEMGKYEDMLRFAVAQSEAARQMGDPE 80
Cdd:pfam10579   1 MGQDQTKQQIEKGLRLYQSNNTEKALRTWRKVLKKTCDREGCFRVLGCLITAHSEMGKYKEMLEFGHQQIGTARELEDPD 80
RING-H2_Rapsyn cd16478
RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) ...
360-404 5.03e-21

RING finger, H2 subclass, found in 43 kDa receptor-associated protein of the synapse (Rapsyn) and similar proteins; Rapsyn, also known as acetylcholine receptor-associated 43 kDa protein or RING finger protein 205 (RNF205), is a 43 kDa postsynaptic protein that plays an essential role in the clustering and maintenance of acetylcholine receptor (AChR) in the postsynaptic membrane of the motor endplate (EP). AChRs enable the transport of rapsyn from the Golgi complex to the plasma membrane through a molecule-specific interaction. Rapsyn also mediates subsynaptic anchoring of protein kinase A (PKA) type I in close proximity to the postsynaptic membrane, which is essential for synapse maintenance. Its mutations in humans cause endplate acetylcholine-receptor deficiency and myasthenic syndrome. Rapsyn contains an N-terminal myristoylation signal required for membrane association, seven tetratricopeptide repeats (TPRs) that subserve rapsyn self-association, a coiled-coil domain responsible for the binding of determinants within the long cytoplasmic loop of each AChR subunit, a C3H2C3-type RING-H2 finger that binds to the cytoplasmic domain of beta-dystroglycan and to S-NRAP and links rapsyn to the subsynaptic cytoskeleton, and a serine phosphorylation site.


Pssm-ID: 319392 [Multi-domain]  Cd Length: 47  Bit Score: 85.18  E-value: 5.03e-21
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 131129   360 ELYCGLCGESIGDQNSQLQALPCSHLFHLKCLQTN--GNRGCPNCKR 404
Cdd:cd16478   1 ELYCGMCGESIGEKNESLQALPCSHIFHLKCLQTNlnGTRGCPNCRR 47
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
9-242 4.52e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 51.00  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129     9 QIEKGLQLYQANETGKALEIWQQVVERStELPGRFRALGCLITAHSEMGKYEDmlrfAVAQSEAARQMGDPERVTEAYLN 88
Cdd:COG0457  62 LLLLALALLKLGRLEEALELLEKALELE-LLPNLAEALLNLGLLLEALGKYEE----ALELLEKALALDPDPDLAEALLA 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131129    89 LArGHEKLCEFSEAVAYCRTCLGAEGGPLRLqfnGQVCLSMGNAFLGLSAFQKALECFEKALRYAHGNDDKMLEcrvccS 168
Cdd:COG0457 137 LG-ALYELGDYEEALELYEKALELDPELNEL---AEALLALGALLEALGRYEEALELLEKALKLNPDDDAEALL-----N 207
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 131129   169 LGAFYVQLKDYEKALFFPCKSAELVADYgrgwslkykAMSRYHMAAAYRKLGRMDDAMECCEESMKIALQHQDR 242
Cdd:COG0457 208 LGLLYLKLGKYEEALEYYEKALELDPDN---------AEALYNLALLLLELGRYEEALEALEKALELDPDLYNL 272
TPR_12 pfam13424
Tetratricopeptide repeat;
206-278 4.07e-06

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 44.30  E-value: 4.07e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 131129     206 AMSRYHMAAAYRKLGRMDDAMECCEESMKIA--LQHQDRPLQALCLLCFADIHRHRSDIGKALPRYESSLNIMTE 278
Cdd:pfam13424   3 ATALNNLAAVLRRLGRYDEALELLEKALEIArrLLGPDHPLTATTLLNLGRLYLELGRYEEALELLERALALAEK 77
RING-H2 cd16448
H2 subclass of RING (RING-H2) finger and its variants; RING finger is a specialized type of ...
363-403 1.31e-05

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


Pssm-ID: 319362 [Multi-domain]  Cd Length: 44  Bit Score: 41.67  E-value: 1.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 131129   363 CGLCGESIGDQNSQLQALPCSHLFHLKCLQ---TNGNRGCPNCK 403
Cdd:cd16448   1 CAICLEEFEEGDCPVRLLPCGHVFHKSCIDkwlESGNRTCPLCR 44
RING-H2_RNF13_like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
363-404 4.55e-04

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. 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 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. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, induces calnexin ubiquitination, and p97-dependent degradation, indicating an ER-associated degradation-like mechanism of calnexin turnover. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and involved in spermatogenesis.


Pssm-ID: 319579 [Multi-domain]  Cd Length: 46  Bit Score: 37.39  E-value: 4.55e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 131129   363 CGLCGESIGDQNsQLQALPCSHLFHLKCLQ---TNGNRGCPNCKR 404
Cdd:cd16665   3 CAICLDDYEEGD-KLRILPCSHAYHCKCIDpwlTQNRRTCPVCKR 46
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
363-404 4.91e-04

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


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 37.33  E-value: 4.91e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 131129   363 CGLCGESIgDQNSQLQALPCSHLFHLKCLQ---TNGNRGCPNCKR 404
Cdd:cd16797   3 CAICLDEY-EEGDKLRVLPCSHAYHSKCVDpwlTQTKKTCPVCKQ 46
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
363-403 6.02e-04

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


Pssm-ID: 319368 [Multi-domain]  Cd Length: 43  Bit Score: 36.90  E-value: 6.02e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 131129   363 CGLCGESIGDqNSQLQALPCSHLFHLKCLQT--NGNRGCPNCK 403
Cdd:cd16454   2 CAICLEEFED-GEEVRVLPCNHLFHSNCIDPwlEQHATCPLCR 43
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
363-403 6.31e-04

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


Pssm-ID: 319371 [Multi-domain]  Cd Length: 44  Bit Score: 36.87  E-value: 6.31e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 131129   363 CGLCGESIGDQNSQLQALPCSHLFHLKCLQTNGNRGCPNCK 403
Cdd:cd16457   3 CPVCLERMDESVSGILTILCNHSFHCDCLKRWGDSTCPVCR 43
RING1-H2_RNF32 cd16677
RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; ...
363-403 1.10e-03

RING finger 1, H2 subclass, found in RING finger protein 32 (RNF32) and similar proteins; RNF32 is mainly expressed in testis spermatogenesis, most likely in spermatocytes and/or in spermatids, suggesting a possible role in sperm formation. RNF32 contains two C3H2C3-type RING-H2 fingers separated by an IQ domain of unknown function. Although the biological function of RNF32 remains unclear, the protein with double RING-H2 fingers may act as a scaffold for binding several proteins that function in the same pathway. This family corresponds to the first RING-H2 finger.


Pssm-ID: 319591 [Multi-domain]  Cd Length: 44  Bit Score: 36.54  E-value: 1.10e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 131129   363 CGLCGESIGDQNSQLqaLPCSHLFHLKCLQT----NGNRGCPNCK 403
Cdd:cd16677   2 CVICKEDFGLQQQVL--LSCSHVFHRACLESferfSGKKTCPMCR 44
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
363-409 1.74e-03

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


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 39.98  E-value: 1.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 131129   363 CGLCGESIgDQNSQLQALPCSHLFHLKCLQT--NGNR-GCPNCkRSSVKP 409
Cdd:COG5540 326 CAICMSNF-IKNDRLRVLPCDHRFHVGCVDKwlLGYSnKCPVC-RTAIPP 373
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
362-403 2.53e-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 [Multi-domain]  Cd Length: 45  Bit Score: 35.61  E-value: 2.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 131129   362 YCGLCGESIgDQNSQLQALPCSHLFHLKCL----QTNGNRGCPNCK 403
Cdd:cd16480   1 YCTICSDFF-DNSRDVAAIHCGHTFHYECLlqwfETAPSRTCPQCR 45
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
363-403 3.08e-03

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


Pssm-ID: 319374 [Multi-domain]  Cd Length: 43  Bit Score: 35.00  E-value: 3.08e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 131129   363 CGLCGESIGDQNsqLQALPCSHLFHLKCLQT--NGNRGCPNCK 403
Cdd:cd16460   3 CVICHENLSPEN--LSVLPCAHKFHSQCIRPwlMQQRTCPTCR 43
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
355-404 5.14e-03

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


Pssm-ID: 319387 [Multi-domain]  Cd Length: 46  Bit Score: 34.58  E-value: 5.14e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 131129   355 CMEDMELYCGLCGesigdqnsqlqaLPCSHLFHLKCLQ---TNGNRGCPNCKR 404
Cdd:cd16473   5 CLENYEEGCLLCG------------LPCGHVFHQNCIDvwlTRDNHCCPVCRW 45
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
362-408 5.24e-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 [Multi-domain]  Cd Length: 49  Bit Score: 34.56  E-value: 5.24e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 131129   362 YCGLCGESIgDQNSQLQALPCSHLFHLKCLQT--NGNRGCPNCKRSSVK 408
Cdd:cd16803   2 HCAVCIEGY-KQNDVVRILPCKHVFHKSCVDPwlNEHCTCPMCKLNILK 49
RING-H2_Pirh2 cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
363-403 6.11e-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: 34.48  E-value: 6.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 131129   363 CGLCGESIGDQNSQLQALPCSHLFHLKCLQT---NGNRGCPNCK 403
Cdd:cd16464   2 CPVCLEDLFTSREPVHVLPCGHLMHSTCFEEylkSGNYRCPLCS 45
zf-RING_2 pfam13639
Ring finger domain;
363-403 6.53e-03

Ring finger domain;


Pssm-ID: 338865 [Multi-domain]  Cd Length: 44  Bit Score: 34.29  E-value: 6.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 131129     363 CGLCGESIGDQNSqLQALPCSHLFHLKCLQ---TNGNRgCPNCK 403
Cdd:pfam13639   3 CPICLEEFEEGDK-VVILPCGHHFHRECLDkwlRSSNT-CPLCR 44
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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