Conserved Protein Domain Family
RING-HC_TRIM50_like_C-IV
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cd16605: RING-HC_TRIM50_like_C-IV 
RING finger, HC subclass, found in tripartite motif-containing protein TRIM50, TRIM73, TRIM74 and similar proteins
TRIM50 is a stomach-specific E3 ubiquitin-protein ligase, encoded by the Williams-Beuren syndrome (WBS) TRIM50 gene, which regulates vesicular trafficking for acid secretion in gastric parietal cells. It colocalizes, interacts with, and increases the level of p62/SQSTM1, a multifunctional adaptor protein implicated in various cellular processes including the autophagy clearance of polyubiquitinated protein aggregates. It also promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through the interaction with histone deacetylase 6 (HDAC6), a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. TRIM50 can be acetylated by PCAF and p300. TRIM50 belongs to the C-IV subclass of the 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. This subfamily also includes two paralogs of TRIM50, tripartite motif-containing protein 73 (TRIM73), also known as tripartite motif-containing protein 50B (TRIM50B), and tripartite motif-containing protein 74 (TRIM74), also known as tripartite motif-containing protein 50C (TRIM50C), both of which are WBS-related genes encoding proteins that may also act as E3 ligases. In contrast with TRIM50, TRIM73 and TRIM74 belong to the C-V subclass of TRIM family of proteins that are defined by N-terminal RBCC domains only.
Links
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Statistics
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PSSM-Id: 438267
Aligned: 10 rows
Threshold Bit Score: 82.8804
Created: 23-Nov-2015
Updated: 17-Oct-2022
Structure
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Aligned Rows:
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Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:C C C H C C C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:based on the structures of other RING-HC fingers with bound zinc
  • Comment:C3HC4-type RING-HC finger consensus motif: 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 and the number of X residues varies in different fingers
  • Comment:A RING finger typically binds two zinc atoms, with its Cys and/or His side chains in a unique "cross-brace" arrangement.
Scroll to Sequence Alignment Display
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1          #  #           # #  #  #             #  #  
Q86XT4        14 LQCPICLEVFKEPLMLQCGHSYCKGCLVSLSCHLDaELRCPVCRQ 58  human
EMP30540      14 LLCPICLEVLKEPLMLQCGHSFCKSCVGSLMCNLDqQLLCPVCRQ 58  green sea turtle
Q86UV6        14 LQCPICLEVFKESLMLQCGHSYCKGCLVSLSYHLDtKVRCPMCWQ 58  human
Q86UV7        14 LQCPICLEVFKESLMLQCGHSYCKGCLVSLSYHLDtKVRCPMCWQ 58  human
XP_005986962  14 LLCPICLEVFKEPLMLQCGHSYCKSCLTSLSGELEgQVLCPVCRK 58  coelacanth
XP_009578514  14 LLCPICLEVFKEPLMLQCGHSYCKSCVVSLSGELDgQFLCPVCRQ 58  northern fulmar
XP_010211498  14 LLCPICLEVFKEPLMLQCGHSYCKSCVVSLSSELPgQFLCPVCRQ 58  white-throated tinamou
XP_015151390  14 LLCPICLEVFKEPLMLQCGHSYCKSCVLSLSGELDeQLLCPVCRK 58  chicken
XP_018120782  14 LTCPICLEVFKEPLMLQCGHSYCKECLWGLMTESSiQLLCPVCRQ 58  African clawed frog
XP_020369047  14 LLCPICLEIFKQPLMLQCGHSYCKNCIHSLSGNLAsCFTCPVCRK 58  whale shark

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