Conserved Protein Domain Family
RING-HC_TRIM13_C-V
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cd16762: RING-HC_TRIM13_C-V 
RING finger, HC subclass, found in tripartite motif-containing protein 13 (TRIM13) and similar proteins
TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). It also targets the known ER proteolytic substrate CD3-delta, but not the N-end rule substrate Ub-R-YFP (yellow fluorescent protein) for degradation. Moreover, TRIM13 regulates ubiquitination and degradation of NEMO to suppress tumor necrosis factor (TNF) induced nuclear factor-kappaB (NF- kappa B) activation. It is also involved in NF-kappaB p65 activation and nuclear factor of activated T-cells (NFAT)-dependent activation of c-Rel upon T-cell receptor engagement. Furthermore, TRIM13 negatively regulates melanoma differentiation-associated gene 5 (MDA5)-mediated type I interferon production. It also regulates caspase-8 ubiquitination, translocation to autophagosomes, and activation during ER stress induced cell death. Meanwhile, TRIM13 enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. TRIM13 belongs to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region. In addition, TRIM13 contains a C-terminal transmembrane domain.
Links
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Statistics
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PSSM-Id: 438418
Aligned: 6 rows
Threshold Bit Score: 114.628
Created: 3-May-2013
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.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1             #  #           # #  #  #                    #  #    
O60858         5 EEDLTCPICCSLFDDPRVLPCSHNFCKKCLEGILEGSvrnslwrpapFKCPTCRKET 61  human
Q503I2         5 EEDLTCPICCCLFEDPRVLPCSHSFCKKCLEGILDGNrspt--wrppFKCPTCRKET 59  zebrafish
F6ZQ54         5 EEDLTCPICCSLFDDPRVLPCSHNFCKKCLDGVLEENsrtmqwrpssFKCPTCRKET 61  western clawed frog
EOB04545       7 EEDLTCPICCSLFDDPRVLPCSHNFCRKCLEGILEGNvrnvlwrpapFKCPTCRKET 63  mallard
XP_007908951   5 EEELTCPICCCLFEDPRVLPCSHNFCKKCLEGILEGSgrsmp-wrvpFKCPTCRKET 60  elephant shark
XP_014346633   5 EEDLTCPICCCLFDDPRVLPCFHNFCKKCLEGILEGSnrtml-wrppFRCPTCRKET 60  coelacanth

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