2YSL,2YSJ


Conserved Protein Domain Family
RING-HC_TRIM31_C-V

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cd16582: RING-HC_TRIM31_C-V 
Click on image for an interactive view with Cn3D
RING finger, HC subclass, found in tripartite motif-containing protein 31 (TRIM31) and similar proteins
TRIM31 is an E3 ubiquitin-protein ligase that primarily localizes to the cytoplasm, but is also associated with the mitochondria. It can negatively regulate cell proliferation and may be a potential biomarker of gastric cancer as it is overexpressed from the early stage of gastric carcinogenesis. TRIM31 is downregulated in non-small cell lung cancer and serves as a potential tumor suppressor. It interacts with p52 (Shc) and inhibits Src-induced anchorage-independent growth. TRIM31 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain.
Statistics
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PSSM-Id: 319496
View PSSM: cd16582
Aligned: 6 rows
Threshold Bit Score: 47.8452
Threshold Setting Gi: 159164817
Created: 14-Apr-2016
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteRING-HC finger
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:2YSL; Homo sapiens TRIM31 binds two Zn2+ ions through its RING-HC finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
Feature 1            #  #           # #  #  #             #  #
2YSL_A         20 EVICPICLDILqKPVTIDCGHNFCLKCITQIGEtscGFFKCPLC 63
2YSJ_A         20 EVICPICLDILqKPVTIDCGHNFCLKCITQIGEtscGFFKCPLC 63
gi 68068082    13 EVICPICLDILqKPVTIDCGHNFCLKCITQIGEtscGFFKCPLC 56
gi 241599212   20 EFVCPICLEIFqKPVTISCGHTFCSTCLAQCKQ---DDPKCPLC 60
gi 557737134  425 ELTCSICLELLqLPVTINCGHTFCRYCISHNKM---SRRSCPLC 465
gi 574967056  463 ELTCPICLDYFyLPVTMNCGHTFCRYCIGHNKL---NGKNCPLC 503

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