2ECJ


Conserved Protein Domain Family
RING-HC_TRIM39_C-IV
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cd16601: RING-HC_TRIM39_C-IV 
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RING finger, HC subclass, found in tripartite motif-containing protein 39 (TRIM39) and similar proteins
TRIM39, also known as RING finger protein 23 (RNF23) or testis-abundant finger protein, is an E3 ubiquitin-protein ligase that plays a role in controlling DNA damage-induced apoptosis through inhibition of the anaphase promoting complex (APC/C), a multiprotein ubiquitin ligase that controls multiple cell cycle regulators, including cyclins, geminin, and others. TRIM39 also functions as a regulator of several key processes in the proliferative cycle. It directly regulates p53 stability. It modulates cell cycle progression and DNA damage responses via stabilizing p21. Moreover, TRIM39 negatively regulates the nuclear factor kappaB (NFkappaB)-mediated signaling pathway through stabilization of Cactin, an inhibitor of NFkappaB- and Toll-like receptor (TLR)-mediated transcription, which is induced by inflammatory stimulants such as tumor necrosis factor alpha. Furthermore, TRIM39 is a MOAP-1-binding protein that can promote apoptosis signaling through stabilization of MOAP-1 via the inhibition of its poly-ubiquitination process. TRIM39 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.
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Statistics
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PSSM-Id: 438263
Aligned: 10 rows
Threshold Bit Score: 74.8284
Created: 21-Apr-2016
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
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Zn binding site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
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:
  • Structure:2ECJ; Homo sapiens tripartite motif-containing protein 39 RING domain binds two Zn2+ ions through its RING-HC finger
    - View structure with Cn3D
  • 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           #  #           # #  #  #               #  #
2ECJ_A        15 EASCSVCLEYLKEPVIIECGHNFCKACITRWWEDLErd--fPCPVC 58  human
Q9HCM9        26 EASCSVCLEYLKEPVIIECGHNFCKACITRWWEDLErd--fPCPVC 69  human
EMP27861      13 EASCSVCLEYLKDPVIIDCGHNFCRVCITRWWEELNrd--fPCPVC 56  green sea turtle
KYO19856     147 EASCSVCLEYLKDPVIIDCGHNFCRACITRWWEELNrd--fPCPVC 190 American alligator
XP_016047677  26 EASCSVCLEYLKDPVIIECGHNFCKACITRWWEDLErd--fPCPVC 69  western European hedgehog
Q5TA31         9 EAACALCQRAPREPVRADCGHRFCRACVVRFWAEEDgp--fPCPEC 52  human
NP_001171022  13 EARCSVCKEYLKNPGTMECGHKVCLSCTSVFWEDLKgs--vPCPSC 56  house mouse
NP_001068571   9 YFNCPLCTELLRDPVAIPCGHSFCMDCISGYWNEADytgiyICPQC 54  zebrafish
NP_001313416   5 QDLCYLCKEDFRDPVSIPCGHVFCSLCIKTYWDHADqtgqyVCPQC 50  zebrafish
NP_001315033 132 HLQCALCKSMLKDPASITCGHNFCRDCINAFWDNCAgd--fVCPQC 175 zebrafish

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