Conserved Protein Domain Family
mRING-HC-C3HC3D_TRIM23_C-IX

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cd16645: mRING-HC-C3HC3D_TRIM23_C-IX 
Modified RING finger, HC subclass (C3HC3D-type), found in tripartite motif-containing protein 23 (TRIM23) and similar proteins
TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX 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 modified C3HC3D-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition.
Statistics
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PSSM-Id: 319559
View PSSM: cd16645
Aligned: 15 rows
Threshold Bit Score: 84.8113
Threshold Setting Gi: 66774189
Created: 17-May-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding sitemodified
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Mus musculus Roquin (4TXA) binds two Zn2+ ions through its modified RING-HC finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
Feature 1           #  #                # #  #               #  #  
gi 543839     28 VLECGVCEDVFslQGDKVPRLLLCGHTVCHDCLTRLPLHGRaIRCPFDRQ 77
gi 47228454    3 VLECGVCEDVFslQGDKVPRLLLCGHTVCHDCLTRLPLHGRaVRCPFDRQ 52
gi 156206362  19 VLECRVCEDVFhlQGDKVPRLLLCGHTVCHDCLARLPVHGRtLQCPFDRQ 68
gi 92081480   29 VLECGVCGEQFslSGEKVPRLLLCGHSFCHDCLTRLPVQAHtLVCPMDRQ 78
gi 390332516  24 VLECRVCEDIFslQGDKVPRLLLCGHTLCHECLSRLTLQGRaILCPFDRQ 73
gi 524901309  29 ILECRVCNEVFrfQGDKVPRLLVCGHTCCHQCLTRLPLHGRaLLCPFDRQ 78
gi 449278707   1 VLECGVCEDVFslQGDKVPRLLLCGHTVCHDCLTRLPLHGRaVRCPFDRQ 50
gi 556982410  37 VLECGVCEDVFslQGEKVPRLLLCGHTVCHDCLTRLPLHGRaVRCPFDRQ 86
gi 646718730  25 VLECRVCEDVFglQGDKVPRLLYCGHTVCHACLLRLPLRDNaVQCPFDRQ 74
gi 919010736  23 VLECRVCNDIFalQGDKVPRLLFCGHTVCHQCLTRLTPHGTaVLCPFDRQ 72

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