Conserved Protein Domain Family
RING-HC_TIF1beta

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cd16765: RING-HC_TIF1beta 
RING finger, HC subclass, found in transcription inknown asiary factor 1-beta (TIF1-beta)
TIF1-beta, also known as Kruppel-associated Box (KRAB)-associated protein 1 (KAP-1), KRAB-interacting protein 1 (KRIP-1), nuclear co-repressor KAP-1, RING finger protein 96, tripartite motif-containing protein 28 (TRIM28), or E3 SUMO-protein ligase TRIM28, belongs to the C-VI subclass of 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 plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. It acts as a nuclear co-repressor that plays a role in transcription and in the DNA damage response. Upon DNA damage, the phosphorylation of KAP-1 on serine 824 by the ataxia telangiectasia-mutated (ATM) kinase enhances cell survival and facilitates chromatin relaxation and heterochromatic DNA repair. It also regulates CHD3 nucleosome remodeling during the DNA double-strand break (DSB) response. Meanwhile, KAP-1 can be dephosphorylated by protein phosphatase PP4C in the DNA damage response. Moreover, KAP-1 is a co-activator of the orphan nuclear receptor NGFI-B (or Nur77) and is involved in NGFI-B-dependent transcription. It is also a coiled-coil binding partner, substrate and activator of the c-Fes protein tyrosine kinase. The N-terminal RBCC domains of TIF1-beta are responsible for the interaction with KRAB zinc finger proteins (KRAB-ZFPs), MDM2, MM1, C/EBPbeta, and the regulation of homo- and heterodimerization. The C-terminal PHD/Bromo domains are involved in interacting with SETDB1, Mi-2alpha and other proteins to form complexes with histone deacetylase or methyltransferase activity.
Statistics
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PSSM-Id: 319679
View PSSM: cd16765
Aligned: 3 rows
Threshold Bit Score: 78.55
Threshold Setting Gi: 642131185
Created: 26-Jul-2013
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Zn binding siteRING-HC finger
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Comment:Based on the structural evidence that Homo sapiens transcription factor PML (1BOR) binds two Zn2+ ions through its RING-HC finger.
  • Citation:PMID 8317827
  • Citation:PMID 7729428

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
Feature 1           #  #              # #  #  #                         #  #    
gi 3183179    62 LEHCGVCRERLRpEREPRLLPCLHSACSACLGPaapaaanssgdggaagdgtVVDCPVCKQQC 124
gi 512854610  31 LESCGVCKKQLRaDTEPQLLPCLHSVCRACLPPetpapevat--nsgdlasaVVNCPICKHQC 91
gi 642131185  22 LDGCGLCCTELKpDRNPQLLPCLHSVCQGCVPLsd----------------fKTECPVCGRQY 68

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