3ZTG,2YUR


Conserved Protein Domain Family
vRING-HC-C4C4_RBBP6

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cd16620: vRING-HC-C4C4_RBBP6 
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Variant RING finger, HC subclass (C4C4-type), found in retinoblastoma-binding protein 6 (RBBP6) and similar proteins
RBBP6, also known as proliferation potential-related protein, protein P2P-R, retinoblastoma-binding Q protein 1 (RBQ-1), or p53-associated cellular protein of testis (PACT), is a nuclear E3 ubiquitin-protein ligase involved in multiple processes, such as the control of gene expression, mitosis, cell differentiation, and cell apoptosis. It plays a role in both promoting and inhibiting apoptosis in many human cancers, including esophageal, lung, hepatocellular, and colon cancers, familial myeloproliferative neoplasms, as well as in human immunodeficiency virus-associated nephropathy (HIVAN). It functions as an Rb- and p53-binding protein that plays an important role in chaperone-mediated ubiquitination and possibly in protein quality control. It acts as a scaffold protein to promote the assembly of the p53/TP53-MDM2 complex, resulting in an increase of MDM2-mediated ubiquitination and degradation of p53/TP53, and leading to both apoptosis and cell growth. It is also a double-stranded RNA-binding protein that plays a role in mRNA processing by regulating the human polyadenylation machinery and modulating expression of mRNAs with AU-rich 3' untranslated regions (UTRs). Moreover, RBBP6 ubiquitinates and destabilizes the transcriptional repressor ZBTB38 that negatively regulates transcription and levels of the MCM10 replication factor on chromatin. Furthermore, RBBP6 is involved in tunicamycin-induced apoptosis through mediating protein kinase (PKR) activation. RBBP6 contains an N-terminal ubiquitin-like domain and a C4C4-type RING finger, whose overall folding is similar to that of the typical C3HC4-type RING-HC finger. RBBP6 interacts with chaperones Hsp70 and Hsp40 through its N-terminal ubiquitin-like domain. It promotes the ubiquitination of p53 by Hdm2 in an E4-like manner through its RING finger. It also interacts directly with the pro-proliferative transcription factor Y-box-binding protein-1 (YB-1) via its RING finger.
Statistics
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PSSM-Id: 319534
View PSSM: cd16620
Aligned: 36 rows
Threshold Bit Score: 47.6238
Threshold Setting Gi: 470319601
Created: 3-May-2013
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:Zn binding site [ion binding site]
Evidence:
  • Structure:3ZTG; Homo sapiens RBBP6 binds two Zn2+ ions through its modified RING-HC finger.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             #  #           ##    #  #                       #    #
3ZTG_A        11 PDELLCLICKDIMtDAVVIPCCGNSYCDECIRTALLesd-----------ehtCPt--C 56   human
CBY18225     220 PDELCCPICNELIqDARKTPCCSSTYCNNCITQKLLesd-----------dglCPk--C 265  Oikopleura dioica
O94264       277 NISLACTLCKKLArNACRTPCCDKLFCEECIQTALLdsd------------feCPn--C 321  Schizosaccharomyces pombe 972h-
EAX88591     189 LQRWMCPICNRIMtHATLTPCCKVAYCDSCITEALLned------------qrCPnkdC 235  Trichomonas vaginalis G3
XP_004998268  63 PDDLKCPVCSKLVkLAIRTPCCNRIICNDCLMSRAGmt-------------svCPm--C 106  Salpingoeca sp. ATCC50818
EMR11220     277 DLTLECTLCHKLMkNPSTIPCCQEEYCEECIQTTLLead------------fvCPk--C 321  Pneumocystis murina B123
CCD82921     254 PKQLVCPLCNKLFsDAVLVSCCGTTYCNECIMGHVFdsqvl--------gshkCPn--C 302  Schistosoma mansoni
XP_667905    392 RDSLTCPICARLFrYAVLTPCCGETYCQECIINFIRnhmdaasgispntikgyCPh--C 448  Cryptosporidium hominis TU502
EJY84839     285 PPSLVCQLCKDFIkRASLTKCCASSGCQKCIQQKLVerk------------fqCPf--C 329  Oxytricha trifallax
ETO23955      16 PSKYSCELCNNVFkNATLTQCCKTTYCQDCILNYLRkhf------------fkCPk--C 60   Reticulomyxa filosa

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