4R8P,2CKL


Conserved Protein Domain Family
RING-HC_RING1-like

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cd16531: RING-HC_RING1-like 
Click on image for an interactive view with Cn3D
RING finger, HC subclass, found in really interesting new gene proteins RING1, RING2 and similar proteins
RING1, also known as polycomb complex protein RING1, RING finger protein 1 (RNF1), or RING finger protein 1A (RING1A), is a transcriptional repressor that is associated with the Polycomb group (PcG) protein complex involved in stable repression of gene activity. RING2, also known as huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, protein DinG, RING finger protein 1B (RING1B), RING finger protein 2 (RNF2), or RING finger protein BAP-1, is an E3 ubiquitin-protein ligase that interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve the specific monoubiquitination of K119 on histone H2A (H2AK119ub), thereby playing a central role in histone code and gene regulation. Both RING1 and RING2 are core components of polycomb repressive complex 1 (PRC1) that functions as an E3-ubuiquitin ligase transferring the mono-ubuiquitin mark to the C-terminal tail of Histone H2A at K118/K119. PRC1 is also capable of chromatin compaction, a function not requiring histone tails, and this activity appears important in gene silencing. RING2 acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Members of this family contain a C3HC4-type RING-HC finger.
Statistics
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PSSM-Id: 438193
Aligned: 34 rows
Threshold Bit Score: 98.8805
Created: 3-May-2013
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
Zn binding siteoligomer
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:2CKL: Human RING1B binds two Zn2+ ions through its RING-HC finger.
  • Structure:4R8P; Homo sapiens RING1B/E2 fusion binds two Zn2+ ions through its RING-HC finger.
  • 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.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #  #            # #  #  #                     #  #                       
4R8P_L       48 ELMCPICLDMLkNTMTTKECLHRFCADCIITALRsg----------nKECPTCRKKLVSKRSLRPDPNFDALISKI 113  human
2CKL_B       54 ELMCPICLDMLkNTMTTKECLHRFCADCIITALRsg----------nKECPTCRKKLVSKRSLRPDPNFDALISKI 119  house mouse
PNR37534     27 EMQCPICLGIIrKTRTVMECLHRFCRECIDKSMRlg----------nNECPACRTHCASRRSLRDDPNFDALVAAI 92   Physcomitrium patens
EFJ38128     11 EMQCPICLGIIrKTRTVMECLHRFCRECIDKSMRlg----------nNECPACRTHCASRRSLRDDPNFDSLIAAL 76   Selaginella moellen...
EJK61509     58 AFQCPICLGYIkNCRTVMECLHRFCEDCIEKYIRlg----------kKECPQCRKPVPSRRSLRTDKSFDALMRSI 123  Thalassiosira oceanica
KYK69303    650 DLSCPICMGIFqNVVVVKDCLHRFCADCIEKCVRtg----------lRECPQCRIHVASRRALRPDPIFERILNKL 715  Toxoplasma gondii T...
PVC54094     55 EISCPICSGIViRCVVIKTCLHRFCLNCIQKCVRig----------lHECPKCRKHVPSKRFLKADPIYDSIISRI 120  Theileria orientalis
CEO97321     27 DLTCAVCMSVInEAWTVKECLHRFCHQCIEQSLRfs----------gPQCPACRVKCPSHRSLRQDKAFDAIISSF 92   Plasmodiophora bras...
GBF88107     45 ETRCPICFGKIkSARVSMVCLHRFCAGCIEQFMRnqleggkrardqgKECPVCRAHLSSRRAVRPDPVFDQIISGL 120  Raphidocelis subcap...
KAA6426212   33 ETRCPVCLGVIkNARLVSGCMHRFCAECIEKWLRvc---------reNNCPQCRMPMQSRRDCKKDGKYDRLLRLL 99   Trebouxia sp. A1-2

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