4UI9,4R2Y,2MT5


Conserved Protein Domain Family
RING-H2_APC11

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cd16456: RING-H2_APC11 
Click on image for an interactive view with Cn3D
RING finger, H2 subclass, found in anaphase-promoting complex subunit 11 (APC11) and similar proteins
APC11, also known as cyclosome subunit 11, or hepatocellular carcinoma-associated RING finger protein, is a C3H2C3-type RING-H2 protein that facilitates ubiquitin chain formation by recruiting ubiquitin-charged ubiquitin conjugating enzymes (E2) through its RING-H2 domain. APC11 and its partner the cullin-like subunit APC2 form the dynamic catalytic core of the gigantic, multisubunit 1.2-MDa anaphase-promoting complex/cyclosome (APC), also known as the cyclosome, which is a ubiquitin-protein ligase (E3) composed of at least 12 subunits and controls cell division by ubiquitinating cell cycle regulators, such as cyclin B and securin, to drive their timely degradation. APC11 can be inhibited by hydrogen peroxide, which may contributes to the delay in cell cycle progression through mitosis that is characteristic of cells subjected to oxidative stress. APC11 contains a canonical RING-H2-finger domain, which includes one histidine and seven cysteine residues that coordinate two Zn2+ ions. In addition, it contains a third Zn2+-binding site and the third Zn2+ ion is not essential for its ligase activity.
Statistics
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PSSM-Id: 319370
View PSSM: cd16456
Aligned: 45 rows
Threshold Bit Score: 83.4762
Threshold Setting Gi: 948278361
Created: 22-Dec-2011
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:2MT5; Homo sapiens APC11 binds three Zn2+ ions through its RING-H2 finger.
    View structure with Cn3D
  • Comment:APC11 contains a third Zn2+-binding site, in addition to the two Zn2+ ions of the canonical RING-H2 finger.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
Feature 1           #  #           #      #      #       #              #  #      
4UI9_B        20 DENCGICRmaFNGCCP-DCKvPGDDCPLVWGqCSHCFHMHCILKWLhaqq-vqqhCPMCRQEWKF 82
2MT5_A         6 DENCGICRmaFNGCCP-DCKvPGDDCPLVWGqCSHCFHMHCILKWLhaqq-vqqhCPMCRQEWKF 68
gi 74996758   21 EECCGICRmaFDGCCV-DCKiPGDDCPPVWGvCNHAFHMHCILKWLnane--lqqCPMCRSEWRF 82
gi 116783412  20 DELCAICKlpFDGCCT-ECKyPGDDCPLVWGaCSHPFHLHCIVKWTgtqn--rahCPLCRRDWQI 81
gi 159469590  21 DDVCGICRa-PFDGCPpECKyPGDDSPVVWGaCQHAFHLQCIQKWLssaa--eqkCPMCRQAWEY 82
gi 294947344 223 EEDCAICCqpFDATCG-ECRiPGDDCPPVWGqCGHHFHVHCISRWIndq----kpCPMCRREFKP 282
gi 307105524  22 DDVCGICRm-PFDGCPpDGKyPGDDSPVVWGiCTHAFHLQCINRWLqsqa--eqkCPFCRRQWEF 83
gi 470433645  55 EDSCGICRmqFDTYCV-DCKkPGDECPPIWGkCNHIFHLHCILKWIqqqg-aeahCPMCRQPWEF 117
gi 570970799  36 EECCGICRyaFEACCP-ECTmPGDGCPPVWGaCNHAFHMHCLVKWLeslqsmrqhCPMCRQDWKF 99
gi 693497993  64 GDVCGICRi-AYDGCPpDAKfPGDDSPVVWGrCGHAFHLQCITKWLsgnaqdaprCPICRGAWEF 127

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