APC11_HUMAN
ID APC11_HUMAN Reviewed; 84 AA.
AC Q9NYG5; A8MTT2; B7ZW64; Q502X9; Q9BW64; Q9P0R2;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Anaphase-promoting complex subunit 11;
DE Short=APC11;
DE AltName: Full=Cyclosome subunit 11;
DE AltName: Full=Hepatocellular carcinoma-associated RING finger protein;
GN Name=ANAPC11; ORFNames=HSPC214;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11573242; DOI=10.1002/jcb.1217;
RA Chan A.H., Lee S.M.Y., Chim S.S., Kok L.D., Waye M.M.Y., Lee C.Y.,
RA Fung K.P., Tsui S.K.W.;
RT "Molecular cloning and characterization of a RING-H2 finger protein,
RT ANAPC11, the human homolog of yeast Apc11p.";
RL J. Cell. Biochem. 83:249-258(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li N., Wan T., Zhang W., Cao X.;
RT "Novel human APC11 anaphase-promoting complex subunit.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION IN APC/C COMPLEX.
RX PubMed=10922056; DOI=10.1073/pnas.97.16.8973;
RA Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.-M.;
RT "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to
RT ubiquitinate substrates of the anaphase-promoting complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8973-8978(2000).
RN [7]
RP FUNCTION, MUTAGENESIS, AND INTERACTION WITH ANAPC2 AND UBE2D2.
RX PubMed=11739784; DOI=10.1091/mbc.12.12.3839;
RA Tang Z., Li B., Bharadwaj R., Zhu H., Oezkan E., Hakala K., Deisenhofer J.,
RA Yu H.;
RT "APC2 cullin protein and APC11 RING protein comprise the minimal ubiquitin
RT ligase module of the anaphase-promoting complex.";
RL Mol. Biol. Cell 12:3839-3851(2001).
RN [8]
RP FUNCTION OF THE APC/C.
RX PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT "Mechanism of ubiquitin-chain formation by the human anaphase-promoting
RT complex.";
RL Cell 133:653-665(2008).
RN [9]
RP ELECTRON MICROSCOPY OF THE APC/C.
RX PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA Engel A., Peters J.-M., Stark H.;
RT "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT cryo-electron microscopy model of vertebrate APC/C.";
RL Mol. Cell 20:867-879(2005).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX PubMed=25043029; DOI=10.1038/nature13543;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL Nature 513:388-393(2014).
RN [11] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX PubMed=26083744; DOI=10.1038/nature14471;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Atomic structure of the APC/C and its mechanism of protein
RT ubiquitination.";
RL Nature 522:450-454(2015).
CC -!- FUNCTION: Together with the cullin protein ANAPC2, constitutes the
CC catalytic component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC progression through mitosis and the G1 phase of the cell cycle. The
CC APC/C complex acts by mediating ubiquitination and subsequent
CC degradation of target proteins: it mainly mediates the formation of
CC 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May
CC recruit the E2 ubiquitin-conjugating enzymes to the complex.
CC {ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:18485873}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The mammalian APC/C is composed at least of 14 distinct
CC subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6,
CC ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and
CC ANAPC16 that assemble into a complex of at least 19 chains with a
CC combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1
CC and FBXO5 (PubMed:26083744, PubMed:10922056, PubMed:25043029).
CC Interacts with the cullin domain of ANAPC2 (PubMed:11739784). Interacts
CC with UBE2D2 (PubMed:11739784). {ECO:0000269|PubMed:10922056,
CC ECO:0000269|PubMed:11739784, ECO:0000269|PubMed:25043029,
CC ECO:0000269|PubMed:26083744}.
CC -!- INTERACTION:
CC Q9NYG5; P28799: GRN; NbExp=3; IntAct=EBI-2130187, EBI-747754;
CC Q9NYG5; O43933: PEX1; NbExp=3; IntAct=EBI-2130187, EBI-988601;
CC Q9NYG5-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-12224467, EBI-11524452;
CC Q9NYG5-2; Q8NDZ0: BEND2; NbExp=3; IntAct=EBI-12224467, EBI-954079;
CC Q9NYG5-2; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12224467, EBI-10192698;
CC Q9NYG5-2; P53672: CRYBA2; NbExp=3; IntAct=EBI-12224467, EBI-750444;
CC Q9NYG5-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12224467, EBI-3867333;
CC Q9NYG5-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-12224467, EBI-740376;
CC Q9NYG5-2; Q12805: EFEMP1; NbExp=3; IntAct=EBI-12224467, EBI-536772;
CC Q9NYG5-2; O95967: EFEMP2; NbExp=3; IntAct=EBI-12224467, EBI-743414;
CC Q9NYG5-2; O43559: FRS3; NbExp=3; IntAct=EBI-12224467, EBI-725515;
CC Q9NYG5-2; O95872: GPANK1; NbExp=3; IntAct=EBI-12224467, EBI-751540;
CC Q9NYG5-2; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-12224467, EBI-3918847;
CC Q9NYG5-2; Q8NA54: IQUB; NbExp=3; IntAct=EBI-12224467, EBI-10220600;
CC Q9NYG5-2; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-12224467, EBI-1052037;
CC Q9NYG5-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-12224467, EBI-11953846;
CC Q9NYG5-2; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-12224467, EBI-12196745;
CC Q9NYG5-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-12224467, EBI-9996449;
CC Q9NYG5-2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-12224467, EBI-3957694;
CC Q9NYG5-2; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-12224467, EBI-12111050;
CC Q9NYG5-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12224467, EBI-11962084;
CC Q9NYG5-2; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-12224467, EBI-12813389;
CC Q9NYG5-2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-12224467, EBI-10181968;
CC Q9NYG5-2; P54646: PRKAA2; NbExp=3; IntAct=EBI-12224467, EBI-1383852;
CC Q9NYG5-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-12224467, EBI-1053424;
CC Q9NYG5-2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-12224467, EBI-740343;
CC Q9NYG5-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-12224467, EBI-11955057;
CC Q9NYG5-2; Q96LM6: TEX37; NbExp=3; IntAct=EBI-12224467, EBI-743976;
CC Q9NYG5-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12224467, EBI-11741437;
CC Q9NYG5-2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-12224467, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11573242}. Nucleus
CC {ECO:0000269|PubMed:11573242}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYG5-2; Sequence=VSP_012347;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in skeletal muscle and
CC heart; in moderate levels in brain, kidney, and liver; and at low
CC levels in colon, thymus, spleen, small intestine, placenta, lung and
CC peripheral blood leukocyte. {ECO:0000269|PubMed:11573242}.
CC -!- DOMAIN: The RING-type zinc finger domain coordinates an additional
CC third zinc ion.
CC -!- PTM: Auto-ubiquitinated.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36134.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF247565; AAF65816.1; -; mRNA.
DR EMBL; AF247789; AAL95694.1; -; mRNA.
DR EMBL; AF151048; AAF36134.1; ALT_FRAME; mRNA.
DR EMBL; AC145207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000607; AAH00607.2; -; mRNA.
DR EMBL; BC066308; AAH66308.1; -; mRNA.
DR EMBL; BC095454; AAH95454.1; -; mRNA.
DR EMBL; BC104641; AAI04642.1; -; mRNA.
DR EMBL; BC171892; AAI71892.1; -; mRNA.
DR EMBL; BC171898; AAI71898.1; -; mRNA.
DR EMBL; BC171899; AAI71899.1; -; mRNA.
DR EMBL; BC171900; AAI71900.1; -; mRNA.
DR CCDS; CCDS11789.1; -. [Q9NYG5-1]
DR CCDS; CCDS32769.1; -. [Q9NYG5-2]
DR RefSeq; NP_001002244.1; NM_001002244.2. [Q9NYG5-2]
DR RefSeq; NP_001002245.1; NM_001002245.2. [Q9NYG5-1]
DR RefSeq; NP_001002246.1; NM_001002246.2. [Q9NYG5-1]
DR RefSeq; NP_001002247.1; NM_001002247.2. [Q9NYG5-1]
DR RefSeq; NP_001002248.1; NM_001002248.2. [Q9NYG5-1]
DR RefSeq; NP_001002249.1; NM_001002249.2. [Q9NYG5-1]
DR RefSeq; NP_001276343.1; NM_001289414.1. [Q9NYG5-1]
DR RefSeq; NP_001276344.1; NM_001289415.1. [Q9NYG5-1]
DR RefSeq; NP_001276345.1; NM_001289416.1. [Q9NYG5-1]
DR RefSeq; NP_001276346.1; NM_001289417.1. [Q9NYG5-1]
DR RefSeq; NP_001276349.1; NM_001289420.1.
DR RefSeq; NP_057560.8; NM_016476.11. [Q9NYG5-1]
DR PDB; 2MT5; NMR; -; A=17-84.
DR PDB; 4R2Y; X-ray; 1.76 A; A/B/C/D=17-84.
DR PDB; 4UI9; EM; 3.60 A; B=1-84.
DR PDB; 5A31; EM; 4.30 A; B=1-84.
DR PDB; 5G04; EM; 4.00 A; B=1-84.
DR PDB; 5G05; EM; 3.40 A; B=1-84.
DR PDB; 5JG6; X-ray; 2.00 A; A/D=17-84.
DR PDB; 5KHR; EM; 6.10 A; B=1-84.
DR PDB; 5KHU; EM; 4.80 A; B=1-84.
DR PDB; 5L9T; EM; 6.40 A; B=1-84.
DR PDB; 5L9U; EM; 6.40 A; B=1-84.
DR PDB; 5LCW; EM; 4.00 A; B=1-84.
DR PDB; 6Q6G; EM; 3.20 A; C=1-84.
DR PDB; 6Q6H; EM; 3.20 A; C=1-84.
DR PDB; 6TLJ; EM; 3.80 A; B=1-84.
DR PDB; 6TM5; EM; 3.90 A; B=1-84.
DR PDB; 6TNT; EM; 3.78 A; B=1-84.
DR PDB; 7QE7; EM; 2.90 A; C=1-84.
DR PDBsum; 2MT5; -.
DR PDBsum; 4R2Y; -.
DR PDBsum; 4UI9; -.
DR PDBsum; 5A31; -.
DR PDBsum; 5G04; -.
DR PDBsum; 5G05; -.
DR PDBsum; 5JG6; -.
DR PDBsum; 5KHR; -.
DR PDBsum; 5KHU; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5L9U; -.
DR PDBsum; 5LCW; -.
DR PDBsum; 6Q6G; -.
DR PDBsum; 6Q6H; -.
DR PDBsum; 6TLJ; -.
DR PDBsum; 6TM5; -.
DR PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9NYG5; -.
DR BMRB; Q9NYG5; -.
DR SMR; Q9NYG5; -.
DR BioGRID; 119591; 73.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR DIP; DIP-52741N; -.
DR IntAct; Q9NYG5; 45.
DR iPTMnet; Q9NYG5; -.
DR PhosphoSitePlus; Q9NYG5; -.
DR BioMuta; ANAPC11; -.
DR DMDM; 19924286; -.
DR EPD; Q9NYG5; -.
DR jPOST; Q9NYG5; -.
DR MassIVE; Q9NYG5; -.
DR MaxQB; Q9NYG5; -.
DR PeptideAtlas; Q9NYG5; -.
DR PRIDE; Q9NYG5; -.
DR ProteomicsDB; 83227; -. [Q9NYG5-1]
DR ProteomicsDB; 83228; -. [Q9NYG5-2]
DR Antibodypedia; 19841; 386 antibodies from 37 providers.
DR DNASU; 51529; -.
DR Ensembl; ENST00000344877.10; ENSP00000339695.5; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000357385.7; ENSP00000349957.3; ENSG00000141552.18. [Q9NYG5-2]
DR Ensembl; ENST00000392376.7; ENSP00000376181.3; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000571024.6; ENSP00000461648.2; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000571570.5; ENSP00000458143.1; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000571874.6; ENSP00000459200.2; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000572639.5; ENSP00000460678.1; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000572851.6; ENSP00000458265.2; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000574924.6; ENSP00000460064.2; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000575195.2; ENSP00000458515.2; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000577747.5; ENSP00000463567.1; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000578550.5; ENSP00000464615.1; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000579978.5; ENSP00000463640.1; ENSG00000141552.18. [Q9NYG5-1]
DR Ensembl; ENST00000583839.1; ENSP00000463598.1; ENSG00000141552.18. [Q9NYG5-1]
DR GeneID; 51529; -.
DR KEGG; hsa:51529; -.
DR MANE-Select; ENST00000344877.10; ENSP00000339695.5; NM_001002248.3; NP_001002248.1.
DR UCSC; uc002kbv.3; human. [Q9NYG5-1]
DR CTD; 51529; -.
DR DisGeNET; 51529; -.
DR GeneCards; ANAPC11; -.
DR HGNC; HGNC:14452; ANAPC11.
DR HPA; ENSG00000141552; Low tissue specificity.
DR MIM; 614534; gene.
DR neXtProt; NX_Q9NYG5; -.
DR OpenTargets; ENSG00000141552; -.
DR PharmGKB; PA24787; -.
DR VEuPathDB; HostDB:ENSG00000141552; -.
DR GeneTree; ENSGT00550000075186; -.
DR HOGENOM; CLU_115512_0_2_1; -.
DR InParanoid; Q9NYG5; -.
DR OMA; QWRWDTG; -.
DR PhylomeDB; Q9NYG5; -.
DR TreeFam; TF354219; -.
DR PathwayCommons; Q9NYG5; -.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9NYG5; -.
DR SIGNOR; Q9NYG5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 51529; 707 hits in 1127 CRISPR screens.
DR ChiTaRS; ANAPC11; human.
DR GeneWiki; ANAPC11; -.
DR GenomeRNAi; 51529; -.
DR Pharos; Q9NYG5; Tbio.
DR PRO; PR:Q9NYG5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NYG5; protein.
DR Bgee; ENSG00000141552; Expressed in right testis and 99 other tissues.
DR ExpressionAtlas; Q9NYG5; baseline and differential.
DR Genevisible; Q9NYG5; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IDA:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IC:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:UniProtKB.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16456; RING-H2_APC11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Metal-binding; Mitosis; Nucleus; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..84
FT /note="Anaphase-promoting complex subunit 11"
FT /id="PRO_0000055747"
FT ZN_FING 34..77
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 38..84
FT /note="KVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE -> P
FT LHGESISRCLGWCPQPVPVLGGRAHPQVPINTASPTPGQHTGSLMSREESSRSPDPTPP
FT ALDQETSSLLRCTSPWCLDHSCDLFGITDQVSADGPRACRQGARRRLPAGVGPVLPLLP
FT HALHPQVAARTAGAAALPHVPPGMEVQGVRPDLALAGGAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012347"
FT MUTAGEN 23
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 26
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 34
FT /note="C->S: Slightly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 37
FT /note="C->S: Slightly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 44
FT /note="C->S: Slightly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 51
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 53
FT /note="H->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 56
FT /note="H->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 58
FT /note="H->S: Slightly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 59
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 73
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT MUTAGEN 76
FT /note="C->S: Greatly reduces autoubiquitination activity;
FT in isoform 1."
FT /evidence="ECO:0000269|PubMed:11739784"
FT STRAND 2..16
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:6Q6G"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:4R2Y"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:4R2Y"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:4R2Y"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4R2Y"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2MT5"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4R2Y"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:4R2Y"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5JG6"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4R2Y"
SQ SEQUENCE 84 AA; 9841 MW; EACBD5A54FDC11AE CRC64;
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI
LKWLHAQQVQ QHCPMCRQEW KFKE
