GenomeNet

Database: UniProt
Entry: Q9NYG5
LinkDB: Q9NYG5
Original site: Q9NYG5 
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   17-JUN-2020, entry version 184.
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:0000244|PDB:4UI9, ECO:0000244|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       Q9NYG5-2; 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};
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   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   SMR; Q9NYG5; -.
DR   BioGRID; 119591; 37.
DR   DIP; DIP-52741N; -.
DR   IntAct; Q9NYG5; 43.
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; 359 antibodies.
DR   Ensembl; ENST00000344877; ENSP00000339695; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000357385; ENSP00000349957; ENSG00000141552. [Q9NYG5-2]
DR   Ensembl; ENST00000392376; ENSP00000376181; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000571024; ENSP00000461648; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000571570; ENSP00000458143; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000571874; ENSP00000459200; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000572639; ENSP00000460678; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000572851; ENSP00000458265; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000574924; ENSP00000460064; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000575195; ENSP00000458515; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000577747; ENSP00000463567; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000578550; ENSP00000464615; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000579978; ENSP00000463640; ENSG00000141552. [Q9NYG5-1]
DR   Ensembl; ENST00000583839; ENSP00000463598; ENSG00000141552. [Q9NYG5-1]
DR   GeneID; 51529; -.
DR   KEGG; hsa:51529; -.
DR   UCSC; uc002kbv.3; human. [Q9NYG5-1]
DR   CTD; 51529; -.
DR   DisGeNET; 51529; -.
DR   EuPathDB; HostDB:ENSG00000141552.17; -.
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   GeneTree; ENSGT00940000164946; -.
DR   HOGENOM; CLU_115512_0_2_1; -.
DR   InParanoid; Q9NYG5; -.
DR   KO; K03358; -.
DR   OMA; PINMASP; -.
DR   PhylomeDB; Q9NYG5; -.
DR   TreeFam; TF354219; -.
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-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; Q9NYG5; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 51529; 656 hits in 791 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 testis and 91 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR024991; 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   METAL           23
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           26
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           34
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000250"
FT   METAL           37
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000250"
FT   METAL           44
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000250"
FT   METAL           51
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           53
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           56
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           58
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000250"
FT   METAL           59
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           73
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           76
FT                   /note="Zinc 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          3..9
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          19..22
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            24..26
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   STRAND          29..32
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           35..37
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   TURN            38..41
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   STRAND          46..49
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   STRAND          50..52
FT                   /evidence="ECO:0000244|PDB:2MT5"
FT   STRAND          54..56
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   HELIX           57..67
FT                   /evidence="ECO:0000244|PDB:4R2Y"
FT   STRAND          68..70
FT                   /evidence="ECO:0000244|PDB:5JG6"
FT   STRAND          76..79
FT                   /evidence="ECO:0000244|PDB:4R2Y"
SQ   SEQUENCE   84 AA;  9841 MW;  EACBD5A54FDC11AE CRC64;
     MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI
     LKWLHAQQVQ QHCPMCRQEW KFKE
//
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