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Database: UniProt
Entry: Q9UM13
LinkDB: Q9UM13
Original site: Q9UM13 
ID   APC10_HUMAN             Reviewed;         185 AA.
AC   Q9UM13; D3DNZ7; Q2V500; Q9UG51; Q9Y5R0;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   17-JUN-2020, entry version 170.
DE   RecName: Full=Anaphase-promoting complex subunit 10;
DE            Short=APC10;
DE   AltName: Full=Cyclosome subunit 10;
GN   Name=ANAPC10; Synonyms=APC10;
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].
RX   PubMed=10318877; DOI=10.1074/jbc.274.20.14500;
RA   Grossberger R., Gieffers C., Zachariae W., Podtelejnikov A.V.,
RA   Schleiffer A., Nasmyth K., Mann M., Peters J.-M.;
RT   "Characterization of the DOC1/APC10 subunit of the yeast and the human
RT   anaphase-promoting complex.";
RL   J. Biol. Chem. 274:14500-14507(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10498862; DOI=10.1038/sj.onc.1203133;
RA   Kurasawa Y., Todokoro K.;
RT   "Identification of human APC10/Doc1 as a subunit of anaphase promoting
RT   complex.";
RL   Oncogene 18:5131-5137(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-46.
RG   NIEHS SNPs program;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [7]
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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND INTERACTION WITH CDC27.
RX   PubMed=11524682; DOI=10.1038/nsb0901-784;
RA   Wendt K.S., Vodermaier H.C., Jacob U., Gieffers C., Gmachl M.,
RA   Peters J.-M., Huber R., Sondermann P.;
RT   "Crystal structure of the APC10/DOC1 subunit of the human anaphase-
RT   promoting complex.";
RL   Nat. Struct. Biol. 8:784-788(2001).
RN   [11]
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   [12]
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   [13] {ECO:0000244|PDB:4UI9, ECO:0000244|PDB:5A31}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 2-185 OF APC/C, AND
RP   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: 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.
CC       {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:25043029). The C-terminus of APC10
CC       binds to CDC27/APC3 (PubMed:11524682). Interacts with PIWIL1;
CC       interaction only takes place when PIWIL1 binds piRNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q8K2H6, ECO:0000269|PubMed:11524682,
CC       ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744}.
CC   -!- SIMILARITY: Belongs to the APC10 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/anapc10/";
DR   EMBL; AF132794; AAD30527.1; -; mRNA.
DR   EMBL; AB012109; BAA86953.1; -; mRNA.
DR   EMBL; AL080090; CAB45705.1; -; mRNA.
DR   EMBL; DQ304649; ABB96248.1; -; Genomic_DNA.
DR   EMBL; CH471056; EAX05050.1; -; Genomic_DNA.
DR   EMBL; CH471056; EAX05051.1; -; Genomic_DNA.
DR   EMBL; BC005217; AAH05217.1; -; mRNA.
DR   CCDS; CCDS43273.1; -.
DR   PIR; T12476; T12476.
DR   RefSeq; NP_001243635.1; NM_001256706.1.
DR   RefSeq; NP_001243636.1; NM_001256707.1.
DR   RefSeq; NP_001243637.1; NM_001256708.1.
DR   RefSeq; NP_001243638.1; NM_001256709.1.
DR   RefSeq; NP_001243639.1; NM_001256710.1.
DR   RefSeq; NP_001305296.1; NM_001318367.1.
DR   RefSeq; NP_055700.2; NM_014885.4.
DR   RefSeq; XP_011529826.1; XM_011531524.2.
DR   PDB; 1JHJ; X-ray; 1.60 A; A=2-172.
DR   PDB; 4UI9; EM; 3.60 A; L=2-185.
DR   PDB; 5A31; EM; 4.30 A; L=1-185.
DR   PDB; 5G04; EM; 4.00 A; L=1-185.
DR   PDB; 5G05; EM; 3.40 A; L=1-185.
DR   PDB; 5KHR; EM; 6.10 A; L=1-185.
DR   PDB; 5KHU; EM; 4.80 A; L=1-185.
DR   PDB; 5L9T; EM; 6.40 A; L=1-185.
DR   PDB; 5L9U; EM; 6.40 A; L=1-185.
DR   PDB; 5LCW; EM; 4.00 A; L=1-185.
DR   PDB; 6Q6G; EM; 3.20 A; L=1-185.
DR   PDB; 6Q6H; EM; 3.20 A; L=1-185.
DR   PDB; 6TLJ; EM; 3.80 A; L=1-185.
DR   PDB; 6TM5; EM; 3.90 A; L=1-185.
DR   PDBsum; 1JHJ; -.
DR   PDBsum; 4UI9; -.
DR   PDBsum; 5A31; -.
DR   PDBsum; 5G04; -.
DR   PDBsum; 5G05; -.
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; Q9UM13; -.
DR   BioGRID; 115665; 57.
DR   CORUM; Q9UM13; -.
DR   DIP; DIP-39885N; -.
DR   ELM; Q9UM13; -.
DR   IntAct; Q9UM13; 35.
DR   MINT; Q9UM13; -.
DR   STRING; 9606.ENSP00000478501; -.
DR   iPTMnet; Q9UM13; -.
DR   PhosphoSitePlus; Q9UM13; -.
DR   BioMuta; ANAPC10; -.
DR   DMDM; 34395509; -.
DR   EPD; Q9UM13; -.
DR   jPOST; Q9UM13; -.
DR   MassIVE; Q9UM13; -.
DR   MaxQB; Q9UM13; -.
DR   PaxDb; Q9UM13; -.
DR   PeptideAtlas; Q9UM13; -.
DR   PRIDE; Q9UM13; -.
DR   ProteomicsDB; 85170; -.
DR   Antibodypedia; 7474; 218 antibodies.
DR   DNASU; 10393; -.
DR   Ensembl; ENST00000309439; ENSP00000310071; ENSG00000164162.
DR   Ensembl; ENST00000451299; ENSP00000403891; ENSG00000164162.
DR   Ensembl; ENST00000507656; ENSP00000423995; ENSG00000164162.
DR   Ensembl; ENST00000613466; ENSP00000478501; ENSG00000164162.
DR   GeneID; 10393; -.
DR   KEGG; hsa:10393; -.
DR   UCSC; uc003iju.6; human.
DR   CTD; 10393; -.
DR   DisGeNET; 10393; -.
DR   EuPathDB; HostDB:ENSG00000164162.12; -.
DR   GeneCards; ANAPC10; -.
DR   HGNC; HGNC:24077; ANAPC10.
DR   HPA; ENSG00000164162; Low tissue specificity.
DR   MIM; 613745; gene.
DR   neXtProt; NX_Q9UM13; -.
DR   OpenTargets; ENSG00000164162; -.
DR   PharmGKB; PA134938672; -.
DR   eggNOG; KOG3437; Eukaryota.
DR   eggNOG; COG5156; LUCA.
DR   GeneTree; ENSGT00390000013722; -.
DR   InParanoid; Q9UM13; -.
DR   KO; K03357; -.
DR   OMA; FGFGPEC; -.
DR   OrthoDB; 804390at2759; -.
DR   PhylomeDB; Q9UM13; -.
DR   TreeFam; TF105446; -.
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   SignaLink; Q9UM13; -.
DR   SIGNOR; Q9UM13; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 10393; 583 hits in 791 CRISPR screens.
DR   ChiTaRS; ANAPC10; human.
DR   EvolutionaryTrace; Q9UM13; -.
DR   GeneWiki; ANAPC10; -.
DR   GenomeRNAi; 10393; -.
DR   Pharos; Q9UM13; Tbio.
DR   PRO; PR:Q9UM13; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9UM13; protein.
DR   Bgee; ENSG00000164162; Expressed in oocyte and 220 other tissues.
DR   ExpressionAtlas; Q9UM13; baseline and differential.
DR   Genevisible; Q9UM13; HS.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked 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; TAS:Reactome.
DR   CDD; cd08366; APC10; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   InterPro; IPR016901; APC10/Doc1.
DR   InterPro; IPR004939; APC_su10/DOC_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12936; PTHR12936; 1.
DR   Pfam; PF03256; ANAPC10; 1.
DR   PIRSF; PIRSF028841; APC10_sub; 1.
DR   SMART; SM01337; APC10; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   PROSITE; PS51284; DOC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Mitosis;
KW   Polymorphism; Reference proteome; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   CHAIN           2..185
FT                   /note="Anaphase-promoting complex subunit 10"
FT                   /id="PRO_0000174011"
FT   DOMAIN          2..185
FT                   /note="DOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00614"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   MOD_RES         169
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K2H6"
FT   VARIANT         46
FT                   /note="R -> Q (in dbSNP:rs35257136)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_025200"
FT   CONFLICT        6
FT                   /note="K -> R (in Ref. 1; AAD30527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="T -> S (in Ref. 3; CAB45705)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="Q -> L (in Ref. 3; CAB45705)"
FT                   /evidence="ECO:0000305"
FT   HELIX           13..18
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          21..24
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           26..28
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          29..34
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           43..46
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          58..74
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          76..82
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           83..86
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           87..89
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          90..101
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           102..104
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          106..112
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          117..123
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          129..144
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   HELIX           145..147
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          155..161
FT                   /evidence="ECO:0000244|PDB:1JHJ"
FT   STRAND          166..170
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           176..179
FT                   /evidence="ECO:0000244|PDB:6Q6G"
SQ   SEQUENCE   185 AA;  21252 MW;  ACA7F245B3861FF5 CRC64;
     MTTPNKTPPG ADPKQLERTG TVREIGSQAV WSLSSCKPGF GVDQLRDDNL ETYWQSDGSQ
     PHLVNIQFRR KTTVKTLCIY ADYKSDESYT PSKISVRVGN NFHNLQEIRQ LELVEPSGWI
     HVPLTDNHKK PTRTFMIQIA VLANHQNGRD THMRQIKIYT PVEESSIGKF PRCTTIDFMM
     YRSIR
//
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