APC10_HUMAN
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 03-AUG-2022, entry version 180.
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:0007744|PDB:4UI9, ECO:0007744|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/";
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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 PDB; 6TNT; EM; 3.78 A; L=1-185.
DR PDB; 7QE7; EM; 2.90 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 PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9UM13; -.
DR SMR; Q9UM13; -.
DR BioGRID; 115665; 69.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
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; 238 antibodies from 31 providers.
DR DNASU; 10393; -.
DR Ensembl; ENST00000309439.9; ENSP00000310071.5; ENSG00000164162.14.
DR Ensembl; ENST00000451299.6; ENSP00000403891.2; ENSG00000164162.14.
DR Ensembl; ENST00000507656.6; ENSP00000423995.1; ENSG00000164162.14.
DR Ensembl; ENST00000613466.4; ENSP00000478501.1; ENSG00000164162.14.
DR GeneID; 10393; -.
DR KEGG; hsa:10393; -.
DR MANE-Select; ENST00000507656.6; ENSP00000423995.1; NM_001256706.2; NP_001243635.1.
DR UCSC; uc003iju.6; human.
DR CTD; 10393; -.
DR DisGeNET; 10393; -.
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 VEuPathDB; HostDB:ENSG00000164162; -.
DR eggNOG; KOG3437; Eukaryota.
DR GeneTree; ENSGT00390000013722; -.
DR InParanoid; Q9UM13; -.
DR OMA; HTISIQF; -.
DR OrthoDB; 804390at2759; -.
DR PhylomeDB; Q9UM13; -.
DR TreeFam; TF105446; -.
DR PathwayCommons; Q9UM13; -.
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; Q9UM13; -.
DR SIGNOR; Q9UM13; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10393; 629 hits in 1088 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 196 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; IC:ComplexPortal.
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:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR CDD; cd08366; APC10; 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 Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|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:0007744|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:0007829|PDB:1JHJ"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1JHJ"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 58..74
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1JHJ"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1JHJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1JHJ"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 129..144
FT /evidence="ECO:0007829|PDB:1JHJ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:1JHJ"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:7QE7"
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
