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Database: UniProt
Entry: Q9H1A4
LinkDB: Q9H1A4
Original site: Q9H1A4 
ID   APC1_HUMAN              Reviewed;        1944 AA.
AC   Q9H1A4; Q2M3H8; Q9BSE6; Q9H8D0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   17-JUN-2020, entry version 173.
DE   RecName: Full=Anaphase-promoting complex subunit 1;
DE            Short=APC1;
DE   AltName: Full=Cyclosome subunit 1;
DE   AltName: Full=Mitotic checkpoint regulator;
DE   AltName: Full=Testis-specific gene 24 protein;
GN   Name=ANAPC1; Synonyms=TSG24;
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=11179667; DOI=10.1016/s0378-1119(00)00511-4;
RA   Joergensen P.M., Graeslund S., Betz R., Stahl S., Larsson C., Hoeoeg C.;
RT   "Characterisation of the human APC1, the largest subunit of the anaphase-
RT   promoting complex.";
RL   Gene 262:51-59(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Ovary;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 510-1944.
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   PHOSPHORYLATION AT SER-202; SER-286; THR-291; SER-355; SER-373; SER-377;
RP   THR-537; TYR-571 AND SER-688.
RX   PubMed=14657031; DOI=10.1093/emboj/cdg627;
RA   Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J.,
RA   Peters J.-M.;
RT   "Mitotic regulation of the human anaphase-promoting complex by
RT   phosphorylation.";
RL   EMBO J. 22:6598-6609(2003).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-377, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377; SER-547 AND SER-555, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-60; THR-291; SER-341;
RP   SER-355; SER-362 AND SER-547, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-547; SER-555 AND
RP   SER-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-291; SER-341;
RP   SER-355; SER-377; SER-547; SER-555; SER-686 AND SER-688, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-688, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291; SER-313; SER-343;
RP   SER-355; SER-362; SER-377; SER-688 AND SER-916, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
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   [17]
RP   INVOLVEMENT IN RTS1.
RX   PubMed=31303264; DOI=10.1016/j.ajhg.2019.06.011;
RA   Ajeawung N.F., Nguyen T.T.M., Lu L., Kucharski T.J., Rousseau J.,
RA   Molidperee S., Atienza J., Gamache I., Jin W., Plon S.E., Lee B.H.,
RA   Teodoro J.G., Wang L.L., Campeau P.M.;
RT   "Mutations in ANAPC1, encoding a scaffold subunit of the anaphase-promoting
RT   complex, cause Rothmund-Thomson syndrome type 1.";
RL   Am. J. Hum. Genet. 105:625-630(2019).
RN   [18]
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   [19] {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: 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. {ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744}.
CC   -!- PTM: Phosphorylated. Phosphorylation on Ser-355 occurs specifically
CC       during mitosis. {ECO:0000269|PubMed:14657031}.
CC   -!- DISEASE: Rothmund-Thomson syndrome 1 (RTS1) [MIM:618625]: An autosomal
CC       recessive disorder characterized by sparse hair, bilateral juvenile
CC       cataracts, and poikiloderma, a genodermatosis presenting with mottled
CC       pigmentation, telangiectasia and epidermal atrophy. Additional features
CC       are short stature, dystrophic and thin nails, and genital, skeletal and
CC       dental abnormalities. RTS1 is not associated with an increased risk of
CC       cancer. {ECO:0000269|PubMed:31303264}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the APC1 family. {ECO:0000305}.
DR   EMBL; AJ278357; CAC19484.1; -; mRNA.
DR   EMBL; BC005089; AAH05089.1; -; mRNA.
DR   EMBL; BC104902; AAI04903.1; -; mRNA.
DR   EMBL; BC104904; AAI04905.1; -; mRNA.
DR   EMBL; AK023807; BAB14687.1; -; mRNA.
DR   CCDS; CCDS2093.1; -.
DR   RefSeq; NP_073153.1; NM_022662.3.
DR   PDB; 4UI9; EM; 3.60 A; A=1-1944.
DR   PDB; 5A31; EM; 4.30 A; A=11-1897.
DR   PDB; 5G04; EM; 4.00 A; A=1-1943.
DR   PDB; 5G05; EM; 3.40 A; A=1-1944.
DR   PDB; 5KHR; EM; 6.10 A; A=1-1944.
DR   PDB; 5KHU; EM; 4.80 A; A=1-1944.
DR   PDB; 5L9T; EM; 6.40 A; A=1-1944.
DR   PDB; 5L9U; EM; 6.40 A; A=1-1944.
DR   PDB; 5LCW; EM; 4.00 A; A=1-1944.
DR   PDB; 5LGG; X-ray; 2.15 A; A=1-33, A=70-306, A=403-613.
DR   PDB; 6Q6G; EM; 3.20 A; A=1-306, A=397-1944.
DR   PDB; 6Q6H; EM; 3.20 A; A=1-1944.
DR   PDB; 6TLJ; EM; 3.80 A; A=1-1944.
DR   PDB; 6TM5; EM; 3.90 A; A=1-1944.
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; 5LGG; -.
DR   PDBsum; 6Q6G; -.
DR   PDBsum; 6Q6H; -.
DR   PDBsum; 6TLJ; -.
DR   PDBsum; 6TM5; -.
DR   SMR; Q9H1A4; -.
DR   BioGRID; 122229; 102.
DR   CORUM; Q9H1A4; -.
DR   DIP; DIP-32940N; -.
DR   IntAct; Q9H1A4; 62.
DR   MINT; Q9H1A4; -.
DR   STRING; 9606.ENSP00000339109; -.
DR   iPTMnet; Q9H1A4; -.
DR   PhosphoSitePlus; Q9H1A4; -.
DR   BioMuta; ANAPC1; -.
DR   DMDM; 37537845; -.
DR   EPD; Q9H1A4; -.
DR   jPOST; Q9H1A4; -.
DR   MassIVE; Q9H1A4; -.
DR   MaxQB; Q9H1A4; -.
DR   PaxDb; Q9H1A4; -.
DR   PeptideAtlas; Q9H1A4; -.
DR   PRIDE; Q9H1A4; -.
DR   ProteomicsDB; 80384; -.
DR   Antibodypedia; 18056; 513 antibodies.
DR   Ensembl; ENST00000341068; ENSP00000339109; ENSG00000153107.
DR   GeneID; 64682; -.
DR   KEGG; hsa:64682; -.
DR   UCSC; uc002thi.4; human.
DR   CTD; 64682; -.
DR   DisGeNET; 64682; -.
DR   EuPathDB; HostDB:ENSG00000153107.11; -.
DR   GeneCards; ANAPC1; -.
DR   HGNC; HGNC:19988; ANAPC1.
DR   HPA; ENSG00000153107; Low tissue specificity.
DR   MalaCards; ANAPC1; -.
DR   MIM; 608473; gene.
DR   MIM; 618625; phenotype.
DR   neXtProt; NX_Q9H1A4; -.
DR   OpenTargets; ENSG00000153107; -.
DR   Orphanet; 221008; Rothmund-Thomson syndrome type 1.
DR   PharmGKB; PA134907013; -.
DR   eggNOG; KOG1858; Eukaryota.
DR   eggNOG; ENOG410XQ83; LUCA.
DR   GeneTree; ENSGT00390000016757; -.
DR   InParanoid; Q9H1A4; -.
DR   KO; K03348; -.
DR   OMA; AIAEWMQ; -.
DR   OrthoDB; 738153at2759; -.
DR   PhylomeDB; Q9H1A4; -.
DR   TreeFam; TF105441; -.
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; Q9H1A4; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 64682; 681 hits in 780 CRISPR screens.
DR   ChiTaRS; ANAPC1; human.
DR   GeneWiki; ANAPC1; -.
DR   GenomeRNAi; 64682; -.
DR   Pharos; Q9H1A4; Tbio.
DR   PRO; PR:Q9H1A4; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9H1A4; protein.
DR   Bgee; ENSG00000153107; Expressed in kidney and 149 other tissues.
DR   ExpressionAtlas; Q9H1A4; baseline and differential.
DR   Genevisible; Q9H1A4; 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; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
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   InterPro; IPR024990; Apc1.
DR   InterPro; IPR041221; APC1_C.
DR   PANTHER; PTHR12827; PTHR12827; 1.
DR   Pfam; PF12859; ANAPC1; 1.
DR   Pfam; PF18122; APC1_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Ectodermal dysplasia;
KW   Hypotrichosis; Mitosis; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1944
FT                   /note="Anaphase-promoting complex subunit 1"
FT                   /id="PRO_0000215871"
FT   REPEAT          1297..1325
FT                   /note="PC 1"
FT   REPEAT          1366..1404
FT                   /note="PC 2"
FT   REPEAT          1467..1501
FT                   /note="PC 3"
FT   REPEAT          1520..1552
FT                   /note="PC 4"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231"
FT   MOD_RES         202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         291
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         313
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18220336,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18220336,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         537
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         547
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:18691976, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231"
FT   MOD_RES         571
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:14657031"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569,
FT                   ECO:0000269|PubMed:14657031"
FT   MOD_RES         916
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   CONFLICT        604
FT                   /note="M -> V (in Ref. 3; BAB14687)"
FT                   /evidence="ECO:0000305"
FT   STRAND          11..13
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          15..19
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   HELIX           23..27
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          72..78
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          89..96
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          99..108
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          113..118
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          125..134
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          146..154
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          159..163
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          168..171
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          177..183
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          186..191
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          209..215
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          220..222
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          224..226
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          244..250
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   TURN            251..254
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          255..260
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   TURN            261..264
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          265..273
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          406..414
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          430..434
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          436..438
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          440..446
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   HELIX           447..449
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          451..459
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          463..475
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          477..482
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   HELIX           483..485
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          487..491
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          493..495
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          497..501
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          504..510
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   HELIX           517..519
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   TURN            580..582
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          584..591
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          594..599
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          604..608
FT                   /evidence="ECO:0000244|PDB:5LGG"
FT   STRAND          614..616
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           617..628
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           631..645
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          652..654
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           656..664
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           666..668
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          672..675
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           705..711
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           714..720
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            723..726
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          751..754
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           755..758
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           759..773
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           777..779
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            780..782
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           783..796
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           800..807
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            811..813
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            823..826
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           844..851
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            852..854
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          860..862
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            864..866
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           868..880
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          894..898
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           926..937
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           944..946
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           949..964
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           972..978
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            981..984
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1021..1027
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1033..1040
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1055..1057
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1059..1077
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1080..1087
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1096..1098
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   STRAND          1108..1111
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1112..1115
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1116..1119
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1120..1122
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   TURN            1129..1132
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1134..1144
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1150..1153
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           1155..1160
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1164..1166
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1169..1180
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1181..1183
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1185..1187
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1190..1197
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1202..1216
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1222..1229
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1232..1235
FT                   /evidence="ECO:0000244|PDB:6Q6H"
FT   HELIX           1247..1260
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1261..1264
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1267..1277
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1284..1287
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           1291..1306
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1315..1319
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1321..1330
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1350..1353
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1360..1374
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1375..1377
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1381..1384
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1386..1388
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1393..1396
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1401..1414
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1416..1418
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           1423..1427
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1432..1436
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1454..1475
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1476..1478
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1482..1499
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1504..1507
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1509..1526
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1533..1543
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1547..1549
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1552..1565
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1567..1570
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1572..1574
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1578..1587
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1594..1597
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1600..1602
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1604..1613
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1614..1616
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1618..1623
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1624..1626
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1633..1638
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1642..1644
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1647..1656
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1662..1669
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1671..1673
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1676..1679
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1684..1692
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1693..1695
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1696..1699
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1708..1710
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1727..1731
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1737..1740
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1745..1753
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1765..1780
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1787..1801
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1809..1820
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1824..1828
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          1832..1834
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   STRAND          1836..1840
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           1845..1862
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1865..1873
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1882..1892
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            1897..1899
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1912..1920
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1925..1930
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           1933..1935
FT                   /evidence="ECO:0000244|PDB:6Q6G"
SQ   SEQUENCE   1944 AA;  216500 MW;  E08B1FE3FC28917E CRC64;
     MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS
     LQEVTIHEKQ KESWQLRKGV SEIGEDVDYD EELYVAGNMV IWSKGSKSQA LAVYKAFTVD
     SPVQQALWCD FIISQDKSEK AYSSNEVEKC ICILQSSCIN MHSIEGKDYI ASLPFQVANV
     WPTKYGLLFE RSASSHEVPP GSPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV
     DHAMKIVFLN TDPSIVMTYD AVQNVHSVWT LRRVKSEEEN VVLKFSEQGG TPQNVATSSS
     LTAHLRSLSK GDSPVTSPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL SRAHSPALGV
     HSFSGVQRFN ISSHNQSPKR HSISHSPNSN SNGSFLAPET EPIVPELCID HLWTETITNI
     REKNSQASKV FITSDLCGQK FLCFLVESQL QLRCVKFQES NDKTQLIFGS VTNIPAKDAA
     PVEKIDTMLV LEGSGNLVLY TGVVRVGKVF IPGLPAPSLT MSNTMPRPST PLDGVSTPKP
     LSKLLGSLDE VVLLSPVPEL RDSSKLHDSL YNEDCTFQQL GTYIHSIRDP VHNRVTLELS
     NGSMVRITIP EIATSELVQT CLQAIKFILP KEIAVQMLVK WYNVHSAPGG PSYHSEWNLF
     VTCLMNMMGY NTDRLAWTRN FDFEGSLSPV IAPKKARPSE TGSDDDWEYL LNSDYHQNVE
     SHLLNRSLCL SPSEASQMKD EDFSQNLSLD SSTLLFTHIP AIFFVLHLVY EELKLNTLMG
     EGICSLVELL VQLARDLKLG PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE
     PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVSD ESSQYLTRIT
     IAPQKLQVEQ EENRFSFRHS TSVSSLAERL VVWMTNVGFT LRDLETLPFG IALPIRDAIY
     HCREQPASDW PEAVCLLIGR QDLSKQACEG NLPKGKSVLS SDVPSGTETE EEDDGMNDMN
     HEVMSLIWSE DLRVQDVRRL LQSAHPVRVN VVQYPELSDH EFIEEKENRL LQLCQRTMAL
     PVGRGMFTLF SYHPVPTEPL PIPKLNLTGR APPRNTTVDL NSGNIDVPPN MTSWASFHNG
     VAAGLKIAPA SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG
     HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HIPALLPPTS TELDVPHNVQ VAAVVGIGLV
     YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL ALGMVCLGHG SNLIGMSDLN
     VPEQLYQYMV GGHRRFQTGM HREKHKSPSY QIKEGDTINV DVTCPGATLA LAMIYLKTNN
     RSIADWLRAP DTMYLLDFVK PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS
     LSEIELPCSE DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFNCLHK FAKDFMTYLS
     APNASVTGPH NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM NYGFHLAHHM
     ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR YHLQALRHLY VLAAEPRLLV
     PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL
     SKGTQHLKSI LSKDGVLYVK LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISA
     FTSDPALLSF AEYFCKPTVN MGQKQEILDL FSSVLYECVT QETPEMLPAY IAMDQAIRRL
     GRREMSETSE LWQIKLVLEF FSSRSHQERL QNHPKRGLFM NSEFLPVVKC TIDNTLDQWL
     QVGGDMCVHA YLSGQPLEES QLSMLACFLV YHSVPAPQHL PPIGLEGSTS FAELLFKFKQ
     LKMPVRALLR LAPLLLGNPQ PMVM
//
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