APC1_HUMAN
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 03-AUG-2022, entry version 183.
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:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX PubMed=26083744; DOI=10.1038/nature14471;
RA Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT "Atomic structure of the APC/C and its mechanism of protein
RT ubiquitination.";
RL Nature 522:450-454(2015).
CC -!- FUNCTION: 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 variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the APC1 family. {ECO:0000305}.
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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 PDB; 6TNT; EM; 3.78 A; A=1-1944.
DR PDB; 7QE7; EM; 2.90 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 PDBsum; 6TNT; -.
DR PDBsum; 7QE7; -.
DR AlphaFoldDB; Q9H1A4; -.
DR SMR; Q9H1A4; -.
DR BioGRID; 122229; 164.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; Q9H1A4; -.
DR DIP; DIP-32940N; -.
DR IntAct; Q9H1A4; 67.
DR MINT; Q9H1A4; -.
DR STRING; 9606.ENSP00000339109; -.
DR GlyGen; Q9H1A4; 1 site, 1 O-linked glycan (1 site).
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; 554 antibodies from 36 providers.
DR DNASU; 64682; -.
DR Ensembl; ENST00000341068.8; ENSP00000339109.3; ENSG00000153107.13.
DR GeneID; 64682; -.
DR KEGG; hsa:64682; -.
DR MANE-Select; ENST00000341068.8; ENSP00000339109.3; NM_022662.4; NP_073153.1.
DR UCSC; uc002thi.4; human.
DR CTD; 64682; -.
DR DisGeNET; 64682; -.
DR GeneCards; ANAPC1; -.
DR GeneReviews; 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 VEuPathDB; HostDB:ENSG00000153107; -.
DR eggNOG; KOG1858; Eukaryota.
DR GeneTree; ENSGT00390000016757; -.
DR InParanoid; Q9H1A4; -.
DR OMA; MQPPDSR; -.
DR OrthoDB; 738153at2759; -.
DR PhylomeDB; Q9H1A4; -.
DR TreeFam; TF105441; -.
DR PathwayCommons; Q9H1A4; -.
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; Q9H1A4; -.
DR SIGNOR; Q9H1A4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 64682; 719 hits in 1046 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 colonic epithelium and 134 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:0060090; F:molecular adaptor activity; IBA:GO_Central.
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:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR024990; Apc1.
DR InterPro; IPR041221; APC1_C.
DR InterPro; IPR011989; ARM-like.
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 REGION 305..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|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:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|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:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 547
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|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:0007744|PubMed:20068231"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 604
FT /note="M -> V (in Ref. 3; BAB14687)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:5LGG"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:5LGG"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 265..273
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 451..459
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 463..475
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5G05"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:5LGG"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:5G05"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:5LGG"
FT STRAND 604..608
FT /evidence="ECO:0007829|PDB:5LGG"
FT HELIX 616..628
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 631..645
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 656..666
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 672..674
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 751..755
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 756..758
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 759..773
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 778..781
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 782..796
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 800..809
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 811..813
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 825..827
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 828..830
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 844..852
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 860..862
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 868..880
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 886..889
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 926..937
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 941..944
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 949..964
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 972..978
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 981..983
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1021..1027
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1033..1041
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1055..1057
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 1059..1077
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1080..1087
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1096..1098
FT /evidence="ECO:0007829|PDB:6Q6H"
FT STRAND 1109..1111
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1112..1115
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1116..1118
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1121..1123
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1129..1132
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1133..1145
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1150..1153
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 1155..1160
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1166..1168
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1169..1182
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1183..1187
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1190..1198
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1202..1216
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1217..1219
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1222..1229
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1233..1235
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1247..1260
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1261..1263
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1267..1277
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1284..1287
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 1291..1306
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1317..1320
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1321..1330
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1343..1345
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1350..1353
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1360..1374
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1375..1377
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1381..1385
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1386..1388
FT /evidence="ECO:0007829|PDB:6Q6G"
FT TURN 1393..1395
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1396..1398
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1401..1414
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1416..1418
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1423..1427
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1432..1443
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1454..1475
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1476..1479
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1482..1499
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1504..1507
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1509..1526
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1533..1544
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1547..1549
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 1552..1565
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1567..1569
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1572..1574
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1578..1587
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1594..1597
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 1600..1602
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1604..1612
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1614..1616
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1618..1623
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1624..1626
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1633..1638
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1642..1644
FT /evidence="ECO:0007829|PDB:6Q6G"
FT STRAND 1647..1656
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1660..1662
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1665..1673
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1676..1679
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1685..1692
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1693..1695
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1696..1699
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1708..1710
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1726..1732
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1735..1738
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1739..1741
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1745..1753
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1762..1764
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1765..1780
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1784..1786
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1787..1801
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1809..1821
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1825..1829
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1830..1832
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 1836..1840
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 1844..1862
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1864..1873
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1879..1881
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1882..1891
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1897..1899
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1905..1907
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1911..1919
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 1920..1922
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 1925..1935
FT /evidence="ECO:0007829|PDB:7QE7"
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
