CDC27_HUMAN
ID CDC27_HUMAN Reviewed; 824 AA.
AC P30260; G3V1C4; Q16349; Q96F35;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Cell division cycle protein 27 homolog;
DE AltName: Full=Anaphase-promoting complex subunit 3;
DE Short=APC3;
DE AltName: Full=CDC27 homolog;
DE Short=CDC27Hs;
DE AltName: Full=H-NUC;
GN Name=CDC27; Synonyms=ANAPC3, D0S1430E, D17S978E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8234252; DOI=10.1073/pnas.90.21.10031;
RA Tugendreich S., Boguski M.S., Seldin M., Hieter P.A.;
RT "Linking yeast genetics to mammalian genomes: identification and mapping of
RT the human homolog of CDC27 via the expressed sequence tag (EST) data
RT base.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10031-10035(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7756179;
RA Chen P.L., Ueng Y.C., Durfee T., Chen K.C., Yang-Feng T., Lee W.H.;
RT "Identification of a human homologue of yeast nuc2 which interacts with the
RT retinoblastoma protein in a specific manner.";
RL Cell Growth Differ. 6:199-210(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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] (ISOFORM 2).
RC TISSUE=Uterus;
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 PHOSPHORYLATION AT THR-205; THR-209; THR-244; SER-291; THR-313; SER-426;
RP THR-430; SER-435 AND THR-446.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426;
RP SER-438 AND THR-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
RP TPR REPEATS.
RX PubMed=21307936; DOI=10.1038/nature09756;
RA Schreiber A., Stengel F., Zhang Z., Enchev R.I., Kong E.H., Morris E.P.,
RA Robinson C.V., da Fonseca P.C., Barford D.;
RT "Structural basis for the subunit assembly of the anaphase-promoting
RT complex.";
RL Nature 470:227-232(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-379; SER-426 AND
RP THR-446, AND IDENTIFICATION BY MASS 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 [18]
RP STRUCTURE BY 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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 821-824 IN COMPLEX WITH MCPH1,
RP PHOSPHORYLATION AT SER-821, AND MUTAGENESIS OF SER-821.
RX PubMed=22139841; DOI=10.1074/jbc.m111.307868;
RA Singh N., Wiltshire T.D., Thompson J.R., Mer G., Couch F.J.;
RT "Molecular basis for the association of microcephalin (MCPH1) protein with
RT the cell division cycle protein 27 (Cdc27) subunit of the anaphase-
RT promoting complex.";
RL J. Biol. Chem. 287:2854-2862(2012).
RN [20]
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 [21] {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).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-270.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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: Homodimer. The mammalian APC/C is composed at least of 14
CC distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5,
CC CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13,
CC ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa; APC/C interacts with
CC FZR1 and FBXO5 (PubMed:26083744, PubMed:25043029). Interacts with RB.
CC Interacts with FAM168B/MANI (By similarity). Interacts with MCPH1
CC (PubMed:22139841). {ECO:0000250, ECO:0000250|UniProtKB:A2A6Q5,
CC ECO:0000269|PubMed:22139841, ECO:0000269|PubMed:25043029,
CC ECO:0000269|PubMed:26083744}.
CC -!- INTERACTION:
CC P30260; Q9UJX5: ANAPC4; NbExp=8; IntAct=EBI-994813, EBI-2554854;
CC P30260; P24385: CCND1; NbExp=3; IntAct=EBI-994813, EBI-375001;
CC P30260; Q12834: CDC20; NbExp=12; IntAct=EBI-994813, EBI-367462;
CC P30260; P12830: CDH1; NbExp=2; IntAct=EBI-994813, EBI-727477;
CC P30260; P21964-2: COMT; NbExp=3; IntAct=EBI-994813, EBI-10200977;
CC P30260; Q9UKT4: FBXO5; NbExp=2; IntAct=EBI-994813, EBI-852298;
CC P30260; O43524: FOXO3; NbExp=2; IntAct=EBI-994813, EBI-1644164;
CC P30260; Q9UM11: FZR1; NbExp=12; IntAct=EBI-994813, EBI-724997;
CC P30260; Q13257: MAD2L1; NbExp=8; IntAct=EBI-994813, EBI-78203;
CC P30260; Q9UI95: MAD2L2; NbExp=2; IntAct=EBI-994813, EBI-77889;
CC P30260; P16333: NCK1; NbExp=3; IntAct=EBI-994813, EBI-389883;
CC P30260; P51955: NEK2; NbExp=2; IntAct=EBI-994813, EBI-633182;
CC P30260; P60484: PTEN; NbExp=7; IntAct=EBI-994813, EBI-696162;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30260-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30260-2; Sequence=VSP_047225;
CC -!- PTM: Phosphorylated. Phosphorylation on Ser-426 and Thr-446 occurs
CC specifically during mitosis. {ECO:0000269|PubMed:14657031,
CC ECO:0000269|PubMed:22139841}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc27/";
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DR EMBL; U00001; AAA60471.1; -; mRNA.
DR EMBL; S78234; AAB34378.1; -; mRNA.
DR EMBL; AY518321; AAR89911.1; -; Genomic_DNA.
DR EMBL; AC002558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471231; EAW57687.1; -; Genomic_DNA.
DR EMBL; BC011656; AAH11656.1; -; mRNA.
DR CCDS; CCDS11509.1; -. [P30260-1]
DR CCDS; CCDS45720.1; -. [P30260-2]
DR PIR; I52835; I52835.
DR RefSeq; NP_001107563.1; NM_001114091.2. [P30260-2]
DR RefSeq; NP_001247.3; NM_001256.4. [P30260-1]
DR PDB; 3T1N; X-ray; 2.60 A; C/D=821-824.
DR PDB; 4RG6; X-ray; 3.30 A; A/B=1-824.
DR PDB; 4RG7; X-ray; 4.25 A; A/B=1-824.
DR PDB; 4RG9; X-ray; 3.25 A; A/B=1-824.
DR PDB; 4UI9; EM; 3.60 A; F/H=1-824.
DR PDB; 5A31; EM; 4.30 A; F/H=1-824.
DR PDB; 5G04; EM; 4.00 A; F/H=1-824.
DR PDB; 5G05; EM; 3.40 A; F/H=1-824.
DR PDB; 5KHR; EM; 6.10 A; F/H=1-824.
DR PDB; 5KHU; EM; 4.80 A; F/H=1-824.
DR PDB; 5L9T; EM; 6.40 A; F/H=1-824.
DR PDB; 5L9U; EM; 6.40 A; F/H=1-824.
DR PDB; 5LCW; EM; 4.00 A; F/H=1-824.
DR PDB; 6Q6G; EM; 3.20 A; J/P=1-824.
DR PDB; 6Q6H; EM; 3.20 A; J/P=1-824.
DR PDB; 6TLJ; EM; 3.80 A; F/H=1-824.
DR PDB; 6TM5; EM; 3.90 A; F/H=1-824.
DR PDB; 6TNT; EM; 3.78 A; F/H=1-824.
DR PDB; 7QE7; EM; 2.90 A; J/P=1-824.
DR PDBsum; 3T1N; -.
DR PDBsum; 4RG6; -.
DR PDBsum; 4RG7; -.
DR PDBsum; 4RG9; -.
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; P30260; -.
DR SMR; P30260; -.
DR BioGRID; 107431; 227.
DR ComplexPortal; CPX-1860; Anaphase-Promoting core complex.
DR CORUM; P30260; -.
DR DIP; DIP-36422N; -.
DR ELM; P30260; -.
DR IntAct; P30260; 91.
DR MINT; P30260; -.
DR STRING; 9606.ENSP00000434614; -.
DR GlyGen; P30260; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30260; -.
DR PhosphoSitePlus; P30260; -.
DR SwissPalm; P30260; -.
DR BioMuta; CDC27; -.
DR DMDM; 12644198; -.
DR EPD; P30260; -.
DR jPOST; P30260; -.
DR MassIVE; P30260; -.
DR MaxQB; P30260; -.
DR PaxDb; P30260; -.
DR PeptideAtlas; P30260; -.
DR PRIDE; P30260; -.
DR ProteomicsDB; 32326; -.
DR ProteomicsDB; 54645; -. [P30260-1]
DR Antibodypedia; 3817; 514 antibodies from 42 providers.
DR DNASU; 996; -.
DR Ensembl; ENST00000066544.8; ENSP00000066544.3; ENSG00000004897.12. [P30260-1]
DR Ensembl; ENST00000531206.5; ENSP00000434614.1; ENSG00000004897.12. [P30260-2]
DR GeneID; 996; -.
DR KEGG; hsa:996; -.
DR MANE-Select; ENST00000066544.8; ENSP00000066544.3; NM_001256.6; NP_001247.3.
DR UCSC; uc002ild.5; human. [P30260-1]
DR CTD; 996; -.
DR DisGeNET; 996; -.
DR GeneCards; CDC27; -.
DR HGNC; HGNC:1728; CDC27.
DR HPA; ENSG00000004897; Low tissue specificity.
DR MIM; 116946; gene.
DR neXtProt; NX_P30260; -.
DR OpenTargets; ENSG00000004897; -.
DR PharmGKB; PA26261; -.
DR VEuPathDB; HostDB:ENSG00000004897; -.
DR eggNOG; KOG1126; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR InParanoid; P30260; -.
DR OMA; ADKRHYN; -.
DR OrthoDB; 280620at2759; -.
DR PhylomeDB; P30260; -.
DR TreeFam; TF101058; -.
DR PathwayCommons; P30260; -.
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; P30260; -.
DR SIGNOR; P30260; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 996; 773 hits in 1078 CRISPR screens.
DR ChiTaRS; CDC27; human.
DR GeneWiki; CDC27; -.
DR GenomeRNAi; 996; -.
DR Pharos; P30260; Tbio.
DR PRO; PR:P30260; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P30260; protein.
DR Bgee; ENSG00000004897; Expressed in secondary oocyte and 200 other tissues.
DR ExpressionAtlas; P30260; baseline and differential.
DR Genevisible; P30260; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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 DisProt; DP01445; -.
DR Gene3D; 1.25.40.10; -; 4.
DR IDEAL; IID00447; -.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 2.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..824
FT /note="Cell division cycle protein 27 homolog"
FT /id="PRO_0000106273"
FT REPEAT 6..35
FT /note="TPR 1"
FT REPEAT 38..65
FT /note="TPR 2"
FT REPEAT 67..99
FT /note="TPR 3"
FT REPEAT 115..145
FT /note="TPR 4"
FT REPEAT 465..495
FT /note="TPR 5"
FT REPEAT 499..528
FT /note="TPR 6"
FT REPEAT 533..563
FT /note="TPR 7"
FT REPEAT 567..598
FT /note="TPR 8"
FT REPEAT 601..631
FT /note="TPR 9"
FT REPEAT 635..667
FT /note="TPR 10"
FT REPEAT 670..702
FT /note="TPR 11"
FT REPEAT 704..734
FT /note="TPR 12"
FT REPEAT 737..768
FT /note="TPR 13"
FT REGION 287..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14657031"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:14657031,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22139841"
FT VAR_SEQ 319
FT /note="K -> KTFRVLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047225"
FT VARIANT 270
FT /note="G -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035861"
FT VARIANT 496
FT /note="Y -> H (in dbSNP:rs202052665)"
FT /id="VAR_014489"
FT MUTAGEN 821
FT /note="S->A: Abolishes binding to MCPH1."
FT /evidence="ECO:0000269|PubMed:22139841"
FT CONFLICT 403
FT /note="K -> E (in Ref. 6; AAH11656)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="Missing (in Ref. 1; AAA60471)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="A -> R (in Ref. 1; AAA60471)"
FT /evidence="ECO:0000305"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 447..477
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 515..528
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 549..562
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 567..579
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 583..596
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 601..612
FT /evidence="ECO:0007829|PDB:7QE7"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 617..630
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 635..647
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 651..664
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 669..681
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 685..698
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6Q6G"
FT HELIX 703..715
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 719..732
FT /evidence="ECO:0007829|PDB:7QE7"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:5G05"
FT HELIX 737..749
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 753..765
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:7QE7"
FT HELIX 773..778
FT /evidence="ECO:0007829|PDB:7QE7"
SQ SEQUENCE 824 AA; 91867 MW; E6C8F59C1EF1DCBA CRC64;
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDIVTEF GDSACFTLSL
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKF TSLQNFSNCL
PNSCTTQVPN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI
SPDTVPLGTG TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ SSGPQTSTTP
QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF PPKIPNRKTK SKTNKGGITQ
PNINDSLEIT KLDSSIISEG KISTITPQIQ AFNLQKAAAE GLMSLLREMG KGYLALCSYN
CKEAINILSH LPSHHYNTGW VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS
TTLWHLQKDV ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK FSLAEMHFQK
ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP KNPLCKFHRA SVLFANEKYK
SALQELEELK QIVPKESLVY FLIGKVYKKL GQTHLALMNF SWAMDLDPKG ANNQIKEAID
KRYLPDDEEP ITQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF
