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Database: UniProt
Entry: P30260
LinkDB: P30260
Original site: P30260 
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   17-JUN-2020, entry version 211.
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   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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20] {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).
RN   [21]
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.
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/";
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   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   SMR; P30260; -.
DR   BioGRID; 107431; 164.
DR   CORUM; P30260; -.
DR   DIP; DIP-36422N; -.
DR   ELM; P30260; -.
DR   IntAct; P30260; 89.
DR   MINT; P30260; -.
DR   STRING; 9606.ENSP00000434614; -.
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; 475 antibodies.
DR   DNASU; 996; -.
DR   Ensembl; ENST00000066544; ENSP00000066544; ENSG00000004897. [P30260-1]
DR   Ensembl; ENST00000531206; ENSP00000434614; ENSG00000004897. [P30260-2]
DR   GeneID; 996; -.
DR   KEGG; hsa:996; -.
DR   UCSC; uc002ild.5; human. [P30260-1]
DR   CTD; 996; -.
DR   DisGeNET; 996; -.
DR   EuPathDB; HostDB:ENSG00000004897.11; -.
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   eggNOG; KOG1126; Eukaryota.
DR   eggNOG; COG0457; LUCA.
DR   GeneTree; ENSGT00950000182950; -.
DR   InParanoid; P30260; -.
DR   KO; K03350; -.
DR   OMA; PSFGIMP; -.
DR   OrthoDB; 280620at2759; -.
DR   PhylomeDB; P30260; -.
DR   TreeFam; TF101058; -.
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; P30260; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 996; 729 hits in 792 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 liver and 226 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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR   GO; GO:0061630; F:ubiquitin protein ligase 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; 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:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   DisProt; DP01445; -.
DR   Gene3D; 1.25.40.10; -; 4.
DR   IDEAL; IID00447; -.
DR   InterPro; IPR013026; TPR-contain_dom.
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; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; TPR repeat; 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   MOD_RES         205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
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:0000244|PubMed:18669648"
FT   MOD_RES         366
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         379
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         426
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
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:0000244|PubMed:18669648"
FT   MOD_RES         446
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163, ECO:0000269|PubMed:14657031"
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:rs13666)"
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:0000244|PDB:6Q6G"
FT   HELIX           21..34
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           38..50
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           54..62
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           69..81
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           85..93
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          96..98
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           103..110
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           111..113
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           114..127
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           131..144
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           149..157
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           164..167
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           452..477
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           481..488
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           493..496
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           499..511
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           515..528
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   TURN            529..531
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           536..545
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           549..562
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           567..579
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           583..596
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           601..613
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           617..630
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           635..647
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           651..664
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           669..681
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           685..698
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          699..701
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           703..715
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           719..730
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   STRAND          733..735
FT                   /evidence="ECO:0000244|PDB:5G05"
FT   HELIX           737..749
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           753..766
FT                   /evidence="ECO:0000244|PDB:6Q6G"
FT   HELIX           772..779
FT                   /evidence="ECO:0000244|PDB:6Q6G"
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
//
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