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UniProtKB/Swiss-Prot entry P30260


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDC27_HUMAN
Primary accession number P30260
Secondary accession numbers Q16349 Q96F35
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 94)
Name and origin of the protein
Protein name Cell division cycle protein 27 homolog
Synonyms CDC27Hs
H-NUC
Gene name
Name: CDC27
Synonyms: D0S1430E, D17S978E
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8234252 [NCBI, ExPASy, EBI, Israel, Japan]
Tugendreich S., Boguski M.S., Seldin M., Hieter P.A.;
"Linking yeast genetics to mammalian genomes: identification and mapping of the human homolog of CDC27 via the expressed sequence tag (EST) data base.";
Proc. Natl. Acad. Sci. U.S.A. 90:10031-10035(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7756179 [NCBI, ExPASy, EBI, Israel, Japan]
Chen P.L., Ueng Y.C., Durfee T., Chen K.C., Yang-Feng T., Lee W.H.;
"Identification of a human homologue of yeast nuc2 which interacts with the retinoblastoma protein in a specific manner.";
Cell Growth Differ. 6:199-210(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION AT THR-205; THR-209; THR-244; SER-291; THR-313; SER-426; THR-430; SER-435 AND THR-446.
DOI=10.1093/emboj/cdg627; PubMed=14657031 [NCBI, ExPASy, EBI, Israel, Japan]
Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.;
"Mitotic regulation of the human anaphase-promoting complex by phosphorylation.";
EMBO J. 22:6598-6609(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-339; SER-426; SER-435; SER-438 AND THR-446, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
ELECTRON MICROSCOPY OF THE APC/C.
DOI=10.1016/j.molcel.2005.11.008; PubMed=16364912 [NCBI, ExPASy, EBI, Israel, Japan]
Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.;
"Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C.";
Mol. Cell 20:867-879(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-438, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[9]
VARIANT [LARGE SCALE ANALYSIS] ALA-270.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U00001; AAA60471.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S78234; AAB34378.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY518321; AAR89911.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011656; AAH11656.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I52835; I52835.
RefSeq NP_001107563.1; -.
NP_001247.3; -.
UniGene Hs.463295
3D structure databases
ModBase P30260.
Protein-protein interaction databases
IntAct P30260; -.
PTM databases
PhosphoSite P30260; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
Polymorphism databases
NIEHS-SNPs CDC27.
Organism-specific databases
H-InvDB HIX0013917; -.
HGNC HGNC:1728; CDC27.
GenAtlas CDC27.
HPA CAB004357; -.
CAB016315; -.
MIM 116946; gene. [NCBI / EBI]
PharmGKB PA142672185; -.
GeneCards P30260.
Gene expression databases
ArrayExpress P30260; -.
CleanEx HS_CDC27; -.
GermOnline ENSG00000004897; Homo sapiens.
Ontologies
GO
GO:0005813; Cellular component: centrosome (inferred from direct assay from MGI).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005876; Cellular component: spindle microtubule (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007091; Biological process: mitotic metaphase/anaphase transition (inferred from mutant phenotype from MGI).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR001440; TPR-1.
IPR011990; TPR-like_helical.
IPR013026; TPR_region.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF00515; TPR_1; 6.
Pfam graphical view of domain structure.
SMART SM00028; TPR; 8.
SMART graphical view of domain structure.
PROSITE PS50005; TPR; 8.
PS50293; TPR_REGION; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30260.
ProtoNet P30260.
Genome annotation databases
Ensembl ENSG00000004897; Homo sapiens. [Contig view]
GeneID 996; -.
KEGG hsa:996; -.
Phylogenomic databases
HOGENOM P30260; -.
HOVERGEN P30260; -.
Other
NextBio 4184; -.
SOURCE CDC27; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Nucleus; Phosphoprotein; Polymorphism; Repeat; TPR repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   824  824     Cell division cycle protein 27 homolog. PRO_0000106273
REPEAT   84   114  31     TPR 1. 
REPEAT   115   148  34     TPR 2. 
REPEAT   499   532  34     TPR 3. 
REPEAT   567   600  34     TPR 4. 
REPEAT   602   634  33     TPR 5. 
REPEAT   635   668  34     TPR 6. 
REPEAT   670   702  33     TPR 7. 
REPEAT   704   736  33     TPR 8. 
REPEAT   737   770  34     TPR 9. 
MOD_RES   205   205        Phosphothreonine. 
MOD_RES   209   209        Phosphothreonine. 
MOD_RES   244   244        Phosphothreonine. 
MOD_RES   291   291        Phosphoserine. 
MOD_RES   313   313        Phosphothreonine. 
MOD_RES   339   339        Phosphoserine. 
MOD_RES   426   426        Phosphoserine. 
MOD_RES   430   430        Phosphothreonine. 
MOD_RES   435   435        Phosphoserine. 
MOD_RES   438   438        Phosphoserine. 
MOD_RES   446   446        Phosphothreonine. 
VARIANT   270   270  1     G -> A (in a breast cancer sample; somatic mutation). VAR_035861 
VARIANT   496   496  1     Y -> H (in dbSNP:rs13666 [NCBI]). VAR_014489 
CONFLICT   319   319        K -> KTFRVLQ (in Ref. 4; AAH11656). 
CONFLICT   403   403        K -> E (in Ref. 4; AAH11656). 
CONFLICT   460   460        Missing (in Ref. 1; AAA60471). 
CONFLICT   715   715        A -> R (in Ref. 1; AAA60471). 
Sequence information
Length: 824 AA [This is the length of the unprocessed precursor] Molecular weight: 91867 Da [This is the MW of the unprocessed precursor] CRC64: E6C8F59C1EF1DCBA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL 

        70         80         90        100        110        120 
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDIVTEF GDSACFTLSL 

       130        140        150        160        170        180 
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKF TSLQNFSNCL 

       190        200        210        220        230        240 
PNSCTTQVPN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI 

       250        260        270        280        290        300 
SPDTVPLGTG TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN 

       310        320        330        340        350        360 
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ SSGPQTSTTP 

       370        380        390        400        410        420 
QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF PPKIPNRKTK SKTNKGGITQ 

       430        440        450        460        470        480 
PNINDSLEIT KLDSSIISEG KISTITPQIQ AFNLQKAAAE GLMSLLREMG KGYLALCSYN 

       490        500        510        520        530        540 
CKEAINILSH LPSHHYNTGW VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS 

       550        560        570        580        590        600 
TTLWHLQKDV ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY 

       610        620        630        640        650        660 
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK FSLAEMHFQK 

       670        680        690        700        710        720 
ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP KNPLCKFHRA SVLFANEKYK 

       730        740        750        760        770        780 
SALQELEELK QIVPKESLVY FLIGKVYKKL GQTHLALMNF SWAMDLDPKG ANNQIKEAID 

       790        800        810        820 
KRYLPDDEEP ITQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF 

P30260 in FASTA format

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