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UniProtKB/Swiss-Prot entry P06493


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

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Entry information
Entry name CDC2_HUMAN
Primary accession number P06493
Secondary accession number O60764
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 124)
Name and origin of the protein
Protein name Cell division control protein 2 homolog
Synonyms EC 2.7.11.22
EC 2.7.11.23
p34 protein kinase
Cyclin-dependent kinase 1
CDK1
Gene name
Name: CDC2
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] (ISOFORM 1).
DOI=10.1038/327031a0; PubMed=3553962 [NCBI, ExPASy, EBI, Israel, Japan]
Lee M.G., Nurse P.;
"Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2.";
Nature 327:31-35(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Mammary cancer;
PubMed=9515786 [NCBI, ExPASy, EBI, Israel, Japan]
Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S., Xiong Y.;
"T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21.";
Cancer Res. 58:1095-1098(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Rieder M.J., Livingston R.J., Braun A.C., Montoya M.A., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[6]
PHOSPHORYLATION, AND ASSOCIATION WITH P13.
DOI=10.1016/0092-8674(88)90175-4; PubMed=3289755 [NCBI, ExPASy, EBI, Israel, Japan]
Draetta G., Beach D.;
"Activation of cdc2 protein kinase during mitosis in human cells: cell cycle-dependent phosphorylation and subunit rearrangement.";
Cell 54:17-26(1988).
[7]
INTERACTION WITH RALBP1.
DOI=10.1074/jbc.M302191200; PubMed=12775724 [NCBI, ExPASy, EBI, Israel, Japan]
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.;
"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis.";
J. Biol. Chem. 278:30597-30604(2003).
[8]
INTERACTION WITH DLGAP5.
DOI=10.1074/jbc.M404950200; PubMed=15145941 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.;
"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region.";
J. Biol. Chem. 279:32592-32602(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND MASS SPECTROMETRY.
DOI=10.1021/pr050048h; PubMed=16083285 [NCBI, ExPASy, EBI, Israel, Japan]
Kim J.-E., Tannenbaum S.R., White F.M.;
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
J. Proteome Res. 4:1339-1346(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.";
Electrophoresis 28:2027-2034(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND TYR-19, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-160 AND THR-161, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
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
X05360; CAA28963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00272; CAA68376.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D88357; BAA26001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF512554; AAM34793.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007004; AAP35650.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014563; AAH14563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29539; A29539.
RefSeq NP_001777.1; -.
UniGene Hs.334562
3D structure databases
PDB
1LC9; Model; -; A=1-297.[ExPASy / RCSB / EBI]
PDBsum 1LC9; -.
ModBase P06493.
Protein-protein interaction databases
DIP DIP:35N; -.
IntAct P06493; -.
PTM databases
PhosphoSite P06493; -.
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.
Polymorphism databases
NIEHS-SNPs CDC2.
2D gel databases
SWISS-2DPAGE P06493; -.
Organism-specific databases
H-InvDB HIX0008851; -.
HGNC HGNC:1722; CDC2.
GenAtlas CDC2.
HPA CAB003799; -.
HPA003387; -.
MIM 116940; gene. [NCBI / EBI]
PharmGKB PA99; -.
GeneCards P06493.
Gene expression databases
ArrayExpress P06493; -.
CleanEx HS_CDC2; -.
GermOnline ENSG00000170312; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0030496; Cellular component: midbody (inferred from direct assay from UniProtKB).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0005876; Cellular component: spindle microtubule (inferred from direct assay from UniProtKB).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0006916; Biological process: anti-apoptosis (inferred from direct assay from UniProtKB).
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 IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P06493.
ProtoNet P06493.
Genome annotation databases
Ensembl ENSG00000170312; Homo sapiens. [Contig view]
GeneID 983; -.
KEGG hsa:983; -.
Phylogenomic databases
HOVERGEN P06493; -.
Other
BindingDB P06493; -.
NextBio 4122; -.
SOURCE CDC2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   297  297     Cell division control protein 2 homolog. PRO_0000085724
DOMAIN   4   287  284     Protein kinase. 
NP_BIND   10    18  9     ATP (By similarity). 
ACT_SITE   128   128        Proton acceptor (By similarity). 
BINDING   33    33        ATP (By similarity). 
MOD_RES   14    14        Phosphothreonine. 
MOD_RES   15    15        Phosphotyrosine. 
MOD_RES   19    19        Phosphotyrosine. 
MOD_RES   160   160        Phosphotyrosine. 
MOD_RES   161   161        Phosphothreonine. 
VAR_SEQ   107   163        Missing (in isoform 2). VSP_021375
STRAND   4    12  9      
STRAND   14    23  10      
TURN   24    26  3      
STRAND   29    36  8      
STRAND   39    42  4      
HELIX   46    57  12      
STRAND   66    71  6      
STRAND   73    81  9      
STRAND   84    86  3      
HELIX   87    93  7      
STRAND   94    96  3      
HELIX   102   121  20      
STRAND   133   136  4      
STRAND   142   144  3      
HELIX   167   169  3      
HELIX   172   176  5      
HELIX   184   199  16      
HELIX   209   220  12      
TURN   225   227  3      
STRAND   234   236  3      
HELIX   249   252  4      
TURN   253   255  3      
HELIX   258   267  10      
TURN   272   274  3      
HELIX   278   283  6      
HELIX   285   287  3      
Sequence information
Length: 297 AA [This is the length of the unprocessed precursor] Molecular weight: 34095 Da [This is the MW of the unprocessed precursor] CRC64: 942D79448EFE490A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR EISLLKELRH 

        70         80         90        100        110        120 
PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM DSSLVKSYLY QILQGIVFCH 

       130        140        150        160        170        180 
SRRVLHRDLK PQNLLIDDKG TIKLADFGLA RAFGIPIRVY THEVVTLWYR SPEVLLGSAR 

       190        200        210        220        230        240 
YSTPVDIWSI GTIFAELATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT 

       250        260        270        280        290 
FPKWKPGSLA SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM 

P06493 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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