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Reviewed, UniProtKB/Swiss-Prot P06493 (CDC2_HUMAN)

Last modified July 22, 2008. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Cell division control protein 2 homolog
    EC=2.7.11.22
    EC=2.7.11.23
Alternative name(s):
    p34 protein kinase
    Cyclin-dependent kinase 1
      Short name(s)=CDK1
Gene names
Name: CDC2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. p34 is a component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulation

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with DLGAP5. Isoform 2 is unable to complex with cyclin B1 and also fails to bind to the CDK inhibitor p21. Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase.

Subcellular location

NucleusBy similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06493-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P06493-2)

Also known as: CDC2deltaT;

The sequence of this isoform differs from the canonical sequence as follows:
     107-163: Missing.
Notes: Found in breast cancer tissues.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 297297Cell division control protein 2 homolog

Regions

Domain4 – 287284Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Binding site331ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine
Modified residue151Phosphotyrosine
Modified residue191Phosphotyrosine
Modified residue1601Phosphotyrosine
Modified residue1611Phosphothreonine

Natural variations

Alternative sequence107 – 16357Missing in isoform 2.

Secondary structure

1 ................................................. 297
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 942D79448EFE490A

FASTA29734,095
        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

« Hide

Isoform 2 (CDC2deltaT) [UniParc].

Checksum: 50FC3D192024E38C
Show »

24027,503

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References

« Hide 'large scale' references
[1]"Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2."
Lee M.G., Nurse P.
Nature 327:31-35(1987) [PubMed: 3553962] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21."
Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S., Xiong Y.
Cancer Res. 58:1095-1098(1998) [PubMed: 9515786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Mammary cancer.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
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.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[6]"Activation of cdc2 protein kinase during mitosis in human cells: cell cycle-dependent phosphorylation and subunit rearrangement."
Draetta G., Beach D.
Cell 54:17-26(1988) [PubMed: 3289755] [Abstract]
Cited for: PHOSPHORYLATION, ASSOCIATION WITH P13.
[7]"RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis."
Rosse C., L'Hoste S., Offner N., Picard A., Camonis J.
J. Biol. Chem. 278:30597-30604(2003) [PubMed: 12775724] [Abstract]
Cited for: INTERACTION WITH RALBP1.
[8]"Fbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich region."
Hsu J.-M., Lee Y.-C.G., Yu C.-T.R., Huang C.-Y.F.
J. Biol. Chem. 279:32592-32602(2004) [PubMed: 15145941] [Abstract]
Cited for: INTERACTION WITH DLGAP5.
[9]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, MASS SPECTROMETRY.
[10]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-19, MASS SPECTROMETRY.
[12]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND TYR-15, MASS SPECTROMETRY.
[14]"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."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; TYR-15 AND TYR-19, MASS SPECTROMETRY.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-160 AND THR-161, MASS SPECTROMETRY.

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Cross-references

Sequence databases

X05360 mRNA. Translation: CAA28963.1.
Y00272 mRNA. Translation: CAA68376.1.
D88357 mRNA. Translation: BAA26001.1.
AF512554 Genomic DNA. Translation: AAM34793.1.
BT007004 mRNA. Translation: AAP35650.1.
BC014563 mRNA. Translation: AAH14563.1.
PIRA29539.
RefSeqNP_001777.1.
NP_203698.1.
UniGeneHs.334562

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LC9model-A1-297[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:35N.
IntActP06493.

PTM databases

PhosphoSiteP06493.

Polymorphism databases

NIEHS-SNPsSearch...

2-D gel databases

SWISS-2DPAGEP06493.

Genome annotation databases

EnsemblENSG00000170312. Homo sapiens. [Contig view]
GeneID983.
KEGGhsa:983.

Organism-specific databases

H-InvDBHIX0008851.
HGNCHGNC:1722. CDC2.
HPACAB003799.
HPA003387.
MIM116940. gene.
PharmGKBPA99.
GenAtlasSearch...
GeneCardsSearch...
GeneLynxSearch...

Phylogenomic databases

HOVERGENP06493.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.

Gene expression databases

ArrayExpressP06493.
CleanExHS_CDC2.
GermOnlineENSG00000170312. Homo sapiens.

Family and domain databases

InterProIPR000719. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

BindingDBP06493.
SOURCE