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P23437 (CDK2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 2

EC=2.7.11.22
Alternative name(s):
CDC2 homolog Eg1 protein kinase
Cell division protein kinase 2
Gene names
Name:cdk2
Synonyms:eg1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the control of the cell cycle. Interacts with cyclins A, B, D, or E. Activity of CDK2 is maximal during S phase and G2. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it By similarity. Activated by spdya. Ref.4

Subunit structure

Interacts with spdya. Ref.4

Developmental stage

Synthesized in unfertilized egg, but no longer made in the early embryo. Ref.1

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Cyclin-dependent kinase 2
PRO_0000085774

Regions

Domain4 – 286283Protein kinase
Nucleotide binding10 – 189ATP By similarity
Nucleotide binding81 – 833ATP By similarity
Nucleotide binding129 – 1324ATP By similarity

Sites

Active site1271Proton acceptor By similarity
Binding site331ATP By similarity
Binding site861ATP By similarity
Binding site1451ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine By similarity
Modified residue1601Phosphothreonine; by CAK Ref.3

Experimental info

Sequence conflict931G → R in CAA32443. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23437 [UniParc].

Last modified May 2, 2006. Version 3.
Checksum: 173ED4E4C12DA397

FASTA29733,870
        10         20         30         40         50         60 
MENFQKVEKI GEGTYGVVYK ARNRETGEIV ALKKIRLDTE TEGVPSTAIR EISLLKELNH 

        70         80         90        100        110        120 
PNIVKLLDVI HTENKLYLVF EFLNQDLKKF MDGSNISGIS LALVKSYLFQ LLQGLAFCHS 

       130        140        150        160        170        180 
HRVLHRDLKP QNLLINSDGA IKLADFGLAR AFGVPVRTFT HEVVTLWYRA PEILLGCKFY 

       190        200        210        220        230        240 
STAVDIWSLG CIFAEMITRR ALFPGDSEID QLFRIFRTLG TPDEVSWPGV TTMPDYKSTF 

       250        260        270        280        290 
PKWIRQDFSK VVPPLDEDGR DLLAQMLQYD SNKRISAKVA LTHPFFRDVS RPTPHLI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning by differential screening of a Xenopus cDNA coding for a protein highly homologous to cdc2."
Paris J., le Guellec R., Couturier A., le Guellec K., Omilli F., Camonis J., Macneill S., Philippe M.
Proc. Natl. Acad. Sci. U.S.A. 88:1039-1043(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
Tissue: Ovary.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Oocyte.
[3]"The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2."
Poon R.Y.C., Yamashita K., Adamczewski J.P., Hunt T., Shuttleworth J.
EMBO J. 12:3123-3132(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-160.
[4]"Speedy: a novel cell cycle regulator of the G2/M transition."
Lenormand J.-L., Dellinger R.W., Knudsen K.E., Subramani S., Donoghue D.J.
EMBO J. 18:1869-1877(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPDYA, ENZYME REGULATION.
Tissue: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14227 mRNA. Translation: CAA32443.1.
BC106636 mRNA. Translation: AAI06637.1.
PIRA37871.
RefSeqNP_001084120.1. NM_001090651.1.
UniGeneXl.4227.

3D structure databases

ProteinModelPortalP23437.
SMRP23437. Positions 1-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid100639. 5 interactions.

Proteomic databases

PRIDEP23437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399314.
KEGGxla:399314.

Organism-specific databases

CTD1017.
XenbaseXB-GENE-1001995. cdk2.

Phylogenomic databases

HOVERGENHBG014652.
KOK02206.

Enzyme and pathway databases

BRENDA2.7.11.22. 6726.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDK2_XENLA
AccessionPrimary (citable) accession number: P23437
Secondary accession number(s): Q3KPN7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: May 2, 2006
Last modified: June 11, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families