P35567 (CDK1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclin-dependent kinase 1-A
Short name=CDK1-A
EC=2.7.11.22
EC=2.7.11.23

Alternative name(s):
Cell division control protein 2 homolog 1
Cell division control protein 2-A
Cell division protein kinase 1-A
p34 protein kinase 1

Gene names

Name:	cdk1-a
Synonyms:	cdc2-a, cdc2x1.1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II By similarity.
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. Ref.1
Subunit structure	Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with spdya. Ref.1 Ref.6 Ref.7
Subcellular location	Nucleus By similarity.
Post-translational modification	Phosphorylation at Tyr-15 by wee1 and wee2 inhibits the protein kinase activity and acts negative regulator of entry into mitosis (G2 to M transition).
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 302	302	Cyclin-dependent kinase 1-A		PRO_0000085735
Regions
	Domain	4 – 287	284	Protein kinase
	Nucleotide binding	10 – 18	9	ATP By similarity
Sites
	Active site	128	1	Proton acceptor By similarity
	Binding site	33	1	ATP By similarity
Amino acid modifications
	Modified residue	14	1	Phosphothreonine By similarity
	Modified residue	15	1	Phosphotyrosine; by wee1 and wee2 Ref.4 Ref.5
	Modified residue	161	1	Phosphothreonine; by CAK Ref.3
	Modified residue	277	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P35567 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 90D2113216DF31DA	FASTA	302	34,506
	10 20 30 40 50 60 MDEYTKIEKI GEGTYGVVYK GRHKATGQVV AMKKIRLENE EEGVPSTAIR EISLLKELQH 70 80 90 100 110 120 PNIVCLLDVL MQDSRLYLIF EFLSMDLKKY LDSIPSGQYI DTMLVKSYLY QILQGIVFCH 130 140 150 160 170 180 SRRVLHRDLK PQNLLIDSKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR APEVLLGSVR 190 200 210 220 230 240 YSTPVDVWSI GTIFAEIATK KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNS 250 260 270 280 290 300 FPKWKGGSLS ANVKNIDKDG LDLLAKMLIY DPAKRISARK ALLHPYFDDL DKSSLPDNQI RN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Requirement of mosXe protein kinase for meiotic maturation of Xenopus oocytes induced by a cdc2 mutant lacking regulatory phosphorylation sites." Pickham K.M., Meyer A.N., Li J., Donoghue D.J. Mol. Cell. Biol. 12:3192-3203(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBUNIT. Tissue: Oocyte.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[3]	"The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues." Fesquet D., Labbe J.-C., Derancourt J., Capony J.-P., Galas S., Girard F., Lorca T., Shuttleworth J., Doree M., Cavadore J.-C. EMBO J. 12:3111-3121(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-161.
[4]	"Cell cycle regulation of a Xenopus Wee1-like kinase." Mueller P.R., Coleman T.R., Dunphy W.G. Mol. Biol. Cell 6:119-134(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-15.
[5]	"Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos." Murakami M.S., Vande Woude G.F. Development 125:237-248(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-15.
[6]	"A novel p34cdc2 binding and activating protein that is necessary and sufficient to trigger G2/M progression in Xenopus oocytes." Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R. Genes Dev. 13:2177-2189(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPDYA.
[7]	"Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins." Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J. Cell Cycle 4:155-165(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPDYA.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60680 mRNA. Translation: AAA63561.1. BC045078 mRNA. Translation: AAH45078.1.
PIR	A44349.
RefSeq	NP_001080554.1. NM_001087085.1.
UniGene	Xl.8917.
3D structure databases
ProteinModelPortal	P35567.
SMR	P35567. Positions 1-292.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-102773.
Proteomic databases
PRIDE	P35567.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380246.
KEGG	xla:380246.
Organism-specific databases
CTD	380246.
Xenbase	XB-GENE-482754. cdk1.
Phylogenomic databases
HOVERGEN	HBG014652.
KO	K02087.
Enzyme and pathway databases
BRENDA	2.7.11.22. 6726.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDK1A_XENLA

Accession

Primary (citable) accession number: P35567
Secondary accession number(s): Q5D0B3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program