Cell division control protein 2-A - Xenopus laevis (African clawed frog)

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Reviewed, UniProtKB/Swiss-Prot P35567 (CDC2A_XENLA)

Last modified January 19, 2010. Version 73. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cell division control protein 2-A
    EC=2.7.11.22
    EC=2.7.11.23
Alternative name(s):
    Cell division control protein 2 homolog 1
    p34 protein kinase 1

Gene names

Name:	cdc2-A
Synonyms:	cdc2x1.1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length	302 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.4 Ref.5
Subcellular location	Nucleus By 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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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 protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
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 kinase activity Inferred from electronic annotation. Source: EC protein binding Ref.4 Ref.5 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 302

302

Cell division control protein 2-A

PRO_0000085735

Regions

Domain

4 – 287

284

Protein kinase

Nucleotide binding

10 – 18

ATP By similarity

Sites

Active site

128

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

161

Phosphothreonine; by CAK Ref.3

Modified residue

277

Phosphoserine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P35567-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 90D2113216DF31DA
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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

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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: 1377775] [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: 8344251] [Abstract] Cited for: PHOSPHORYLATION AT THR-161.
[4]	"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: 10465793] [Abstract] Cited for: INTERACTION WITH SPDYA.
[5]	"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: 15611625] [Abstract] Cited for: INTERACTION WITH SPDYA.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	M60680 mRNA. Translation: AAA63561.1. BC045078 mRNA. Translation: AAH45078.1.
PIR	A44349.
RefSeq	NP_001080554.1.
UniGene	Xl.8917
3D structure databases
SMR	P35567. Positions 1-292.
ModBase	Search...
Genome annotation databases
GeneID	380246.
KEGG	xla:380246.
Organism-specific databases
CTD	380246.
Xenbase	XB-FEAT-482749. cdc2.
Phylogenomic databases
HOVERGEN	P35567.
Enzyme and pathway databases
BRENDA	2.7.11.22. 648. 2.7.11.23. 648.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

CDC2A_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:	January 19, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents