[1]	NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, AND SUBUNIT. TISSUE=Oocyte; PubMed=1377775 [NCBI, ExPASy, EBI, Israel, Japan] Pickham K.M., Meyer A.N., Li J., Donoghue D.J.; "Requirement of mosXe protein kinase for meiotic maturation of Xenopus oocytes induced by a cdc2 mutant lacking regulatory phosphorylation sites."; Mol. Cell. Biol. 12:3192-3203(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Tadpole; NIH - Xenopus Gene Collection (XGC) project; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]	PHOSPHORYLATION AT THR-161. PubMed=8344251 [NCBI, ExPASy, EBI, Israel, Japan] Fesquet D., Labbe J.-C., Derancourt J., Capony J.-P., Galas S., Girard F., Lorca T., Shuttleworth J., Doree M., Cavadore J.-C.; "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."; EMBO J. 12:3111-3121(1993).
[4]	INTERACTION WITH SPDYA. PubMed=10465793 [NCBI, ExPASy, EBI, Israel, Japan] Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R.; "A novel p34cdc2 binding and activating protein that is necessary and sufficient to trigger G2/M progression in Xenopus oocytes."; Genes Dev. 13:2177-2189(1999).
[5]	INTERACTION WITH SPDYA. PubMed=15611625 [NCBI, ExPASy, EBI, Israel, Japan] Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.; "Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins."; Cell Cycle 4:155-165(2005).

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.
CATALYTIC ACTIVITY: 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: Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with spdya.
SUBCELLULAR LOCATION: Nucleus (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
SIMILARITY: Contains 1 protein kinase domain.

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

M60681; AAA63562.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054146; AAH54146.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B44349; B44349.

NP_001080093.1; -.

3D structure databases

HSSP

P24941; 1P2A. [HSSP ENTRY / PDB]

ModBase

P24033.

Ontologies

GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693;	Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008353;	Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007067;	Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
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).

ProtoNet

P24033.

Genome annotation databases

GeneID

379785; -.

KEGG

xla:379785; -.

Phylogenomic databases

HOVERGEN

P24033; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 302`	`302`	`Cell division control protein 2-B.`	`PRO_0000085736`
`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 (By similarity).`
`MOD_RES`	`15 15`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`161 161`		`Phosphothreonine; by CAK.`
`MOD_RES`	`277 277`		`Phosphoserine (By similarity).`
`CONFLICT`	`87 87`		`L -> V (in Ref. 1; AAA63562).`
`CONFLICT`	`123 123`		`R -> G (in Ref. 1; AAA63562).`
`CONFLICT`	`172 172`		`S -> P (in Ref. 1; AAA63562).`

Sequence information

Length: 302 AA [This is the length of the unprocessed precursor]

Molecular weight: 34532 Da [This is the MW of the unprocessed precursor]

CRC64: FA9DC156392D7CBC [This is a checksum on the sequence]

        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 PQNLLIDNKG VIKLADFGLA RAFGIPVRVY THEVVTLWYR ASEVLLGSVR 

       190        200        210        220        230        240 
YSTPVDVWSV GTIFAEIATK KPLFHGDSEI DQLFRIFRSL GTPNNEVWPE VESLQDYKNT 

       250        260        270        280        290        300 
FPKWKGGSLS SNVKNIDEDG LDLLSKMLVY DPAKRISARK AMLHPYFDDL DKSSLPANQI 


RN

P24033 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools