NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0166-6851(98)00104-2; PubMed=9803415 [NCBI, ExPASy, EBI, Israel, Japan]
Vinkenoog R., Speranca M.A., Ramesar J., Thomas A.W., del Portillo H.A., Janse C.J., Waters A.P.;
"Characterisation of the Cdc2-related kinase 2 gene from Plasmodium knowlesi and P. berghei.";
Mol. Biochem. Parasitol. 95:229-240(1998).

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-158 activates it (By similarity).
SUBUNIT: Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (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

AJ224155; CAA11852.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q07785; 1OB3. [HSSP ENTRY / PDB]

SMR

O96821; 1-286.

ModBase

O96821.

Ontologies

GO:0005737;	Cellular component: cytoplasm (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:0008353;	Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
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).

Other

ProtoNet

O96821.

UniRef

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

Keywords

ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 288`	`288`	`Cell division control protein 2 homolog.`	`PRO_0000232670`
`DOMAIN`	`4 284`	`281`	`Protein kinase.`
`NP_BIND`	`10 18`	`9`	`ATP (By similarity).`
`ACT_SITE`	`125 125`		`Proton acceptor (By similarity).`
`BINDING`	`32 32`		`ATP (By similarity).`
`MOD_RES`	`14 14`		`Phosphothreonine (By similarity).`
`MOD_RES`	`15 15`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`158 158`		`Phosphothreonine; by CAK (By similarity).`

Sequence information

Length: 288 AA [This is the length of the unprocessed precursor]

Molecular weight: 32946 Da [This is the MW of the unprocessed precursor]

CRC64: 02B0F83D5187AC68 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKYHGLEKI GEGTYGVVYK AQNNYGETFA LKKIRLEKED EGIPSTAIRE ISILKELKHS 

        70         80         90        100        110        120 
NIVKLYDVIH TKKRLILVFE HLDQDLKKLL DVCDGGLESV TAKSFLLQLL SGIAYCHEHR 

       130        140        150        160        170        180 
VLHRDLKPQN LLINREGELK IADFGLARAF GIPVRKYTHE VVTLWYRAPD ILMGSKKYST 

       190        200        210        220        230        240 
PIDIWSVGCI FAEMVNGRPL FPGVSETDQL MRIFRILGTP NSANWPSVTE LPKYDPDFIV 

       250        260        270        280 
YEPLPWETFL KGLDDTGIDL LSKMLRLDPN QRITAKEALQ HAYFKESS

O96821 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