[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Alaska; DOI=10.1007/BF00040628; PubMed=1883993 [NCBI, ExPASy, EBI, Israel, Japan] Feiler H.S., Jacobs T.W.; "Cloning of the pea cdc2 homologue by efficient immunological screening of PCR products."; Plant Mol. Biol. 17:321-333(1991).

Comments

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
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

X56554; CAA39904.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S17451; S17451.

3D structure databases

HSSP

P24941; 1H1R. [HSSP ENTRY / PDB]

ModBase

P28567.

Ontologies

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.
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]

PROSITE

PS00107; PROTEIN_KINASE_ATP; PARTIAL.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >151`	`>151`	`Cell division control protein 2 homolog 2.`	`PRO_0000085758`
`DOMAIN`	`<1 >151`	`>151`	`Protein kinase.`
`ACT_SITE`	`113 113`		`Proton acceptor (By similarity).`
`BINDING`	`3 3`		`ATP (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`151 151`

Sequence information

Length: 151 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 17463 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: E29AFBA3E0641479 [This is a checksum on the sequence]

        10         20         30         40         50         60 
ALKEIRMDNE REGFPITAIR EIKILKKLHH ENVIKLKEIV TSPGPEKDDQ GRPDGNKYKR 

        70         80         90        100        110        120 
LAIYMVFEYM DHDLTGLADR PGMRFTVPQI KCYMRQLLTG LHYCHVNQVL HRDIKGSNLL 

       130        140        150 
IDNEGNLKLA DFGLARSFSN EIMQTLQIES L

P28567 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