[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2014258 [NCBI, ExPASy, EBI, Israel, Japan] Colasanti J., Tyers M., Sundaresan V.; "Isolation and characterization of cDNA clones encoding a functional p34cdc2 homologue from Zea mays."; Proc. Natl. Acad. Sci. U.S.A. 88:3377-3381(1991).

Comments

FUNCTION: Plays a key role in the control of the eukaryotic cell cycle. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II.
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 (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

M60526; AAA33479.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40444; A40444.
B40444; B40444.

RefSeq

NP_001105342.1; -.

UniGene

Zm.95674

3D structure databases

HSSP

P24941; 1H06. [HSSP ENTRY / PDB]

ModBase

P23111.

Organism-specific databases

Gramene

P23111; -.

MaizeGDB

60686; -.

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: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

P23111.

Genome annotation databases

GeneID

542270; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 294`	`294`	`Cell division control protein 2 homolog.`	`PRO_0000085752`
`DOMAIN`	`4 287`	`284`	`Protein kinase.`
`NP_BIND`	`10 18`	`9`	`ATP (By similarity).`
`ACT_SITE`	`127 127`		`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 (By similarity).`

Sequence information

Length: 294 AA [This is the length of the unprocessed precursor]

Molecular weight: 33834 Da [This is the MW of the unprocessed precursor]

CRC64: 5063ECFCC2D5FFDD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEQYEKVEKI GEGTYGVVYK ALDKATNETI ALKKIRLEQE DEGVPSTAIR EISLLKEMNH 

        70         80         90        100        110        120 
GNIVRLHDVV HSEKRIYLVF EYLDLDLKKF MDSCPEFAKN PTLIKSYLYQ ILHGVAYCHS 

       130        140        150        160        170        180 
HRVLHRDLKP QNLLIDRRTN ALKLADFGLA RAFGIPVRTF THEVVTLWYR APEILLGARQ 

       190        200        210        220        230        240 
YSTPVDVWSV GCIFAEMVNQ KPLFPGDSEI DELFKIFRIL GTPNEQSWPG VSCLPDFKTA 

       250        260        270        280        290 
FPRWQAQDLA TVVPNLDPAG LDLLSKMLRY EPSKRITARQ ALEHEYFKDL EVVQ

P23111 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