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Q26671 (CDC2H_THEAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division control protein 2 homolog

EC=2.7.11.22
EC=2.7.11.23
Gene names
Name:CRK2
ORF Names:TA06730
OrganismTheileria annulata [Reference proteome]
Taxonomic identifier5874 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaPiroplasmidaTheileriidaeTheileria

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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-158 activates it By similarity.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Cell division control protein 2 homolog
PRO_0000232673

Regions

Domain4 – 284281Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1251Proton acceptor By similarity
Binding site321ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine By similarity
Modified residue1581Phosphothreonine; by CAK By similarity

Sequences

Sequence LengthMass (Da)Tools
Q26671 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A4F8526448B4F727

FASTA29834,231
        10         20         30         40         50         60 
MRRYHKMEKI GEGTYGVVYK AQNNHGEICA LKKIRVEEED EGIPSTAIRE ISLLKELHHP 

        70         80         90        100        110        120 
NIVWLRDVIH SEKCLTLVFE YLDQDLKKLL DACDGGLEPT TAKSFLYQIL RGISYCHDHR 

       130        140        150        160        170        180 
ILHRDLKPQN LLINREGVLK LADFGLARAF AIPVRSYTHE VVTLWYRAPD VLMGSKKYST 

       190        200        210        220        230        240 
AVDIWSVGCI FAEMINGVPL FPGISEQDQL KRIFKILGTP NVDSWPQVVN LPAYNPDFCY 

       250        260        270        280        290 
YEKQAWSSIV PKLNESGIDL ISRMLQLDPV QRISAKEALK HDYFKDLHRP SEFLNGVH 

« Hide

References

« Hide 'large scale' references
[1]"The isolation and characterisation of genomic and cDNA clones coding for a cdc2-related kinase (ThCRK2) from the bovine protozoan parasite Theileria."
Kinnaird J.H., Logan M., Kirvar E., Tait A., Carrington M.
Mol. Microbiol. 22:293-302(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Ankara.
[2]"Genome of the host-cell transforming parasite Theileria annulata compared with T. parva."
Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W., Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R., Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A. expand/collapse author list , Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P., McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C., Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D., Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R., Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D., Shiels B., Tait A., Barrell B.G., Hall N.
Science 309:131-133(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ankara.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98768 mRNA. Translation: CAA67306.1.
CR940347 Genomic DNA. Translation: CAI73372.1.
RefSeqXP_954049.1. XM_948956.1.

3D structure databases

ProteinModelPortalQ26671.
SMRQ26671. Positions 1-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5874.Q26671.

Proteomic databases

PRIDEQ26671.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3863999.
KEGGtan:TA06730.

Organism-specific databases

EuPathDBPiroplasmaDB:TA06730.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04563.
ProtClustDBCLSZ2432515.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDC2H_THEAN
AccessionPrimary (citable) accession number: Q26671
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families