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Q00646 (CDK1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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:
Cyclin-dependent kinase 1

Short name=CDK1
EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Cell division control protein 2
Cell division protein kinase 1
Never in mitosis protein X
Gene names
Name:nimX
Synonyms:cdk1
ORF Names:AN4182
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length323 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 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-180 activates it By similarity.

Subunit structure

Forms a stable but non-covalent complex with a regulatory subunit (SUC1) and with a cyclin.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processHulle cell development

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

cellular response to light stimulus

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

conidium formation

Inferred from mutant phenotype PubMed 19210625PubMed 9670015. Source: ASPGD

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of Hulle cell development

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

negative regulation of sexual sporulation resulting in formation of a cellular spore

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

positive regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: ASPGD

positive regulation of sterigmatocystin biosynthetic process

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

protein phosphorylation

Inferred from direct assay Ref.1. Source: ASPGD

regulation of conidium formation

Inferred from mutant phenotype PubMed 19210625PubMed 9670015. Source: ASPGD

sexual sporulation resulting in formation of a cellular spore

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

sporocarp development involved in sexual reproduction

Inferred from mutant phenotype PubMed 9670015. Source: ASPGD

sterigmatocystin biosynthetic process

Inferred from mutant phenotype PubMed 19210625. Source: ASPGD

   Cellular_componentnucleus

Inferred from direct assay PubMed 19210625PubMed 9647650. Source: ASPGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: ASPGD

protein kinase activity

Inferred from sequence alignment PubMed 19210625. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Cyclin-dependent kinase 1
PRO_0000085719

Regions

Domain4 – 306303Protein kinase
Nucleotide binding10 – 189ATP By similarity

Sites

Active site1471Proton acceptor By similarity
Binding site341ATP By similarity

Amino acid modifications

Modified residue141Phosphothreonine By similarity
Modified residue151Phosphotyrosine By similarity
Modified residue1801Phosphothreonine; by CAK By similarity

Sequences

Sequence LengthMass (Da)Tools
Q00646 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3178CAFBDDC32224

FASTA32336,779
        10         20         30         40         50         60 
MENYQKIEKI GEGTYGVVYK ARELTHPNRI VALKKIRLEA EDEGVPSTAI REISLLKEMN 

        70         80         90        100        110        120 
DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE GGRGRALPDG STLSRNLGLG 

       130        140        150        160        170        180 
DAMVKKFMAQ LIEGIRFCHS HRVLHRDLKP QNLLIDRDGN LKLADFGLAR AFGVPLRTYT 

       190        200        210        220        230        240 
HEVVTLWYRS PEILLGGRQY STGVDMWSCG AIFAEMCTRK PLFPGDSEID EIFKIFRILG 

       250        260        270        280        290        300 
TPDETIWPGV TSFPDFKPTF PKWKREDIQN VVPGLEEDGL DLLEALLEYD PARRISAKQA 

       310        320 
CMHPYFQHGS SYYSGRARRN GFH 

« Hide

References

« Hide 'large scale' references
[1]"A single p34cdc2 protein kinase (encoded by nimXcdc2) is required at G1 and G2 in Aspergillus nidulans."
Osmani A.H., van Peij N., Mischke M., O'Connell M.J., Osmani S.A.
J. Cell Sci. 107:1519-1528(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mycelium.
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07169 mRNA. Translation: AAA20597.1.
AACD01000068 Genomic DNA. Translation: EAA59281.1.
BN001302 Genomic DNA. Translation: CBF74540.1.
RefSeqXP_661786.1. XM_656694.1.

3D structure databases

ProteinModelPortalQ00646.
SMRQ00646. Positions 1-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-242233.

Proteomic databases

PRIDEQ00646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00004488; CADANIAP00004488; CADANIAG00004488.
GeneID2873604.
KEGGani:AN4182.2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
KOK04563.
OMAEMMLVYD.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BRENDA2.7.11.22. 2065.

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 nameCDK1_EMENI
AccessionPrimary (citable) accession number: Q00646
Secondary accession number(s): C8V4M9, Q5B5J8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families