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Protein

Cyclin-dependent kinase 1

Gene

CDC2

Organism
Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-181 activates it.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei34ATPPROSITE-ProRule annotation1
Active sitei148Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 18ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22 221

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22)
Short name:
CDK1
Alternative name(s):
Cell division protein kinase 1
Gene namesi
Name:CDC2
Synonyms:CDK1
OrganismiAjellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri5037 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000857181 – 324Cyclin-dependent kinase 1Add BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphothreonineBy similarity1
Modified residuei15PhosphotyrosineBy similarity1
Modified residuei181Phosphothreonine; by CAKBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP54119

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP54119
SMRiP54119
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 307Protein kinasePROSITE-ProRule annotationAdd BLAST304

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0594 Eukaryota
ENOG410XPP3 LUCA

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

P54119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENYQKIEKI GEGTYGVVYK ARDLTHPNRI VALKKIRLEA EDEGVPSTAI
60 70 80 90 100
REISLLKEMH DPNIVRLLNI VHADGHKLYL VFEFLDLDLK KYMEALPVSE
110 120 130 140 150
GGRGKALPDG STLDMNRLGL GEAMVKKFMA QLVEGIRYCH SHRVLHRDLK
160 170 180 190 200
PQNLLIDREG NLKLADFGLA RAFGVPLRTY THEVVTLWYR APEILLGGRQ
210 220 230 240 250
YSTGVDMWSV GAIFAEMCTR KPLFPGDSEI DEIFKIFKLL GTPDENTWPG
260 270 280 290 300
VTSFPDFKAS FPKWKREDTR KLVPGLERNG LDLLDAMLEY DPARRISAKQ
310 320
ACMHPYFQAG SSAYSGRERL QPYP
Length:324
Mass (Da):36,824
Last modified:October 1, 1996 - v1
Checksum:i3B80A7F5BD4E748B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74361 Genomic DNA Translation: CAA52405.1
PIRiS36437

Similar proteinsi

Entry informationi

Entry nameiCDK1_AJECA
AccessioniPrimary (citable) accession number: P54119
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health