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Protein

Cyclin-dependent kinase 1-B

Gene

cdk1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331ATPPROSITE-ProRule annotation
Active sitei128 – 1281Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. mitotic nuclear division Source: UniProtKB-KW
  3. regulation of cell cycle Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 6726.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 1-B (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDK1-B
Alternative name(s):
Cell division control protein 2 homolog 2
Cell division control protein 2-B
Cell division protein kinase 1
p34 protein kinase 2
Gene namesi
Name:cdk1-b
Synonyms:cdc2, cdc2x1.2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254942. cdk1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Cyclin-dependent kinase 1-BPRO_0000085736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphothreonineBy similarity
Modified residuei15 – 151Phosphotyrosine; by wee1 and wee22 Publications
Modified residuei161 – 1611Phosphothreonine; by cak1 Publication
Modified residuei277 – 2771PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Tyr-15 by wee1 and wee2 inhibits the protein kinase activity and acts negative regulator of entry into mitosis (G2 to M transition).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP24033.

Interactioni

Subunit structurei

Forms a stable but non-covalent complex with a regulatory subunit and with a cyclin. Interacts with spdya.3 Publications

Structurei

3D structure databases

ProteinModelPortaliP24033.
SMRiP24033. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 287284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG014652.
KOiK02087.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P24033-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEYTKIEKI GEGTYGVVYK GRHKATGQVV AMKKIRLENE EEGVPSTAIR
60 70 80 90 100
EISLLKELQH PNIVCLLDVL MQDSRLYLIF EFLSMDLKKY LDSIPSGQYI
110 120 130 140 150
DTMLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDNKG VIKLADFGLA
160 170 180 190 200
RAFGIPVRVY THEVVTLWYR ASEVLLGSVR YSTPVDVWSV GTIFAEIATK
210 220 230 240 250
KPLFHGDSEI DQLFRIFRSL GTPNNEVWPE VESLQDYKNT FPKWKGGSLS
260 270 280 290 300
SNVKNIDEDG LDLLSKMLVY DPAKRISARK AMLHPYFDDL DKSSLPANQI

RN
Length:302
Mass (Da):34,532
Last modified:May 30, 2006 - v2
Checksum:iFA9DC156392D7CBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871L → V in AAA63562 (PubMed:1377775).Curated
Sequence conflicti123 – 1231R → G in AAA63562 (PubMed:1377775).Curated
Sequence conflicti172 – 1721S → P in AAA63562 (PubMed:1377775).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60681 mRNA. Translation: AAA63562.1.
BC054146 mRNA. Translation: AAH54146.1.
PIRiB44349.
RefSeqiNP_001080093.1. NM_001086624.1.
UniGeneiXl.3815.

Genome annotation databases

GeneIDi379785.
KEGGixla:379785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60681 mRNA. Translation: AAA63562.1.
BC054146 mRNA. Translation: AAH54146.1.
PIRiB44349.
RefSeqiNP_001080093.1. NM_001086624.1.
UniGeneiXl.3815.

3D structure databases

ProteinModelPortaliP24033.
SMRiP24033. Positions 1-292.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP24033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi379785.
KEGGixla:379785.

Organism-specific databases

CTDi379785.
XenbaseiXB-GENE-6254942. cdk1.

Phylogenomic databases

HOVERGENiHBG014652.
KOiK02087.

Enzyme and pathway databases

BRENDAi2.7.11.22. 6726.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Requirement of mosXe protein kinase for meiotic maturation of Xenopus oocytes induced by a cdc2 mutant lacking regulatory phosphorylation sites."
    Pickham K.M., Meyer A.N., Li J., Donoghue D.J.
    Mol. Cell. Biol. 12:3192-3203(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, SUBUNIT.
    Tissue: Oocyte.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tadpole.
  3. "The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues."
    Fesquet D., Labbe J.-C., Derancourt J., Capony J.-P., Galas S., Girard F., Lorca T., Shuttleworth J., Doree M., Cavadore J.-C.
    EMBO J. 12:3111-3121(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-161.
  4. "Cell cycle regulation of a Xenopus Wee1-like kinase."
    Mueller P.R., Coleman T.R., Dunphy W.G.
    Mol. Biol. Cell 6:119-134(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-15.
  5. "Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos."
    Murakami M.S., Vande Woude G.F.
    Development 125:237-248(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-15.
  6. "A novel p34cdc2 binding and activating protein that is necessary and sufficient to trigger G2/M progression in Xenopus oocytes."
    Ferby I., Blazquez M., Palmer A., Eritja R., Nebreda A.R.
    Genes Dev. 13:2177-2189(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA.
  7. "Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins."
    Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.
    Cell Cycle 4:155-165(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA.

Entry informationi

Entry nameiCDK1B_XENLA
AccessioniPrimary (citable) accession number: P24033
Secondary accession number(s): Q7SZ44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: May 30, 2006
Last modified: February 4, 2015
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.