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UniProtKB - P06493 (CDK1_HUMAN)

Entry version 259 (29 Sep 2021)
Sequence version 3 (31 May 2011)
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Protein

Cyclin-dependent kinase 1

Gene

CDK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair. Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression. In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons. The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis. NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation. In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis. The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis. In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration. CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (PubMed:26549230).

Regulates the amplitude of the cyclic expression of the core clock gene ARNTL/BMAL1 by phosphorylating its transcriptional repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of NR1D1 (PubMed:27238018).

Phosphorylates EML3 at 'Thr-881' which is essential for its interaction with HAUS augmin-like complex and TUBG1 (PubMed:30723163).

21 Publications

(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry.

1 Publication

Miscellaneous

As a key regulator of the cell cycle, CDK1 is a potent therapeutic target for inhibitors in cancer treatment.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-161 activates it. Activated through a multistep process; binding to cyclin-B is required for relocation of cyclin-kinase complexes to the nucleus, activated by CAK/CDK7-mediated phosphorylation on Thr-161, and CDC25-mediated dephosphorylation of inhibitory phosphorylation on Thr-14 and Tyr-15. Inhibited by flavopiridol and derivatives, pyrimidine derivatives, pyridine derivatives, purine derivatives, staurosporine, paullones, oxoindoles, indazole analogs, indolin-2-ones, pyrazolo[3,4-b]pyridines, imidazo[1,2-a]pyridine (AZ703), thiazolinone analogs(RO-3306), thiazol urea, macrocyclic quinoxalin-2-one, pyrrolo[2,3-a]carbazole, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine (Dinaciclib, SCH 727965), 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine), olomoucine, AG-024322, AT-7519, P276-00, R547/Ro-4584820 and SNS-032/BMS-387032. Repressed by the CDK inhibitors CDKN1A/p21 and CDKN1B/p27 during the G1 phase and by CDKN1A/p21 at the G1-S checkpoint upon DNA damage. Transient activation by rapid and transient dephosphorylation at Tyr-15 triggered by TGFB1.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei33ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei128Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi10 – 18ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHost cell receptor for virus entry, Kinase, Receptor, Serine/threonine-protein kinase, Transferase
Biological processApoptosis, Biological rhythms, Cell cycle, Cell division, Host-virus interaction, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.11.22, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P06493

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-110056, MAPK3 (ERK1) activation
R-HSA-113507, E2F-enabled inhibition of pre-replication complex formation
R-HSA-1362300, Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-162658, Golgi Cisternae Pericentriolar Stack Reorganization
R-HSA-170145, Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes
R-HSA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176408, Regulation of APC/C activators between G1/S and early anaphase
R-HSA-176412, Phosphorylation of the APC/C
R-HSA-176417, Phosphorylation of Emi1
R-HSA-2299718, Condensation of Prophase Chromosomes
R-HSA-2465910, MASTL Facilitates Mitotic Progression
R-HSA-2500257, Resolution of Sister Chromatid Cohesion
R-HSA-2514853, Condensation of Prometaphase Chromosomes
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-2980767, Activation of NIMA Kinases NEK9, NEK6, NEK7
R-HSA-2995383, Initiation of Nuclear Envelope (NE) Reformation
R-HSA-3301854, Nuclear Pore Complex (NPC) Disassembly
R-HSA-380259, Loss of Nlp from mitotic centrosomes
R-HSA-380270, Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-4419969, Depolymerisation of the Nuclear Lamina
R-HSA-5620912, Anchoring of the basal body to the plasma membrane
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689896, Ovarian tumor domain proteases
R-HSA-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-68875, Mitotic Prophase
R-HSA-69205, G1/S-Specific Transcription
R-HSA-69273, Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69478, G2/M DNA replication checkpoint
R-HSA-75035, Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518, AURKA Activation by TPX2
R-HSA-8878166, Transcriptional regulation by RUNX2

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P06493

SIGNOR Signaling Network Open Resource

More...SIGNORi		P06493

Protein family/group databases

Transport Classification Database

More...TCDBi		1.I.1.1.3, the nuclear pore complex (npc) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cyclin-dependent kinase 1 (EC:2.7.11.22, EC:2.7.11.23)
Short name:
CDK1
Alternative name(s):
Cell division control protein 2 homolog
Cell division protein kinase 1
p34 protein kinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CDK1
Synonyms:CDC2, CDC28A, CDKN1, P34CDC2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:1722, CDK1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		116940, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P06493

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000170312

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4Y → D or E: Constitutive polyubiquitination. 1 Publication1
Mutagenesisi14 – 15TY → AF: Abnormal cell cycle exhibiting only M-phase without completing either karyokinesis or cytokinesis. 1 Publication2

Organism-specific databases

DisGeNET

More...DisGeNETi		983

Open Targets

More...OpenTargetsi		ENSG00000170312

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA99

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P06493, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL308

Drug and drug target database

More...DrugBanki		DB04014, Alsterpaullone
DB03496, Alvocidib
DB08142, AT-7519
DB12010, Fostamatinib
DB02950, Hymenialdisine
DB02052, Indirubin-3'-monoxime
DB02116, Olomoucine
DB06195, Seliciclib
DB03428, SU9516

DrugCentral

More...DrugCentrali		P06493

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1961

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CDK1

Domain mapping of disease mutations (DMDM)

More...DMDMi		334302921

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000857241 – 297Cyclin-dependent kinase 1Add BLAST297

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei4Phosphotyrosine; by PKR1 Publication1
Modified residuei6N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei9N6-acetyllysine; alternateBy similarity1
Cross-linki9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei14Phosphothreonine; by PKMYT1Combined sources1 Publication1
Modified residuei15Phosphotyrosine; by PKMYT1, WEE1, WEE2 and PKC/PRKCDCombined sources2 Publications1
Modified residuei19PhosphotyrosineCombined sources1
Cross-linki20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei39PhosphoserineCombined sources1
Modified residuei77PhosphotyrosineCombined sources1
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei141PhosphothreonineCombined sources1
Modified residuei161Phosphothreonine; by CAKCombined sources1 Publication1
Modified residuei178PhosphoserineCombined sources1
Modified residuei222PhosphothreonineCombined sources1
Modified residuei245N6-succinyllysineBy similarity1
Modified residuei248PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Thr-161 by CAK/CDK7 activates kinase activity. Phosphorylation at Thr-14 and Tyr-15 by PKMYT1 prevents nuclear translocation. Phosphorylation at Tyr-15 by WEE1 and WEE2 inhibits the protein kinase activity and acts as a negative regulator of entry into mitosis (G2 to M transition). Phosphorylation by PKMYT1 and WEE1 takes place during mitosis to keep CDK1-cyclin-B complexes inactive until the end of G2. By the end of G2, PKMYT1 and WEE1 are inactivated, but CDC25A and CDC25B are activated. Dephosphorylation by active CDC25A and CDC25B at Thr-14 and Tyr-15, leads to CDK1 activation at the G2-M transition. Phosphorylation at Tyr-15 by WEE2 during oogenesis is required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, leading to prevent meiotic reentry. Phosphorylation by WEE2 is also required for metaphase II exit during egg activation to ensure exit from meiosis in oocytes and promote pronuclear formation. Phosphorylated at Tyr-4 by PKR/EIF2AK2 upon genotoxic stress. This phosphorylation triggers CDK1 polyubiquitination and subsequent proteolysis, thus leading to G2 arrest. In response to UV irradiation, phosphorylation at Tyr-15 by PRKCD activates the G2/M DNA damage checkpoint.5 Publications
Polyubiquitinated upon genotoxic stress.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1040
CPTAC-1041
CPTAC-1042
CPTAC-1200
CPTAC-797
CPTAC-798
CPTAC-801

Encyclopedia of Proteome Dynamics

More...EPDi		P06493

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06493

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P06493

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06493

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06493

PeptideAtlas

More...PeptideAtlasi		P06493

PRoteomics IDEntifications database

More...PRIDEi		P06493

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51905 [P06493-1]
51906 [P06493-2]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P06493

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P06493, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06493

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P06493

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P06493

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P06493

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 2 is found in breast cancer tissues.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Follows a cyclic expression; during interphase, accumulates gradually following G1, S to reach a critical threshold at the end of G2, which promotes self-activation and triggers onset of mitosis. Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis, but later repressed. Triggered by CKS1B during mitotic entry in breast cancer cells. Down-regulated under genotoxic stresses triggered by PKR/EIF2AK2-mediated phosphorylation.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000170312, Expressed in ventricular zone and 186 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P06493, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P06493, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000170312, Tissue enriched (lymphoid)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Interacts with cyclins-B (CCNB1, CCNB2 and CCNB3) to form a serine/threonine kinase holoenzyme complex also known as maturation promoting factor (MPF). The cyclin subunit imparts substrate specificity to the complex. Can also form CDK1-cylin-D and CDK1-cyclin-E complexes that phosphorylate RB1 in vitro. Binds to RB1 and other transcription factors such as FOXO1 and RUNX2. Promotes G2-M transition when in complex with a cyclin-B.

Interacts with DLGAP5. Binds to the CDK inhibitors CDKN1A/p21 and CDKN1B/p27. Isoform 2 is unable to complex with cyclin-B1 and also fails to bind to CDKN1A/p21.

Interacts with catalytically active CCNB1 and RALBP1 during mitosis to form an endocytotic complex during interphase. Associates with cyclins-A and B1 during S-phase in regenerating hepatocytes.

Interacts with FANCC.

Interacts with CEP63; this interaction recruits CDK1 to centrosomes.

Interacts with CENPA (PubMed:25556658).

Interacts with NR1D1 (PubMed:27238018).

Interacts with proteasome subunit PSMA8; to participate in meiosis progression during spermatogenesis (By similarity).

By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107420, 357 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2003, Cyclin A1-CDK1 complex
CPX-2004, Cyclin A2-CDK1 complex
CPX-2007, Cyclin B1-CDK1 complex
CPX-2008, Cyclin B2-CDK1 complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P06493

Database of interacting proteins

More...DIPi		DIP-35N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P06493

Protein interaction database and analysis system

More...IntActi		P06493, 169 interactors

Molecular INTeraction database

More...MINTi		P06493

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000378699

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06493

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P06493, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06493

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 287Protein kinasePROSITE-ProRule annotationAdd BLAST284

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0594, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153335

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_181_6_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06493

Identification of Orthologs from Complete Genome Data

More...OMAi		NYTHEIV

Database of Orthologous Groups

More...OrthoDBi		286319at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06493

TreeFam database of animal gene trees

More...TreeFami		TF101021

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P06493-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEDYTKIEKI GEGTYGVVYK GRHKTTGQVV AMKKIRLESE EEGVPSTAIR 
        60         70         80         90        100
EISLLKELRH PNIVSLQDVL MQDSRLYLIF EFLSMDLKKY LDSIPPGQYM 
       110        120        130        140        150
DSSLVKSYLY QILQGIVFCH SRRVLHRDLK PQNLLIDDKG TIKLADFGLA 
       160        170        180        190        200
RAFGIPIRVY THEVVTLWYR SPEVLLGSAR YSTPVDIWSI GTIFAELATK 
       210        220        230        240        250
KPLFHGDSEI DQLFRIFRAL GTPNNEVWPE VESLQDYKNT FPKWKPGSLA 
       260        270        280        290 
SHVKNLDENG LDLLSKMLIY DPAKRISGKM ALNHPYFNDL DNQIKKM
Length:297
Mass (Da):34,095
Last modified:May 31, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i942D79448EFE490A
GO
Isoform 2 (identifier: P06493-2) [UniParc]FASTAAdd to basket
Also known as: CDC2deltaT

The sequence of this isoform differs from the canonical sequence as follows:
     107-163: Missing.

Show »
Length:240
Mass (Da):27,503
Checksum:i50FC3D192024E38C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A024QZP7A0A024QZP7_HUMAN
Cell division cycle 2, G1 to S and ...
CDK1 CDC2, hCG_40242
297Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RIU6E5RIU6_HUMAN
Cyclin-dependent kinase 1
CDK1
189Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WZZ9A0A087WZZ9_HUMAN
Cyclin-dependent kinase 1
CDK1
224Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence EAW54204 differs from that shown. Reason: Erroneous gene model prediction.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_021375107 – 163Missing in isoform 2. 1 PublicationAdd BLAST57

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X05360 mRNA Translation: CAA28963.1
Y00272 mRNA Translation: CAA68376.1
D88357 mRNA Translation: BAA26001.1
AK291939 mRNA Translation: BAF84628.1
BT007004 mRNA Translation: AAP35650.1
AF512554 Genomic DNA Translation: AAM34793.1
AC022390 Genomic DNA No translation available.
CH471083 Genomic DNA Translation: EAW54204.1 Sequence problems.
BC014563 mRNA Translation: AAH14563.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS44408.1 [P06493-1]
CCDS7260.1 [P06493-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A29539

NCBI Reference Sequences

More...RefSeqi		NP_001307847.1, NM_001320918.1 [P06493-1]
NP_001777.1, NM_001786.4 [P06493-1]
NP_203698.1, NM_033379.4 [P06493-2]
XP_005270360.1, XM_005270303.3 [P06493-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000316629; ENSP00000325970; ENSG00000170312 [P06493-2]
ENST00000373809; ENSP00000362915; ENSG00000170312 [P06493-2]
ENST00000395284; ENSP00000378699; ENSG00000170312 [P06493-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		983

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:983

UCSC genome browser

More...UCSCi		uc001jld.3, human [P06493-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05360 mRNA Translation: CAA28963.1
Y00272 mRNA Translation: CAA68376.1
D88357 mRNA Translation: BAA26001.1
AK291939 mRNA Translation: BAF84628.1
BT007004 mRNA Translation: AAP35650.1
AF512554 Genomic DNA Translation: AAM34793.1
AC022390 Genomic DNA No translation available.
CH471083 Genomic DNA Translation: EAW54204.1 Sequence problems.
BC014563 mRNA Translation: AAH14563.1
CCDSiCCDS44408.1 [P06493-1]
CCDS7260.1 [P06493-2]
PIRiA29539
RefSeqiNP_001307847.1, NM_001320918.1 [P06493-1]
NP_001777.1, NM_001786.4 [P06493-1]
NP_203698.1, NM_033379.4 [P06493-2]
XP_005270360.1, XM_005270303.3 [P06493-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LC9model-A1-297[»]
4Y72X-ray2.30A1-297[»]
4YC3X-ray2.70A1-297[»]
4YC6X-ray2.60A/C/E/G1-297[»]
5HQ0X-ray2.30A1-297[»]
5LQFX-ray2.06A/D1-297[»]
6GU2X-ray2.00A1-297[»]
6GU3X-ray2.65A1-297[»]
6GU4X-ray2.73A1-297[»]
6GU6X-ray2.33A1-297[»]
6GU7X-ray2.75A/C/E/G1-297[»]
6TWNX-ray2.28C/D207-223[»]
SMRiP06493
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107420, 357 interactors
ComplexPortaliCPX-2003, Cyclin A1-CDK1 complex
CPX-2004, Cyclin A2-CDK1 complex
CPX-2007, Cyclin B1-CDK1 complex
CPX-2008, Cyclin B2-CDK1 complex
CORUMiP06493
DIPiDIP-35N
ELMiP06493
IntActiP06493, 169 interactors
MINTiP06493
STRINGi9606.ENSP00000378699

Chemistry databases

BindingDBiP06493
ChEMBLiCHEMBL308
DrugBankiDB04014, Alsterpaullone
DB03496, Alvocidib
DB08142, AT-7519
DB12010, Fostamatinib
DB02950, Hymenialdisine
DB02052, Indirubin-3'-monoxime
DB02116, Olomoucine
DB06195, Seliciclib
DB03428, SU9516
DrugCentraliP06493
GuidetoPHARMACOLOGYi1961

Protein family/group databases

TCDBi1.I.1.1.3, the nuclear pore complex (npc) family

PTM databases

GlyGeniP06493, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP06493
MetOSiteiP06493
PhosphoSitePlusiP06493
SwissPalmiP06493

Genetic variation databases

BioMutaiCDK1
DMDMi334302921

2D gel databases

SWISS-2DPAGEiP06493

Proteomic databases

CPTACiCPTAC-1040
CPTAC-1041
CPTAC-1042
CPTAC-1200
CPTAC-797
CPTAC-798
CPTAC-801
EPDiP06493
jPOSTiP06493
MassIVEiP06493
MaxQBiP06493
PaxDbiP06493
PeptideAtlasiP06493
PRIDEiP06493
ProteomicsDBi51905 [P06493-1]
51906 [P06493-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1134, 2684 antibodies

The CPTC Antibody Portal

More...CPTCi		P06493, 1 antibody

The DNASU plasmid repository

More...DNASUi		983

Genome annotation databases

EnsembliENST00000316629; ENSP00000325970; ENSG00000170312 [P06493-2]
ENST00000373809; ENSP00000362915; ENSG00000170312 [P06493-2]
ENST00000395284; ENSP00000378699; ENSG00000170312 [P06493-1]
GeneIDi983
KEGGihsa:983
UCSCiuc001jld.3, human [P06493-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		983
DisGeNETi983

GeneCards: human genes, protein and diseases

More...GeneCardsi		CDK1
HGNCiHGNC:1722, CDK1
HPAiENSG00000170312, Tissue enriched (lymphoid)
MIMi116940, gene
neXtProtiNX_P06493
OpenTargetsiENSG00000170312
PharmGKBiPA99
VEuPathDBiHostDB:ENSG00000170312

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0594, Eukaryota
GeneTreeiENSGT00940000153335
HOGENOMiCLU_000288_181_6_1
InParanoidiP06493
OMAiNYTHEIV
OrthoDBi286319at2759
PhylomeDBiP06493
TreeFamiTF101021

Enzyme and pathway databases

BRENDAi2.7.11.22, 2681
PathwayCommonsiP06493
ReactomeiR-HSA-110056, MAPK3 (ERK1) activation
R-HSA-113507, E2F-enabled inhibition of pre-replication complex formation
R-HSA-1362300, Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1
R-HSA-162658, Golgi Cisternae Pericentriolar Stack Reorganization
R-HSA-170145, Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes
R-HSA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-176408, Regulation of APC/C activators between G1/S and early anaphase
R-HSA-176412, Phosphorylation of the APC/C
R-HSA-176417, Phosphorylation of Emi1
R-HSA-2299718, Condensation of Prophase Chromosomes
R-HSA-2465910, MASTL Facilitates Mitotic Progression
R-HSA-2500257, Resolution of Sister Chromatid Cohesion
R-HSA-2514853, Condensation of Prometaphase Chromosomes
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-2980767, Activation of NIMA Kinases NEK9, NEK6, NEK7
R-HSA-2995383, Initiation of Nuclear Envelope (NE) Reformation
R-HSA-3301854, Nuclear Pore Complex (NPC) Disassembly
R-HSA-380259, Loss of Nlp from mitotic centrosomes
R-HSA-380270, Recruitment of mitotic centrosome proteins and complexes
R-HSA-380284, Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320, Recruitment of NuMA to mitotic centrosomes
R-HSA-4419969, Depolymerisation of the Nuclear Lamina
R-HSA-5620912, Anchoring of the basal body to the plasma membrane
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689896, Ovarian tumor domain proteases
R-HSA-6804114, TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-68875, Mitotic Prophase
R-HSA-69205, G1/S-Specific Transcription
R-HSA-69273, Cyclin A/B1/B2 associated events during G2/M transition
R-HSA-69478, G2/M DNA replication checkpoint
R-HSA-75035, Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854518, AURKA Activation by TPX2
R-HSA-8878166, Transcriptional regulation by RUNX2
SignaLinkiP06493
SIGNORiP06493

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		983, 808 hits in 994 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CDK1, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Cdk1
Cyclin-dependent_kinase_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		983
PharosiP06493, Tchem

Protein Ontology

More...PROi		PR:P06493
RNActiP06493, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000170312, Expressed in ventricular zone and 186 other tissues
ExpressionAtlasiP06493, baseline and differential
GenevisibleiP06493, HS

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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCDK1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06493
Secondary accession number(s): A8K7C4, C9J497, O60764
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: May 31, 2011
Last modified: September 29, 2021
This is version 259 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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