Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P24941 (CDK2_HUMAN)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cyclin-dependent kinase 2

Gene

CDK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus. Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in human embryonic stem cells (hESCs). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase. EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing. Phosphorylates CABLES1 (By similarity). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC. Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis. In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation. Phosphorylation of RB1 disturbs its interaction with E2F1. NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication. Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase. Required for vitamin D-mediated growth inhibition by being itself inactivated. Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner. USP37 is activated by phosphorylation and thus triggers G1-S transition. CTNNB1 phosphorylation regulates insulin internalization. Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates CDK2AP2 (PubMed:12944431).By similarity18 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+1 PublicationNote: Binds 2 Mg2+ ions.1 Publication

Enzyme regulationi

Phosphorylation at Thr-14 or Tyr-15 inactivates the enzyme, while phosphorylation at Thr-160 activates it. Inhibited by 1,25-dihydroxyvitamin D3 (1,25-(OH)2D3), AG-024322, N-(4-Piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), R547 (Ro-4584820), purine, pyrimidine and pyridine derivatives, 2-aminopyrimidines, paullones, thiazo derivatives, macrocyclic quinoxalin-2-one, pyrazolo[1,5-a]-1,3,5-triazine, pyrazolo[1,5-a]pyrimidine, 2-(1-ethyl-2-hydroxyethylamino)-6-benzylamino-9-isopropylpurine (roscovitine, seliciclib and CYC202), SNS-032 (BMS-387032), triazolo[1,5-a]pyrimidines, staurosporine and olomoucine. Stimulated by MYC. Inactivated by CDKN1A (p21).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei9CDK7 binding1
Binding sitei33ATPPROSITE-ProRule annotation2 Publications1
Binding sitei86ATPPROSITE-ProRule annotation2 Publications1
Sitei88 – 89CDK7 binding2
Active sitei127Proton acceptor1
Metal bindingi132Magnesium1 Publication1
Metal bindingi145Magnesium1 Publication1
Binding sitei145ATPPROSITE-ProRule annotation2 Publications1
Sitei166CDK7 binding1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 18ATPPROSITE-ProRule annotation2 Publications9
Nucleotide bindingi81 – 83ATPPROSITE-ProRule annotation2 Publications3
Nucleotide bindingi129 – 132ATPPROSITE-ProRule annotation2 Publications4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cyclin binding Source: UniProtKB
  • cyclin-dependent protein kinase activity Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • kinase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • protein domain specific binding Source: CAFA
  • protein serine/threonine kinase activity Source: Reactome
Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-6804116. TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-68911. G2 Phase.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69200. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
R-HSA-69202. Cyclin E associated events during G1/S transition.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69563. p53-Dependent G1 DNA Damage Response.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-HSA-8849470. PTK6 Regulates Cell Cycle.
R-HSA-912446. Meiotic recombination.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP24941.
SIGNORiP24941.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 2 (EC:2.7.11.22)
Alternative name(s):
Cell division protein kinase 2
p33 protein kinase
Gene namesi
Name:CDK2
Synonyms:CDKN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1771. CDK2.

Subcellular locationi

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • centrosome Source: UniProtKB
  • chromosome, telomeric region Source: Ensembl
  • condensed chromosome Source: Ensembl
  • cyclin A1-CDK2 complex Source: Ensembl
  • cyclin A2-CDK2 complex Source: UniProtKB
  • cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  • cyclin E1-CDK2 complex Source: Ensembl
  • cyclin E2-CDK2 complex Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endosome Source: UniProtKB
  • nucleoplasm Source: CAFA
  • nucleus Source: UniProtKB
  • transcription factor complex Source: Ensembl
  • X chromosome Source: Ensembl
  • Y chromosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Endosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9K → F: Reduced phosphorylation by CAK. 1 Publication1
Mutagenesisi14T → A: 2-fold increase in activity. 1 Publication1
Mutagenesisi15Y → F: 2-fold increase in activity. 1 Publication1
Mutagenesisi88 – 89KK → EV: Reduced phosphorylation by CAK. 1 Publication2
Mutagenesisi160T → A: Abolishes activity. 1 Publication1
Mutagenesisi166L → R: Reduced phosphorylation by CAK and reduced kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi1017.
OpenTargetsiENSG00000123374.
PharmGKBiPA101.

Chemistry databases

ChEMBLiCHEMBL301.
DrugBankiDB07054. (2R)-1-(DIMETHYLAMINO)-3-{4-[(6-{[2-FLUORO-5-(TRIFLUOROMETHYL)PHENYL]AMINO}PYRIMIDIN-4-YL)AMINO]PHENOXY}PROPAN-2-OL.
DB07504. (2R)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OL.
DB08463. (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol.
DB07501. (2S)-1-{4-[(4-ANILINO-5-BROMOPYRIMIDIN-2-YL)AMINO]PHENOXY}-3-(DIMETHYLAMINO)PROPAN-2-OL.
DB07137. (2S)-N-[(3Z)-5-CYCLOPROPYL-3H-PYRAZOL-3-YLIDENE]-2-[4-(2-OXOIMIDAZOLIDIN-1-YL)PHENYL]PROPANAMIDE.
DB08137. (4E)-N-(4-fluorophenyl)-4-[(phenylcarbonyl)imino]-4H-pyrazole-3-carboxamide.
DB02603. 1-Amino-6-Cyclohex-3-Enylmethyloxypurine.
DB04288. 2-[Trans-(4-Aminocyclohexyl)Amino]-6-(Benzyl-Amino)-9-Cyclopentylpurine.
DB02297. 2-Amino-6-Chloropyrazine.
DB06948. 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE.
DB07982. 2-{4-[4-({4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-yl}amino)phenyl]piperazin-1-yl}-2-oxoethanol.
DB08248. 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE.
DB08309. 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL.
DB02973. 4-(5-Bromo-2-Oxo-2h-Indol-3-Ylazo)-Benzenesulfonamide.
DB08241. 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE.
DB08136. 4-(acetylamino)-N-(4-fluorophenyl)-1H-pyrazole-3-carboxamide.
DB03307. 4-[(6-Amino-4-Pyrimidinyl)Amino]Benzenesulfonamide.
DB08134. 4-[(6-chloropyrazin-2-yl)amino]benzenesulfonamide.
DB04407. 4-[4-(4-Methyl-2-Methylamino-Thiazol-5-Yl)-Pyrimidin-2-Ylamino]-Phenol.
DB07791. 4-{[4-(1-CYCLOPROPYL-2-METHYL-1H-IMIDAZOL-5-YL)PYRIMIDIN-2-YL]AMINO}-N-METHYLBENZENESULFONAMIDE.
DB08572. 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE.
DB07163. 5-[(2-AMINOETHYL)AMINO]-6-FLUORO-3-(1H-PYRROL-2-YL)BENZO[CD]INDOL-2(1H)-ONE.
DB08132. 5-hydroxynaphthalene-1-sulfonamide.
DB02898. 5-{[(2-Amino-9h-Purin-6-Yl)Oxy]Methyl}-2-Pyrrolidinone.
DB07612. 6-(3-AMINOPHENYL)-N-(TERT-BUTYL)-2-(TRIFLUOROMETHYL)QUINAZOLIN-4-AMINE.
DB08247. 6-(CYCLOHEXYLMETHOXY)-8-ISOPROPYL-9H-PURIN-2-AMINE.
DB07203. 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE.
DB08233. 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE.
DB02407. 6-O-Cyclohexylmethyl Guanine.
DB02833. [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine.
DB05037. AT7519.
DB06616. Bosutinib.
DB03496. Flavopiridol.
DB02950. Hymenialdisine.
DB02052. Indirubin-3'-Monoxime.
DB03801. Lysine Nz-Carboxylic Acid.
DB07790. N-(2-METHOXYETHYL)-4-({4-[2-METHYL-1-(1-METHYLETHYL)-1H-IMIDAZOL-5-YL]PYRIMIDIN-2-YL}AMINO)BENZENESULFONAMIDE.
DB06944. N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide.
DB08768. N-(3-METHYLBUT-2-EN-1-YL)-9H-PURIN-6-AMINE.
DB08133. N-(4-sulfamoylphenyl)-1H-indazole-3-carboxamide.
DB07936. N-(4-{[(3S)-3-(dimethylamino)pyrrolidin-1-yl]carbonyl}phenyl)-5-fluoro-4-[2-methyl-1-(1-methylethyl)-1H-imidazol-5-yl]pyrimidin-2-amine.
DB02647. N-(5-Cyclopropyl-1h-Pyrazol-3-Yl)Benzamide.
DB08677. N-(5-ISOPROPYL-THIAZOL-2-YL)-2-PYRIDIN-3-YL-ACETAMIDE.
DB08066. N-[3-(1H-BENZIMIDAZOL-2-YL)-1H-PYRAZOL-4-YL]BENZAMIDE.
DB08135. N-phenyl-1H-pyrazole-3-carboxamide.
DB07126. O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE.
DB02116. Olomoucine.
DB04662. OLOMOUCINE II.
DB02733. Purvalanol.
DB02010. Staurosporine.
DB03428. SU9516.
DB04669. TRIAZOLOPYRIMIDINE.
GuidetoPHARMACOLOGYi1973.

Polymorphism and mutation databases

BioMutaiCDK2.
DMDMi116051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000857691 – 298Cyclin-dependent kinase 2Add BLAST298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei14Phosphothreonine2 Publications1
Modified residuei15Phosphotyrosine; by WEE1Combined sources2 Publications1
Modified residuei19PhosphotyrosineCombined sources1
Modified residuei160Phosphothreonine; by CAK and CCRK8 Publications1

Post-translational modificationi

Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A.11 Publications
Nitrosylated after treatment with nitric oxide (DETA-NO).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP24941.
MaxQBiP24941.
PaxDbiP24941.
PeptideAtlasiP24941.
PRIDEiP24941.

PTM databases

iPTMnetiP24941.
PhosphoSitePlusiP24941.
SwissPalmiP24941.

Expressioni

Inductioni

Induced transiently by TGFB1 at an early phase of TGFB1-mediated apoptosis.

Gene expression databases

BgeeiENSG00000123374.
CleanExiHS_CDK2.
ExpressionAtlasiP24941. baseline and differential.
GenevisibleiP24941. HS.

Organism-specific databases

HPAiCAB013115.
HPA066915.

Interactioni

Subunit structurei

Found in a complex with CABLES1, CCNA1 and CCNE1. Interacts with CABLES1 (By similarity). Interacts with UHRF2. Part of a complex consisting of UHRF2, CDK2 and CCNE1. Interacts with the Speedy/Ringo proteins SPDYA and SPDYC. Found in a complex with both SPDYA and CDKN1B/KIP1. Binds to RB1 and CDK7. Binding to CDKN1A (p21) leads to CDK2/cyclin E inactivation at the G1-S phase DNA damage checkpoint, thereby arresting cells at the G1-S transition during DNA repair. Associated with PTPN6 and beta-catenin/CTNNB1. Interacts with CACUL1. May interact with CEP63. Interacts with ANKRD17. Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Forms a ternary complex with CCNA2 and CDKN1B; CDKN1B inhibits the kinase activity of CDK2 through conformational rearrangements (PubMed:8684460). Interacts with cyclins A, B1, B3, D, or E (PubMed:10499802, PubMed:10884347, PubMed:12185076, PubMed:23781148). Interacts with CDK2AP2 (PubMed:23781148).By similarity28 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • cyclin binding Source: UniProtKB
  • protein domain specific binding Source: CAFA
Complete GO annotation...

Protein-protein interaction databases

BioGridi107452. 674 interactors.
DIPiDIP-161N.
IntActiP24941. 150 interactors.
MINTiMINT-96328.
STRINGi9606.ENSP00000266970.

Chemistry databases

BindingDBiP24941.

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 3Combined sources3
Beta strandi4 – 12Combined sources9
Beta strandi14 – 23Combined sources10
Turni24 – 26Combined sources3
Beta strandi29 – 35Combined sources7
Beta strandi39 – 41Combined sources3
Beta strandi42 – 44Combined sources3
Helixi46 – 54Combined sources9
Helixi55 – 57Combined sources3
Beta strandi66 – 72Combined sources7
Beta strandi75 – 81Combined sources7
Beta strandi84 – 86Combined sources3
Helixi87 – 93Combined sources7
Turni94 – 97Combined sources4
Helixi101 – 120Combined sources20
Helixi130 – 132Combined sources3
Beta strandi133 – 135Combined sources3
Turni137 – 139Combined sources3
Beta strandi141 – 143Combined sources3
Helixi148 – 152Combined sources5
Helixi156 – 158Combined sources3
Beta strandi159 – 161Combined sources3
Helixi162 – 168Combined sources7
Helixi171 – 174Combined sources4
Beta strandi178 – 180Combined sources3
Helixi183 – 198Combined sources16
Helixi208 – 219Combined sources12
Turni224 – 226Combined sources3
Helixi230 – 232Combined sources3
Helixi248 – 251Combined sources4
Beta strandi252 – 254Combined sources3
Helixi257 – 266Combined sources10
Turni271 – 273Combined sources3
Helixi277 – 281Combined sources5
Helixi284 – 286Combined sources3
Turni287 – 289Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AQ1X-ray2.00A1-298[»]
1B38X-ray2.00A1-298[»]
1B39X-ray2.10A1-298[»]
1BUHX-ray2.60A1-298[»]
1CKPX-ray2.05A1-298[»]
1DI8X-ray2.20A1-298[»]
1DM2X-ray2.10A1-298[»]
1E1VX-ray1.95A1-298[»]
1E1XX-ray1.85A1-298[»]
1E9HX-ray2.50A/C1-296[»]
1F5QX-ray2.50A/C1-298[»]
1FINX-ray2.30A/C1-298[»]
1FQ1X-ray3.00B1-298[»]
1FVTX-ray2.20A1-298[»]
1FVVX-ray2.80A/C1-298[»]
1G5SX-ray2.61A1-298[»]
1GIHX-ray2.80A1-298[»]
1GIIX-ray2.00A1-298[»]
1GIJX-ray2.20A1-298[»]
1GY3X-ray2.70A/C1-296[»]
1GZ8X-ray1.30A1-298[»]
1H00X-ray1.60A1-298[»]
1H01X-ray1.79A1-298[»]
1H07X-ray1.85A1-298[»]
1H08X-ray1.80A1-298[»]
1H0VX-ray1.90A1-298[»]
1H0WX-ray2.10A1-298[»]
1H1PX-ray2.10A/C1-298[»]
1H1QX-ray2.50A/C1-298[»]
1H1RX-ray2.00A/C1-298[»]
1H1SX-ray2.00A/C1-298[»]
1H24X-ray2.50A/C1-298[»]
1H25X-ray2.50A/C1-298[»]
1H26X-ray2.24A/C1-298[»]
1H27X-ray2.20A/C1-298[»]
1H28X-ray2.80A/C1-298[»]
1HCKX-ray1.90A1-298[»]
1HCLX-ray1.80A1-298[»]
1JSTX-ray2.60A/C1-298[»]
1JSUX-ray2.30A1-298[»]
1JSVX-ray1.96A1-298[»]
1JVPX-ray1.53P1-298[»]
1KE5X-ray2.20A1-298[»]
1KE6X-ray2.00A1-298[»]
1KE7X-ray2.00A1-298[»]
1KE8X-ray2.00A1-298[»]
1KE9X-ray2.00A1-298[»]
1OGUX-ray2.60A/C1-298[»]
1OI9X-ray2.10A/C1-298[»]
1OIQX-ray2.31A1-298[»]
1OIRX-ray1.91A1-298[»]
1OITX-ray1.60A1-298[»]
1OIUX-ray2.00A/C1-298[»]
1OIYX-ray2.40A/C1-298[»]
1OKVX-ray2.40A/C1-298[»]
1OKWX-ray2.50A/C1-298[»]
1OL1X-ray2.90A/C1-298[»]
1OL2X-ray2.60A/C1-298[»]
1P2AX-ray2.50A1-298[»]
1P5EX-ray2.22A/C1-298[»]
1PF8X-ray2.51A1-298[»]
1PKDX-ray2.30A/C1-296[»]
1PW2X-ray1.95A1-298[»]
1PXIX-ray1.95A1-298[»]
1PXJX-ray2.30A1-298[»]
1PXKX-ray2.80A1-298[»]
1PXLX-ray2.50A1-298[»]
1PXMX-ray2.53A1-298[»]
1PXNX-ray2.50A1-298[»]
1PXOX-ray1.96A1-298[»]
1PXPX-ray2.30A1-298[»]
1PYEX-ray2.00A1-298[»]
1QMZX-ray2.20A/C1-298[»]
1R78X-ray2.00A1-298[»]
1URCX-ray2.60A/C1-298[»]
1URWX-ray1.60A1-298[»]
1V1KX-ray2.31A1-298[»]
1VYWX-ray2.30A/C1-298[»]
1VYZX-ray2.21A1-298[»]
1W0XX-ray2.20C1-298[»]
1W8CX-ray2.05A1-298[»]
1W98X-ray2.15A1-297[»]
1WCCX-ray2.20A1-298[»]
1Y8YX-ray2.00A1-298[»]
1Y91X-ray2.15A1-298[»]
1YKRX-ray1.80A1-298[»]
2A0CX-ray1.95X1-298[»]
2A4LX-ray2.40A1-298[»]
2B52X-ray1.88A1-298[»]
2B53X-ray2.00A1-298[»]
2B54X-ray1.85A1-298[»]
2B55X-ray1.85A1-298[»]
2BHEX-ray1.90A1-298[»]
2BHHX-ray2.60A1-298[»]
2BKZX-ray2.60A/C1-298[»]
2BPMX-ray2.40A/C1-298[»]
2BTRX-ray1.85A1-298[»]
2BTSX-ray1.99A1-298[»]
2C4GX-ray2.70A/C1-298[»]
2C5NX-ray2.10A/C1-298[»]
2C5OX-ray2.10A/C1-298[»]
2C5VX-ray2.90A/C1-298[»]
2C5XX-ray2.90A/C1-298[»]
2C5YX-ray2.25A1-298[»]
2C68X-ray1.95A1-298[»]
2C69X-ray2.10A1-298[»]
2C6IX-ray1.80A1-298[»]
2C6KX-ray1.90A1-298[»]
2C6LX-ray2.30A1-298[»]
2C6MX-ray1.90A1-298[»]
2C6OX-ray2.10A1-298[»]
2C6TX-ray2.61A/C1-298[»]
2CCHX-ray1.70A/C1-298[»]
2CCIX-ray2.70A/C1-298[»]
2CJMX-ray2.30A/C1-298[»]
2CLXX-ray1.80A1-298[»]
2DS1X-ray2.00A1-298[»]
2DUVX-ray2.20A1-298[»]
2EXMX-ray1.80A1-298[»]
2FVDX-ray1.85A1-298[»]
2G9XX-ray2.50A/C1-298[»]
2HICmodel-A1-298[»]
2I40X-ray2.80A/C1-298[»]
2IW6X-ray2.30A/C1-298[»]
2IW8X-ray2.30A/C1-298[»]
2IW9X-ray2.00A/C1-298[»]
2J9MX-ray2.50A1-298[»]
2JGZX-ray2.90A1-288[»]
2R3FX-ray1.50A1-298[»]
2R3GX-ray1.55A1-298[»]
2R3HX-ray1.50A1-298[»]
2R3IX-ray1.28A1-298[»]
2R3JX-ray1.65A1-298[»]
2R3KX-ray1.70A1-298[»]
2R3LX-ray1.65A1-298[»]
2R3MX-ray1.70A1-298[»]
2R3NX-ray1.63A1-298[»]
2R3OX-ray1.80A1-298[»]
2R3PX-ray1.66A1-298[»]
2R3QX-ray1.35A1-298[»]
2R3RX-ray1.47A1-298[»]
2R64X-ray2.30A1-298[»]
2UUEX-ray2.06A/C1-298[»]
2UZBX-ray2.70A/C1-298[»]
2UZDX-ray2.72A/C1-298[»]
2UZEX-ray2.40A/C1-298[»]
2UZLX-ray2.40A/C1-298[»]
2UZNX-ray2.30A1-298[»]
2UZOX-ray2.30A1-298[»]
2V0DX-ray2.20A1-298[»]
2V22X-ray2.60A/C1-298[»]
2VTAX-ray2.00A1-298[»]
2VTHX-ray1.90A1-298[»]
2VTIX-ray2.00A1-298[»]
2VTJX-ray2.20A1-298[»]
2VTLX-ray2.00A1-298[»]
2VTMX-ray2.25A1-298[»]
2VTNX-ray2.20A1-298[»]
2VTOX-ray2.19A1-298[»]
2VTPX-ray2.15A1-298[»]
2VTQX-ray1.90A1-298[»]
2VTRX-ray1.90A1-298[»]
2VTSX-ray1.90A1-298[»]
2VTTX-ray1.68A1-298[»]
2VU3X-ray1.85A1-298[»]
2VV9X-ray1.90A1-298[»]
2W05X-ray1.90A1-298[»]
2W06X-ray2.04A1-298[»]
2W17X-ray2.15A1-298[»]
2W1HX-ray2.15A1-298[»]
2WEVX-ray2.30A/C1-298[»]
2WFYX-ray2.53A/C1-298[»]
2WHBX-ray2.90A/C1-298[»]
2WIHX-ray2.50A/C1-298[»]
2WIPX-ray2.80A/C1-298[»]
2WMAX-ray2.80A/C1-298[»]
2WMBX-ray2.60A/C1-298[»]
2WPAX-ray2.51A/C1-298[»]
2WXVX-ray2.60A/C1-298[»]
2X1NX-ray2.75A/C1-298[»]
2XMYX-ray1.90A1-298[»]
2XNBX-ray1.85A1-298[»]
3BHTX-ray2.00A/C1-298[»]
3BHUX-ray2.30A/C1-298[»]
3BHVX-ray2.10A/C1-298[»]
3DDPX-ray2.70A/C1-298[»]
3DDQX-ray1.80A/C1-298[»]
3DOGX-ray2.70A/C1-298[»]
3EIDX-ray3.15A/C1-298[»]
3EJ1X-ray3.22A/C1-298[»]
3EOCX-ray3.20A/C1-298[»]
3EZRX-ray1.90A1-298[»]
3EZVX-ray1.99A1-298[»]
3F5XX-ray2.40A/C1-298[»]
3FZ1X-ray1.90A1-298[»]
3IG7X-ray1.80A1-298[»]
3IGGX-ray1.80A1-298[»]
3LE6X-ray2.00A1-298[»]
3LFNX-ray2.28A1-298[»]
3LFQX-ray2.03A1-298[»]
3LFSX-ray2.40A1-298[»]
3MY5X-ray2.10A/C1-298[»]
3NS9X-ray1.78A1-298[»]
3PJ8X-ray1.96A1-298[»]
3PXFX-ray1.80A1-298[»]
3PXQX-ray1.90A1-298[»]
3PXRX-ray2.00A1-298[»]
3PXYX-ray1.80A1-298[»]
3PXZX-ray1.70A1-298[»]
3PY0X-ray1.75A1-298[»]
3PY1X-ray2.05A1-298[»]
3QHRX-ray2.17A/C1-296[»]
3QHWX-ray1.91A/C1-296[»]
3QL8X-ray1.90A1-298[»]
3QQFX-ray1.75A1-298[»]
3QQGX-ray1.90A1-298[»]
3QQHX-ray1.87A1-298[»]
3QQJX-ray1.70A1-298[»]
3QQKX-ray1.86A1-298[»]
3QQLX-ray1.85A1-298[»]
3QRTX-ray1.75A1-298[»]
3QRUX-ray1.95A1-298[»]
3QTQX-ray1.80A1-298[»]
3QTRX-ray1.85A1-298[»]
3QTSX-ray1.90A1-298[»]
3QTUX-ray1.82A1-298[»]
3QTWX-ray1.85A1-298[»]
3QTXX-ray1.95A1-298[»]
3QTZX-ray2.00A1-298[»]
3QU0X-ray1.95A1-298[»]
3QWJX-ray1.75A1-298[»]
3QWKX-ray1.85A1-298[»]
3QX2X-ray1.75A1-298[»]
3QX4X-ray1.92A1-298[»]
3QXOX-ray1.75A1-298[»]
3QXPX-ray1.75A1-298[»]
3QZFX-ray2.00A1-298[»]
3QZGX-ray1.75A1-298[»]
3QZHX-ray1.95A1-298[»]
3QZIX-ray1.75A1-298[»]
3R1QX-ray1.85A1-298[»]
3R1SX-ray1.80A1-298[»]
3R1YX-ray1.80A1-298[»]
3R28X-ray1.75A1-298[»]
3R6XX-ray1.75A1-298[»]
3R71X-ray1.75A1-298[»]
3R73X-ray1.70A1-298[»]
3R7EX-ray1.90A1-298[»]
3R7IX-ray1.85A1-298[»]
3R7UX-ray1.75A1-298[»]
3R7VX-ray1.95A1-298[»]
3R7YX-ray1.90A1-298[»]
3R83X-ray1.75A1-298[»]
3R8LX-ray1.90A1-298[»]
3R8MX-ray1.80A1-298[»]
3R8PX-ray1.80A1-298[»]
3R8UX-ray2.00A1-298[»]
3R8VX-ray1.90A1-298[»]
3R8ZX-ray1.85A1-298[»]
3R9DX-ray1.95A1-298[»]
3R9HX-ray2.10A1-298[»]
3R9NX-ray1.75A1-298[»]
3R9OX-ray1.90A1-298[»]
3RAHX-ray1.75A1-298[»]
3RAIX-ray1.70A1-298[»]
3RAKX-ray1.75A1-298[»]
3RALX-ray1.75A1-298[»]
3RJCX-ray1.85A1-298[»]
3RK5X-ray2.00A1-298[»]
3RK7X-ray1.80A1-298[»]
3RK9X-ray1.85A1-298[»]
3RKBX-ray2.00A1-298[»]
3RM6X-ray1.60A1-298[»]
3RM7X-ray1.85A1-298[»]
3RMFX-ray1.75A1-298[»]
3RNIX-ray1.95A1-298[»]
3ROYX-ray1.75A1-298[»]
3RPOX-ray1.75A1-298[»]
3RPRX-ray1.75A1-298[»]
3RPVX-ray1.80A1-298[»]
3RPYX-ray1.90A1-298[»]
3RZBX-ray1.90A1-298[»]
3S00X-ray1.80A1-298[»]
3S0OX-ray2.00A1-298[»]
3S1HX-ray1.75A1-298[»]
3S2PX-ray2.30A1-298[»]
3SQQX-ray1.85A1-298[»]
3SW4X-ray1.70A1-298[»]
3SW7X-ray1.80A1-298[»]
3TI1X-ray1.99A1-298[»]
3TIYX-ray1.84A1-298[»]
3TIZX-ray2.02A1-298[»]
3TNWX-ray2.00A/C1-298[»]
3ULIX-ray2.00A1-298[»]
3UNJX-ray1.90A1-298[»]
3UNKX-ray2.10A1-298[»]
3WBLX-ray2.00A1-298[»]
4ACMX-ray1.63A1-298[»]
4BCKX-ray2.05A/C1-298[»]
4BCMX-ray2.45A/C1-298[»]
4BCNX-ray2.10A/C1-298[»]
4BCOX-ray2.05A/C1-298[»]
4BCPX-ray2.26A/C1-298[»]
4BCQX-ray2.40A/C1-298[»]
4BGHX-ray1.95A1-298[»]
4BZDX-ray1.83A1-298[»]
4CFMX-ray2.85A/C1-298[»]
4CFNX-ray2.20A/C1-298[»]
4CFUX-ray2.20A/C1-298[»]
4CFVX-ray2.00A/C1-298[»]
4CFWX-ray2.45A/C1-298[»]
4CFXX-ray3.50A/C1-298[»]
4D1XX-ray2.10A1-298[»]
4D1ZX-ray1.85A1-298[»]
4EK3X-ray1.34A1-298[»]
4EK4X-ray1.26A1-298[»]
4EK5X-ray1.60A1-298[»]
4EK6X-ray1.52A1-298[»]
4EK8X-ray1.70A1-298[»]
4EOIX-ray2.00A/C1-298[»]
4EOJX-ray1.65A/C1-298[»]
4EOKX-ray2.57A/C1-297[»]
4EOLX-ray2.40A/C1-297[»]
4EOMX-ray2.10A/C1-297[»]
4EONX-ray2.40A/C1-298[»]
4EOOX-ray2.10A/C1-297[»]
4EOPX-ray1.99A/C1-297[»]
4EOQX-ray2.15A/C1-297[»]
4EORX-ray2.20A/C1-297[»]
4EOSX-ray2.57A/C1-297[»]
4ERWX-ray2.00A1-298[»]
4EZ3X-ray2.00A1-298[»]
4EZ7X-ray2.49A1-298[»]
4FKGX-ray1.51A1-298[»]
4FKIX-ray1.60A1-298[»]
4FKJX-ray1.63A1-298[»]
4FKLX-ray1.26A1-298[»]
4FKOX-ray1.55A1-298[»]
4FKPX-ray1.60A1-298[»]
4FKQX-ray1.75A1-298[»]
4FKRX-ray1.90A1-298[»]
4FKSX-ray1.55A1-298[»]
4FKTX-ray1.60A1-298[»]
4FKUX-ray1.47A1-298[»]
4FKVX-ray1.70A1-298[»]
4FKWX-ray1.80A1-298[»]
4FX3X-ray2.75A/C1-298[»]
4GCJX-ray1.42A1-298[»]
4I3ZX-ray2.05A/C1-296[»]
4II5X-ray2.15A/C1-298[»]
4KD1X-ray1.70A1-298[»]
4LYNX-ray2.00A1-298[»]
4NJ3X-ray1.85A1-298[»]
4RJ3X-ray1.63A1-298[»]
5A14X-ray2.00A1-298[»]
5ANDX-ray2.30A1-298[»]
5ANEX-ray1.70A1-298[»]
5ANGX-ray1.90A1-298[»]
5ANIX-ray1.90A1-298[»]
5ANJX-ray1.60A1-298[»]
5ANKX-ray1.90A1-298[»]
5ANOX-ray1.70A1-298[»]
5CYIX-ray2.00A/C1-298[»]
5D1JX-ray1.80A1-298[»]
5FP5X-ray2.16A1-298[»]
5FP6X-ray1.85A1-298[»]
5IEVX-ray2.03A1-298[»]
5IEXX-ray2.03A1-298[»]
5IEYX-ray1.66A1-298[»]
5IF1X-ray2.61A/C1-298[»]
5JQ5X-ray1.94A1-298[»]
5JQ8X-ray1.94A1-298[»]
5K4JX-ray1.60A1-298[»]
5L2WX-ray2.80A1-298[»]
5LMKX-ray2.40A1-298[»]
C1-296[»]
5NEVX-ray2.97A/C1-298[»]
ProteinModelPortaliP24941.
SMRiP24941.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24941.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 286Protein kinasePROSITE-ProRule annotationAdd BLAST283

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0594. Eukaryota.
ENOG410XPP3. LUCA.
GeneTreeiENSGT00830000128256.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP24941.
KOiK02206.
PhylomeDBiP24941.
TreeFamiTF101021.

Family and domain databases

InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P24941-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR 
        60         70         80         90        100
EISLLKELNH PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP 
       110        120        130        140        150
LPLIKSYLFQ LLQGLAFCHS HRVLHRDLKP QNLLINTEGA IKLADFGLAR 
       160        170        180        190        200
AFGVPVRTYT HEVVTLWYRA PEILLGCKYY STAVDIWSLG CIFAEMVTRR 
       210        220        230        240        250
ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF PKWARQDFSK 
       260        270        280        290 
VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL
Length:298
Mass (Da):33,930
Last modified:August 1, 1992 - v2
Checksum:iF90A0F4E70910B51
GO
Isoform 2 (identifier: P24941-2) [UniParc]FASTAAdd to basket
Also known as: CDK2deltaT

The sequence of this isoform differs from the canonical sequence as follows:
     163-196: Missing.

Show »
Length:264
Mass (Da):30,035
Checksum:i50CE890992AC71EE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8 – 12EKIGE → AQIGQ in BAA32794 (Ref. 5) Curated5
Sequence conflicti25 – 29LTGEV → STGQM in BAA32794 (Ref. 5) Curated5
Sequence conflicti272 – 277NKRISA → YKRFST in BAA32794 (Ref. 5) Curated6
Sequence conflicti286 – 287FQ → LE in BAA32794 (Ref. 5) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01615715Y → S. Corresponds to variant dbSNP:rs3087335Ensembl.1
Natural variantiVAR_05392718V → L. Corresponds to variant dbSNP:rs11554376Ensembl.1
Natural variantiVAR_04197245P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_019988290T → S2 PublicationsCorresponds to variant dbSNP:rs2069413Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041998163 – 196Missing in isoform 2. CuratedAdd BLAST34

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61622 mRNA. Translation: CAA43807.1.
X62071 mRNA. Translation: CAA43985.1.
M68520 mRNA. Translation: AAA35667.1.
AB012305 mRNA. Translation: BAA32794.1.
BT006821 mRNA. Translation: AAP35467.1.
AF512553 Genomic DNA. Translation: AAM34794.1.
AK291941 mRNA. Translation: BAF84630.1.
AC025162 Genomic DNA. No translation available.
AC034102 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96858.1.
BC003065 mRNA. Translation: AAH03065.1.
CCDSiCCDS8898.1. [P24941-1]
CCDS8899.1. [P24941-2]
PIRiA41227.
RefSeqiNP_001277159.1. NM_001290230.1.
NP_001789.2. NM_001798.4. [P24941-1]
NP_439892.2. NM_052827.3. [P24941-2]
UniGeneiHs.19192.
Hs.689624.

Genome annotation databases

EnsembliENST00000266970; ENSP00000266970; ENSG00000123374. [P24941-1]
ENST00000354056; ENSP00000243067; ENSG00000123374. [P24941-2]
GeneIDi1017.
KEGGihsa:1017.
UCSCiuc001sit.5. human. [P24941-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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 one 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.

Entry informationi

Entry nameiCDK2_HUMAN
AccessioniPrimary (citable) accession number: P24941
Secondary accession number(s): A8K7C6, O75100
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: August 1, 1992
Last modified: July 5, 2017
This is version 221 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families