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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. Interacts with cyclins A, B1, B3, D, or E. 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).By similarity17 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei9 – 91CDK7 binding
Binding sitei33 – 331ATPPROSITE-ProRule annotation2 Publications
Binding sitei86 – 861ATPPROSITE-ProRule annotation2 Publications
Sitei88 – 892CDK7 binding
Active sitei127 – 1271Proton acceptor
Metal bindingi132 – 1321Magnesium1 Publication
Metal bindingi145 – 1451Magnesium1 Publication
Binding sitei145 – 1451ATPPROSITE-ProRule annotation2 Publications
Sitei166 – 1661CDK7 binding

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 189ATPPROSITE-ProRule annotation2 Publications
Nucleotide bindingi81 – 833ATPPROSITE-ProRule annotation2 Publications
Nucleotide bindingi129 – 1324ATPPROSITE-ProRule annotation2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cyclin binding Source: UniProtKB
  • cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  • kinase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Meiosis, Mitosis

Keywords - Ligandi

ATP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
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-dependent protein kinase holoenzyme complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91K → F: Reduced phosphorylation by CAK. 1 Publication
Mutagenesisi14 – 141T → A: 2-fold increase in activity. 1 Publication
Mutagenesisi15 – 151Y → F: 2-fold increase in activity. 1 Publication
Mutagenesisi88 – 892KK → EV: Reduced phosphorylation by CAK. 1 Publication
Mutagenesisi160 – 1601T → A: Abolishes activity. 1 Publication
Mutagenesisi166 – 1661L → R: Reduced phosphorylation by CAK and reduced kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA101.

Chemistry

ChEMBLiCHEMBL2094126.
DrugBankiDB06616. Bosutinib.
GuidetoPHARMACOLOGYi1973.

Polymorphism and mutation databases

BioMutaiCDK2.
DMDMi116051.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Cyclin-dependent kinase 2PRO_0000085769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei6 – 61N6-acetyllysineCombined sources
Modified residuei14 – 141Phosphothreonine2 Publications
Modified residuei15 – 151Phosphotyrosine; by WEE1Combined sources2 Publications
Modified residuei19 – 191PhosphotyrosineCombined sources
Modified residuei160 – 1601Phosphothreonine; by CAK and CCRK8 Publications

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.10 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.
PhosphoSiteiP24941.
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).By similarity27 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNA2P2024824EBI-375096,EBI-457097
CCNB2O950672EBI-375096,EBI-375024
CCND1P243853EBI-375096,EBI-375001
CCNE1P2486416EBI-375096,EBI-519526
CCNE2O960209EBI-375096,EBI-375033
CCNHP519463EBI-375096,EBI-741406
CDKN1AP3893619EBI-375096,EBI-375077
CDKN1BP4652720EBI-375096,EBI-519280
CDKN3Q166676EBI-375096,EBI-1031527
CKS1BP610246EBI-375096,EBI-456371
E7P031292EBI-375096,EBI-866453From a different organism.
EP300Q094725EBI-375096,EBI-447295
FBXW7Q969H0-42EBI-375096,EBI-6502391
Ifi205bQ086192EBI-375096,EBI-8064290From a different organism.
IKBKGQ9Y6K94EBI-375096,EBI-81279
MAPK15Q8TD084EBI-375096,EBI-1383794
RB1P064003EBI-375096,EBI-491274
STOML1Q9UBI42EBI-375096,EBI-2681162
UHRF2Q96PU45EBI-375096,EBI-625304

GO - Molecular functioni

  • cyclin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107452. 670 interactions.
DIPiDIP-161N.
IntActiP24941. 150 interactions.
MINTiMINT-96328.
STRINGi9606.ENSP00000266970.

Chemistry

BindingDBiP24941.

Structurei

Secondary structure

298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 33Combined sources
Beta strandi4 – 129Combined sources
Beta strandi14 – 2310Combined sources
Turni24 – 263Combined sources
Beta strandi29 – 357Combined sources
Beta strandi39 – 413Combined sources
Beta strandi42 – 443Combined sources
Helixi46 – 549Combined sources
Helixi55 – 573Combined sources
Beta strandi66 – 727Combined sources
Beta strandi75 – 817Combined sources
Beta strandi84 – 863Combined sources
Helixi87 – 937Combined sources
Turni94 – 974Combined sources
Helixi101 – 12020Combined sources
Helixi130 – 1323Combined sources
Beta strandi133 – 1353Combined sources
Turni137 – 1393Combined sources
Beta strandi141 – 1433Combined sources
Helixi148 – 1525Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1613Combined sources
Helixi162 – 1687Combined sources
Helixi171 – 1744Combined sources
Beta strandi178 – 1803Combined sources
Helixi183 – 19816Combined sources
Helixi208 – 21912Combined sources
Turni224 – 2263Combined sources
Helixi230 – 2323Combined sources
Helixi248 – 2514Combined sources
Beta strandi252 – 2543Combined sources
Helixi257 – 26610Combined sources
Turni271 – 2733Combined sources
Helixi277 – 2815Combined sources
Helixi284 – 2863Combined sources
Turni287 – 2893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24941.
SMRiP24941. Positions 1-298.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24941.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 286283Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 125EKIGE → AQIGQ in BAA32794 (Ref. 5) Curated
Sequence conflicti25 – 295LTGEV → STGQM in BAA32794 (Ref. 5) Curated
Sequence conflicti272 – 2776NKRISA → YKRFST in BAA32794 (Ref. 5) Curated
Sequence conflicti286 – 2872FQ → LE in BAA32794 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151Y → S.
Corresponds to variant rs3087335 [ dbSNP | Ensembl ].
VAR_016157
Natural varianti18 – 181V → L.
Corresponds to variant rs11554376 [ dbSNP | Ensembl ].
VAR_053927
Natural varianti45 – 451P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041972
Natural varianti290 – 2901T → S.2 Publications
Corresponds to variant rs2069413 [ dbSNP | Ensembl ].
VAR_019988

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 19634Missing in isoform 2. CuratedVSP_041998Add
BLAST

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

Cross-referencesi

Web resourcesi

NIEHS-SNPs

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP24941.
SMRiP24941. Positions 1-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107452. 670 interactions.
DIPiDIP-161N.
IntActiP24941. 150 interactions.
MINTiMINT-96328.
STRINGi9606.ENSP00000266970.

Chemistry

BindingDBiP24941.
ChEMBLiCHEMBL2094126.
DrugBankiDB06616. Bosutinib.
GuidetoPHARMACOLOGYi1973.

PTM databases

iPTMnetiP24941.
PhosphoSiteiP24941.
SwissPalmiP24941.

Polymorphism and mutation databases

BioMutaiCDK2.
DMDMi116051.

Proteomic databases

EPDiP24941.
MaxQBiP24941.
PaxDbiP24941.
PeptideAtlasiP24941.
PRIDEiP24941.

Protocols and materials databases

DNASUi1017.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1017.
GeneCardsiCDK2.
HGNCiHGNC:1771. CDK2.
HPAiCAB013115.
HPA066915.
MIMi116953. gene.
neXtProtiNX_P24941.
PharmGKBiPA101.
GenAtlasiSearch...

Phylogenomic databases

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

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.

Miscellaneous databases

ChiTaRSiCDK2. human.
EvolutionaryTraceiP24941.
GeneWikiiCyclin-dependent_kinase_2.
GenomeRNAii1017.
PROiP24941.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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...

Entry informationi

Entry nameiCDK2_HUMAN
AccessioniPrimary (citable) accession number: P24941
Secondary accession number(s): A8K7C6, O75100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: August 1, 1992
Last modified: September 7, 2016
This is version 212 of the entry and version 2 of the sequence. [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

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.