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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.

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 – 1321Magnesium; catalytic1 Publication
Metal bindingi145 – 1451Magnesium; catalytic1 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

  1. ATP binding Source: UniProtKB-KW
  2. cyclin binding Source: UniProtKB
  3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. blood coagulation Source: Reactome
  3. cell division Source: UniProtKB-KW
  4. cellular response to nitric oxide Source: UniProtKB
  5. centrosome duplication Source: UniProtKB
  6. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  7. DNA repair Source: UniProtKB-KW
  8. DNA replication Source: UniProtKB
  9. G1/S transition of mitotic cell cycle Source: Reactome
  10. G2/M transition of mitotic cell cycle Source: UniProtKB
  11. histone phosphorylation Source: GOC
  12. meiotic nuclear division Source: UniProtKB
  13. mitotic cell cycle Source: Reactome
  14. mitotic G1 DNA damage checkpoint Source: UniProtKB
  15. mitotic nuclear division Source: UniProtKB-KW
  16. peptidyl-serine phosphorylation Source: UniProtKB
  17. positive regulation of cell proliferation Source: UniProtKB
  18. positive regulation of DNA-dependent DNA replication initiation Source: Ensembl
  19. positive regulation of transcription, DNA-templated Source: Ensembl
  20. potassium ion transport Source: Ensembl
  21. Ras protein signal transduction Source: BHF-UCL
  22. regulation of gene silencing Source: UniProtKB
  23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
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.
ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1625. p53-Dependent G1 DNA Damage Response.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_27271. Meiotic recombination.
REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP24941.

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
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:1771. CDK2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. NucleusCajal body. Cytoplasm. Endosome
Note: Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cytoplasmic trafficking is mediated during the inhibition by 1,25-(OH)2D3.

GO - Cellular componenti

  1. Cajal body Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. chromosome, telomeric region Source: Ensembl
  4. condensed chromosome Source: Ensembl
  5. cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  6. cytoplasm Source: UniProtKB
  7. cytosol Source: Reactome
  8. endosome Source: UniProtKB
  9. nucleoplasm Source: Reactome
  10. nucleus Source: UniProtKB
  11. transcription factor complex Source: Ensembl
  12. X chromosome Source: Ensembl
  13. 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.

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-acetylmethionine2 Publications
Modified residuei6 – 61N6-acetyllysine1 Publication
Modified residuei14 – 141Phosphothreonine2 Publications
Modified residuei15 – 151Phosphotyrosine; by WEE13 Publications
Modified residuei19 – 191Phosphotyrosine1 Publication
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

MaxQBiP24941.
PaxDbiP24941.
PRIDEiP24941.

PTM databases

PhosphoSiteiP24941.

Expressioni

Inductioni

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

Gene expression databases

BgeeiP24941.
CleanExiHS_CDK2.
ExpressionAtlasiP24941. baseline and differential.
GenevestigatoriP24941.

Organism-specific databases

HPAiCAB013115.

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
CCNA2P2024819EBI-375096,EBI-457097
CCNB2O950672EBI-375096,EBI-375024
CCNE1P2486410EBI-375096,EBI-519526
CCNE2O960207EBI-375096,EBI-375033
CCNHP519462EBI-375096,EBI-741406
CDKN1AP3893614EBI-375096,EBI-375077
CDKN1BP4652716EBI-375096,EBI-519280
CDKN3Q166673EBI-375096,EBI-1031527
CKS1BP610243EBI-375096,EBI-456371
EP300Q094725EBI-375096,EBI-447295
FBXW7Q969H0-42EBI-375096,EBI-6502391
Ifi205bQ086192EBI-375096,EBI-8064290From a different organism.
IKBKGQ9Y6K94EBI-375096,EBI-81279
RB1P064003EBI-375096,EBI-491274
STOML1Q9UBI42EBI-375096,EBI-2681162
UHRF2Q96PU45EBI-375096,EBI-625304

Protein-protein interaction databases

BioGridi107452. 581 interactions.
DIPiDIP-161N.
IntActiP24941. 67 interactions.
MINTiMINT-96328.
STRINGi9606.ENSP00000266970.

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[»]
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[»]
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

eggNOGiCOG0515.
GeneTreeiENSGT00780000121869.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP24941.
KOiK02206.
OrthoDBiEOG7966H8.
PhylomeDBiP24941.
TreeFamiTF101021.

Family and domain databases

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

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:July 31, 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.4. human. [P24941-1]
uc001siu.4. human. [P24941-2]

Polymorphism databases

DMDMi116051.

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[»]
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[»]
ProteinModelPortaliP24941.
SMRiP24941. Positions 1-298.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107452. 581 interactions.
DIPiDIP-161N.
IntActiP24941. 67 interactions.
MINTiMINT-96328.
STRINGi9606.ENSP00000266970.

Chemistry

BindingDBiP24941.
ChEMBLiCHEMBL1907605.
DrugBankiDB06616. Bosutinib.
GuidetoPHARMACOLOGYi1973.

PTM databases

PhosphoSiteiP24941.

Polymorphism databases

DMDMi116051.

Proteomic databases

MaxQBiP24941.
PaxDbiP24941.
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.4. human. [P24941-1]
uc001siu.4. human. [P24941-2]

Organism-specific databases

CTDi1017.
GeneCardsiGC12P056360.
HGNCiHGNC:1771. CDK2.
HPAiCAB013115.
MIMi116953. gene.
neXtProtiNX_P24941.
PharmGKBiPA101.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00780000121869.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP24941.
KOiK02206.
OrthoDBiEOG7966H8.
PhylomeDBiP24941.
TreeFamiTF101021.

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_111214. G0 and Early G1.
REACT_1156. Orc1 removal from chromatin.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1625. p53-Dependent G1 DNA Damage Response.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1915. G2 Phase.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_27271. Meiotic recombination.
REACT_308. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
SignaLinkiP24941.

Miscellaneous databases

ChiTaRSiCDK2. human.
EvolutionaryTraceiP24941.
GeneWikiiCyclin-dependent_kinase_2.
GenomeRNAii1017.
NextBioi4273.
PROiP24941.
SOURCEiSearch...

Gene expression databases

BgeeiP24941.
CleanExiHS_CDK2.
ExpressionAtlasiP24941. baseline and differential.
GenevestigatoriP24941.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "A new human p34 protein kinase, CDK2, identified by complementation of a cdc28 mutation in Saccharomyces cerevisiae, is a homolog of Xenopus Eg1."
    Elledge S.J., Spottswood M.R.
    EMBO J. 10:2653-2659(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase."
    Tsai L.-H., Harlow E., Meyerson M.
    Nature 353:174-177(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation."
    Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S.I., Matsumoto K.
    Proc. Natl. Acad. Sci. U.S.A. 88:9006-9010(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Sequence of deletion type cdk2 variant in human breast cancer."
    Nishikawa T., Ohta T., Fukuda M., Ogata H., Okamoto K., Isohashi F., Arima K., Yamaguchi S.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. NIEHS SNPs program
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-290.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  11. "Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15."
    Gu Y., Rosenblatt J., O'Morgan D.O.
    EMBO J. 11:3995-4005(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160, MUTAGENESIS OF THR-14; TYR-15 AND THR-160.
  12. "Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 and cdk5."
    Meijer L., Borgne A., Mulner O., Chong J.P.J., Blow J.J., Inagaki N., Inagaki M., Delcros J.-G., Moulinoux J.-P.
    Eur. J. Biochem. 243:527-536(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION BY ROSCOVITINE AND OLOMOUCINE.
  13. "Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1."
    Harbour J.W., Luo R.X., Dei Santi A., Postigo A.A., Dean D.C.
    Cell 98:859-869(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS RB1 KINASE, INTERACTION WITH CYCLIN E.
  14. Cited for: FUNCTION AS NPM1 KINASE.
  15. "NPAT links cyclin E-Cdk2 to the regulation of replication-dependent histone gene transcription."
    Zhao J., Kennedy B.K., Lawrence B.D., Barbie D.A., Matera A.G., Fletcher J.A., Harlow E.
    Genes Dev. 14:2283-2297(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NPAT KINASE.
  16. "Cell cycle-regulated phosphorylation of p220(NPAT) by cyclin E/Cdk2 in Cajal bodies promotes histone gene transcription."
    Ma T., Van Tine B.A., Wei Y., Garrett M.D., Nelson D., Adams P.D., Wang J., Qin J., Chow L.T., Harper J.W.
    Genes Dev. 14:2298-2313(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NPAT KINASE, SUBCELLULAR LOCATION.
  17. "The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A."
    Luciani M.G., Hutchins J.R.A., Zheleva D., Hupp T.R.
    J. Mol. Biol. 300:503-518(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS P53/TP53 KINASE, INTERACTION WITH CYCLIN A AND CYCLIN B1.
  18. "Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop."
    Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.
    Mol. Cell. Biol. 21:88-99(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS CDK7 KINASE, PHOSPHORYLATION BY CDK7.
  19. "Characterization and expression of mammalian cyclin b3, a prepachytene meiotic cyclin."
    Nguyen T.B., Manova K., Capodieci P., Lindon C., Bottega S., Wang X.-Y., Refik-Rogers J., Pines J., Wolgemuth D.J., Koff A.
    J. Biol. Chem. 277:41960-41969(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNB3.
  20. "Human Speedy: a novel cell cycle regulator that enhances proliferation through activation of Cdk2."
    Porter L.A., Dellinger R.W., Tynan J.A., Barnes E.A., Kong M., Lenormand J.-L., Donoghue D.J.
    J. Cell Biol. 157:357-366(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA.
  21. "Human Spy1 promotes survival of mammalian cells following DNA damage."
    Barnes E.A., Porter L.A., Lenormand J.-L., Dellinger R.W., Donoghue D.J.
    Cancer Res. 63:3701-3707(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA.
  22. "Spy1 interacts with p27Kip1 to allow G1/S progression."
    Porter L.A., Kong-Beltran M., Donoghue D.J.
    Mol. Biol. Cell 14:3664-3674(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA, IDENTIFICATION IN A COMPLEX WITH CDKN1B AND SPDYA.
  23. Cited for: INTERACTION WITH UHRF2, IDENTIFICATION IN A COMPLEX WITH UHRF2 AND CCNE1.
  24. "Liver tumors escape negative control of proliferation via PI3K/Akt-mediated block of C/EBP alpha growth inhibitory activity."
    Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.
    Genes Dev. 18:912-925(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEBPA.
  25. "p42, a novel cyclin-dependent kinase-activating kinase in mammalian cells."
    Liu Y., Wu C., Galaktionov K.
    J. Biol. Chem. 279:4507-4514(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-160.
  26. "Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins."
    Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.
    Cell Cycle 4:155-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPDYA AND SPDYC.
  27. "CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair."
    Esashi F., Christ N., Gannon J., Liu Y., Hunt T., Jasin M., West S.C.
    Nature 434:598-604(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS BRCA2 KINASE.
  28. Cited for: PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND LEU-166, INTERACTION WITH CDK7.
  29. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: FUNCTION IN MITOSE REGULATION, SUBCELLULAR LOCATION.
  31. "Identification and characterization of CAC1 as a novel CDK2-associated cullin."
    Kong Y., Nan K., Yin Y.
    Cell Cycle 8:3544-3553(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACUL1.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Nuclear targeting of cyclin-dependent kinase 2 reveals essential roles of cyclin-dependent kinase 2 localization and cyclin E in vitamin D-mediated growth inhibition."
    Flores O., Wang Z., Knudsen K.E., Burnstein K.L.
    Endocrinology 151:896-908(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-160.
  36. "Cdk2 nitrosylation and loss of mitochondrial potential mediate NO-dependent biphasic effect on HL-60 cell cycle."
    Kumar S., Barthwal M.K., Dikshit M.
    Free Radic. Biol. Med. 48:851-861(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, S-NITROSYLATION.
  37. "Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at the G2/M transition."
    Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.
    J. Biol. Chem. 285:16978-16990(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-160 BY CAK, DEPHOSPHORYLATION BY CDC25A.
  38. "Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2."
    Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A., Simon J.A., Huang H.
    Nat. Cell Biol. 12:1108-1114(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS EZH2 KINASE.
  39. "Cdk2 is required for p53-independent G2/M checkpoint control."
    Chung J.H., Bunz F.
    PLoS Genet. 6:E1000863-E1000863(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA DAMAGE CHECKPOINT.
  40. Cited for: FUNCTION AS MYC KINASE.
  41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  42. "Cep63 recruits Cdk1 to the centrosome: implications for regulation of mitotic entry, centrosome amplification, and genome maintenance."
    Loffler H., Fechter A., Matuszewska M., Saffrich R., Mistrik M., Marhold J., Hornung C., Westermann F., Bartek J., Kramer A.
    Cancer Res. 71:2129-2139(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEP63.
  43. "Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization."
    Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.
    Cell. Signal. 23:911-919(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, INTERACTION WITH PTPN6 AND CTNNB1.
  44. "Discovery of a novel class of 2-aminopyrimidines as CDK1 and CDK2 inhibitors."
    Lee J., Kim K.H., Jeong S.
    Bioorg. Med. Chem. Lett. 21:4203-4205(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITORS.
  45. "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry."
    Huang X., Summers M.K., Pham V., Lill J.R., Liu J., Lee G., Kirkpatrick D.S., Jackson P.K., Fang G., Dixit V.M.
    Mol. Cell 42:511-523(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS USP37 KINASE.
  46. "An important role for CDK2 in G1 to S checkpoint activation and DNA damage response in human embryonic stem cells."
    Neganova I., Vilella F., Atkinson S.P., Lloret M., Passos J.F., von Zglinicki T., O'Connor J.-E., Burks D., Jones R., Armstrong L., Lako M.
    Stem Cells 29:651-659(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE REGULATION.
  47. "A dual role of Cdk2 in DNA damage response."
    Satyanarayana A., Kaldis P.
    Cell Div. 4:9-9(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON DNA REPAIR, INTERACTION WITH CDKN1A/P21.
  48. "Cell cycle, CDKs and cancer: a changing paradigm."
    Malumbres M., Barbacid M.
    Nat. Rev. Cancer 9:153-166(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON CELL CYCLE CONTROL, INHIBITORS, GENE FAMILY.
  49. "Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms."
    Satyanarayana A., Kaldis P.
    Oncogene 28:2925-2939(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, GENE FAMILY.
  50. "Tipping the balance: Cdk2 enables Myc to suppress senescence."
    Hydbring P., Larsson L.-G.
    Cancer Res. 70:6687-6691(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON SENESCENCE.
  51. "Cyclin dependent kinase 1 inhibitors: a review of recent progress."
    Wang Q., Su L., Liu N., Zhang L., Xu W., Fang H.
    Curr. Med. Chem. 18:2025-2043(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON INHIBITORS.
  52. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  53. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  54. "Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex."
    Jeffrey P.D., Russo A.A., Polyak K., Gibbs E., Hurwitz J., Massague J., Pavletich N.P.
    Nature 376:313-320(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CYCLIN A.
  55. "Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1."
    Bourne Y., Watson M.H., Hickey M.J., Holmes W., Rocque W., Reed S.I., Tainer J.A.
    Cell 84:863-874(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITG CKS1.
  56. "High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design."
    Schulze-Gahmen U., de Bondt H.L., Kim S.-H.
    J. Med. Chem. 39:4540-4546(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  57. "Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex."
    Russo A.A., Jeffrey P.D., Patten A.K., Massague J., Pavletich N.P.
    Nature 382:325-331(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CG2A AND KIP1.
  58. "Structural basis of cyclin-dependent kinase activation by phosphorylation."
    Russo A.A., Jeffrey P.D., Pavletich N.P.
    Nat. Struct. Biol. 3:696-700(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CG2A.
  59. "Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase."
    de Azevedo W.F. Jr., Mueller-Dieckmann H.-J., Schulze-Gahmen U., Worland P.J., Sausville E., Kim S.-H.
    Proc. Natl. Acad. Sci. U.S.A. 93:2735-2740(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH L868276.
  60. "Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2."
    Lawrie A.M., Noble M.E.M., Tunnah P., Brown N.R., Johnson L.N., Endicott J.A.
    Nat. Struct. Biol. 4:796-801(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE, ENZYME REGULATION.
  61. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
  62. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
  63. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
  64. "Cyclin B and cyclin A confer different substrate recognition properties on CDK2."
    Brown N.R., Lowe E.D., Petri E., Skamnaki V., Antrobus R., Johnson L.N.
    Cell Cycle 6:1350-1359(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, FUNCTION.
  65. "How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A."
    Welburn J.P.I., Tucker J.A., Johnson T., Lindert L., Morgan M., Willis A., Noble M.E.M., Endicott J.A.
    J. Biol. Chem. 282:3173-3181(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP, PHOSPHORYLATION AT THR-14; TYR-15 AND THR-160.
  66. Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  67. "Identification of N-(4-piperidinyl)-4-(2,6-dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-ray crystallography and structure based drug design."
    Wyatt P.G., Woodhead A.J., Berdini V., Boulstridge J.A., Carr M.G., Cross D.M., Davis D.J., Devine L.A., Early T.R., Feltell R.E., Lewis E.J., McMenamin R.L., Navarro E.F., O'Brien M.A., O'Reilly M., Reule M., Saxty G., Seavers L.C.
    , Smith D.M., Squires M.S., Trewartha G., Walker M.T., Woolford A.J.
    J. Med. Chem. 51:4986-4999(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
  68. "Briefly bound to activate: transient binding of a second catalytic magnesium activates the structure and dynamics of CDK2 kinase for catalysis."
    Bao Z.Q., Jacobsen D.M., Young M.A.
    Structure 19:675-690(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-296 IN COMPLEX WITH ATP AND MAGNESIUM, PHOSPHORYLATION AT THR-160.
  69. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.
  70. "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and Nod2-mediated inflammatory responses."
    Menning M., Kufer T.A.
    FEBS Lett. 587:2137-2142(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD17.

Entry informationi

Entry nameiCDK2_HUMAN
AccessioniPrimary (citable) accession number: P24941
Secondary accession number(s): A8K7C6, O75100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 29, 1992
Last sequence update: July 31, 1992
Last modified: March 31, 2015
This is version 196 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

External Data

Dasty 3

Similar proteinsi

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