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P24941

- CDK2_HUMAN

UniProt

P24941 - CDK2_HUMAN

Protein

Cyclin-dependent kinase 2

Gene

CDK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    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.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 – 331ATP2 PublicationsPROSITE-ProRule annotation
    Binding sitei86 – 861ATP2 PublicationsPROSITE-ProRule annotation
    Sitei88 – 892CDK7 binding
    Active sitei127 – 1271Proton acceptor
    Metal bindingi132 – 1321Magnesium; catalytic1 Publication
    Metal bindingi145 – 1451Magnesium; catalytic1 Publication
    Binding sitei145 – 1451ATP2 PublicationsPROSITE-ProRule annotation
    Sitei166 – 1661CDK7 binding

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATP2 PublicationsPROSITE-ProRule annotation
    Nucleotide bindingi81 – 833ATP2 PublicationsPROSITE-ProRule annotation
    Nucleotide bindingi129 – 1324ATP2 PublicationsPROSITE-ProRule annotation

    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
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. blood coagulation Source: Reactome
    3. cellular response to nitric oxide Source: UniProtKB
    4. centrosome duplication Source: UniProtKB
    5. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    6. DNA repair Source: UniProtKB-KW
    7. DNA replication Source: UniProtKB
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. G2/M transition of mitotic cell cycle Source: UniProtKB
    10. histone phosphorylation Source: GOC
    11. meiotic nuclear division Source: UniProtKB
    12. mitotic cell cycle Source: Reactome
    13. mitotic G1 DNA damage checkpoint Source: UniProtKB
    14. mitotic G2 phase Source: Reactome
    15. mitotic nuclear division Source: UniProtKB-KW
    16. positive regulation of cell proliferation Source: UniProtKB
    17. positive regulation of DNA-dependent DNA replication initiation Source: Ensembl
    18. positive regulation of transcription, DNA-templated Source: Ensembl
    19. potassium ion transport Source: Ensembl
    20. Ras protein signal transduction Source: BHF-UCL
    21. regulation of gene silencing Source: UniProtKB
    22. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome

    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_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: 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

    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.
    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.12 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

    ArrayExpressiP24941.
    BgeeiP24941.
    CleanExiHS_CDK2.
    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.By similarity25 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. 569 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 – 33
    Beta strandi4 – 129
    Beta strandi14 – 2310
    Turni24 – 263
    Beta strandi29 – 357
    Beta strandi39 – 413
    Beta strandi42 – 443
    Helixi46 – 549
    Helixi55 – 573
    Beta strandi66 – 727
    Beta strandi75 – 817
    Beta strandi84 – 863
    Helixi87 – 937
    Turni94 – 974
    Helixi101 – 12020
    Helixi130 – 1323
    Beta strandi133 – 1353
    Turni137 – 1393
    Beta strandi141 – 1433
    Helixi148 – 1525
    Helixi156 – 1583
    Beta strandi159 – 1613
    Helixi162 – 1687
    Helixi171 – 1744
    Beta strandi178 – 1803
    Helixi183 – 19816
    Helixi208 – 21912
    Turni224 – 2263
    Helixi230 – 2323
    Helixi248 – 2514
    Beta strandi252 – 2543
    Helixi257 – 26610
    Turni271 – 2733
    Helixi277 – 2815
    Helixi284 – 2863
    Turni287 – 2893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    4CFNX-ray2.20A/C1-298[»]
    4CFWX-ray2.45A/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[»]
    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.
    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_dom.
    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. Align

    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

    MENFQKVEKI GEGTYGVVYK ARNKLTGEVV ALKKIRLDTE TEGVPSTAIR    50
    EISLLKELNH PNIVKLLDVI HTENKLYLVF EFLHQDLKKF MDASALTGIP 100
    LPLIKSYLFQ LLQGLAFCHS HRVLHRDLKP QNLLINTEGA IKLADFGLAR 150
    AFGVPVRTYT HEVVTLWYRA PEILLGCKYY STAVDIWSLG CIFAEMVTRR 200
    ALFPGDSEID QLFRIFRTLG TPDEVVWPGV TSMPDYKPSF PKWARQDFSK 250
    VVPPLDEDGR SLLSQMLHYD PNKRISAKAA LAHPFFQDVT KPVPHLRL 298
    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. 1 PublicationCurated
    Sequence conflicti25 – 295LTGEV → STGQM in BAA32794. 1 PublicationCurated
    Sequence conflicti272 – 2776NKRISA → YKRFST in BAA32794. 1 PublicationCurated
    Sequence conflicti286 – 2872FQ → LE in BAA32794. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8898.1. [P24941-1 ]
    CCDS8899.1. [P24941-2 ]
    PIRi A41227.
    RefSeqi NP_001277159.1. NM_001290230.1.
    NP_001789.2. NM_001798.4. [P24941-1 ]
    NP_439892.2. NM_052827.3. [P24941-2 ]
    UniGenei Hs.19192.
    Hs.689624.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AQ1 X-ray 2.00 A 1-298 [» ]
    1B38 X-ray 2.00 A 1-298 [» ]
    1B39 X-ray 2.10 A 1-298 [» ]
    1BUH X-ray 2.60 A 1-298 [» ]
    1CKP X-ray 2.05 A 1-298 [» ]
    1DI8 X-ray 2.20 A 1-298 [» ]
    1DM2 X-ray 2.10 A 1-298 [» ]
    1E1V X-ray 1.95 A 1-298 [» ]
    1E1X X-ray 1.85 A 1-298 [» ]
    1E9H X-ray 2.50 A/C 1-296 [» ]
    1F5Q X-ray 2.50 A/C 1-298 [» ]
    1FIN X-ray 2.30 A/C 1-298 [» ]
    1FQ1 X-ray 3.00 B 1-298 [» ]
    1FVT X-ray 2.20 A 1-298 [» ]
    1FVV X-ray 2.80 A/C 1-298 [» ]
    1G5S X-ray 2.61 A 1-298 [» ]
    1GIH X-ray 2.80 A 1-298 [» ]
    1GII X-ray 2.00 A 1-298 [» ]
    1GIJ X-ray 2.20 A 1-298 [» ]
    1GY3 X-ray 2.70 A/C 1-296 [» ]
    1GZ8 X-ray 1.30 A 1-298 [» ]
    1H00 X-ray 1.60 A 1-298 [» ]
    1H01 X-ray 1.79 A 1-298 [» ]
    1H07 X-ray 1.85 A 1-298 [» ]
    1H08 X-ray 1.80 A 1-298 [» ]
    1H0V X-ray 1.90 A 1-298 [» ]
    1H0W X-ray 2.10 A 1-298 [» ]
    1H1P X-ray 2.10 A/C 1-298 [» ]
    1H1Q X-ray 2.50 A/C 1-298 [» ]
    1H1R X-ray 2.00 A/C 1-298 [» ]
    1H1S X-ray 2.00 A/C 1-298 [» ]
    1H24 X-ray 2.50 A/C 1-298 [» ]
    1H25 X-ray 2.50 A/C 1-298 [» ]
    1H26 X-ray 2.24 A/C 1-298 [» ]
    1H27 X-ray 2.20 A/C 1-298 [» ]
    1H28 X-ray 2.80 A/C 1-298 [» ]
    1HCK X-ray 1.90 A 1-298 [» ]
    1HCL X-ray 1.80 A 1-298 [» ]
    1JST X-ray 2.60 A/C 1-298 [» ]
    1JSU X-ray 2.30 A 1-298 [» ]
    1JSV X-ray 1.96 A 1-298 [» ]
    1JVP X-ray 1.53 P 1-298 [» ]
    1KE5 X-ray 2.20 A 1-298 [» ]
    1KE6 X-ray 2.00 A 1-298 [» ]
    1KE7 X-ray 2.00 A 1-298 [» ]
    1KE8 X-ray 2.00 A 1-298 [» ]
    1KE9 X-ray 2.00 A 1-298 [» ]
    1OGU X-ray 2.60 A/C 1-298 [» ]
    1OI9 X-ray 2.10 A/C 1-298 [» ]
    1OIQ X-ray 2.31 A 1-298 [» ]
    1OIR X-ray 1.91 A 1-298 [» ]
    1OIT X-ray 1.60 A 1-298 [» ]
    1OIU X-ray 2.00 A/C 1-298 [» ]
    1OIY X-ray 2.40 A/C 1-298 [» ]
    1OKV X-ray 2.40 A/C 1-298 [» ]
    1OKW X-ray 2.50 A/C 1-298 [» ]
    1OL1 X-ray 2.90 A/C 1-298 [» ]
    1OL2 X-ray 2.60 A/C 1-298 [» ]
    1P2A X-ray 2.50 A 1-298 [» ]
    1P5E X-ray 2.22 A/C 1-298 [» ]
    1PF8 X-ray 2.51 A 1-298 [» ]
    1PKD X-ray 2.30 A/C 1-296 [» ]
    1PW2 X-ray 1.95 A 1-298 [» ]
    1PXI X-ray 1.95 A 1-298 [» ]
    1PXJ X-ray 2.30 A 1-298 [» ]
    1PXK X-ray 2.80 A 1-298 [» ]
    1PXL X-ray 2.50 A 1-298 [» ]
    1PXM X-ray 2.53 A 1-298 [» ]
    1PXN X-ray 2.50 A 1-298 [» ]
    1PXO X-ray 1.96 A 1-298 [» ]
    1PXP X-ray 2.30 A 1-298 [» ]
    1PYE X-ray 2.00 A 1-298 [» ]
    1QMZ X-ray 2.20 A/C 1-298 [» ]
    1R78 X-ray 2.00 A 1-298 [» ]
    1URC X-ray 2.60 A/C 1-298 [» ]
    1URW X-ray 1.60 A 1-298 [» ]
    1V1K X-ray 2.31 A 1-298 [» ]
    1VYW X-ray 2.30 A/C 1-298 [» ]
    1VYZ X-ray 2.21 A 1-298 [» ]
    1W0X X-ray 2.20 C 1-298 [» ]
    1W8C X-ray 2.05 A 1-298 [» ]
    1W98 X-ray 2.15 A 1-297 [» ]
    1WCC X-ray 2.20 A 1-298 [» ]
    1Y8Y X-ray 2.00 A 1-298 [» ]
    1Y91 X-ray 2.15 A 1-298 [» ]
    1YKR X-ray 1.80 A 1-298 [» ]
    2A0C X-ray 1.95 X 1-298 [» ]
    2A4L X-ray 2.40 A 1-298 [» ]
    2B52 X-ray 1.88 A 1-298 [» ]
    2B53 X-ray 2.00 A 1-298 [» ]
    2B54 X-ray 1.85 A 1-298 [» ]
    2B55 X-ray 1.85 A 1-298 [» ]
    2BHE X-ray 1.90 A 1-298 [» ]
    2BHH X-ray 2.60 A 1-298 [» ]
    2BKZ X-ray 2.60 A/C 1-298 [» ]
    2BPM X-ray 2.40 A/C 1-298 [» ]
    2BTR X-ray 1.85 A 1-298 [» ]
    2BTS X-ray 1.99 A 1-298 [» ]
    2C4G X-ray 2.70 A/C 1-298 [» ]
    2C5N X-ray 2.10 A/C 1-298 [» ]
    2C5O X-ray 2.10 A/C 1-298 [» ]
    2C5V X-ray 2.90 A/C 1-298 [» ]
    2C5X X-ray 2.90 A/C 1-298 [» ]
    2C5Y X-ray 2.25 A 1-298 [» ]
    2C68 X-ray 1.95 A 1-298 [» ]
    2C69 X-ray 2.10 A 1-298 [» ]
    2C6I X-ray 1.80 A 1-298 [» ]
    2C6K X-ray 1.90 A 1-298 [» ]
    2C6L X-ray 2.30 A 1-298 [» ]
    2C6M X-ray 1.90 A 1-298 [» ]
    2C6O X-ray 2.10 A 1-298 [» ]
    2C6T X-ray 2.61 A/C 1-298 [» ]
    2CCH X-ray 1.70 A/C 1-298 [» ]
    2CCI X-ray 2.70 A/C 1-298 [» ]
    2CJM X-ray 2.30 A/C 1-298 [» ]
    2CLX X-ray 1.80 A 1-298 [» ]
    2DS1 X-ray 2.00 A 1-298 [» ]
    2DUV X-ray 2.20 A 1-298 [» ]
    2EXM X-ray 1.80 A 1-298 [» ]
    2FVD X-ray 1.85 A 1-298 [» ]
    2G9X X-ray 2.50 A/C 1-298 [» ]
    2HIC model - A 1-298 [» ]
    2I40 X-ray 2.80 A/C 1-298 [» ]
    2IW6 X-ray 2.30 A/C 1-298 [» ]
    2IW8 X-ray 2.30 A/C 1-298 [» ]
    2IW9 X-ray 2.00 A/C 1-298 [» ]
    2J9M X-ray 2.50 A 1-298 [» ]
    2JGZ X-ray 2.90 A 1-288 [» ]
    2R3F X-ray 1.50 A 1-298 [» ]
    2R3G X-ray 1.55 A 1-298 [» ]
    2R3H X-ray 1.50 A 1-298 [» ]
    2R3I X-ray 1.28 A 1-298 [» ]
    2R3J X-ray 1.65 A 1-298 [» ]
    2R3K X-ray 1.70 A 1-298 [» ]
    2R3L X-ray 1.65 A 1-298 [» ]
    2R3M X-ray 1.70 A 1-298 [» ]
    2R3N X-ray 1.63 A 1-298 [» ]
    2R3O X-ray 1.80 A 1-298 [» ]
    2R3P X-ray 1.66 A 1-298 [» ]
    2R3Q X-ray 1.35 A 1-298 [» ]
    2R3R X-ray 1.47 A 1-298 [» ]
    2R64 X-ray 2.30 A 1-298 [» ]
    2UUE X-ray 2.06 A/C 1-298 [» ]
    2UZB X-ray 2.70 A/C 1-298 [» ]
    2UZD X-ray 2.72 A/C 1-298 [» ]
    2UZE X-ray 2.40 A/C 1-298 [» ]
    2UZL X-ray 2.40 A/C 1-298 [» ]
    2UZN X-ray 2.30 A 1-298 [» ]
    2UZO X-ray 2.30 A 1-298 [» ]
    2V0D X-ray 2.20 A 1-298 [» ]
    2V22 X-ray 2.60 A/C 1-298 [» ]
    2VTA X-ray 2.00 A 1-298 [» ]
    2VTH X-ray 1.90 A 1-298 [» ]
    2VTI X-ray 2.00 A 1-298 [» ]
    2VTJ X-ray 2.20 A 1-298 [» ]
    2VTL X-ray 2.00 A 1-298 [» ]
    2VTM X-ray 2.25 A 1-298 [» ]
    2VTN X-ray 2.20 A 1-298 [» ]
    2VTO X-ray 2.19 A 1-298 [» ]
    2VTP X-ray 2.15 A 1-298 [» ]
    2VTQ X-ray 1.90 A 1-298 [» ]
    2VTR X-ray 1.90 A 1-298 [» ]
    2VTS X-ray 1.90 A 1-298 [» ]
    2VTT X-ray 1.68 A 1-298 [» ]
    2VU3 X-ray 1.85 A 1-298 [» ]
    2VV9 X-ray 1.90 A 1-298 [» ]
    2W05 X-ray 1.90 A 1-298 [» ]
    2W06 X-ray 2.04 A 1-298 [» ]
    2W17 X-ray 2.15 A 1-298 [» ]
    2W1H X-ray 2.15 A 1-298 [» ]
    2WEV X-ray 2.30 A/C 1-298 [» ]
    2WFY X-ray 2.53 A/C 1-298 [» ]
    2WHB X-ray 2.90 A/C 1-298 [» ]
    2WIH X-ray 2.50 A/C 1-298 [» ]
    2WIP X-ray 2.80 A/C 1-298 [» ]
    2WMA X-ray 2.80 A/C 1-298 [» ]
    2WMB X-ray 2.60 A/C 1-298 [» ]
    2WPA X-ray 2.51 A/C 1-298 [» ]
    2WXV X-ray 2.60 A/C 1-298 [» ]
    2X1N X-ray 2.75 A/C 1-298 [» ]
    2XMY X-ray 1.90 A 1-298 [» ]
    2XNB X-ray 1.85 A 1-298 [» ]
    3BHT X-ray 2.00 A/C 1-298 [» ]
    3BHU X-ray 2.30 A/C 1-298 [» ]
    3BHV X-ray 2.10 A/C 1-298 [» ]
    3DDP X-ray 2.70 A/C 1-298 [» ]
    3DDQ X-ray 1.80 A/C 1-298 [» ]
    3DOG X-ray 2.70 A/C 1-298 [» ]
    3EID X-ray 3.15 A/C 1-298 [» ]
    3EJ1 X-ray 3.22 A/C 1-298 [» ]
    3EOC X-ray 3.20 A/C 1-298 [» ]
    3EZR X-ray 1.90 A 1-298 [» ]
    3EZV X-ray 1.99 A 1-298 [» ]
    3F5X X-ray 2.40 A/C 1-298 [» ]
    3FZ1 X-ray 1.90 A 1-298 [» ]
    3IG7 X-ray 1.80 A 1-298 [» ]
    3IGG X-ray 1.80 A 1-298 [» ]
    3LE6 X-ray 2.00 A 1-298 [» ]
    3LFN X-ray 2.28 A 1-298 [» ]
    3LFQ X-ray 2.03 A 1-298 [» ]
    3LFS X-ray 2.40 A 1-298 [» ]
    3MY5 X-ray 2.10 A/C 1-298 [» ]
    3NS9 X-ray 1.78 A 1-298 [» ]
    3PJ8 X-ray 1.96 A 1-298 [» ]
    3PXF X-ray 1.80 A 1-298 [» ]
    3PXQ X-ray 1.90 A 1-298 [» ]
    3PXR X-ray 2.00 A 1-298 [» ]
    3PXY X-ray 1.80 A 1-298 [» ]
    3PXZ X-ray 1.70 A 1-298 [» ]
    3PY0 X-ray 1.75 A 1-298 [» ]
    3PY1 X-ray 2.05 A 1-298 [» ]
    3QHR X-ray 2.17 A/C 1-296 [» ]
    3QHW X-ray 1.91 A/C 1-296 [» ]
    3QL8 X-ray 1.90 A 1-298 [» ]
    3QQF X-ray 1.75 A 1-298 [» ]
    3QQG X-ray 1.90 A 1-298 [» ]
    3QQH X-ray 1.87 A 1-298 [» ]
    3QQJ X-ray 1.70 A 1-298 [» ]
    3QQK X-ray 1.86 A 1-298 [» ]
    3QQL X-ray 1.85 A 1-298 [» ]
    3QRT X-ray 1.75 A 1-298 [» ]
    3QRU X-ray 1.95 A 1-298 [» ]
    3QTQ X-ray 1.80 A 1-298 [» ]
    3QTR X-ray 1.85 A 1-298 [» ]
    3QTS X-ray 1.90 A 1-298 [» ]
    3QTU X-ray 1.82 A 1-298 [» ]
    3QTW X-ray 1.85 A 1-298 [» ]
    3QTX X-ray 1.95 A 1-298 [» ]
    3QTZ X-ray 2.00 A 1-298 [» ]
    3QU0 X-ray 1.95 A 1-298 [» ]
    3QWJ X-ray 1.75 A 1-298 [» ]
    3QWK X-ray 1.85 A 1-298 [» ]
    3QX2 X-ray 1.75 A 1-298 [» ]
    3QX4 X-ray 1.92 A 1-298 [» ]
    3QXO X-ray 1.75 A 1-298 [» ]
    3QXP X-ray 1.75 A 1-298 [» ]
    3QZF X-ray 2.00 A 1-298 [» ]
    3QZG X-ray 1.75 A 1-298 [» ]
    3QZH X-ray 1.95 A 1-298 [» ]
    3QZI X-ray 1.75 A 1-298 [» ]
    3R1Q X-ray 1.85 A 1-298 [» ]
    3R1S X-ray 1.80 A 1-298 [» ]
    3R1Y X-ray 1.80 A 1-298 [» ]
    3R28 X-ray 1.75 A 1-298 [» ]
    3R6X X-ray 1.75 A 1-298 [» ]
    3R71 X-ray 1.75 A 1-298 [» ]
    3R73 X-ray 1.70 A 1-298 [» ]
    3R7E X-ray 1.90 A 1-298 [» ]
    3R7I X-ray 1.85 A 1-298 [» ]
    3R7U X-ray 1.75 A 1-298 [» ]
    3R7V X-ray 1.95 A 1-298 [» ]
    3R7Y X-ray 1.90 A 1-298 [» ]
    3R83 X-ray 1.75 A 1-298 [» ]
    3R8L X-ray 1.90 A 1-298 [» ]
    3R8M X-ray 1.80 A 1-298 [» ]
    3R8P X-ray 1.80 A 1-298 [» ]
    3R8U X-ray 2.00 A 1-298 [» ]
    3R8V X-ray 1.90 A 1-298 [» ]
    3R8Z X-ray 1.85 A 1-298 [» ]
    3R9D X-ray 1.95 A 1-298 [» ]
    3R9H X-ray 2.10 A 1-298 [» ]
    3R9N X-ray 1.75 A 1-298 [» ]
    3R9O X-ray 1.90 A 1-298 [» ]
    3RAH X-ray 1.75 A 1-298 [» ]
    3RAI X-ray 1.70 A 1-298 [» ]
    3RAK X-ray 1.75 A 1-298 [» ]
    3RAL X-ray 1.75 A 1-298 [» ]
    3RJC X-ray 1.85 A 1-298 [» ]
    3RK5 X-ray 2.00 A 1-298 [» ]
    3RK7 X-ray 1.80 A 1-298 [» ]
    3RK9 X-ray 1.85 A 1-298 [» ]
    3RKB X-ray 2.00 A 1-298 [» ]
    3RM6 X-ray 1.60 A 1-298 [» ]
    3RM7 X-ray 1.85 A 1-298 [» ]
    3RMF X-ray 1.75 A 1-298 [» ]
    3RNI X-ray 1.95 A 1-298 [» ]
    3ROY X-ray 1.75 A 1-298 [» ]
    3RPO X-ray 1.75 A 1-298 [» ]
    3RPR X-ray 1.75 A 1-298 [» ]
    3RPV X-ray 1.80 A 1-298 [» ]
    3RPY X-ray 1.90 A 1-298 [» ]
    3RZB X-ray 1.90 A 1-298 [» ]
    3S00 X-ray 1.80 A 1-298 [» ]
    3S0O X-ray 2.00 A 1-298 [» ]
    3S1H X-ray 1.75 A 1-298 [» ]
    3S2P X-ray 2.30 A 1-298 [» ]
    3SQQ X-ray 1.85 A 1-298 [» ]
    3SW4 X-ray 1.70 A 1-298 [» ]
    3SW7 X-ray 1.80 A 1-298 [» ]
    3TI1 X-ray 1.99 A 1-298 [» ]
    3TIY X-ray 1.84 A 1-298 [» ]
    3TIZ X-ray 2.02 A 1-298 [» ]
    3TNW X-ray 2.00 A/C 1-298 [» ]
    3ULI X-ray 2.00 A 1-298 [» ]
    3UNJ X-ray 1.90 A 1-298 [» ]
    3UNK X-ray 2.10 A 1-298 [» ]
    3WBL X-ray 2.00 A 1-298 [» ]
    4ACM X-ray 1.63 A 1-298 [» ]
    4BCK X-ray 2.05 A/C 1-298 [» ]
    4BCM X-ray 2.45 A/C 1-298 [» ]
    4BCN X-ray 2.10 A/C 1-298 [» ]
    4BCO X-ray 2.05 A/C 1-298 [» ]
    4BCP X-ray 2.26 A/C 1-298 [» ]
    4BCQ X-ray 2.40 A/C 1-298 [» ]
    4BGH X-ray 1.95 A 1-298 [» ]
    4CFN X-ray 2.20 A/C 1-298 [» ]
    4CFW X-ray 2.45 A/C 1-298 [» ]
    4EK3 X-ray 1.34 A 1-298 [» ]
    4EK4 X-ray 1.26 A 1-298 [» ]
    4EK5 X-ray 1.60 A 1-298 [» ]
    4EK6 X-ray 1.52 A 1-298 [» ]
    4EK8 X-ray 1.70 A 1-298 [» ]
    4EOI X-ray 2.00 A/C 1-298 [» ]
    4EOJ X-ray 1.65 A/C 1-298 [» ]
    4EOK X-ray 2.57 A/C 1-297 [» ]
    4EOL X-ray 2.40 A/C 1-297 [» ]
    4EOM X-ray 2.10 A/C 1-297 [» ]
    4EON X-ray 2.40 A/C 1-298 [» ]
    4EOO X-ray 2.10 A/C 1-297 [» ]
    4EOP X-ray 1.99 A/C 1-297 [» ]
    4EOQ X-ray 2.15 A/C 1-297 [» ]
    4EOR X-ray 2.20 A/C 1-297 [» ]
    4EOS X-ray 2.57 A/C 1-297 [» ]
    4ERW X-ray 2.00 A 1-298 [» ]
    4EZ3 X-ray 2.00 A 1-298 [» ]
    4EZ7 X-ray 2.49 A 1-298 [» ]
    4FKG X-ray 1.51 A 1-298 [» ]
    4FKI X-ray 1.60 A 1-298 [» ]
    4FKJ X-ray 1.63 A 1-298 [» ]
    4FKL X-ray 1.26 A 1-298 [» ]
    4FKO X-ray 1.55 A 1-298 [» ]
    4FKP X-ray 1.60 A 1-298 [» ]
    4FKQ X-ray 1.75 A 1-298 [» ]
    4FKR X-ray 1.90 A 1-298 [» ]
    4FKS X-ray 1.55 A 1-298 [» ]
    4FKT X-ray 1.60 A 1-298 [» ]
    4FKU X-ray 1.47 A 1-298 [» ]
    4FKV X-ray 1.70 A 1-298 [» ]
    4FKW X-ray 1.80 A 1-298 [» ]
    4FX3 X-ray 2.75 A/C 1-298 [» ]
    4GCJ X-ray 1.42 A 1-298 [» ]
    4I3Z X-ray 2.05 A/C 1-296 [» ]
    4II5 X-ray 2.15 A/C 1-298 [» ]
    4KD1 X-ray 1.70 A 1-298 [» ]
    4LYN X-ray 2.00 A 1-298 [» ]
    4NJ3 X-ray 1.85 A 1-298 [» ]
    ProteinModelPortali P24941.
    SMRi P24941. Positions 1-298.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107452. 569 interactions.
    DIPi DIP-161N.
    IntActi P24941. 67 interactions.
    MINTi MINT-96328.
    STRINGi 9606.ENSP00000266970.

    Chemistry

    BindingDBi P24941.
    ChEMBLi CHEMBL2094126.
    GuidetoPHARMACOLOGYi 1973.

    PTM databases

    PhosphoSitei P24941.

    Polymorphism databases

    DMDMi 116051.

    Proteomic databases

    MaxQBi P24941.
    PaxDbi P24941.
    PRIDEi P24941.

    Protocols and materials databases

    DNASUi 1017.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266970 ; ENSP00000266970 ; ENSG00000123374 . [P24941-1 ]
    ENST00000354056 ; ENSP00000243067 ; ENSG00000123374 . [P24941-2 ]
    GeneIDi 1017.
    KEGGi hsa:1017.
    UCSCi uc001sit.4. human. [P24941-1 ]
    uc001siu.4. human. [P24941-2 ]

    Organism-specific databases

    CTDi 1017.
    GeneCardsi GC12P056360.
    HGNCi HGNC:1771. CDK2.
    HPAi CAB013115.
    MIMi 116953. gene.
    neXtProti NX_P24941.
    PharmGKBi PA101.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi P24941.
    KOi K02206.
    OrthoDBi EOG7966H8.
    PhylomeDBi P24941.
    TreeFami TF101021.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 2681.
    Reactomei REACT_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_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.
    SignaLinki P24941.

    Miscellaneous databases

    ChiTaRSi CDK2. human.
    EvolutionaryTracei P24941.
    GeneWikii Cyclin-dependent_kinase_2.
    GenomeRNAii 1017.
    NextBioi 4273.
    PROi P24941.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24941.
    Bgeei P24941.
    CleanExi HS_CDK2.
    Genevestigatori P24941.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1991) [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(1991) [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(1991) [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 (MAR-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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (MAY-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(2004) [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(2006) [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(2004) [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(1992) [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(1997) [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(1999) [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(2000) [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(2000) [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(2000) [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(2001) [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(2002) [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(2002) [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(2003) [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(2003) [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. "p42, a novel cyclin-dependent kinase-activating kinase in mammalian cells."
      Liu Y., Wu C., Galaktionov K.
      J. Biol. Chem. 279:4507-4514(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-160.
    25. "Identification and comparative analysis of multiple mammalian Speedy/Ringo proteins."
      Cheng A., Xiong W., Ferrell J.E. Jr., Solomon M.J.
      Cell Cycle 4:155-165(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPDYA AND SPDYC.
    26. "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(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS BRCA2 KINASE.
    27. Cited for: PHOSPHORYLATION BY CAK, MUTAGENESIS OF LYS-9; 88-LYS-LYS-89 AND LEU-166, INTERACTION WITH CDK7.
    28. "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(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. Cited for: FUNCTION IN MITOSE REGULATION, SUBCELLULAR LOCATION.
    30. "Identification and characterization of CAC1 as a novel CDK2-associated cullin."
      Kong Y., Nan K., Yin Y.
      Cell Cycle 8:3544-3553(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACUL1.
    31. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "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(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND LYS-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN VITAMIN D-MEDIATED GROWTH INHIBITION, SUBCELLULAR LOCATION, ENZYME REGULATION, PHOSPHORYLATION AT THR-160.
    35. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, S-NITROSYLATION.
    36. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-160 BY CAK, DEPHOSPHORYLATION BY CDC25A.
    37. "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(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS EZH2 KINASE.
    38. "Cdk2 is required for p53-independent G2/M checkpoint control."
      Chung J.H., Bunz F.
      PLoS Genet. 6:E1000863-E1000863(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DAMAGE CHECKPOINT.
    39. Cited for: FUNCTION AS MYC KINASE.
    40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP63.
    42. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CTNNB1 KINASE, SUBCELLULAR LOCATION, INTERACTION WITH PTPN6 AND CTNNB1.
    43. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORS.
    44. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS USP37 KINASE.
    45. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL CYCLE REGULATION.
    46. "A dual role of Cdk2 in DNA damage response."
      Satyanarayana A., Kaldis P.
      Cell Div. 4:9-9(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON DNA REPAIR, INTERACTION WITH CDKN1A/P21.
    47. "Cell cycle, CDKs and cancer: a changing paradigm."
      Malumbres M., Barbacid M.
      Nat. Rev. Cancer 9:153-166(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON CELL CYCLE CONTROL, INHIBITORS, GENE FAMILY.
    48. "Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms."
      Satyanarayana A., Kaldis P.
      Oncogene 28:2925-2939(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, GENE FAMILY.
    49. "Tipping the balance: Cdk2 enables Myc to suppress senescence."
      Hydbring P., Larsson L.-G.
      Cancer Res. 70:6687-6691(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON SENESCENCE.
    50. "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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON INHIBITORS.
    51. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    52. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    53. "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(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CYCLIN A.
    54. "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(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITG CKS1.
    55. "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(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
    56. "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(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CG2A AND KIP1.
    57. "Structural basis of cyclin-dependent kinase activation by phosphorylation."
      Russo A.A., Jeffrey P.D., Pavletich N.P.
      Nat. Struct. Biol. 3:696-700(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CG2A.
    58. "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(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH L868276.
    59. "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(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH STAUROSPORINE, ENZYME REGULATION.
    60. Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
    61. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
    62. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH INHIBITORS, PHOSPHORYLATION AT THR-160.
    63. "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(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-288 IN COMPLEX WITH CCNB1, FUNCTION.
    64. "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(2007) [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.
    65. Cited for: X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
    66. "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(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
    67. "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(2011) [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.
    68. "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(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-45 AND SER-290.

    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: October 1, 2014
    This is version 190 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