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Q00537

- CDK17_HUMAN

UniProt

Q00537 - CDK17_HUMAN

Protein

Cyclin-dependent kinase 17

Gene

CDK17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei221 – 2211ATPPROSITE-ProRule annotation
    Active sitei313 – 3131Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi198 – 2069ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein phosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 2681.
    SignaLinkiQ00537.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 17 (EC:2.7.11.22)
    Alternative name(s):
    Cell division protein kinase 17
    PCTAIRE-motif protein kinase 2
    Serine/threonine-protein kinase PCTAIRE-2
    Gene namesi
    Name:CDK17
    Synonyms:PCTAIRE2, PCTK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8750. CDK17.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33096.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 523523Cyclin-dependent kinase 17PRO_0000086487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei105 – 1051Phosphoserine1 Publication
    Modified residuei137 – 1371Phosphoserine3 Publications
    Modified residuei146 – 1461Phosphoserine1 Publication
    Modified residuei165 – 1651Phosphoserine4 Publications
    Modified residuei180 – 1801Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ00537.
    PaxDbiQ00537.
    PRIDEiQ00537.

    PTM databases

    PhosphoSiteiQ00537.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00537.
    BgeeiQ00537.
    CleanExiHS_PCTK2.
    GenevestigatoriQ00537.

    Organism-specific databases

    HPAiHPA015325.

    Interactioni

    Subunit structurei

    Found in a complex containing CABLES1, CDK16 and TDRD7. Interacts with TDRD7 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YWHAZP631042EBI-624648,EBI-347088

    Protein-protein interaction databases

    BioGridi111155. 18 interactions.
    IntActiQ00537. 13 interactions.
    MINTiMINT-1681036.
    STRINGi9606.ENSP00000261211.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00537.
    SMRiQ00537. Positions 142-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini192 – 473282Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiQ00537.
    KOiK15595.
    OMAiMKHAYFR.
    OrthoDBiEOG7966H8.
    PhylomeDBiQ00537.
    TreeFamiTF106508.

    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: Q00537-1) [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

    MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEENSSKDNE PIVKNGRPPT    50
    SHSMHSFLHQ YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN 100
    LKMGSDGESD QASGTSSDEV QSPTGVCLRN RIHRRISMED LNKRLSLPAD 150
    IRIPDGYLEK LQINSPPFDQ PMSRRSRRAS LSEIGFGKME TYIKLEKLGE 200
    GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS LLKDLKHANI 250
    VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG 300
    LAYCHRRKVL HRDLKPQNLL INEKGELKLA DFGLARAKSV PTKTYSNEVV 350
    TLWYRPPDVL LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL 400
    IFRLLGTPSQ ETWPGISSNE EFKNYNFPKY KPQPLINHAP RLDSEGIELI 450
    TKFLQYESKK RVSAEEAMKH VYFRSLGPRI HALPESVSIF SLKEIQLQKD 500
    PGFRNSSYPE TGHGKNRRQS MLF 523
    Length:523
    Mass (Da):59,582
    Last modified:February 15, 2005 - v2
    Checksum:i429ABD1DCBB5A082
    GO
    Isoform 2 (identifier: Q00537-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         513-523: HGKNRRQSMLF → VFVINHFTCRS

    Note: No experimental confirmation available.

    Show »
    Length:523
    Mass (Da):59,531
    Checksum:i5FD1C9DFC4B050C6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti367 – 3671S → L in CAA47004. (PubMed:1639063)Curated
    Sequence conflicti433 – 4331Q → E in CAA47004. (PubMed:1639063)Curated
    Sequence conflicti451 – 4511T → R in CAA47004. (PubMed:1639063)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti214 – 2141T → I Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
    VAR_064743

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei513 – 52311HGKNRRQSMLF → VFVINHFTCRS in isoform 2. 1 PublicationVSP_043295Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66360 mRNA. Translation: CAA47004.1.
    AK290011 mRNA. Translation: BAF82700.1.
    AK315214 mRNA. Translation: BAG37649.1.
    AC125612 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97566.1.
    CH471054 Genomic DNA. Translation: EAW97567.1.
    BC033005 mRNA. Translation: AAH33005.1.
    CCDSiCCDS53819.1. [Q00537-2]
    CCDS9061.1. [Q00537-1]
    PIRiS23384.
    RefSeqiNP_001163935.1. NM_001170464.2. [Q00537-2]
    NP_002586.2. NM_002595.4. [Q00537-1]
    XP_006719507.1. XM_006719444.1. [Q00537-2]
    UniGeneiHs.506415.

    Genome annotation databases

    EnsembliENST00000261211; ENSP00000261211; ENSG00000059758. [Q00537-1]
    ENST00000543119; ENSP00000444459; ENSG00000059758. [Q00537-2]
    GeneIDi5128.
    KEGGihsa:5128.
    UCSCiuc001tep.2. human. [Q00537-1]
    uc009ztk.3. human. [Q00537-2]

    Polymorphism databases

    DMDMi59803097.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66360 mRNA. Translation: CAA47004.1 .
    AK290011 mRNA. Translation: BAF82700.1 .
    AK315214 mRNA. Translation: BAG37649.1 .
    AC125612 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW97566.1 .
    CH471054 Genomic DNA. Translation: EAW97567.1 .
    BC033005 mRNA. Translation: AAH33005.1 .
    CCDSi CCDS53819.1. [Q00537-2 ]
    CCDS9061.1. [Q00537-1 ]
    PIRi S23384.
    RefSeqi NP_001163935.1. NM_001170464.2. [Q00537-2 ]
    NP_002586.2. NM_002595.4. [Q00537-1 ]
    XP_006719507.1. XM_006719444.1. [Q00537-2 ]
    UniGenei Hs.506415.

    3D structure databases

    ProteinModelPortali Q00537.
    SMRi Q00537. Positions 142-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111155. 18 interactions.
    IntActi Q00537. 13 interactions.
    MINTi MINT-1681036.
    STRINGi 9606.ENSP00000261211.

    Chemistry

    BindingDBi Q00537.
    ChEMBLi CHEMBL5790.
    GuidetoPHARMACOLOGYi 1970.

    PTM databases

    PhosphoSitei Q00537.

    Polymorphism databases

    DMDMi 59803097.

    Proteomic databases

    MaxQBi Q00537.
    PaxDbi Q00537.
    PRIDEi Q00537.

    Protocols and materials databases

    DNASUi 5128.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261211 ; ENSP00000261211 ; ENSG00000059758 . [Q00537-1 ]
    ENST00000543119 ; ENSP00000444459 ; ENSG00000059758 . [Q00537-2 ]
    GeneIDi 5128.
    KEGGi hsa:5128.
    UCSCi uc001tep.2. human. [Q00537-1 ]
    uc009ztk.3. human. [Q00537-2 ]

    Organism-specific databases

    CTDi 5128.
    GeneCardsi GC12M096673.
    HGNCi HGNC:8750. CDK17.
    HPAi HPA015325.
    MIMi 603440. gene.
    neXtProti NX_Q00537.
    PharmGKBi PA33096.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi Q00537.
    KOi K15595.
    OMAi MKHAYFR.
    OrthoDBi EOG7966H8.
    PhylomeDBi Q00537.
    TreeFami TF106508.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 2681.
    SignaLinki Q00537.

    Miscellaneous databases

    ChiTaRSi CDK17. human.
    GeneWikii PCTK2.
    GenomeRNAii 5128.
    NextBioi 19768.
    PROi Q00537.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00537.
    Bgeei Q00537.
    CleanExi HS_PCTK2.
    Genevestigatori Q00537.

    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 family of human cdc2-related protein kinases."
      Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C., Harlow E., Tsai L.-H.
      EMBO J. 11:2909-2917(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Trachea.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Testis.
    6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-146 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-105; SER-137 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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 SER-165 AND SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: VARIANT ILE-214.

    Entry informationi

    Entry nameiCDK17_HUMAN
    AccessioniPrimary (citable) accession number: Q00537
    Secondary accession number(s): A8K1U6, B2RCQ2, Q8NEB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 144 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

    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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3