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Q9UPZ9

- ICK_HUMAN

UniProt

Q9UPZ9 - ICK_HUMAN

Protein

Serine/threonine-protein kinase ICK

Gene

ICK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    May play a key role in the development of multiple organ systems and particularly in cardiac development.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331ATP1 PublicationPROSITE-ProRule annotation
    Active sitei125 – 1251Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 189ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. intracellular signal transduction Source: UniProtKB
    2. multicellular organismal development Source: UniProtKB-KW
    3. protein phosphorylation Source: UniProtKB
    4. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9UPZ9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase ICK (EC:2.7.11.22)
    Alternative name(s):
    Intestinal cell kinase
    Short name:
    hICK
    Laryngeal cancer kinase 2
    Short name:
    LCK2
    MAK-related kinase
    Short name:
    MRK
    Gene namesi
    Name:ICK
    Synonyms:KIAA0936
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21219. ICK.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytosol By similarity
    Note: Nuclear localization has been observed with a GFP-tagged construct in transfected HeLa cells (PubMed:12103360). Cytosolic localization was shown in rat embryonic cardiomyocytes by immunostaining (PubMed:8570168).1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Endocrine-cerebroosteodysplasia (ECO) [MIM:612651]: Previously unidentified neonatal lethal recessive disorder with multiple anomalies involving the endocrine, cerebral, and skeletal systems.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti272 – 2721R → Q in ECO; fails to localize at the nucleus and significantly impairs kinase activity. 1 Publication
    VAR_057994

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331K → R: Loss of activity and autophosphorylation; when associated with R-34; R-36 and R-38. 1 Publication
    Mutagenesisi34 – 341K → R: Loss of activity and autophosphorylation; when associated with R-33; R-36 and R-38. 1 Publication
    Mutagenesisi36 – 361K → R: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-38. 1 Publication
    Mutagenesisi38 – 381K → R: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-36. 1 Publication
    Mutagenesisi157 – 1571T → A: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with F-159. 1 Publication
    Mutagenesisi159 – 1591Y → F: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with A-157. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi612651. phenotype.
    Orphaneti199332. Endocrine-cerebro-osteodysplasia syndrome.
    PharmGKBiPA134894544.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Serine/threonine-protein kinase ICKPRO_0000086007Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei157 – 1571Phosphothreonine1 Publication
    Modified residuei159 – 1591Phosphotyrosine1 Publication

    Post-translational modificationi

    Autophosphorylated on serine and threonine residues. May play a role in enzyme activation.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UPZ9.
    PRIDEiQ9UPZ9.

    PTM databases

    PhosphoSiteiQ9UPZ9.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, pancreas, thymus, prostate, testis, ovary, small intestine and colon, with highest levels in placenta and testis. Not detected in spleen. Also expressed in many cancer cell lines.2 Publications

    Gene expression databases

    BgeeiQ9UPZ9.
    CleanExiHS_ICK.
    GenevestigatoriQ9UPZ9.

    Organism-specific databases

    HPAiHPA001113.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-6381479,EBI-352572

    Protein-protein interaction databases

    BioGridi116527. 18 interactions.
    IntActiQ9UPZ9. 8 interactions.
    MINTiMINT-1200416.
    STRINGi9606.ENSP00000263043.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UPZ9.
    SMRiQ9UPZ9. Positions 1-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 284281Protein kinaseCuratedPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG014652.
    InParanoidiQ9UPZ9.
    KOiK08828.
    OMAiCIMAEVY.
    OrthoDBiEOG7NCV37.
    PhylomeDBiQ9UPZ9.
    TreeFamiTF328769.

    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 11 Publication (identifier: Q9UPZ9-1) [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

    MNRYTTIRQL GDGTYGSVLL GRSIESGELI AIKKMKRKFY SWEECMNLRE    50
    VKSLKKLNHA NVVKLKEVIR ENDHLYFIFE YMKENLYQLI KERNKLFPES 100
    AIRNIMYQIL QGLAFIHKHG FFHRDLKPEN LLCMGPELVK IADFGLAREI 150
    RSKPPYTDYV STRWYRAPEV LLRSTNYSSP IDVWAVGCIM AEVYTLRPLF 200
    PGASEIDTIF KICQVLGTPK KTDWPEGYQL SSAMNFRWPQ CVPNNLKTLI 250
    PNASSEAVQL LRDMLQWDPK KRPTASQALR YPYFQVGHPL GSTTQNLQDS 300
    EKPQKGILEK AGPPPYIKPV PPAQPPAKPH TRISSRQHQA SQPPLHLTYP 350
    YKAEVSRTDH PSHLQEDKPS PLLFPSLHNK HPQSKITAGL EHKNGEIKPK 400
    SRRRWGLISR STKDSDDWAD LDDLDFSPSL SRIDLKNKKR QSDDTLCRFE 450
    SVLDLKPSEP VGTGNSAPTQ TSYQRRDTPT LRSAAKQHYL KHSRYLPGIS 500
    IRNGILSNPG KEFIPPNPWS SSGLSGKSSG TMSVISKVNS VGSSSTSSSG 550
    LTGNYVPSFL KKEIGSAMQR VHLAPIPDPS PGYSSLKAMR PHPGRPFFHT 600
    QPRSTPGLIP RPPAAQPVHG RTDWASKYAS RR 632
    Length:632
    Mass (Da):71,427
    Last modified:May 1, 2000 - v1
    Checksum:iF4C22C6CCD5878D2
    GO
    Isoform 2Curated (identifier: Q9UPZ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-292: ALRYPYFQVGHPLGS → VFFHFLVITFISNSE
         293-632: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:292
    Mass (Da):34,071
    Checksum:iAB4CA7370E16F983
    GO

    Sequence cautioni

    The sequence BAA76780.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 481L → Q in AAF37278. (PubMed:10699974)Curated
    Sequence conflicti119 – 1191H → L in AAF37278. (PubMed:10699974)Curated
    Sequence conflicti310 – 3101K → R in AAF37278. (PubMed:10699974)Curated
    Sequence conflicti598 – 5992FH → LD in AAF37278. (PubMed:10699974)Curated
    Sequence conflicti629 – 6291A → P in AAF37278. (PubMed:10699974)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981P → L.
    Corresponds to variant rs1493105 [ dbSNP | Ensembl ].
    VAR_053931
    Natural varianti115 – 1151F → Y in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042001
    Natural varianti272 – 2721R → Q in ECO; fails to localize at the nucleus and significantly impairs kinase activity. 1 Publication
    VAR_057994
    Natural varianti320 – 3201V → I.1 Publication
    Corresponds to variant rs33936662 [ dbSNP | Ensembl ].
    VAR_042002
    Natural varianti471 – 4711T → K.1 Publication
    Corresponds to variant rs56164633 [ dbSNP | Ensembl ].
    VAR_042003
    Natural varianti476 – 4761R → Q.1 Publication
    Corresponds to variant rs55895113 [ dbSNP | Ensembl ].
    VAR_042004
    Natural varianti615 – 6151A → T.1 Publication
    Corresponds to variant rs55932059 [ dbSNP | Ensembl ].
    VAR_042005

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei278 – 29215ALRYP…HPLGS → VFFHFLVITFISNSE in isoform 2. 1 PublicationVSP_050752Add
    BLAST
    Alternative sequencei293 – 632340Missing in isoform 2. 1 PublicationVSP_050753Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF225919 mRNA. Translation: AAF37278.1.
    AF152469 mRNA. Translation: AAG43364.1.
    AB023153 mRNA. Translation: BAA76780.2. Different initiation.
    AL031178, AL162581 Genomic DNA. Translation: CAI20261.1.
    AL162581, AL031178 Genomic DNA. Translation: CAI19518.1.
    CH471081 Genomic DNA. Translation: EAX04400.1.
    BC035807 mRNA. Translation: AAH35807.1.
    BC136420 mRNA. Translation: AAI36421.1.
    BC136421 mRNA. Translation: AAI36422.1.
    BC152464 mRNA. Translation: AAI52465.1.
    CCDSiCCDS4949.1. [Q9UPZ9-1]
    RefSeqiNP_055735.1. NM_014920.3. [Q9UPZ9-1]
    NP_057597.2. NM_016513.4. [Q9UPZ9-1]
    UniGeneiHs.417022.

    Genome annotation databases

    EnsembliENST00000350082; ENSP00000263043; ENSG00000112144. [Q9UPZ9-1]
    ENST00000356971; ENSP00000349458; ENSG00000112144. [Q9UPZ9-1]
    GeneIDi22858.
    KEGGihsa:22858.
    UCSCiuc003pbh.2. human. [Q9UPZ9-1]
    uc003pbj.3. human. [Q9UPZ9-2]

    Polymorphism databases

    DMDMi48428273.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF225919 mRNA. Translation: AAF37278.1 .
    AF152469 mRNA. Translation: AAG43364.1 .
    AB023153 mRNA. Translation: BAA76780.2 . Different initiation.
    AL031178 , AL162581 Genomic DNA. Translation: CAI20261.1 .
    AL162581 , AL031178 Genomic DNA. Translation: CAI19518.1 .
    CH471081 Genomic DNA. Translation: EAX04400.1 .
    BC035807 mRNA. Translation: AAH35807.1 .
    BC136420 mRNA. Translation: AAI36421.1 .
    BC136421 mRNA. Translation: AAI36422.1 .
    BC152464 mRNA. Translation: AAI52465.1 .
    CCDSi CCDS4949.1. [Q9UPZ9-1 ]
    RefSeqi NP_055735.1. NM_014920.3. [Q9UPZ9-1 ]
    NP_057597.2. NM_016513.4. [Q9UPZ9-1 ]
    UniGenei Hs.417022.

    3D structure databases

    ProteinModelPortali Q9UPZ9.
    SMRi Q9UPZ9. Positions 1-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116527. 18 interactions.
    IntActi Q9UPZ9. 8 interactions.
    MINTi MINT-1200416.
    STRINGi 9606.ENSP00000263043.

    Chemistry

    BindingDBi Q9UPZ9.
    ChEMBLi CHEMBL1163126.
    GuidetoPHARMACOLOGYi 2038.

    PTM databases

    PhosphoSitei Q9UPZ9.

    Polymorphism databases

    DMDMi 48428273.

    Proteomic databases

    PaxDbi Q9UPZ9.
    PRIDEi Q9UPZ9.

    Protocols and materials databases

    DNASUi 22858.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000350082 ; ENSP00000263043 ; ENSG00000112144 . [Q9UPZ9-1 ]
    ENST00000356971 ; ENSP00000349458 ; ENSG00000112144 . [Q9UPZ9-1 ]
    GeneIDi 22858.
    KEGGi hsa:22858.
    UCSCi uc003pbh.2. human. [Q9UPZ9-1 ]
    uc003pbj.3. human. [Q9UPZ9-2 ]

    Organism-specific databases

    CTDi 22858.
    GeneCardsi GC06M052912.
    HGNCi HGNC:21219. ICK.
    HPAi HPA001113.
    MIMi 612325. gene.
    612651. phenotype.
    neXtProti NX_Q9UPZ9.
    Orphaneti 199332. Endocrine-cerebro-osteodysplasia syndrome.
    PharmGKBi PA134894544.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG014652.
    InParanoidi Q9UPZ9.
    KOi K08828.
    OMAi CIMAEVY.
    OrthoDBi EOG7NCV37.
    PhylomeDBi Q9UPZ9.
    TreeFami TF328769.

    Enzyme and pathway databases

    SignaLinki Q9UPZ9.

    Miscellaneous databases

    GeneWikii ICK_(gene).
    GenomeRNAii 22858.
    NextBioi 43345.
    PROi Q9UPZ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UPZ9.
    CleanExi HS_ICK.
    Genevestigatori Q9UPZ9.

    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. "Intestinal cell kinase (ICK) localizes to the crypt region and requires a dual phosphorylation site found in map kinases."
      Togawa K., Yan Y.-X., Inomoto T., Slaugenhaupt S.A., Rustgi A.K.
      J. Cell. Physiol. 183:129-139(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-33; LYS-34; LYS-36; LYS-38; THR-157 AND TYR-159, PHOSPHORYLATION AT THR-157 AND TYR-159.
      Tissue: Colon1 Publication.
    2. "The identification and subcellular localization of human MRK."
      Yang T., Jiang Y., Chen J.
      Biomol. Eng. 19:1-4(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: BrainImported.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 2).
      Tissue: BrainImported.
    7. "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.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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] TYR-115; ILE-320; LYS-471; GLN-476 AND THR-615.
    10. "A multiplex human syndrome implicates a key role for intestinal cell kinase in development of central nervous, skeletal, and endocrine systems."
      Lahiry P., Wang J., Robinson J.F., Turowec J.P., Litchfield D.W., Lanktree M.B., Gloor G.B., Puffenberger E.G., Strauss K.A., Martens M.B., Ramsay D.A., Rupar C.A., Siu V., Hegele R.A.
      Am. J. Hum. Genet. 84:134-147(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ECO GLN-272, CHARACTERIZATION OF VARIANT ECO GLN-272, POSSIBLE FUNCTION.

    Entry informationi

    Entry nameiICK_HUMAN
    AccessioniPrimary (citable) accession number: Q9UPZ9
    Secondary accession number(s): A7MD41
    , O75985, Q5THL2, Q8IYH8, Q9BX17, Q9NYX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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 6
      Human chromosome 6: 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