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P41240

- CSK_HUMAN

UniProt

P41240 - CSK_HUMAN

Protein

Tyrosine-protein kinase CSK

Gene

CSK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK.2 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei222 – 2221ATPPROSITE-ProRule annotation
    Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi201 – 2099ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: ProtInc
    6. protein tyrosine kinase activity Source: Reactome

    GO - Biological processi

    1. adherens junction organization Source: Ensembl
    2. blood coagulation Source: Reactome
    3. brain development Source: Ensembl
    4. cellular response to peptide hormone stimulus Source: Ensembl
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. negative regulation of bone resorption Source: Ensembl
    7. negative regulation of cell proliferation Source: Ensembl
    8. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    9. negative regulation of Golgi to plasma membrane protein transport Source: UniProtKB
    10. negative regulation of interleukin-6 production Source: Ensembl
    11. negative regulation of kinase activity Source: Ensembl
    12. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
    13. negative regulation of phagocytosis Source: Ensembl
    14. oligodendrocyte differentiation Source: Ensembl
    15. peptidyl-tyrosine phosphorylation Source: GOC
    16. platelet activation Source: Reactome
    17. positive regulation of MAP kinase activity Source: Ensembl
    18. protein autophosphorylation Source: Ensembl
    19. protein phosphorylation Source: ProtInc
    20. regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
    21. T cell costimulation Source: Reactome
    22. T cell receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_12578. GAB1 signalosome.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_19324. PD-1 signaling.
    SignaLinkiP41240.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase CSK (EC:2.7.10.2)
    Alternative name(s):
    C-Src kinase
    Protein-tyrosine kinase CYL
    Gene namesi
    Name:CSK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2444. CSK.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Mainly cytoplasmic, also present in lipid rafts.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. cytoplasm Source: HGNC
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. membrane raft Source: Ensembl
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi184 – 1841Y → F: Abolishes phosphorylation. 1 Publication
    Mutagenesisi304 – 3041Y → F: Decreases activity by two-thirds and alters conformation. 1 Publication
    Mutagenesisi364 – 3641S → A: Strong decrease of phosphorylation by PRKACA (catalytic subunit of PKA). 1 Publication

    Organism-specific databases

    PharmGKBiPA26946.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 450449Tyrosine-protein kinase CSKPRO_0000088070Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei184 – 1841Phosphotyrosine1 Publication
    Modified residuei304 – 3041Phosphotyrosine1 Publication
    Modified residuei364 – 3641Phosphoserine; by PKA1 Publication
    Modified residuei416 – 4161Phosphotyrosine

    Post-translational modificationi

    Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP41240.
    PaxDbiP41240.
    PRIDEiP41240.

    2D gel databases

    OGPiP41240.

    PTM databases

    PhosphoSiteiP41240.

    Expressioni

    Tissue specificityi

    Expressed in lung and macrophages.1 Publication

    Gene expression databases

    ArrayExpressiP41240.
    BgeeiP41240.
    CleanExiHS_CSK.
    GenevestigatoriP41240.

    Organism-specific databases

    HPAiCAB011203.
    HPA026488.
    HPA028425.

    Interactioni

    Subunit structurei

    Homodimer (via SH3-domain). Interacts with PTPN8 By similarity. Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases. Interacts with SRCIN1. Interacts with RHOH. Interacts (via SH2 domain) with SCIMP.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-1380630,EBI-1380630
    IGF1RP080695EBI-1380630,EBI-475981
    PTPRCP085753EBI-1380630,EBI-1341
    PXNP490232EBI-1380630,EBI-702209
    SRCP005236EBI-1380630,EBI-848039From a different organism.

    Protein-protein interaction databases

    BioGridi107832. 45 interactions.
    IntActiP41240. 32 interactions.
    MINTiMINT-85878.
    STRINGi9606.ENSP00000220003.

    Structurei

    Secondary structure

    1
    450
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 187
    Beta strandi35 – 417
    Beta strandi47 – 515
    Beta strandi57 – 615
    Beta strandi64 – 663
    Helixi77 – 793
    Beta strandi83 – 864
    Helixi89 – 957
    Beta strandi103 – 1086
    Beta strandi116 – 1227
    Beta strandi125 – 1306
    Beta strandi132 – 1343
    Beta strandi137 – 1448
    Beta strandi146 – 1483
    Helixi149 – 15810
    Beta strandi163 – 1653
    Helixi192 – 1943
    Beta strandi195 – 2039
    Beta strandi208 – 2147
    Beta strandi217 – 2237
    Helixi231 – 2355
    Helixi237 – 2404
    Beta strandi251 – 2555
    Beta strandi263 – 2664
    Helixi274 – 28512
    Helixi288 – 30720
    Helixi317 – 3193
    Beta strandi320 – 3223
    Beta strandi328 – 3303
    Turni350 – 3523
    Helixi355 – 3606
    Helixi365 – 38016
    Helixi392 – 3943
    Helixi395 – 3995
    Turni400 – 4023
    Helixi413 – 42210
    Helixi427 – 4293
    Helixi433 – 44614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BYGX-ray2.40A173-450[»]
    1CSKX-ray2.50A/B/C/D1-71[»]
    3D7TX-ray2.90A188-450[»]
    3D7UX-ray4.11A/C188-450[»]
    3EACX-ray1.37A73-178[»]
    3EAZX-ray1.31A73-178[»]
    ProteinModelPortaliP41240.
    SMRiP41240. Positions 4-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41240.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 7062SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini82 – 17190SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini195 – 449255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni9 – 7062Interaction with PTPN8By similarityAdd
    BLAST

    Domaini

    The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP41240.
    KOiK05728.
    OMAiERLLCPP.
    OrthoDBiEOG7SV0V5.
    PhylomeDBiP41240.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P41240-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA    50
    KNKVGREGII PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE 100
    TGLFLVREST NYPGDYTLCV SCDGKVEHYR IMYHASKLSI DEEVYFENLM 150
    QLVEHYTSDA DGLCTRLIKP KVMEGTVAAQ DEFYRSGWAL NMKELKLLQT 200
    IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM TQLRHSNLVQ 250
    LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE 300
    AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV 350
    KWTAPEALRE KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE 400
    KGYKMDAPDG CPPAVYEVMK NCWHLDAAMR PSFLQLREQL EHIKTHELHL 450
    Length:450
    Mass (Da):50,704
    Last modified:February 1, 1995 - v1
    Checksum:i431023A88C54E00C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451P → L.1 Publication
    VAR_041678
    Natural varianti287 – 2871G → D.1 Publication
    Corresponds to variant rs34866753 [ dbSNP | Ensembl ].
    VAR_025203
    Natural varianti398 – 3981R → Q.1 Publication
    Corresponds to variant rs34616395 [ dbSNP | Ensembl ].
    VAR_025204
    Natural varianti442 – 4421H → R.1 Publication
    Corresponds to variant rs35556162 [ dbSNP | Ensembl ].
    VAR_025205

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60114 mRNA. Translation: CAA42713.1.
    X59932 mRNA. Translation: CAA42556.1.
    X74765 Genomic DNA. Translation: CAB58562.1.
    CR541960 mRNA. Translation: CAG46758.1.
    DQ075211 Genomic DNA. Translation: AAY57329.1.
    BC104847 mRNA. Translation: AAI04848.1.
    BC104875 mRNA. Translation: AAI04876.1.
    BC106073 mRNA. Translation: AAI06074.1.
    CCDSiCCDS10269.1.
    PIRiJH0559.
    RefSeqiNP_001120662.1. NM_001127190.1.
    NP_004374.1. NM_004383.2.
    XP_005254222.1. XM_005254165.2.
    UniGeneiHs.77793.

    Genome annotation databases

    EnsembliENST00000220003; ENSP00000220003; ENSG00000103653.
    ENST00000439220; ENSP00000414764; ENSG00000103653.
    ENST00000567571; ENSP00000454906; ENSG00000103653.
    GeneIDi1445.
    KEGGihsa:1445.
    UCSCiuc002ays.2. human.

    Polymorphism databases

    DMDMi729887.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60114 mRNA. Translation: CAA42713.1 .
    X59932 mRNA. Translation: CAA42556.1 .
    X74765 Genomic DNA. Translation: CAB58562.1 .
    CR541960 mRNA. Translation: CAG46758.1 .
    DQ075211 Genomic DNA. Translation: AAY57329.1 .
    BC104847 mRNA. Translation: AAI04848.1 .
    BC104875 mRNA. Translation: AAI04876.1 .
    BC106073 mRNA. Translation: AAI06074.1 .
    CCDSi CCDS10269.1.
    PIRi JH0559.
    RefSeqi NP_001120662.1. NM_001127190.1.
    NP_004374.1. NM_004383.2.
    XP_005254222.1. XM_005254165.2.
    UniGenei Hs.77793.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BYG X-ray 2.40 A 173-450 [» ]
    1CSK X-ray 2.50 A/B/C/D 1-71 [» ]
    3D7T X-ray 2.90 A 188-450 [» ]
    3D7U X-ray 4.11 A/C 188-450 [» ]
    3EAC X-ray 1.37 A 73-178 [» ]
    3EAZ X-ray 1.31 A 73-178 [» ]
    ProteinModelPortali P41240.
    SMRi P41240. Positions 4-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107832. 45 interactions.
    IntActi P41240. 32 interactions.
    MINTi MINT-85878.
    STRINGi 9606.ENSP00000220003.

    Chemistry

    BindingDBi P41240.
    ChEMBLi CHEMBL2634.
    GuidetoPHARMACOLOGYi 1994.

    PTM databases

    PhosphoSitei P41240.

    Polymorphism databases

    DMDMi 729887.

    2D gel databases

    OGPi P41240.

    Proteomic databases

    MaxQBi P41240.
    PaxDbi P41240.
    PRIDEi P41240.

    Protocols and materials databases

    DNASUi 1445.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000220003 ; ENSP00000220003 ; ENSG00000103653 .
    ENST00000439220 ; ENSP00000414764 ; ENSG00000103653 .
    ENST00000567571 ; ENSP00000454906 ; ENSG00000103653 .
    GeneIDi 1445.
    KEGGi hsa:1445.
    UCSCi uc002ays.2. human.

    Organism-specific databases

    CTDi 1445.
    GeneCardsi GC15P075075.
    HGNCi HGNC:2444. CSK.
    HPAi CAB011203.
    HPA026488.
    HPA028425.
    MIMi 124095. gene.
    neXtProti NX_P41240.
    PharmGKBi PA26946.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P41240.
    KOi K05728.
    OMAi ERLLCPP.
    OrthoDBi EOG7SV0V5.
    PhylomeDBi P41240.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_12578. GAB1 signalosome.
    REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_19324. PD-1 signaling.
    SignaLinki P41240.

    Miscellaneous databases

    EvolutionaryTracei P41240.
    GeneWikii C-src_tyrosine_kinase.
    GenomeRNAii 1445.
    NextBioi 5937.
    PROi P41240.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41240.
    Bgeei P41240.
    CleanExi HS_CSK.
    Genevestigatori P41240.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CYL encodes a putative cytoplasmic tyrosine kinase lacking the conserved tyrosine autophosphorylation site (Y416src)."
      Partanen J., Armstrong E., Bergman M., Maekelae T.P., Hirvonen H., Huebner K., Alitalo K.
      Oncogene 6:2013-2018(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase."
      Braeuninger A., Holtrich U., Strebhardt K., Ruebsamen-Waigmann H.
      Proc. Natl. Acad. Sci. U.S.A. 88:10411-10415(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Isolation and characterization of a human gene that encodes a new subclass of protein tyrosine kinases."
      Brauninger A., Holtrich U., Strebhardt K., Rubsamen-Waigmann H.
      Gene 110:205-211(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    4. "Characterization of the human CSK locus."
      Braeuninger A., Karn T., Strebhardt K., Ruebsamen-Waigmann H.
      Oncogene 8:1365-1369(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-287; GLN-398 AND ARG-442.
    7. "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].
      Tissue: Brain and Uterus.
    8. "The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity."
      Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A., Amrein K.E., Autero M., Burn P., Alitalo K.
      EMBO J. 11:2919-2924(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LCK.
    9. "Recombinant Csk expressed in Escherichia coli is autophosphorylated on tyrosine residue(s)."
      Bougeret C., Rothhut B., Jullien P., Fischer S., Benarous R.
      Oncogene 8:1241-1247(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION.
    10. "Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system."
      Sun G., Budde R.J.
      Arch. Biochem. Biophys. 345:135-142(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF YES1.
    11. "Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure."
      Joukov V., Vihinen M., Vainikka S., Sowadski J.M., Alitalo K., Bergman M.
      Biochem. J. 322:927-935(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-184 AND TYR-304, MUTAGENESIS OF TYR-184 AND TYR-304.
    12. "Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."
      Ishino M., Aoto H., Sasaski H., Suzuki R., Sasaki T.
      FEBS Lett. 474:179-183(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    13. "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
      Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
      J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAG1.
    14. "Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)."
      Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A., Spicka J., Hilgert I., Scherer J., Schraven B.
      Eur. J. Immunol. 31:1825-1836(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIT1.
    15. "Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor."
      Vang T., Torgersen K.M., Sundvold V., Saxena M., Levy F.O., Skalhegg B.S., Hansson V., Mustelin T., Tasken K.
      J. Exp. Med. 193:497-507(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-364 BY PKA, MUTAGENESIS OF SER-364.
    16. "LIME: a new membrane raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling."
      Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.
      J. Exp. Med. 198:1453-1462(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIME1.
    17. "C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases."
      Chong Y.P., Mulhern T.D., Cheng H.C.
      Growth Factors 23:233-244(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity."
      Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A., Piva R., Cavallo F., Forni G., Silengo L., Tarone G., Turco E., Defilippi P.
      EMBO J. 26:2843-2855(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRCIN1.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    20. "The tyrosine kinase Csk dimerizes through Its SH3 domain."
      Levinson N.M., Visperas P.R., Kuriyan J.
      PLoS ONE 4:E7683-E7683(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "RhoH modulates pre-TCR and TCR signalling by regulating LCK."
      Wang H., Zeng X., Fan Z., Lim B.
      Cell. Signal. 23:249-258(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RHOH.
    23. "SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling."
      Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.
      Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCIMP.
    24. "The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop."
      Borchert T.V., Mathieu M., Zeelen J.P., Courtneidge S.A., Wierenga R.K.
      FEBS Lett. 341:79-85(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-71.
    25. "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: VARIANT [LARGE SCALE ANALYSIS] LEU-45.

    Entry informationi

    Entry nameiCSK_HUMAN
    AccessioniPrimary (citable) accession number: P41240
    Secondary accession number(s): Q2M3N2, Q6FGZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 169 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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