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P41241

- CSK_MOUSE

UniProt

P41241 - CSK_MOUSE

Protein

Tyrosine-protein kinase CSK

Gene

Csk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 By similarity.By similarity

    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: HGNC
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. protein binding Source: HGNC
    4. protein tyrosine kinase activity Source: HGNC
    5. transferase activity Source: HGNC

    GO - Biological processi

    1. adherens junction organization Source: Ensembl
    2. brain development Source: Ensembl
    3. cellular response to peptide hormone stimulus Source: Ensembl
    4. immune system process Source: UniProtKB-KW
    5. intracellular signal transduction Source: HGNC
    6. negative regulation of bone resorption Source: Ensembl
    7. negative regulation of cell proliferation Source: MGI
    8. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    9. negative regulation of Golgi to plasma membrane protein transport Source: Ensembl
    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. positive regulation of MAP kinase activity Source: Ensembl
    17. protein autophosphorylation Source: Ensembl
    18. protein phosphorylation Source: HGNC
    19. regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
    20. regulation of T cell activation Source: HGNC

    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. 3474.
    ReactomeiREACT_206286. GAB1 signalosome.
    REACT_216080. Phosphorylation of CD3 and TCR zeta chains.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase CSK (EC:2.7.10.2)
    Alternative name(s):
    C-Src kinase
    Protein-tyrosine kinase MPK-2
    p50CSK
    Gene namesi
    Name:Csk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:88537. Csk.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication
    Note: Mainly cytoplasmic, also present in lipid rafts.

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. centrosome Source: Ensembl
    3. Golgi apparatus Source: Ensembl
    4. membrane raft Source: Ensembl
    5. plasma membrane Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice die between day 9 and day 10 of gestation with several defects including a non-functional neural tube. SRC and FYN kinases show increased activity when CSK is missing.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 450449Tyrosine-protein kinase CSKPRO_0000088071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei184 – 1841PhosphotyrosineBy similarity
    Modified residuei304 – 3041PhosphotyrosineBy similarity
    Modified residuei364 – 3641Phosphoserine; by PKABy similarity
    Modified residuei416 – 4161Phosphotyrosine

    Post-translational modificationi

    Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP41241.
    PaxDbiP41241.
    PRIDEiP41241.

    PTM databases

    PhosphoSiteiP41241.

    Expressioni

    Tissue specificityi

    Ubiquitous, but most abundant in thymus and spleen, as well as in neonatal brain.

    Gene expression databases

    BgeeiP41241.
    CleanExiMM_CSK.
    GenevestigatoriP41241.

    Interactioni

    Subunit structurei

    Homodimer (via SH3-domain). Interacts with PTPN8. 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 similarity.By similarity

    Protein-protein interaction databases

    BioGridi198936. 9 interactions.
    IntActiP41241. 6 interactions.
    MINTiMINT-1345201.

    Structurei

    Secondary structure

    1
    450
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 186
    Beta strandi35 – 417
    Beta strandi43 – 519
    Beta strandi57 – 615
    Helixi62 – 643
    Beta strandi65 – 673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JEGNMR-A1-83[»]
    ProteinModelPortaliP41241.
    SMRiP41241. Positions 4-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41241.

    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 PTPN8Add
    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.By similarity

    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.
    GeneTreeiENSGT00750000117264.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiQ8VCW1.
    KOiK05728.
    OMAiERLLCPP.
    OrthoDBiEOG7SV0V5.
    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.

    P41241-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA    50
    KNKVGREGII PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE 100
    TGLFLVREST NYPGDYTLCV SCEGKVEHYR IMYHASKLSI DEEVYFENLM 150
    QLVEHYTTDA 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 NCWHLDAATR PTFLQLREQL EHIKTHELHL 450
    Length:450
    Mass (Da):50,716
    Last modified:July 27, 2011 - v2
    Checksum:iE8D3EC9357B86277
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti299 – 2991C → L in AAA18766. (PubMed:7511815)Curated
    Sequence conflicti417 – 4171E → D in AAA18766. (PubMed:7511815)Curated
    Sequence conflicti423 – 4231W → S in AAA18766. (PubMed:7511815)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05247 mRNA. Translation: AAA18766.1.
    AY902339 Genomic DNA. Translation: AAX90624.1.
    AK156058 mRNA. Translation: BAE33565.1.
    AK170815 mRNA. Translation: BAE42047.1.
    BC018394 mRNA. Translation: AAH18394.1.
    BC052006 mRNA. Translation: AAH52006.2.
    X57242 mRNA. Translation: CAA40518.1.
    CCDSiCCDS23228.1.
    PIRiI48929.
    RefSeqiNP_031809.2. NM_007783.2.
    XP_006510864.1. XM_006510801.1.
    XP_006510865.1. XM_006510802.1.
    XP_006510866.1. XM_006510803.1.
    UniGeneiMm.21974.

    Genome annotation databases

    EnsembliENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
    GeneIDi12988.
    KEGGimmu:12988.
    UCSCiuc009pvk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05247 mRNA. Translation: AAA18766.1 .
    AY902339 Genomic DNA. Translation: AAX90624.1 .
    AK156058 mRNA. Translation: BAE33565.1 .
    AK170815 mRNA. Translation: BAE42047.1 .
    BC018394 mRNA. Translation: AAH18394.1 .
    BC052006 mRNA. Translation: AAH52006.2 .
    X57242 mRNA. Translation: CAA40518.1 .
    CCDSi CCDS23228.1.
    PIRi I48929.
    RefSeqi NP_031809.2. NM_007783.2.
    XP_006510864.1. XM_006510801.1.
    XP_006510865.1. XM_006510802.1.
    XP_006510866.1. XM_006510803.1.
    UniGenei Mm.21974.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JEG NMR - A 1-83 [» ]
    ProteinModelPortali P41241.
    SMRi P41241. Positions 4-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198936. 9 interactions.
    IntActi P41241. 6 interactions.
    MINTi MINT-1345201.

    Chemistry

    BindingDBi P41241.

    PTM databases

    PhosphoSitei P41241.

    Proteomic databases

    MaxQBi P41241.
    PaxDbi P41241.
    PRIDEi P41241.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034863 ; ENSMUSP00000034863 ; ENSMUSG00000032312 .
    GeneIDi 12988.
    KEGGi mmu:12988.
    UCSCi uc009pvk.1. mouse.

    Organism-specific databases

    CTDi 1445.
    MGIi MGI:88537. Csk.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117264.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi Q8VCW1.
    KOi K05728.
    OMAi ERLLCPP.
    OrthoDBi EOG7SV0V5.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_206286. GAB1 signalosome.
    REACT_216080. Phosphorylation of CD3 and TCR zeta chains.

    Miscellaneous databases

    EvolutionaryTracei P41241.
    NextBioi 282780.
    PROi P41241.
    SOURCEi Search...

    Gene expression databases

    Bgeei P41241.
    CleanExi MM_CSK.
    Genevestigatori P41241.

    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. "Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme family."
      Klages S., Adam D., Class K., Fargnoli J., Bolen J.B., Penhallow R.C.
      Proc. Natl. Acad. Sci. U.S.A. 91:2597-2601(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
      Farber C.R., Corva P.M., Medrano J.F.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CAST/Ei.
      Tissue: Brain.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Spleen.
    4. "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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Colon.
    5. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
      Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
      Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 316-367.
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    6. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 338-347, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice."
      Imamoto A., Soriano P.
      Cell 73:1117-1124(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    8. "Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells."
      Cloutier J.-F., Veillette A.
      EMBO J. 15:4909-4918(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN8.
    9. "Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin."
      Thomas S.M., Hagel M., Turner C.E.
      J. Cell Sci. 112:181-190(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    10. "Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
      Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
      J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAG1.
    11. "Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor."
      Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.
      Mol. Cell. Biol. 23:2017-2028(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAG1.
    12. "Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development."
      Xu S., Huo J., Tan J.E.-L., Lam K.-P.
      Mol. Cell. Biol. 25:8486-8495(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAG1, SUBCELLULAR LOCATION.
    13. "A novel, specific interaction involving the Csk SH3 domain and its natural ligand."
      Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.
      Nat. Struct. Biol. 8:998-1004(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-83.

    Entry informationi

    Entry nameiCSK_MOUSE
    AccessioniPrimary (citable) accession number: P41241
    Secondary accession number(s): Q03143, Q80WU4, Q8VCW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3