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P06240

- LCK_MOUSE

UniProt

P06240 - LCK_MOUSE

Protein

Proto-oncogene tyrosine-protein kinase LCK

Gene

Lck

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP By similarity. Interacts with UNC119; this interaction plays a crucial role in activation of LCK By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    The relative activities of the inhibitory tyrosine-protein kinase CSK and the activating tyrosine-protein phosphatase PTPRC/CD45 determine the level of LCK activity. These interactions allow rapid and efficient activation of LCK in response to TCR stimulation By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei273 – 2731ATPPROSITE-ProRule annotation
    Active sitei364 – 3641Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi251 – 2599ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. protein serine/threonine phosphatase activity Source: UniProtKB
    5. protein tyrosine kinase activity Source: UniProtKB
    6. SH2 domain binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    2. B cell receptor signaling pathway Source: MGI
    3. cell surface receptor signaling pathway Source: MGI
    4. cellular zinc ion homeostasis Source: UniProtKB
    5. dephosphorylation Source: GOC
    6. peptidyl-tyrosine phosphorylation Source: MGI
    7. positive regulation of gamma-delta T cell differentiation Source: MGI
    8. positive regulation of gene expression Source: MGI
    9. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    10. positive regulation of T cell activation Source: UniProtKB
    11. positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
    12. protein autophosphorylation Source: MGI
    13. protein phosphorylation Source: MGI
    14. regulation of T cell receptor signaling pathway Source: MGI
    15. release of sequestered calcium ion into cytosol Source: UniProtKB
    16. response to drug Source: UniProtKB
    17. T cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_204081. CD28 co-stimulation.
    REACT_215414. Translocation of ZAP-70 to Immunological synapse.
    REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225145. Downstream TCR signaling.
    REACT_225768. Generation of second messenger molecules.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_227425. Regulation of KIT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene tyrosine-protein kinase LCK (EC:2.7.10.2)
    Alternative name(s):
    Leukocyte C-terminal Src kinase
    Short name:
    LSK
    Lymphocyte cell-specific protein-tyrosine kinase
    p56-LCK
    Gene namesi
    Name:Lck
    Synonyms:Lsk-t
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:96756. Lck.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication
    Note: Present in lipid rafts in an inactive form.

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytosol Source: Reactome
    3. membrane raft Source: UniProtKB
    4. pericentriolar material Source: UniProtKB
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show a dramatic reduction in the level of peripheral T-cells, with 5-10% of wild-type levels. T-cells also exhibit a 10-fold decrease in proliferative response.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes myristoylation and palmitoylation. 1 Publication
    Mutagenesisi3 – 53CVC → SVK: Complete loss of interaction with CD4 or CD8. 2 Publications
    Mutagenesisi3 – 31C → S: Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level. 2 Publications
    Mutagenesisi5 – 51C → K: Reduced palmitoylation level. 2 Publications
    Mutagenesisi5 – 51C → S: Abolishes plasma membrane association; when associated with S-21. 2 Publications
    Mutagenesisi20 – 201C → S: Complete loss of interaction with CD4 or CD8. 1 Publication
    Mutagenesisi23 – 231C → S: Complete loss of interaction with CD4 or CD8. 1 Publication
    Mutagenesisi269 – 2691K → N: Reduced activity.
    Mutagenesisi270 – 2701V → L: Reduced activity.
    Mutagenesisi271 – 2711A → S: Reduced activity.
    Mutagenesisi272 – 2721V → A: Reduced activity.
    Mutagenesisi273 – 2731K → R: Loss of activity. 1 Publication
    Mutagenesisi274 – 2741S → N: Reduced activity.
    Mutagenesisi275 – 2751L → M: Reduced activity.
    Mutagenesisi276 – 2761K → V: Reduced activity.
    Mutagenesisi505 – 5051Y → F: Causes thymic tumors. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedCurated
    Chaini2 – 509508Proto-oncogene tyrosine-protein kinase LCKPRO_0000088125Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Lipidationi3 – 31S-palmitoyl cysteine2 Publications
    Lipidationi5 – 51S-palmitoyl cysteine2 Publications
    Modified residuei102 – 1021PhosphoserineBy similarity
    Modified residuei159 – 1591PhosphothreonineBy similarity
    Modified residuei162 – 1621PhosphoserineBy similarity
    Modified residuei194 – 1941PhosphoserineBy similarity
    Modified residuei394 – 3941Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei505 – 5051Phosphotyrosine; by CSKBy similarity

    Post-translational modificationi

    Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells differentiation By similarity.By similarity
    Myristoylation is required prior to palmitoylation.2 Publications
    Palmitoylation regulates subcellular location.By similarity

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP06240.
    PaxDbiP06240.
    PRIDEiP06240.

    PTM databases

    PhosphoSiteiP06240.

    Expressioni

    Tissue specificityi

    Present at a low level in most T-cells, and at an elevated level in LSTRA and Thy19 (T-cell lymphoma) cells.

    Developmental stagei

    Levels remain relatively constant throughout T-cell ontogeny.

    Gene expression databases

    ArrayExpressiP06240.
    BgeeiP06240.
    CleanExiMM_LCK.
    GenevestigatoriP06240.

    Interactioni

    Subunit structurei

    Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through its SH2 domain. Interacts with SQSTM1. Interacts with phosphorylated LIME1. Interacts with CBLB and PTPRH. Interacts with RUNX3. Forms a signaling complex with EPHA1, PTK2B AND PI3-KINASE; upon activation by EFNA1 which may regulate T-lymphocytes migration. Associates with ZAP70 and RHOH; these interactions allow LCK-mediated RHOH and CD3 subunit phosphorylation in the presence of functional ZAP70 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    O929722EBI-1401,EBI-710506From a different organism.
    P279583EBI-1401,EBI-706378From a different organism.
    Cd4P063323EBI-1401,EBI-1404
    Cd8aP017312EBI-1401,EBI-1433
    KHDRBS1Q076662EBI-1401,EBI-1364From a different organism.
    PTPRCP085752EBI-1401,EBI-1341From a different organism.
    PtprcP068003EBI-1401,EBI-1672
    Sh2d2aQ9QXK93EBI-1401,EBI-1644

    Protein-protein interaction databases

    BioGridi201120. 12 interactions.
    IntActiP06240. 18 interactions.
    MINTiMINT-85459.

    Structurei

    3D structure databases

    ProteinModelPortaliP06240.
    SMRiP06240. Positions 7-33, 64-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 12161SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini127 – 22498SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini245 – 498254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 7271Interactions with CD4 and CD8Add
    BLAST
    Regioni154 – 24289Interaction with PTPRHBy similarityAdd
    BLAST

    Domaini

    The SH2 domain mediates interaction with SQSTM1. Interaction is regulated by Ser-59 phosphorylation By similarity.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC 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.
    GeneTreeiENSGT00620000087866.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP06240.
    KOiK05856.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP06240.
    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.
    PR00452. SH3DOMAIN.
    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.

    P06240-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGCVCSSNPE DDWMENIDVC ENCHYPIVPL DSKISLPIRN GSEVRDPLVT    50
    YEGSLPPASP LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA 100
    QSLTTGQEGF IPFNFVAKAN SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS 150
    FLIRESESTA GSFSLSVRDF DQNQGEVVKH YKIRNLDNGG FYISPRITFP 200
    GLHDLVRHYT NASDGLCTKL SRPCQTQKPQ KPWWEDEWEV PRETLKLVER 250
    LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHPRL 300
    VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLNVNK LLDMAAQIAE 350
    GMAFIEEQNY IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA 400
    KFPIKWTAPE AINYGTFTIK SDVWSFGILL TEIVTHGRIP YPGMTNPEVI 450
    QNLERGYRMV RPDNCPEELY HLMMLCWKER PEDRPTFDYL RSVLDDFFTA 500
    TEGQYQPQP 509
    Length:509
    Mass (Da):57,943
    Last modified:January 23, 2007 - v4
    Checksum:i3513102F49A7FD0B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12056 mRNA. Translation: AAB59674.1.
    X03533 mRNA. Translation: CAA27234.1.
    X03533 mRNA. Translation: CAA27235.1. Sequence problems.
    X03533 mRNA. Translation: CAA27236.1. Sequence problems.
    AK088001 mRNA. Translation: BAC40086.1.
    BC011474 mRNA. Translation: AAH11474.1.
    M21511 Genomic DNA. Translation: AAA39422.1. Sequence problems.
    M18098 Genomic DNA. Translation: AAA39421.1.
    CCDSiCCDS18697.1.
    PIRiI48845.
    RefSeqiNP_001155905.1. NM_001162433.1.
    NP_034823.1. NM_010693.3.
    XP_006502881.1. XM_006502818.1.
    XP_006502882.1. XM_006502819.1.
    XP_006537018.1. XM_006536955.1.
    XP_006537019.1. XM_006536956.1.
    XP_006537020.1. XM_006536957.1.
    UniGeneiMm.293753.

    Genome annotation databases

    EnsembliENSMUST00000067240; ENSMUSP00000066209; ENSMUSG00000000409.
    ENSMUST00000102596; ENSMUSP00000099656; ENSMUSG00000000409.
    GeneIDi16818.
    KEGGimmu:16818.
    UCSCiuc008uxi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12056 mRNA. Translation: AAB59674.1 .
    X03533 mRNA. Translation: CAA27234.1 .
    X03533 mRNA. Translation: CAA27235.1 . Sequence problems.
    X03533 mRNA. Translation: CAA27236.1 . Sequence problems.
    AK088001 mRNA. Translation: BAC40086.1 .
    BC011474 mRNA. Translation: AAH11474.1 .
    M21511 Genomic DNA. Translation: AAA39422.1 . Sequence problems.
    M18098 Genomic DNA. Translation: AAA39421.1 .
    CCDSi CCDS18697.1.
    PIRi I48845.
    RefSeqi NP_001155905.1. NM_001162433.1.
    NP_034823.1. NM_010693.3.
    XP_006502881.1. XM_006502818.1.
    XP_006502882.1. XM_006502819.1.
    XP_006537018.1. XM_006536955.1.
    XP_006537019.1. XM_006536956.1.
    XP_006537020.1. XM_006536957.1.
    UniGenei Mm.293753.

    3D structure databases

    ProteinModelPortali P06240.
    SMRi P06240. Positions 7-33, 64-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201120. 12 interactions.
    IntActi P06240. 18 interactions.
    MINTi MINT-85459.

    Chemistry

    BindingDBi P06240.
    ChEMBLi CHEMBL2480.

    PTM databases

    PhosphoSitei P06240.

    Proteomic databases

    MaxQBi P06240.
    PaxDbi P06240.
    PRIDEi P06240.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067240 ; ENSMUSP00000066209 ; ENSMUSG00000000409 .
    ENSMUST00000102596 ; ENSMUSP00000099656 ; ENSMUSG00000000409 .
    GeneIDi 16818.
    KEGGi mmu:16818.
    UCSCi uc008uxi.2. mouse.

    Organism-specific databases

    CTDi 3932.
    MGIi MGI:96756. Lck.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087866.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P06240.
    KOi K05856.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P06240.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_188185. DAP12 signaling.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_204081. CD28 co-stimulation.
    REACT_215414. Translocation of ZAP-70 to Immunological synapse.
    REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225145. Downstream TCR signaling.
    REACT_225768. Generation of second messenger molecules.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_227425. Regulation of KIT signaling.

    Miscellaneous databases

    NextBioi 290704.
    PROi P06240.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06240.
    Bgeei P06240.
    CleanExi MM_LCK.
    Genevestigatori P06240.

    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.
    PR00452. SH3DOMAIN.
    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. "A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA."
      Marth J.D., Peet R., Krebs E.G., Perlmutter R.M.
      Cell 43:393-404(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion."
      Voronova A.F., Sefton B.M.
      Nature 319:682-685(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Thymus.
    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: FVB/N.
      Tissue: Salivary gland.
    5. "Structure of the murine lck gene and its rearrangement in a murine lymphoma cell line."
      Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.
      Mol. Cell. Biol. 8:3058-3064(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
    6. "Two lck transcripts containing different 5' untranslated regions are present in T cells."
      Voronova A.F., Adler H.T., Sefton B.M.
      Mol. Cell. Biol. 7:4407-4413(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    7. "Avian reovirus mRNAs are nonfunctional in infected mouse cells: translational basis for virus host-range restriction."
      Amrein K.E., Sefton B.M.
      Proc. Natl. Acad. Sci. U.S.A. 85:4257-4261(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-505.
    8. "Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs."
      Turner J.M., Brodsky M.H., Irving B.A., Levin S.D., Perlmutter R.M., Littman D.R.
      Cell 60:755-765(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD4 AND CD8, MUTAGENESIS OF 3-CYS--CYS-5; CYS-20 AND CYS-23.
    9. "Creation and characterization of temperature-sensitive mutants of the lck tyrosine protein kinase."
      Hurley T.R., Amrein K.E., Sefton B.M.
      J. Virol. 66:7406-7413(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    10. "Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck."
      Abraham N., Miceli M.C., Parnes J.C., Veillette A.
      Nature 350:62-66(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-273.
    11. Cited for: PHOSPHORYLATION AT TYR-505, MUTAGENESIS OF TYR-505.
    12. Cited for: DISRUPTION PHENOTYPE.
    13. "Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk."
      Chow L.M., Fournel M., Davidson D., Veillette A.
      Nature 365:156-160(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CSK.
    14. "The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP."
      Carrera A.C., Alexandrov K., Roberts T.M.
      Proc. Natl. Acad. Sci. U.S.A. 90:442-446(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    15. "Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins."
      Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.
      Mol. Cell. Biol. 13:6385-6392(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3 AND CYS-5, MUTAGENESIS OF CYS-3 AND CYS-5.
    16. "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
      Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
      Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-3 AND CYS-5, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-5.
    17. Cited for: INTERACTION WITH CBLB.
    18. "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: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLCK_MOUSE
    AccessioniPrimary (citable) accession number: P06240
    Secondary accession number(s): Q61794
    , Q61795, Q62320, Q91X65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 172 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3