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Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)

 LCK_MOUSE               Reviewed;         509 AA.
P06240; Q61794; Q61795; Q62320; Q91X65;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 203.
RecName: Full=Proto-oncogene tyrosine-protein kinase LCK;
EC=2.7.10.2;
AltName: Full=Leukocyte C-terminal Src kinase;
Short=LSK;
AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase;
AltName: Full=p56-LCK;
Name=Lck; Synonyms=Lsk-t;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2416464; DOI=10.1016/0092-8674(85)90169-2;
Marth J.D., Peet R., Krebs E.G., Perlmutter R.M.;
"A lymphocyte-specific protein-tyrosine kinase gene is rearranged and
overexpressed in the murine T cell lymphoma LSTRA.";
Cell 43:393-404(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3081813; DOI=10.1038/319682a0;
Voronova A.F., Sefton B.M.;
"Expression of a new tyrosine protein kinase is stimulated by
retrovirus promoter insertion.";
Nature 319:682-685(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
PubMed=2850479; DOI=10.1128/MCB.8.8.3058;
Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.;
"Structure of the murine lck gene and its rearrangement in a murine
lymphoma cell line.";
Mol. Cell. Biol. 8:3058-3064(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=3501824; DOI=10.1128/MCB.7.12.4407;
Voronova A.F., Adler H.T., Sefton B.M.;
"Two lck transcripts containing different 5' untranslated regions are
present in T cells.";
Mol. Cell. Biol. 7:4407-4413(1987).
[7]
MUTAGENESIS OF TYR-505.
PubMed=3380790; DOI=10.1073/pnas.85.12.4257;
Amrein K.E., Sefton B.M.;
"Avian reovirus mRNAs are nonfunctional in infected mouse cells:
translational basis for virus host-range restriction.";
Proc. Natl. Acad. Sci. U.S.A. 85:4257-4261(1988).
[8]
INTERACTION WITH CD4 AND CD8, AND MUTAGENESIS OF 3-CYS--CYS-5; CYS-20
AND CYS-23.
PubMed=2107025; DOI=10.1016/0092-8674(90)90090-2;
Turner J.M., Brodsky M.H., Irving B.A., Levin S.D., Perlmutter R.M.,
Littman D.R.;
"Interaction of the unique N-terminal region of tyrosine kinase p56lck
with cytoplasmic domains of CD4 and CD8 is mediated by cysteine
motifs.";
Cell 60:755-765(1990).
[9]
MUTAGENESIS.
PubMed=1279202;
Hurley T.R., Amrein K.E., Sefton B.M.;
"Creation and characterization of temperature-sensitive mutants of the
lck tyrosine protein kinase.";
J. Virol. 66:7406-7413(1992).
[10]
MUTAGENESIS OF LYS-273.
PubMed=1706070; DOI=10.1038/350062a0;
Abraham N., Miceli M.C., Parnes J.C., Veillette A.;
"Enhancement of T-cell responsiveness by the lymphocyte-specific
tyrosine protein kinase p56lck.";
Nature 350:62-66(1991).
[11]
PHOSPHORYLATION AT TYR-505, AND MUTAGENESIS OF TYR-505.
PubMed=1708890; DOI=10.1073/pnas.88.9.3977;
Abraham K.M., Levin S.D., Marth J.D., Forbush K.A., Perlmutter R.M.;
"Thymic tumorigenesis induced by overexpression of p56lck.";
Proc. Natl. Acad. Sci. U.S.A. 88:3977-3981(1991).
[12]
DISRUPTION PHENOTYPE.
PubMed=1579166; DOI=10.1038/357161a0;
Molina T.J., Kishihara K., Siderovski D.P., van Ewijk W.,
Narendran A., Timms E., Wakeham A., Paige C.J., Hartmann K.U.,
Veillette A.;
"Profound block in thymocyte development in mice lacking p56lck.";
Nature 357:161-164(1992).
[13]
PHOSPHORYLATION BY CSK.
PubMed=8371758; DOI=10.1038/365156a0;
Chow L.M., Fournel M., Davidson D., Veillette A.;
"Negative regulation of T-cell receptor signalling by tyrosine protein
kinase p50csk.";
Nature 365:156-160(1993).
[14]
MUTAGENESIS.
PubMed=8421674; DOI=10.1073/pnas.90.2.442;
Carrera A.C., Alexandrov K., Roberts T.M.;
"The conserved lysine of the catalytic domain of protein kinases is
actively involved in the phosphotransfer reaction and not required for
anchoring ATP.";
Proc. Natl. Acad. Sci. U.S.A. 90:442-446(1993).
[15]
PALMITOYLATION AT CYS-3 AND CYS-5, AND MUTAGENESIS OF CYS-3 AND CYS-5.
PubMed=8413237; DOI=10.1128/MCB.13.10.6385;
Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.;
"Palmitylation of an amino-terminal cysteine motif of protein tyrosine
kinases p56lck and p59fyn mediates interaction with glycosyl-
phosphatidylinositol-anchored proteins.";
Mol. Cell. Biol. 13:6385-6392(1993).
[16]
PALMITOYLATION AT CYS-3 AND CYS-5, MYRISTOYLATION AT GLY-2, AND
MUTAGENESIS OF GLY-2; CYS-3 AND CYS-5.
PubMed=7980442; DOI=10.1042/bj3030749;
Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.;
"Palmitoylation of multiple Src-family kinases at a homologous N-
terminal motif.";
Biochem. J. 303:749-753(1994).
[17]
INTERACTION WITH CBLB.
PubMed=10646608; DOI=10.1038/35003228;
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A.,
Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S.,
Penninger J.M.;
"Negative regulation of lymphocyte activation and autoimmunity by the
molecular adaptor Cbl-b.";
Nature 403:211-216(2000).
[18]
SUBCELLULAR LOCATION.
PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T.,
Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
"Fyn is essential for tyrosine phosphorylation of Csk-binding
protein/phosphoprotein associated with glycolipid-enriched
microdomains in lipid rafts in resting T cells.";
J. Immunol. 169:2813-2817(2002).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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 tyrosine 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: 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). {ECO:0000250}.
-!- SUBUNIT: 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, FYB1
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. Interacts
with CEACAM1 (via cytoplasmic domain); mediates CEACAM1
phosphorylation resulting in PTPN6 recruitment that
dephosphorylates TCR stimulation-induced CD247 and ZAP70.
Interacts with FYB2 (By similarity).
{ECO:0000250|UniProtKB:P06239}.
-!- INTERACTION:
O92972:- (xeno); NbExp=2; IntAct=EBI-1401, EBI-710506;
P27958:- (xeno); NbExp=3; IntAct=EBI-1401, EBI-706378;
Q63767:Bcar1 (xeno); NbExp=2; IntAct=EBI-1401, EBI-1176801;
P22681:CBL (xeno); NbExp=2; IntAct=EBI-1401, EBI-518228;
P06332:Cd4; NbExp=3; IntAct=EBI-1401, EBI-1404;
P01731:Cd8a; NbExp=2; IntAct=EBI-1401, EBI-1433;
P49710:Hcls1; NbExp=6; IntAct=EBI-1401, EBI-924601;
Q07666:KHDRBS1 (xeno); NbExp=2; IntAct=EBI-1401, EBI-1364;
P08575:PTPRC (xeno); NbExp=2; IntAct=EBI-1401, EBI-1341;
P06800:Ptprc; NbExp=3; IntAct=EBI-1401, EBI-1672;
Q9QXK9:Sh2d2a; NbExp=3; IntAct=EBI-1401, EBI-1644;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218089}.
Cell membrane {ECO:0000269|PubMed:12218089}; Lipid-anchor
{ECO:0000269|PubMed:12218089}; Cytoplasmic side
{ECO:0000269|PubMed:12218089}. Note=Present in lipid rafts in an
inactive form.
-!- TISSUE SPECIFICITY: Present at a low level in most T-cells, and at
an elevated level in LSTRA and Thy19 (T-cell lymphoma) cells.
-!- DEVELOPMENTAL STAGE: Levels remain relatively constant throughout
T-cell ontogeny.
-!- DOMAIN: The SH2 domain mediates interaction with SQSTM1.
Interaction is regulated by Ser-59 phosphorylation (By
similarity). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Myristoylation is required prior to palmitoylation.
{ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237}.
-!- PTM: Palmitoylation regulates subcellular location. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:1579166}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M12056; AAB59674.1; -; mRNA.
EMBL; X03533; CAA27234.1; -; mRNA.
EMBL; X03533; CAA27235.1; ALT_SEQ; mRNA.
EMBL; X03533; CAA27236.1; ALT_SEQ; mRNA.
EMBL; AK088001; BAC40086.1; -; mRNA.
EMBL; BC011474; AAH11474.1; -; mRNA.
EMBL; M21511; AAA39422.1; ALT_SEQ; Genomic_DNA.
EMBL; M18098; AAA39421.1; -; Genomic_DNA.
CCDS; CCDS18697.1; -.
PIR; I48845; I48845.
RefSeq; NP_001155905.1; NM_001162433.1.
RefSeq; NP_034823.1; NM_010693.3.
RefSeq; XP_006502881.1; XM_006502818.3.
UniGene; Mm.293753; -.
ProteinModelPortal; P06240; -.
SMR; P06240; -.
BioGrid; 201120; 28.
CORUM; P06240; -.
ELM; P06240; -.
IntAct; P06240; 38.
MINT; MINT-85459; -.
STRING; 10090.ENSMUSP00000125777; -.
BindingDB; P06240; -.
ChEMBL; CHEMBL2480; -.
iPTMnet; P06240; -.
PhosphoSitePlus; P06240; -.
SwissPalm; P06240; -.
EPD; P06240; -.
MaxQB; P06240; -.
PaxDb; P06240; -.
PRIDE; P06240; -.
Ensembl; ENSMUST00000067240; ENSMUSP00000066209; ENSMUSG00000000409.
Ensembl; ENSMUST00000102596; ENSMUSP00000099656; ENSMUSG00000000409.
GeneID; 16818; -.
KEGG; mmu:16818; -.
UCSC; uc008uxi.2; mouse.
CTD; 3932; -.
MGI; MGI:96756; Lck.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P06240; -.
KO; K05856; -.
PhylomeDB; P06240; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-MMU-202433; Generation of second messenger molecules.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-389356; CD28 co-stimulation.
Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-389948; PD-1 signaling.
Reactome; R-MMU-451927; Interleukin-2 family signaling.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:P06240; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000000409; -.
CleanEx; MM_LCK; -.
ExpressionAtlas; P06240; baseline and differential.
Genevisible; P06240; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0001772; C:immunological synapse; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051117; F:ATPase binding; ISO:MGI.
GO; GO:0042609; F:CD4 receptor binding; IPI:UniProtKB.
GO; GO:0042610; F:CD8 receptor binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
GO; GO:1990405; F:protein antigen binding; IPI:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0006882; P:cellular zinc ion homeostasis; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IGI:MGI.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IDA:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; ISS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd10362; SH2_Src_Lck; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR035850; Lck_SH2.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Kinase;
Lipoprotein; Membrane; Myristate; Nucleotide-binding; Palmitate;
Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 509 Proto-oncogene tyrosine-protein kinase
LCK.
/FTId=PRO_0000088125.
DOMAIN 61 121 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 127 224 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 245 498 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 251 259 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 72 Interactions with CD4 and CD8.
REGION 154 242 Interaction with PTPRH. {ECO:0000250}.
ACT_SITE 364 364 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 273 273 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 192 192 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 394 394 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8371758}.
MOD_RES 505 505 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P06239}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000305|PubMed:7980442}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
LIPID 5 5 S-palmitoyl cysteine.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
MUTAGEN 2 2 G->A: Abolishes myristoylation and
palmitoylation.
{ECO:0000269|PubMed:7980442}.
MUTAGEN 3 5 CVC->SVK: Complete loss of interaction
with CD4 or CD8.
{ECO:0000269|PubMed:2107025}.
MUTAGEN 3 3 C->S: Abolishes plasma membrane
association; when associated with S-41.
Reduced palmitoylation level.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
MUTAGEN 5 5 C->K: Reduced palmitoylation level.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
MUTAGEN 5 5 C->S: Abolishes plasma membrane
association; when associated with S-21.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
MUTAGEN 20 20 C->S: Complete loss of interaction with
CD4 or CD8. {ECO:0000269|PubMed:2107025}.
MUTAGEN 23 23 C->S: Complete loss of interaction with
CD4 or CD8. {ECO:0000269|PubMed:2107025}.
MUTAGEN 269 269 K->N: Reduced activity.
MUTAGEN 270 270 V->L: Reduced activity.
MUTAGEN 271 271 A->S: Reduced activity.
MUTAGEN 272 272 V->A: Reduced activity.
MUTAGEN 273 273 K->R: Loss of activity.
{ECO:0000269|PubMed:1706070}.
MUTAGEN 274 274 S->N: Reduced activity.
MUTAGEN 275 275 L->M: Reduced activity.
MUTAGEN 276 276 K->V: Reduced activity.
MUTAGEN 505 505 Y->F: Causes thymic tumors.
{ECO:0000269|PubMed:1708890,
ECO:0000269|PubMed:3380790}.
SEQUENCE 509 AA; 57943 MW; 3513102F49A7FD0B CRC64;
MGCVCSSNPE DDWMENIDVC ENCHYPIVPL DSKISLPIRN GSEVRDPLVT YEGSLPPASP
LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN
SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH
YKIRNLDNGG FYISPRITFP GLHDLVRHYT NASDGLCTKL SRPCQTQKPQ KPWWEDEWEV
PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHPRL
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLNVNK LLDMAAQIAE GMAFIEEQNY
IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK
SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY HLMMLCWKER
PEDRPTFDYL RSVLDDFFTA TEGQYQPQP


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