P06240 (LCK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Lck
Synonyms:	Lsk-t

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 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.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
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.
Subunit structure	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. Ref.8 Ref.17
Subcellular location	Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Present in lipid rafts in an inactive form. Ref.18
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.
Post-translational modification	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 By similarity. Ref.11 Ref.13 Myristoylation is required prior to palmitoylation. Ref.15 Ref.16 Palmitoylation regulates subcellular location By similarity. Ref.15 Ref.16
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. Ref.12
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from direct assay PubMed 7499277. Source: MGI T cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB cellular zinc ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 7499277PubMed 8175795. Source: MGI positive regulation of gamma-delta T cell differentiation Inferred from mutant phenotype PubMed 7807014. Source: MGI positive regulation of gene expression Inferred from direct assay PubMed 21357543. Source: MGI positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from direct assay PubMed 11254359. Source: MGI protein autophosphorylation Inferred from direct assay PubMed 8175795. Source: MGI regulation of T cell receptor signaling pathway Inferred from direct assay PubMed 14752163. Source: MGI release of sequestered calcium ion into cytosol Inferred from direct assay PubMed 1505025. Source: UniProtKB response to drug Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane raft Inferred from sequence or structural similarity. Source: UniProtKB pericentriolar material Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SH2 domain binding Inferred from sequence or structural similarity. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB protein tyrosine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-1401,EBI-710506	From a different organism.
	P27958	3	EBI-1401,EBI-706378	From a different organism.
KHDRBS1	Q07666	2	EBI-1401,EBI-1364	From a different organism.
PTPRC	P08575	2	EBI-1401,EBI-1341	From a different organism.
Sh2d2a	Q9QXK9	3	EBI-1401,EBI-1644

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 509	509	Proto-oncogene tyrosine-protein kinase LCK		PRO_0000088125
Regions
	Domain	61 – 121	61	SH3
	Domain	127 – 224	98	SH2
	Domain	245 – 498	254	Protein kinase
	Nucleotide binding	251 – 259	9	ATP By similarity
	Region	1 – 72	72	Interactions with CD4 and CD8
	Region	154 – 242	89	Interaction with PTPRH By similarity
Sites
	Active site	364	1	Proton acceptor By similarity
	Binding site	273	1	ATP By similarity
Amino acid modifications
	Modified residue	102	1	Phosphoserine By similarity
	Modified residue	159	1	Phosphothreonine By similarity
	Modified residue	162	1	Phosphoserine By similarity
	Modified residue	194	1	Phosphoserine By similarity
	Modified residue	394	1	Phosphotyrosine; by autocatalysis Ref.19
	Modified residue	505	1	Phosphotyrosine; by CSK By similarity
	Lipidation	2	1	N-myristoyl glycine Probable
	Lipidation	3	1	S-palmitoyl cysteine Ref.15 Ref.16
	Lipidation	5	1	S-palmitoyl cysteine Ref.15 Ref.16
Experimental info
	Mutagenesis	2	1	G → A: Abolishes myristoylation and palmitoylation. Ref.16
	Mutagenesis	3 – 5	3	CVC → SVK: Complete loss of interaction with CD4 or CD8. Ref.8 Ref.15 Ref.16
	Mutagenesis	3	1	C → S: Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level. Ref.15 Ref.16
	Mutagenesis	5	1	C → K: Reduced palmitoylation level. Ref.15 Ref.16
	Mutagenesis	5	1	C → S: Abolishes plasma membrane association; when associated with S-21. Ref.15 Ref.16
	Mutagenesis	20	1	C → S: Complete loss of interaction with CD4 or CD8. Ref.8
	Mutagenesis	23	1	C → S: Complete loss of interaction with CD4 or CD8. Ref.8
	Mutagenesis	269	1	K → N: Reduced activity.
	Mutagenesis	270	1	V → L: Reduced activity.
	Mutagenesis	271	1	A → S: Reduced activity.
	Mutagenesis	272	1	V → A: Reduced activity.
	Mutagenesis	273	1	K → R: Loss of activity. Ref.10
	Mutagenesis	274	1	S → N: Reduced activity.
	Mutagenesis	275	1	L → M: Reduced activity.
	Mutagenesis	276	1	K → V: Reduced activity.
	Mutagenesis	505	1	Y → F: Causes thymic tumors. Ref.7 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P06240 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 3513102F49A7FD0B	FASTA	509	57,943
	10 20 30 40 50 60 MGCVCSSNPE DDWMENIDVC ENCHYPIVPL DSKISLPIRN GSEVRDPLVT YEGSLPPASP 70 80 90 100 110 120 LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN 130 140 150 160 170 180 SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH 190 200 210 220 230 240 YKIRNLDNGG FYISPRITFP GLHDLVRHYT NASDGLCTKL SRPCQTQKPQ KPWWEDEWEV 250 260 270 280 290 300 PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHPRL 310 320 330 340 350 360 VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLNVNK LLDMAAQIAE GMAFIEEQNY 370 380 390 400 410 420 IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK 430 440 450 460 470 480 SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY HLMMLCWKER 490 500 PEDRPTFDYL RSVLDDFFTA TEGQYQPQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Thymic tumorigenesis induced by overexpression of p56lck." Abraham K.M., Levin S.D., Marth J.D., Forbush K.A., Perlmutter R.M. Proc. Natl. Acad. Sci. U.S.A. 88:3977-3981(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-505, MUTAGENESIS OF TYR-505.
[12]	"Profound block in thymocyte development in mice lacking p56lck." 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. Nature 357:161-164(1992) [PubMed] [Europe PMC] [Abstract] 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]	"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b." 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. Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract] 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.
[19]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-394, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00555017.
PIR	I48845.
RefSeq	NP_001155905.1. NM_001162433.1. NP_034823.1. NM_010693.3.
UniGene	Mm.293753.
3D structure databases
ProteinModelPortal	P06240.
SMR	P06240. Positions 7-33, 64-509.
ModBase	Search...
Protein-protein interaction databases
IntAct	P06240. 14 interactions.
MINT	MINT-85459.
PTM databases
PhosphoSite	P06240.
Proteomic databases
PaxDb	P06240.
PRIDE	P06240.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000067240; ENSMUSP00000066209; ENSMUSG00000000409. ENSMUST00000102596; ENSMUSP00000099656; ENSMUSG00000000409.
GeneID	16818.
KEGG	mmu:16818.
Organism-specific databases
CTD	3932.
MGI	MGI:96756. Lck.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00620000087866.
HOGENOM	HOG000233858.
HOVERGEN	HBG008761.
InParanoid	P06240.
KO	K05856.
OrthoDB	EOG4640BM.
Enzyme and pathway databases
BRENDA	2.7.10.2. 3474.
Reactome	REACT_107772. Immune System. REACT_115202. Signal Transduction.
Gene expression databases
ArrayExpress	P06240.
Bgee	P06240.
CleanEx	MM_LCK.
Genevestigator	P06240.
GermOnline	ENSMUSG00000000409. Mus musculus.
Family and domain databases
Gene3D	3.30.505.10. 1 hit.
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
BindingDB	P06240.
ChEMBL	CHEMBL2480.
NextBio	290704.
SOURCE	Search...

Entry information

Entry name

LCK_MOUSE

Accession

Primary (citable) accession number: P06240
Secondary accession number(s): Q61794 , Q61795, Q62320, Q91X65

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 156 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program