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P06240 (LCK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cells differentiation 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 componentCell membrane
Cytoplasm
Membrane
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB 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

cell surface receptor signaling pathway

Inferred from direct assay PubMed 9177270. Source: MGI

cellular zinc ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7499277PubMed 8175795. Source: MGI

positive regulation of T cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

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 intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

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

protein phosphorylation

Inferred from direct assay PubMed 9169414. 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_componentcell-cell junction

Inferred from direct assay PubMed 23793062. Source: MGI

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_functionATP 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: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 10713104PubMed 16111633. Source: UniProtKB

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 509508Proto-oncogene tyrosine-protein kinase LCK
PRO_0000088125

Regions

Domain61 – 12161SH3
Domain127 – 22498SH2
Domain245 – 498254Protein kinase
Nucleotide binding251 – 2599ATP By similarity
Region2 – 7271Interactions with CD4 and CD8
Region154 – 24289Interaction with PTPRH By similarity

Sites

Active site3641Proton acceptor By similarity
Binding site2731ATP By similarity

Amino acid modifications

Modified residue1021Phosphoserine By similarity
Modified residue1591Phosphothreonine By similarity
Modified residue1621Phosphoserine By similarity
Modified residue1941Phosphoserine By similarity
Modified residue3941Phosphotyrosine; by autocatalysis
Modified residue5051Phosphotyrosine; by CSK By similarity
Lipidation21N-myristoyl glycine Probable
Lipidation31S-palmitoyl cysteine Ref.15 Ref.16
Lipidation51S-palmitoyl cysteine Ref.15 Ref.16

Experimental info

Mutagenesis21G → A: Abolishes myristoylation and palmitoylation. Ref.16
Mutagenesis3 – 53CVC → SVK: Complete loss of interaction with CD4 or CD8. Ref.8 Ref.15 Ref.16
Mutagenesis31C → S: Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level. Ref.15 Ref.16
Mutagenesis51C → K: Reduced palmitoylation level. Ref.15 Ref.16
Mutagenesis51C → S: Abolishes plasma membrane association; when associated with S-21. Ref.15 Ref.16
Mutagenesis201C → S: Complete loss of interaction with CD4 or CD8. Ref.8
Mutagenesis231C → S: Complete loss of interaction with CD4 or CD8. Ref.8
Mutagenesis2691K → N: Reduced activity.
Mutagenesis2701V → L: Reduced activity.
Mutagenesis2711A → S: Reduced activity.
Mutagenesis2721V → A: Reduced activity.
Mutagenesis2731K → R: Loss of activity. Ref.10
Mutagenesis2741S → N: Reduced activity.
Mutagenesis2751L → M: Reduced activity.
Mutagenesis2761K → V: Reduced activity.
Mutagenesis5051Y → F: Causes thymic tumors. Ref.7 Ref.11

Sequences

Sequence LengthMass (Da)Tools
P06240 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3513102F49A7FD0B

FASTA50957,943
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
+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.
CCDSCCDS18697.1.
PIRI48845.
RefSeqNP_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.
UniGeneMm.293753.

3D structure databases

ProteinModelPortalP06240.
SMRP06240. Positions 7-33, 64-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201120. 12 interactions.
IntActP06240. 18 interactions.
MINTMINT-85459.

Chemistry

BindingDBP06240.
ChEMBLCHEMBL2480.

PTM databases

PhosphoSiteP06240.

Proteomic databases

MaxQBP06240.
PaxDbP06240.
PRIDEP06240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067240; ENSMUSP00000066209; ENSMUSG00000000409.
ENSMUST00000102596; ENSMUSP00000099656; ENSMUSG00000000409.
GeneID16818.
KEGGmmu:16818.
UCSCuc008uxi.2. mouse.

Organism-specific databases

CTD3932.
MGIMGI:96756. Lck.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087866.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP06240.
KOK05856.
OrthoDBEOG7GTT2V.
PhylomeDBP06240.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_188257. Signal Transduction.

Gene expression databases

ArrayExpressP06240.
BgeeP06240.
CleanExMM_LCK.
GenevestigatorP06240.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

NextBio290704.
PROP06240.
SOURCESearch...

Entry information

Entry nameLCK_MOUSE
AccessionPrimary (citable) accession number: P06240
Secondary accession number(s): Q61794 expand/collapse secondary AC list , Q61795, Q62320, Q91X65
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 170 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot