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Protein

Proto-oncogene tyrosine-protein kinase LCK

Gene

Lck

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. ATPase binding Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. CD4 receptor binding Source: MGI
  4. CD8 receptor binding Source: MGI
  5. glycoprotein binding Source: MGI
  6. identical protein binding Source: MGI
  7. non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  8. phosphatidylinositol 3-kinase binding Source: MGI
  9. protein C-terminus binding Source: MGI
  10. protein kinase binding Source: MGI
  11. protein phosphatase binding Source: MGI
  12. protein serine/threonine phosphatase activity Source: UniProtKB
  13. protein tyrosine kinase activity Source: UniProtKB
  14. receptor binding Source: GO_Central
  15. 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 response to peptide hormone stimulus Source: GO_Central
  5. cellular zinc ion homeostasis Source: UniProtKB
  6. dephosphorylation Source: MGI
  7. innate immune response Source: GO_Central
  8. peptidyl-tyrosine autophosphorylation Source: GO_Central
  9. peptidyl-tyrosine phosphorylation Source: MGI
  10. positive regulation of gamma-delta T cell differentiation Source: MGI
  11. positive regulation of gene expression Source: MGI
  12. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  13. positive regulation of T cell activation Source: UniProtKB
  14. positive regulation of T cell receptor signaling pathway Source: GO_Central
  15. positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
  16. protein autophosphorylation Source: MGI
  17. protein phosphorylation Source: MGI
  18. regulation of apoptotic process Source: GO_Central
  19. regulation of cell proliferation Source: GO_Central
  20. regulation of T cell receptor signaling pathway Source: MGI
  21. release of sequestered calcium ion into cytosol Source: UniProtKB
  22. response to drug Source: UniProtKB
  23. T cell differentiation Source: UniProtKB
  24. transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_273845. Interleukin-2 signaling.
REACT_280649. Downstream TCR signaling.
REACT_301936. DAP12 signaling.
REACT_309115. PD-1 signaling.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_327235. CD28 dependent PI3K/Akt signaling.
REACT_327841. Signaling by SCF-KIT.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_333474. PIP3 activates AKT signaling.
REACT_334692. Generation of second messenger molecules.
REACT_334921. CD28 co-stimulation.
REACT_337915. GPVI-mediated activation cascade.
REACT_345130. Translocation of ZAP-70 to Immunological synapse.
REACT_345471. Phosphorylation of CD3 and TCR zeta chains.
REACT_354765. 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 Componenti: 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. extracellular vesicular exosome Source: MGI
  4. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  5. immunological synapse Source: MGI
  6. membrane raft Source: UniProtKB
  7. pericentriolar material Source: UniProtKB
  8. plasma membrane Source: MGI
Complete GO annotation...

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. 1 Publication
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 residuei6 – 61PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineBy similarity
Modified residuei159 – 1591PhosphothreonineBy similarity
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei192 – 1921PhosphotyrosineBy similarity
Modified residuei194 – 1941PhosphoserineBy similarity
Modified residuei263 – 2631PhosphotyrosineBy similarity
Modified residuei304 – 3041PhosphotyrosineBy similarity
Modified residuei313 – 3131PhosphotyrosineBy similarity
Modified residuei394 – 3941Phosphotyrosine; by autocatalysis1 Publication
Modified residuei457 – 4571PhosphotyrosineBy similarity
Modified residuei470 – 4701PhosphotyrosineBy similarity
Modified residuei486 – 4861PhosphothreonineBy similarity
Modified residuei499 – 4991PhosphothreonineBy similarity
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

BgeeiP06240.
CleanExiMM_LCK.
ExpressionAtlasiP06240. baseline and differential.
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, 63-509.
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.
GeneTreeiENSGT00760000118938.
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

        10         20         30         40         50
MGCVCSSNPE DDWMENIDVC ENCHYPIVPL DSKISLPIRN GSEVRDPLVT
60 70 80 90 100
YEGSLPPASP LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA
110 120 130 140 150
QSLTTGQEGF IPFNFVAKAN SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS
160 170 180 190 200
FLIRESESTA GSFSLSVRDF DQNQGEVVKH YKIRNLDNGG FYISPRITFP
210 220 230 240 250
GLHDLVRHYT NASDGLCTKL SRPCQTQKPQ KPWWEDEWEV PRETLKLVER
260 270 280 290 300
LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHPRL
310 320 330 340 350
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLNVNK LLDMAAQIAE
360 370 380 390 400
GMAFIEEQNY IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA
410 420 430 440 450
KFPIKWTAPE AINYGTFTIK SDVWSFGILL TEIVTHGRIP YPGMTNPEVI
460 470 480 490 500
QNLERGYRMV RPDNCPEELY HLMMLCWKER PEDRPTFDYL RSVLDDFFTA

TEGQYQPQP
Length:509
Mass (Da):57,943
Last modified:January 22, 2007 - v4
Checksum:i3513102F49A7FD0B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006502818.2.
XP_006537018.1. XM_006536955.2.
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:
EMBLi
GenBanki
DDBJi
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_006502818.2.
XP_006537018.1. XM_006536955.2.
UniGeneiMm.293753.

3D structure databases

ProteinModelPortaliP06240.
SMRiP06240. Positions 7-33, 63-509.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP06240.
ChEMBLiCHEMBL2480.

PTM databases

PhosphoSiteiP06240.

Proteomic databases

MaxQBiP06240.
PaxDbiP06240.
PRIDEiP06240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3932.
MGIiMGI:96756. Lck.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP06240.
KOiK05856.
OrthoDBiEOG7GTT2V.
PhylomeDBiP06240.
TreeFamiTF351634.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.
ReactomeiREACT_273845. Interleukin-2 signaling.
REACT_280649. Downstream TCR signaling.
REACT_301936. DAP12 signaling.
REACT_309115. PD-1 signaling.
REACT_311393. CTLA4 inhibitory signaling.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_327235. CD28 dependent PI3K/Akt signaling.
REACT_327841. Signaling by SCF-KIT.
REACT_328674. Constitutive PI3K/AKT Signaling in Cancer.
REACT_333474. PIP3 activates AKT signaling.
REACT_334692. Generation of second messenger molecules.
REACT_334921. CD28 co-stimulation.
REACT_337915. GPVI-mediated activation cascade.
REACT_345130. Translocation of ZAP-70 to Immunological synapse.
REACT_345471. Phosphorylation of CD3 and TCR zeta chains.
REACT_354765. Regulation of KIT signaling.

Miscellaneous databases

NextBioi290704.
PROiP06240.
SOURCEiSearch...

Gene expression databases

BgeeiP06240.
CleanExiMM_LCK.
ExpressionAtlasiP06240. baseline and differential.
GenevestigatoriP06240.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1984) [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(1985) [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(2004) [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(2003) [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(1987) [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(1986) [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(1987) [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(1989) [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(1991) [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(1990) [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(1992) [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(1992) [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(1992) [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(1993) [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(2001) [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: December 31, 1987
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 178 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.