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P06240

- LCK_MOUSE

UniProt

P06240 - LCK_MOUSE

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Protein
Proto-oncogene tyrosine-protein kinase LCK
Gene
Lck, Lsk-t
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei273 – 2731ATP By similarity
Active sitei364 – 3641Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi251 – 2599ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. B cell receptor signaling pathway Source: MGI
  2. T cell differentiation Source: UniProtKB
  3. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. cell surface receptor signaling pathway Source: MGI
  5. cellular zinc ion homeostasis Source: UniProtKB
  6. dephosphorylation Source: GOC
  7. peptidyl-tyrosine phosphorylation Source: MGI
  8. positive regulation of T cell activation Source: UniProtKB
  9. positive regulation of gamma-delta T cell differentiation Source: MGI
  10. positive regulation of gene expression Source: MGI
  11. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  12. positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
  13. protein autophosphorylation Source: MGI
  14. protein phosphorylation Source: MGI
  15. regulation of T cell receptor signaling pathway Source: MGI
  16. release of sequestered calcium ion into cytosol Source: UniProtKB
  17. response to drug Source: UniProtKB
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_188185. DAP12 signaling.
REACT_188578. Signaling by SCF-KIT.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_204081. CD28 co-stimulation.
REACT_215414. Translocation of ZAP-70 to Immunological synapse.
REACT_216080. Phosphorylation of CD3 and TCR zeta chains.
REACT_220092. GPVI-mediated activation cascade.
REACT_225145. Downstream TCR signaling.
REACT_225768. Generation of second messenger molecules.
REACT_226151. CD28 dependent PI3K/Akt signaling.
REACT_226341. PIP3 activates AKT signaling.
REACT_227425. Regulation of KIT signaling.

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:96756. Lck.

Subcellular locationi

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

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytosol Source: Reactome
  3. membrane raft Source: UniProtKB
  4. pericentriolar material Source: UniProtKB
  5. plasma membrane Source: UniProtKB-SubCell
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. 3 Publications
Mutagenesisi3 – 31C → S: Abolishes plasma membrane association; when associated with S-41. Reduced palmitoylation level. 2 Publications
Mutagenesisi5 – 51C → K: Reduced palmitoylation level. 2 Publications
Mutagenesisi5 – 51C → S: Abolishes plasma membrane association; when associated with S-21. 2 Publications
Mutagenesisi20 – 201C → S: Complete loss of interaction with CD4 or CD8. 1 Publication
Mutagenesisi23 – 231C → S: Complete loss of interaction with CD4 or CD8. 1 Publication
Mutagenesisi269 – 2691K → N: Reduced activity.
Mutagenesisi270 – 2701V → L: Reduced activity.
Mutagenesisi271 – 2711A → S: Reduced activity.
Mutagenesisi272 – 2721V → A: Reduced activity.
Mutagenesisi273 – 2731K → R: Loss of activity. 1 Publication
Mutagenesisi274 – 2741S → N: Reduced activity.
Mutagenesisi275 – 2751L → M: Reduced activity.
Mutagenesisi276 – 2761K → V: Reduced activity.
Mutagenesisi505 – 5051Y → F: Causes thymic tumors. 2 Publications

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Inferred
Chaini2 – 509508Proto-oncogene tyrosine-protein kinase LCK
PRO_0000088125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Inferred
Lipidationi3 – 31S-palmitoyl cysteine2 Publications
Lipidationi5 – 51S-palmitoyl cysteine2 Publications
Modified residuei102 – 1021Phosphoserine By similarity
Modified residuei159 – 1591Phosphothreonine By similarity
Modified residuei162 – 1621Phosphoserine By similarity
Modified residuei194 – 1941Phosphoserine By similarity
Modified residuei394 – 3941Phosphotyrosine; by autocatalysis
Modified residuei505 – 5051Phosphotyrosine; by CSK By 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.2 Publications
Myristoylation is required prior to palmitoylation.2 Publications
Palmitoylation regulates subcellular location By similarity.2 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP06240.
PaxDbiP06240.
PRIDEiP06240.

PTM databases

PhosphoSiteiP06240.

Expressioni

Tissue specificityi

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

Developmental stagei

Levels remain relatively constant throughout T-cell ontogeny.

Gene expression databases

ArrayExpressiP06240.
BgeeiP06240.
CleanExiMM_LCK.
GenevestigatoriP06240.

Interactioni

Subunit structurei

Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through its SH2 domain. Interacts with SQSTM1. Interacts with phosphorylated LIME1. Interacts with CBLB and PTPRH. Interacts with RUNX3. Forms a signaling complex with EPHA1, PTK2B AND PI3-KINASE; upon activation by EFNA1 which may regulate T-lymphocytes migration. Associates with ZAP70 and RHOH; these interactions allow LCK-mediated RHOH and CD3 subunit phosphorylation in the presence of functional ZAP70 By similarity.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12161SH3
Add
BLAST
Domaini127 – 22498SH2
Add
BLAST
Domaini245 – 498254Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 7271Interactions with CD4 and CD8
Add
BLAST
Regioni154 – 24289Interaction with PTPRH By similarity
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00620000087866.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP06240.
KOiK05856.
OrthoDBiEOG7GTT2V.
PhylomeDBiP06240.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06240-1 [UniParc]FASTAAdd to Basket

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

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBi P06240.
ChEMBLi CHEMBL2480.

PTM databases

PhosphoSitei P06240.

Proteomic databases

MaxQBi P06240.
PaxDbi P06240.
PRIDEi P06240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 3932.
MGIi MGI:96756. Lck.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 290704.
PROi P06240.
SOURCEi Search...

Gene expression databases

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

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« 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(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion."
    Voronova A.F., Sefton B.M.
    Nature 319:682-685(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  5. "Structure of the murine lck gene and its rearrangement in a murine lymphoma cell line."
    Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.
    Mol. Cell. Biol. 8:3058-3064(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
  6. "Two lck transcripts containing different 5' untranslated regions are present in T cells."
    Voronova A.F., Adler H.T., Sefton B.M.
    Mol. Cell. Biol. 7:4407-4413(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  7. "Avian reovirus mRNAs are nonfunctional in infected mouse cells: translational basis for virus host-range restriction."
    Amrein K.E., Sefton B.M.
    Proc. Natl. Acad. Sci. U.S.A. 85:4257-4261(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-505.
  8. "Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs."
    Turner J.M., Brodsky M.H., Irving B.A., Levin S.D., Perlmutter R.M., Littman D.R.
    Cell 60:755-765(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD4 AND CD8, MUTAGENESIS OF 3-CYS--CYS-5; CYS-20 AND CYS-23.
  9. "Creation and characterization of temperature-sensitive mutants of the lck tyrosine protein kinase."
    Hurley T.R., Amrein K.E., Sefton B.M.
    J. Virol. 66:7406-7413(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  10. "Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck."
    Abraham N., Miceli M.C., Parnes J.C., Veillette A.
    Nature 350:62-66(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-273.
  11. Cited for: PHOSPHORYLATION AT TYR-505, MUTAGENESIS OF TYR-505.
  12. Cited for: DISRUPTION PHENOTYPE.
  13. "Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk."
    Chow L.M., Fournel M., Davidson D., Veillette A.
    Nature 365:156-160(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSK.
  14. "The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP."
    Carrera A.C., Alexandrov K., Roberts T.M.
    Proc. Natl. Acad. Sci. U.S.A. 90:442-446(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  15. "Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins."
    Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.
    Mol. Cell. Biol. 13:6385-6392(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-3 AND CYS-5, MUTAGENESIS OF CYS-3 AND CYS-5.
  16. "Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
    Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
    Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-3 AND CYS-5, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-5.
  17. Cited for: INTERACTION WITH CBLB.
  18. "Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
    Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
    J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLCK_MOUSE
AccessioniPrimary (citable) accession number: P06240
Secondary accession number(s): Q61794
, Q61795, Q62320, Q91X65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 171 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

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