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P06239

- LCK_HUMAN

UniProt

P06239 - LCK_HUMAN

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Protein

Tyrosine-protein kinase Lck

Gene
LCK
Organism
Homo sapiens (Human)
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.7 Publications

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.1 Publication

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. antigen binding Source: Ensembl
  2. ATPase binding Source: UniProtKB
  3. ATP binding Source: UniProtKB-KW
  4. CD4 receptor binding Source: UniProtKB
  5. CD8 receptor binding Source: UniProtKB
  6. glycoprotein binding Source: UniProtKB
  7. identical protein binding Source: IntAct
  8. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  9. phosphatidylinositol 3-kinase binding Source: UniProtKB
  10. protein binding Source: UniProtKB
  11. protein C-terminus binding Source: UniProtKB
  12. protein kinase binding Source: UniProtKB
  13. protein phosphatase binding Source: UniProtKB
  14. protein serine/threonine phosphatase activity Source: UniProtKB
  15. protein tyrosine kinase activity Source: UniProtKB
  16. SH2 domain binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. aging Source: Ensembl
  3. B cell receptor signaling pathway Source: Ensembl
  4. blood coagulation Source: Reactome
  5. cellular zinc ion homeostasis Source: UniProtKB
  6. dephosphorylation Source: GOC
  7. epidermal growth factor receptor signaling pathway Source: Reactome
  8. Fc-epsilon receptor signaling pathway Source: Reactome
  9. fibroblast growth factor receptor signaling pathway Source: Reactome
  10. hemopoiesis Source: UniProtKB
  11. innate immune response Source: Reactome
  12. leukocyte migration Source: Reactome
  13. neurotrophin TRK receptor signaling pathway Source: Reactome
  14. phosphatidylinositol-mediated signaling Source: Reactome
  15. platelet activation Source: Reactome
  16. positive regulation of gamma-delta T cell differentiation Source: Ensembl
  17. positive regulation of gene expression Source: Ensembl
  18. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  19. positive regulation of T cell activation Source: UniProtKB
  20. positive regulation of T cell receptor signaling pathway Source: UniProtKB
  21. positive regulation of tyrosine phosphorylation of Stat5 protein Source: Ensembl
  22. positive regulation of uterine smooth muscle contraction Source: Ensembl
  23. protein autophosphorylation Source: Ensembl
  24. protein phosphorylation Source: UniProtKB
  25. regulation of defense response to virus by virus Source: Reactome
  26. regulation of lymphocyte activation Source: UniProtKB
  27. release of sequestered calcium ion into cytosol Source: UniProtKB
  28. response to drug Source: UniProtKB
  29. response to hydrogen peroxide Source: Ensembl
  30. response to mechanical stimulus Source: Ensembl
  31. response to zinc ion Source: Ensembl
  32. T cell costimulation Source: Reactome
  33. T cell differentiation Source: UniProtKB
  34. T cell receptor signaling pathway Source: Reactome
  35. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_11068. Nef and signal transduction.
REACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_12519. PECAM1 interactions.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_1695. GPVI-mediated activation cascade.
REACT_19183. CD28 co-stimulation.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19324. PD-1 signaling.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_19405. CTLA4 inhibitory signaling.
REACT_27283. Interleukin-2 signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP06239.

Names & Taxonomyi

Protein namesi
Recommended name:
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
Protein YT16
Proto-oncogene Lck
T cell-specific protein-tyrosine kinase
p56-LCK
Gene namesi
Name:LCK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6524. 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. cytosol Source: Reactome
  2. endocytic vesicle Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. immunological synapse Source: MGI
  5. membrane raft Source: UniProtKB
  6. pericentriolar material Source: UniProtKB
  7. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving LCK is found in leukemias. Translocation t(1;7)(p34;q34) with TCRB.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi59 – 591S → E: Allows interaction with SQSTM1. 1 Publication
Mutagenesisi154 – 1541R → K: No effect on interaction with SQSTM1. 1 Publication

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

Orphaneti280142. Severe combined immunodeficiency due to LCK deficiency.
PharmGKBiPA30307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 509508Tyrosine-protein kinase LckPRO_0000088124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine By similarity
Lipidationi3 – 31S-palmitoyl cysteine By similarity
Lipidationi5 – 51S-palmitoyl cysteine By similarity
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei159 – 1591Phosphothreonine1 Publication
Modified residuei162 – 1621Phosphoserine1 Publication
Modified residuei194 – 1941Phosphoserine1 Publication
Modified residuei394 – 3941Phosphotyrosine; by autocatalysis2 Publications
Modified residuei505 – 5051Phosphotyrosine; by CSK8 Publications

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-cell receptor signaling.5 Publications
Myristoylation is required prior to palmitoylation By similarity.
Palmitoylation regulates subcellular location By similarity.

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP06239.
PaxDbiP06239.
PRIDEiP06239.

PTM databases

PhosphoSiteiP06239.

Expressioni

Tissue specificityi

Expressed specifically in lymphoid cells.

Gene expression databases

ArrayExpressiP06239.
BgeeiP06239.
CleanExiHS_LCK.
GenevestigatoriP06239.

Organism-specific databases

HPAiCAB003816.
HPA003494.

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. Binds to HIV-1 Nef through its SH3 domain. This interaction inhibits its tyrosine-kinase activity. 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-lymphocyte migration. Associates with ZAP70 and RHOH; these interactions allow LCK-mediated RHOH and CD3 subunit phosphorylation in the presence of functional ZAP70.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1348,EBI-1348
P225757EBI-1348,EBI-866709From a different organism.
Q9YJQ82EBI-1348,EBI-7709835From a different organism.
ADAM15Q134443EBI-1348,EBI-77818
ARP102757EBI-1348,EBI-608057
BCL3P207493EBI-1348,EBI-958997
CD4P017302EBI-1348,EBI-353826
GAB1Q1348010EBI-1348,EBI-517684
HSP90AB1P082382EBI-1348,EBI-352572
KHDRBS1Q076665EBI-1348,EBI-1364
KITP107218EBI-1348,EBI-1379503
LATO435612EBI-1348,EBI-1222766
MED28Q9H2044EBI-1348,EBI-514199
METP085813EBI-1348,EBI-1039152
NR3C1P041503EBI-1348,EBI-493507
PRKCQQ047592EBI-1348,EBI-374762
PTPN22Q9Y2R25EBI-1348,EBI-1211241
PTPN6P293505EBI-1348,EBI-78260
PTPRCP085757EBI-1348,EBI-1341
SH2D2AQ9NP3112EBI-1348,EBI-490630
SYKP434057EBI-1348,EBI-78302
UBCP0CG482EBI-1348,EBI-3390054
ZAP70P434032EBI-1348,EBI-1211276

Protein-protein interaction databases

BioGridi110124. 81 interactions.
DIPiDIP-553N.
IntActiP06239. 62 interactions.
MINTiMINT-110378.

Structurei

Secondary structure

1
509
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 154
Beta strandi21 – 233
Beta strandi24 – 274
Turni60 – 634
Beta strandi65 – 706
Beta strandi76 – 794
Beta strandi87 – 926
Beta strandi95 – 1028
Turni103 – 1053
Beta strandi108 – 1125
Helixi113 – 1153
Beta strandi116 – 1183
Beta strandi128 – 1314
Helixi134 – 1418
Beta strandi151 – 1555
Beta strandi157 – 1593
Beta strandi163 – 1719
Turni172 – 1743
Beta strandi175 – 18511
Turni187 – 1893
Beta strandi191 – 1944
Beta strandi199 – 2013
Helixi202 – 21110
Beta strandi216 – 2183
Turni233 – 2353
Beta strandi237 – 2393
Helixi242 – 2443
Beta strandi245 – 25410
Beta strandi257 – 2648
Turni265 – 2673
Beta strandi268 – 2758
Turni277 – 2793
Helixi282 – 29413
Beta strandi303 – 3075
Beta strandi309 – 3113
Beta strandi313 – 3175
Helixi324 – 3274
Helixi331 – 3344
Helixi338 – 35720
Helixi367 – 3693
Beta strandi370 – 3723
Beta strandi378 – 3803
Helixi383 – 3853
Helixi386 – 3894
Beta strandi390 – 3923
Beta strandi393 – 3953
Turni404 – 4063
Helixi409 – 4146
Helixi419 – 43416
Turni435 – 4373
Helixi446 – 4549
Helixi467 – 47610
Helixi481 – 4833
Helixi487 – 50014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHFX-ray1.80A119-226[»]
1BHHX-ray1.90A119-226[»]
B124-226[»]
1CWDX-ray2.25L127-222[»]
1CWEX-ray2.30A/C127-222[»]
1FBZX-ray2.40A/B123-226[»]
1H92NMR-A59-120[»]
1IJRX-ray2.20A124-226[»]
1KIKNMR-A64-120[»]
1LCJX-ray1.80A119-226[»]
1LCKX-ray2.50A53-226[»]
B502-509[»]
1LKKX-ray1.00A122-226[»]
1LKLX-ray1.80A123-226[»]
1Q68NMR-B7-35[»]
1Q69NMR-B7-35[»]
1QPCX-ray1.60A231-509[»]
1QPDX-ray2.00A231-509[»]
1QPEX-ray2.00A231-509[»]
1QPJX-ray2.20A231-509[»]
1X27X-ray2.70A/B/C/D/E/F64-226[»]
2IIMX-ray1.00A59-119[»]
2OF2X-ray2.00A231-501[»]
2OF4X-ray2.70A231-501[»]
2OFUX-ray2.00A229-501[»]
2OFVX-ray2.00A/B232-498[»]
2OG8X-ray2.30A/B237-499[»]
2PL0X-ray2.80A225-509[»]
2ZM1X-ray2.10A225-509[»]
2ZM4X-ray2.70A225-509[»]
2ZYBX-ray2.55A225-509[»]
3AC1X-ray1.99A225-509[»]
3AC2X-ray2.10A225-509[»]
3AC3X-ray2.55A225-509[»]
3AC4X-ray2.70A225-509[»]
3AC5X-ray2.50A225-509[»]
3AC8X-ray2.30A225-509[»]
3ACJX-ray2.20A225-509[»]
3ACKX-ray2.60A225-509[»]
3AD4X-ray2.20A225-509[»]
3AD5X-ray2.00A225-509[»]
3AD6X-ray2.15A225-509[»]
3B2WX-ray2.30A226-502[»]
3BRHX-ray2.20C/D391-397[»]
3BYMX-ray2.00A230-501[»]
3BYOX-ray2.00A231-501[»]
3BYSX-ray2.20A225-501[»]
3BYUX-ray2.30A225-501[»]
3KMMX-ray2.80A229-509[»]
3KXZX-ray2.37A225-509[»]
3LCKX-ray1.70A231-501[»]
3MPMX-ray1.95A237-501[»]
4C3FX-ray1.72A237-501[»]
4D8KX-ray2.36A53-226[»]
ProteinModelPortaliP06239.
SMRiP06239. Positions 7-35, 64-509.

Miscellaneous databases

EvolutionaryTraceiP06239.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12161SH3Add
BLAST
Domaini127 – 22498SH2Add
BLAST
Domaini245 – 498254Protein kinaseAdd
BLAST

Region

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

Domaini

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

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG008761.
KOiK05856.
OMAiEYMENDT.
OrthoDBiEOG7GTT2V.
PhylomeDBiP06239.
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]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P06239-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT    50
YEGSNPPASP LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA 100
QSLTTGQEGF IPFNFVAKAN SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS 150
FLIRESESTA GSFSLSVRDF DQNQGEVVKH YKIRNLDNGG FYISPRITFP 200
GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV PRETLKLVER 250
LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 300
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQIAE 350
GMAFIEERNY IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA 400
KFPIKWTAPE AINYGTFTIK SDVWSFGILL TEIVTHGRIP YPGMTNPEVI 450
QNLERGYRMV RPDNCPEELY QLMRLCWKER PEDRPTFDYL RSVLEDFFTA 500
TEGQYQPQP 509
Length:509
Mass (Da):58,001
Last modified:January 23, 2007 - v6
Checksum:i44BFF0D43FFB420D
GO
Isoform Short (identifier: P06239-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     348-363: IAEGMAFIEERNYIHR → VRRLGRGAGQGNRPVT
     364-509: Missing.

Note: No experimental confirmation available.

Show »
Length:363
Mass (Da):40,866
Checksum:iAC4AF1AB58D32577
GO
Isoform 3 (identifier: P06239-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: N → NDTLLDSQLEEKGLGASPWGNLGQQLLLLPT

Note: No experimental confirmation available.

Show »
Length:539
Mass (Da):61,190
Checksum:iD1024F47D18B289C
GO

Sequence cautioni

The sequence CAI22320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAI22321.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Mass spectrometryi

Molecular mass is 57869.42 Da from positions 2 - 509. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281V → L in leukemia. 1 Publication
VAR_013463
Natural varianti201 – 2011G → S.
Corresponds to variant rs11567841 [ dbSNP | Ensembl ].
VAR_051697
Natural varianti232 – 2321P → PQKP in leukemia.
VAR_013464
Natural varianti353 – 3531A → V in leukemia. 1 Publication
VAR_013465
Natural varianti447 – 4471P → L in leukemia. 1 Publication
VAR_013466

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei321 – 3211N → NDTLLDSQLEEKGLGASPWG NLGQQLLLLPT in isoform 3. VSP_016049
Alternative sequencei348 – 36316IAEGM…NYIHR → VRRLGRGAGQGNRPVT in isoform Short. VSP_005000Add
BLAST
Alternative sequencei364 – 509146Missing in isoform Short. VSP_005001Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291P → R in AAA59502. 1 Publication
Sequence conflicti35 – 351T → R in AAA59502. 1 Publication
Sequence conflicti87 – 871Q → P in CAA31884. 1 Publication
Sequence conflicti87 – 871Q → P in AAA59502. 1 Publication
Sequence conflicti206 – 2116VRHYTN → ASAITPI in CAA28691. 1 Publication
Sequence conflicti254 – 2541G → A in AAA59502. 1 Publication
Sequence conflicti258 – 26710EVWMGYYNGH → RCGWGTTTGT in CAA28691. 1 Publication
Sequence conflicti282 – 2865PDAFL → AGRLP in CAA28691. 1 Publication
Sequence conflicti375 – 3751T → A in CAA28165. 1 Publication
Sequence conflicti472 – 4721L → H in CAA29667. 1 Publication
Sequence conflicti504 – 5096QYQPQP → STA in CAA28691. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05027 mRNA. Translation: CAA28691.1.
X13529 mRNA. Translation: CAA31884.1.
M36881 mRNA. Translation: AAA59502.1.
X14055, X14053, X14054 Genomic DNA. Translation: CAA32211.1.
U07236 mRNA. Translation: AAA18225.1.
U23852 mRNA. Translation: AAC50287.1.
BN000073 Genomic DNA. Translation: CAD55807.1.
AL121991 Genomic DNA. Translation: CAI22320.1. Different initiation.
AL121991 Genomic DNA. Translation: CAI22321.1. Different initiation.
CH471059 Genomic DNA. Translation: EAX07543.1.
CH471059 Genomic DNA. Translation: EAX07546.1.
BC013200 mRNA. Translation: AAH13200.1.
M21510 Genomic DNA. Translation: AAA59501.1. Different termination.
M26692 Genomic DNA. Translation: AAA59503.1.
AF228313 mRNA. Translation: AAF34794.1.
X06369 mRNA. Translation: CAA29667.1.
X04476 mRNA. Translation: CAA28165.1.
CCDSiCCDS359.1. [P06239-1]
PIRiJQ0152. OKHULK.
RefSeqiNP_001036236.1. NM_001042771.2. [P06239-1]
NP_005347.3. NM_005356.4. [P06239-1]
UniGeneiHs.470627.

Genome annotation databases

EnsembliENST00000333070; ENSP00000328213; ENSG00000182866. [P06239-3]
ENST00000336890; ENSP00000337825; ENSG00000182866. [P06239-1]
GeneIDi3932.
KEGGihsa:3932.
UCSCiuc001bux.3. human. [P06239-1]
uc001buz.3. human. [P06239-3]

Polymorphism databases

DMDMi125474.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Lck entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X05027 mRNA. Translation: CAA28691.1 .
X13529 mRNA. Translation: CAA31884.1 .
M36881 mRNA. Translation: AAA59502.1 .
X14055 , X14053 , X14054 Genomic DNA. Translation: CAA32211.1 .
U07236 mRNA. Translation: AAA18225.1 .
U23852 mRNA. Translation: AAC50287.1 .
BN000073 Genomic DNA. Translation: CAD55807.1 .
AL121991 Genomic DNA. Translation: CAI22320.1 . Different initiation.
AL121991 Genomic DNA. Translation: CAI22321.1 . Different initiation.
CH471059 Genomic DNA. Translation: EAX07543.1 .
CH471059 Genomic DNA. Translation: EAX07546.1 .
BC013200 mRNA. Translation: AAH13200.1 .
M21510 Genomic DNA. Translation: AAA59501.1 . Different termination.
M26692 Genomic DNA. Translation: AAA59503.1 .
AF228313 mRNA. Translation: AAF34794.1 .
X06369 mRNA. Translation: CAA29667.1 .
X04476 mRNA. Translation: CAA28165.1 .
CCDSi CCDS359.1. [P06239-1 ]
PIRi JQ0152. OKHULK.
RefSeqi NP_001036236.1. NM_001042771.2. [P06239-1 ]
NP_005347.3. NM_005356.4. [P06239-1 ]
UniGenei Hs.470627.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BHF X-ray 1.80 A 119-226 [» ]
1BHH X-ray 1.90 A 119-226 [» ]
B 124-226 [» ]
1CWD X-ray 2.25 L 127-222 [» ]
1CWE X-ray 2.30 A/C 127-222 [» ]
1FBZ X-ray 2.40 A/B 123-226 [» ]
1H92 NMR - A 59-120 [» ]
1IJR X-ray 2.20 A 124-226 [» ]
1KIK NMR - A 64-120 [» ]
1LCJ X-ray 1.80 A 119-226 [» ]
1LCK X-ray 2.50 A 53-226 [» ]
B 502-509 [» ]
1LKK X-ray 1.00 A 122-226 [» ]
1LKL X-ray 1.80 A 123-226 [» ]
1Q68 NMR - B 7-35 [» ]
1Q69 NMR - B 7-35 [» ]
1QPC X-ray 1.60 A 231-509 [» ]
1QPD X-ray 2.00 A 231-509 [» ]
1QPE X-ray 2.00 A 231-509 [» ]
1QPJ X-ray 2.20 A 231-509 [» ]
1X27 X-ray 2.70 A/B/C/D/E/F 64-226 [» ]
2IIM X-ray 1.00 A 59-119 [» ]
2OF2 X-ray 2.00 A 231-501 [» ]
2OF4 X-ray 2.70 A 231-501 [» ]
2OFU X-ray 2.00 A 229-501 [» ]
2OFV X-ray 2.00 A/B 232-498 [» ]
2OG8 X-ray 2.30 A/B 237-499 [» ]
2PL0 X-ray 2.80 A 225-509 [» ]
2ZM1 X-ray 2.10 A 225-509 [» ]
2ZM4 X-ray 2.70 A 225-509 [» ]
2ZYB X-ray 2.55 A 225-509 [» ]
3AC1 X-ray 1.99 A 225-509 [» ]
3AC2 X-ray 2.10 A 225-509 [» ]
3AC3 X-ray 2.55 A 225-509 [» ]
3AC4 X-ray 2.70 A 225-509 [» ]
3AC5 X-ray 2.50 A 225-509 [» ]
3AC8 X-ray 2.30 A 225-509 [» ]
3ACJ X-ray 2.20 A 225-509 [» ]
3ACK X-ray 2.60 A 225-509 [» ]
3AD4 X-ray 2.20 A 225-509 [» ]
3AD5 X-ray 2.00 A 225-509 [» ]
3AD6 X-ray 2.15 A 225-509 [» ]
3B2W X-ray 2.30 A 226-502 [» ]
3BRH X-ray 2.20 C/D 391-397 [» ]
3BYM X-ray 2.00 A 230-501 [» ]
3BYO X-ray 2.00 A 231-501 [» ]
3BYS X-ray 2.20 A 225-501 [» ]
3BYU X-ray 2.30 A 225-501 [» ]
3KMM X-ray 2.80 A 229-509 [» ]
3KXZ X-ray 2.37 A 225-509 [» ]
3LCK X-ray 1.70 A 231-501 [» ]
3MPM X-ray 1.95 A 237-501 [» ]
4C3F X-ray 1.72 A 237-501 [» ]
4D8K X-ray 2.36 A 53-226 [» ]
ProteinModelPortali P06239.
SMRi P06239. Positions 7-35, 64-509.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110124. 81 interactions.
DIPi DIP-553N.
IntActi P06239. 62 interactions.
MINTi MINT-110378.

Chemistry

BindingDBi P06239.
ChEMBLi CHEMBL2363074.
DrugBanki DB01254. Dasatinib.
GuidetoPHARMACOLOGYi 2053.

PTM databases

PhosphoSitei P06239.

Polymorphism databases

DMDMi 125474.

Proteomic databases

MaxQBi P06239.
PaxDbi P06239.
PRIDEi P06239.

Protocols and materials databases

DNASUi 3932.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000333070 ; ENSP00000328213 ; ENSG00000182866 . [P06239-3 ]
ENST00000336890 ; ENSP00000337825 ; ENSG00000182866 . [P06239-1 ]
GeneIDi 3932.
KEGGi hsa:3932.
UCSCi uc001bux.3. human. [P06239-1 ]
uc001buz.3. human. [P06239-3 ]

Organism-specific databases

CTDi 3932.
GeneCardsi GC01P032716.
H-InvDB HIX0019954.
HGNCi HGNC:6524. LCK.
HPAi CAB003816.
HPA003494.
MIMi 153390. gene.
neXtProti NX_P06239.
Orphaneti 280142. Severe combined immunodeficiency due to LCK deficiency.
PharmGKBi PA30307.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG008761.
KOi K05856.
OMAi EYMENDT.
OrthoDBi EOG7GTT2V.
PhylomeDBi P06239.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_11068. Nef and signal transduction.
REACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_12519. PECAM1 interactions.
REACT_12555. Downstream TCR signaling.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_12596. Translocation of ZAP-70 to Immunological synapse.
REACT_12623. Generation of second messenger molecules.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
REACT_147814. DAP12 signaling.
REACT_1695. GPVI-mediated activation cascade.
REACT_19183. CD28 co-stimulation.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19324. PD-1 signaling.
REACT_19358. CD28 dependent PI3K/Akt signaling.
REACT_19405. CTLA4 inhibitory signaling.
REACT_27283. Interleukin-2 signaling.
REACT_75829. PIP3 activates AKT signaling.
SignaLinki P06239.

Miscellaneous databases

ChiTaRSi LCK. human.
EvolutionaryTracei P06239.
GeneWikii Lck.
GenomeRNAii 3932.
NextBioi 15441.
PROi P06239.
SOURCEi Search...

Gene expression databases

ArrayExpressi P06239.
Bgeei P06239.
CleanExi HS_LCK.
Genevestigatori P06239.

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 human T cell-specific cDNA clone (YT16) encodes a protein with extensive homology to a family of protein-tyrosine kinases."
    Koga Y., Caccia N., Toyonaga B., Spolski R., Yanagi Y., Yoshikai Y., Mak T.W.
    Eur. J. Immunol. 16:1643-1646(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure and expression of lck transcripts in human lymphoid cells."
    Perlmutter R.M., Marth J.D., Lewis D.B., Peet R., Ziegler S.F., Wilson C.B.
    J. Cell. Biochem. 38:117-126(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Structure of the human lck gene: differences in genomic organisation within src-related genes affect only N-terminal exons."
    Rouer E., van Huynh T., de Souza S.L., Lang M.C., Fischer S., Benarous R.
    Gene 84:105-113(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Oncogenic activation of the Lck protein accompanies translocation of the LCK gene in the human HSB2 T-cell leukemia."
    Wright D.D., Sefton B.M., Kamps M.P.
    Mol. Cell. Biol. 14:2429-2437(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-28; GLN-LYS-PRO-232 INS; VAL-353 AND LEU-447, PHOSPHORYLATION AT TYR-394 AND TYR-505.
    Tissue: Leukemia.
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), ALTERNATIVE SPLICING.
    Tissue: Leukemic T-cell.
  6. "No association between lck gene polymorphisms and protein level in type 1 diabetes."
    Nervi S., Nicodeme S., Gartioux C., Atlan C., Lathrop M., Reviron D., Naquet P., Matsuda F., Imbert J., Vialettes B.
    Diabetes 51:3326-3330(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 3).
    Tissue: Lymph.
  10. "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.
  11. "Structure of the two promoters of the human lck gene: differential accumulation of two classes of lck transcripts in T cells."
    Takadera T., Leung S., Gernone A., Koga Y., Takihara Y., Miyamoto N.G., Mak T.W.
    Mol. Cell. Biol. 9:2173-2180(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
  12. "Defective recruitment and activation of ZAP-70 in common variable immunodeficiency patients with T cell defects."
    Boncristiano M., Majolini M.B., D'Elios M.M., Pacini S., Valensin S., Ulivieri C., Amedei A., Falini B., Del Prete G., Telford J.L., Baldari C.T.
    Eur. J. Immunol. 30:2632-2638(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-509.
    Tissue: Peripheral blood lymphocyte.
  13. "Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines."
    Veillette A., Foss F.M., Sausville E.A., Bolen J.B., Rosen N.
    Oncogene Res. 1:357-374(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 368-509.
  14. "Human T lymphocytes express a protein-tyrosine kinase homologous to p56LSTRA."
    Trevillyan J.M., Lin Y., Chen S.J., Phillips C.A., Canna C., Linna T.J.
    Biochim. Biophys. Acta 888:286-295(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-509.
  15. "The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity."
    Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A., Amrein K.E., Autero M., Burn P., Alitalo K.
    EMBO J. 11:2919-2924(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-505.
  16. "The SH3 domain of p56lck is involved in binding to phosphatidylinositol 3'-kinase from T lymphocytes."
    Vogel L.B., Fujita D.J.
    Mol. Cell. Biol. 13:7408-7417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PI3K.
  17. "p70 phosphorylation and binding to p56lck is an early event in interleukin-2-induced onset of cell cycle progression in T-lymphocytes."
    Vogel L.B., Fujita D.J.
    J. Biol. Chem. 270:2506-2511(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KHDRBS1.
  18. "Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region."
    Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.
    Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1, MUTAGENESIS OF SER-59 AND ARG-154.
  19. "Detection of a physical and functional interaction between Csk and Lck which involves the SH2 domain of Csk and is mediated by autophosphorylation of Lck on tyrosine 394."
    Bougeret C., Delaunay T., Romero F., Jullien P., Sabe H., Hanafusa H., Benarous R., Fischer S.
    J. Biol. Chem. 271:7465-7472(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-505 BY CSK, AUTOPHOSPHORYLATION.
  20. "Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity."
    Greenway A.L., Azad A., Mills J., McPhee D.A.
    J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 NEF.
  21. "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
    Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
    Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXL.
  22. "Lck protein tyrosine kinase is a key regulator of T-cell activation and a target for signal intervention by Herpesvirus saimiri and other viral gene products."
    Isakov N., Biesinger B.
    Eur. J. Biochem. 267:3413-3421(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  23. "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.
  24. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
    Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
    Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Tissue: Mammary cancer.
  25. "LIME: a new membrane raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling."
    Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.
    J. Exp. Med. 198:1453-1462(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  26. "LIME, a novel transmembrane adaptor protein, associates with p56lck and mediates T cell activation."
    Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.
    J. Exp. Med. 198:1463-1473(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  27. "Interaction of SAP-1, a transmembrane-type protein-tyrosine phosphatase, with the tyrosine kinase Lck. Roles in regulation of T cell function."
    Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H., Kuwano H., Kosugi A., Matozaki T.
    J. Biol. Chem. 278:34854-34863(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRH.
  28. "T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315."
    Gelkop S., Gish G.D., Babichev Y., Pawson T., Isakov N.
    J. Immunol. 175:8123-8132(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ZAP70.
  29. "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-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: DEPHOSPHORYLATION BY PTN22.
  31. "Regulation of Ly49D/DAP12 signal transduction by Src-family kinases and CD45."
    Mason L.H., Willette-Brown J., Taylor L.S., McVicar D.W.
    J. Immunol. 176:6615-6623(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TYROBP.
  32. "Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes."
    Hjorthaug H.S., Aasheim H.C.
    Eur. J. Immunol. 37:2326-2336(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA1; PTK2B AND PI3-KINASE.
  33. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-159; SER-162; SER-194 AND TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  36. "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm."
    Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.
    J. Biol. Chem. 285:10122-10129(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RUNX3.
  37. "The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems."
    Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B., Houtman J.C.
    J. Leukoc. Biol. 87:691-701(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
  38. "RhoH modulates pre-TCR and TCR signalling by regulating LCK."
    Wang H., Zeng X., Fan Z., Lim B.
    Cell. Signal. 23:249-258(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RHOH.
  39. "T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice."
    Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C., Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.
    J. Clin. Invest. 121:4758-4774(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION AT TYR-394 BY PTPN2.
  40. Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
  41. "Feedback circuits monitor and adjust Basal lck-dependent events in T cell receptor signaling."
    Schoenborn J.R., Tan Y.X., Zhang C., Shokat K.M., Weiss A.
    Sci. Signal. 4:RA59-RA59(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  42. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  43. "Structure of the regulatory domains of the Src-family tyrosine kinase Lck."
    Eck M.J., Atweell S.K., Shoelson S.E., Harrison S.C.
    Nature 368:764-769(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 53-226.
  44. "The crystal structures of the SH2 domain of p56lck complexed with two phosphonopeptides suggest a gated peptide binding site."
    Mikol V., Baumann G., Keller T.H., Manning U.M., Zurini M.G.M.
    J. Mol. Biol. 246:344-355(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 127-221.
  45. "Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0-A and 1.8-A resolution."
    Tong L., Warren T.C., King J., Betageri R., Rose J., Jakes S.
    J. Mol. Biol. 256:601-610(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 122-226.
  46. "Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation."
    Yamaguchi H., Hendrickson W.A.
    Nature 384:484-489(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 231-501.
  47. "Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in SH2 domain binding."
    Tong L., Warren T.C., Lukas S., Schembri-King J., Betageri R., Proudfoot J.R., Jakes S.
    J. Biol. Chem. 273:20238-20242(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 119-226.

Entry informationi

Entry nameiLCK_HUMAN
AccessioniPrimary (citable) accession number: P06239
Secondary accession number(s): D3DPP8
, P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 200 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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