P06239 (LCK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

LCK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Ref.28 Ref.31 Ref.36 Ref.37 Ref.38 Ref.39
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Enzyme regulation	The relative activities of the inhibitory tyrosine-protein kinase CSK and the activating tyrosine-protein phosphatase PTPRC/CD45 determine the level of LCK activity. These interactions allow rapid and efficient activation of LCK in response to TCR stimulation. Ref.40
Subunit structure	Binds to the cytoplasmic domain of cell surface receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122. Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB and to other protein kinases including CDK1, RAF1, ZAP70 and SYK. Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes through its SH3 domain and to the tyrosine phosphorylated form of KHDRBS1/p70 through its SH2 domain. 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. Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.25 Ref.26 Ref.27 Ref.32
Subcellular location	Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Present in lipid rafts in an inactive form. Ref.23
Tissue specificity	Expressed specifically in lymphoid cells.
Domain	The SH2 domain mediates interaction with SQSTM1. Interaction is regulated by Ser-59 phosphorylation.
Post-translational modification	Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Ref.4 Ref.15 Ref.19 Ref.30 Myristoylation is required prior to palmitoylation By similarity. Palmitoylation regulates subcellular location By similarity.
Involvement in disease	A chromosomal aberration involving LCK is found in leukemias. Translocation t(1;7)(p34;q34) with TCRB.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.
Mass spectrometry	Molecular mass is 57869.42 Da from positions 2 - 509. Determined by MALDI. Ref.24
Sequence caution	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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Disease mutation Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from electronic annotation. Source: Compara T cell costimulation Traceable author statement. Source: Reactome T cell differentiation Inferred from mutant phenotype PubMed 1579166. Source: UniProtKB T cell receptor signaling pathway Traceable author statement. Source: Reactome activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 16116473. Source: UniProtKB aging Inferred from electronic annotation. Source: Compara cellular zinc ion homeostasis Inferred from expression pattern PubMed 11739864. Source: UniProtKB epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome induction of apoptosis Inferred from mutant phenotype PubMed 16116473. Source: UniProtKB innate immune response Traceable author statement. Source: Reactome leukocyte migration Traceable author statement. Source: Reactome neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome positive regulation of T cell receptor signaling pathway Non-traceable author statement PubMed 12614355. Source: UniProtKB positive regulation of gamma-delta T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from electronic annotation. Source: Compara positive regulation of uterine smooth muscle contraction Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of defense response to virus by virus Traceable author statement. Source: Reactome release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from direct assay PubMed 16116473. Source: UniProtKB response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome endocytic vesicle Inferred from electronic annotation. Source: Compara immunological synapse Inferred from direct assay PubMed 20007709. Source: MGI membrane raft Inferred from direct assay PubMed 12732664. Source: UniProtKB pericentriolar material Inferred from direct assay PubMed 7513706. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW SH2 domain binding Inferred from sequence or structural similarity. Source: UniProtKB antigen binding Inferred from electronic annotation. Source: Compara non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein serine/threonine phosphatase activity Inferred from direct assay PubMed 8506364. Source: UniProtKB protein tyrosine kinase activity Inferred from direct assay PubMed 214242. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP90AB1	P08238	2	EBI-1348,EBI-352572
KHDRBS1	Q07666	3	EBI-1348,EBI-1364
LAT	O43561	2	EBI-1348,EBI-1222766
MED28	Q9H204	4	EBI-1348,EBI-514199
PRKCQ	Q04759	2	EBI-1348,EBI-374762
PTPN22	Q9Y2R2	5	EBI-1348,EBI-1211241
PTPRC	P08575	2	EBI-1348,EBI-1341

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P06239-1)

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.

Isoform Short (identifier: P06239-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P06239-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 509

509

Tyrosine-protein kinase Lck

PRO_0000088124

Regions

Domain

61 – 121

61

SH3

Domain

127 – 224

98

SH2

Domain

245 – 498

254

Protein kinase

Nucleotide binding

251 – 259

9

ATP By similarity

Region

1 – 72

72

Interactions with CD4 and CD8 By similarity

Region

154 – 242

89

Interaction with PTPRH

Sites

Active site

364

1

Proton acceptor By similarity

Binding site

273

1

ATP By similarity

Amino acid modifications

Modified residue

102

1

Phosphoserine Ref.35

Modified residue

159

1

Phosphothreonine Ref.35

Modified residue

162

1

Phosphoserine Ref.35

Modified residue

194

1

Phosphoserine Ref.35

Modified residue

394

1

Phosphotyrosine; by autocatalysis Ref.4

Modified residue

505

1

Phosphotyrosine; by CSK Ref.4 Ref.15 Ref.19 Ref.29 Ref.33 Ref.34 Ref.35 Ref.41

Lipidation

2

1

N-myristoyl glycine By similarity

Lipidation

3

1

S-palmitoyl cysteine By similarity

Lipidation

5

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

321

1

N → NDTLLDSQLEEKGLGASPWG NLGQQLLLLPT in isoform 3.

VSP_016049

Alternative sequence

348 – 363

16

IAEGM…NYIHR → VRRLGRGAGQGNRPVT in isoform Short.

VSP_005000

Alternative sequence

364 – 509

146

Missing in isoform Short.

VSP_005001

Natural variant

28

1

V → L in leukemia. Ref.4

VAR_013463

Natural variant

201

1

G → S.
Corresponds to variant rs11567841 [ dbSNP | Ensembl ].

VAR_051697

Natural variant

232

1

P → PQKP in leukemia.

VAR_013464

Natural variant

353

1

A → V in leukemia. Ref.4

VAR_013465

Natural variant

447

1

P → L in leukemia. Ref.4

VAR_013466

Experimental info

Mutagenesis

59

1

S → E: Allows interaction with SQSTM1. Ref.18

Mutagenesis

154

1

R → K: No effect on interaction with SQSTM1. Ref.18

Sequence conflict

29

1

P → R in AAA59502. Ref.2

Sequence conflict

35

1

T → R in AAA59502. Ref.2

Sequence conflict

87

1

Q → P in CAA31884. Ref.2

Sequence conflict

87

1

Q → P in AAA59502. Ref.2

Sequence conflict

206 – 211

6

VRHYTN → ASAITPI in CAA28691. Ref.1

Sequence conflict

254

1

G → A in AAA59502. Ref.2

Sequence conflict

258 – 267

10

EVWMGYYNGH → RCGWGTTTGT in CAA28691. Ref.1

Sequence conflict

282 – 286

5

PDAFL → AGRLP in CAA28691. Ref.1

Sequence conflict

375

1

T → A in CAA28165. Ref.14

Sequence conflict

472

1

L → H in CAA29667. Ref.13

Sequence conflict

504 – 509

6

QYQPQP → STA in CAA28691. Ref.1

Secondary structure

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509

Helix Strand Turn

Details...

Helix

12 – 15

4

Beta strand

21 – 23

3

Beta strand

24 – 27

4

Turn

60 – 63

4

Beta strand

65 – 70

6

Beta strand

76 – 79

4

Beta strand

87 – 92

6

Beta strand

95 – 102

8

Turn

103 – 105

3

Beta strand

108 – 112

5

Helix

113 – 115

3

Beta strand

116 – 118

3

Beta strand

128 – 131

4

Helix

134 – 141

8

Beta strand

151 – 155

5

Beta strand

157 – 159

3

Beta strand

163 – 171

9

Turn

172 – 174

3

Beta strand

175 – 185

11

Turn

187 – 189

3

Beta strand

191 – 194

4

Beta strand

199 – 201

3

Helix

202 – 211

10

Beta strand

216 – 218

3

Turn

233 – 235

3

Beta strand

237 – 239

3

Helix

242 – 244

3

Beta strand

245 – 254

10

Beta strand

257 – 264

8

Turn

265 – 267

3

Beta strand

268 – 275

8

Turn

277 – 279

3

Helix

282 – 294

13

Beta strand

303 – 307

5

Beta strand

309 – 311

3

Beta strand

313 – 317

5

Helix

324 – 327

4

Helix

331 – 334

4

Helix

338 – 357

20

Helix

367 – 369

3

Beta strand

370 – 372

3

Beta strand

378 – 380

3

Helix

383 – 385

3

Helix

386 – 389

4

Beta strand

390 – 392

3

Beta strand

393 – 395

3

Turn

404 – 406

3

Helix

409 – 414

6

Helix

419 – 434

16

Turn

435 – 437

3

Helix

446 – 454

9

Helix

467 – 476

10

Helix

481 – 483

3

Helix

487 – 500

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 23, 2007. Version 6. Checksum: 44BFF0D43FFB420D	FASTA	509	58,001
	10 20 30 40 50 60 MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT YEGSNPPASP 70 80 90 100 110 120 LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN 130 140 150 160 170 180 SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH 190 200 210 220 230 240 YKIRNLDNGG FYISPRITFP GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV 250 260 270 280 290 300 PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 310 320 330 340 350 360 VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQIAE GMAFIEERNY 370 380 390 400 410 420 IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK 430 440 450 460 470 480 SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY QLMRLCWKER 490 500 PEDRPTFDYL RSVLEDFFTA TEGQYQPQP
	Isoform Short [UniParc]. Checksum: AC4AF1AB58D32577	FASTA	363	40,866
	10 20 30 40 50 60 MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT YEGSNPPASP 70 80 90 100 110 120 LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN 130 140 150 160 170 180 SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH 190 200 210 220 230 240 YKIRNLDNGG FYISPRITFP GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV 250 260 270 280 290 300 PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 310 320 330 340 350 360 VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQVRR LGRGAGQGNR PVT
	Isoform 3 [UniParc]. Checksum: D1024F47D18B289C	FASTA	539	61,190
	10 20 30 40 50 60 MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT YEGSNPPASP 70 80 90 100 110 120 LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN 130 140 150 160 170 180 SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH 190 200 210 220 230 240 YKIRNLDNGG FYISPRITFP GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV 250 260 270 280 290 300 PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 310 320 330 340 350 360 VRLYAVVTQE PIYIITEYME NDTLLDSQLE EKGLGASPWG NLGQQLLLLP TGSLVDFLKT 370 380 390 400 410 420 PSGIKLTINK LLDMAAQIAE GMAFIEERNY IHRDLRAANI LVSDTLSCKI ADFGLARLIE 430 440 450 460 470 480 DNEYTAREGA KFPIKWTAPE AINYGTFTIK SDVWSFGILL TEIVTHGRIP YPGMTNPEVI 490 500 510 520 530 QNLERGYRMV RPDNCPEELY QLMRLCWKER PEDRPTFDYL RSVLEDFFTA TEGQYQPQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"An aberrant lck mRNA in two human T-cell lines." Vogel L.B., Arthur R., Fujita D.J. Biochim. Biophys. Acta 1264:168-172(1995) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY.
[30]	"Identification of substrates of human protein-tyrosine phosphatase PTPN22." Wu J., Katrekar A., Honigberg L.A., Smith A.M., Conn M.T., Tang J., Jeffery D., Mortara K., Sampang J., Williams S.R., Buggy J., Clark J.M. J. Biol. Chem. 281:11002-11010(2006) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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]	"Tyrosine phosphorylation of tau by the SRC family kinases lck and fyn." Scales T.M., Derkinderen P., Leung K.Y., Byers H.L., Ward M.A., Price C., Bird I.N., Perera T., Kellie S., Williamson R., Anderton B.H., Reynolds C.H. Mol. Neurodegener. 6:12-12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[40]	"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.
[41]	"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, MASS SPECTROMETRY.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Lck entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00411413.
IPI00515097.
IPI00940423.

PIR

OKHULK. JQ0152.

RefSeq

NP_001036236.1. NM_001042771.1.
NP_005347.3. NM_005356.3.

UniGene

Hs.470627.

3D structure databases

PDBe
RCSB PDB
PDBj

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	59-119	[»]
1IJR	X-ray	2.20	A	124-226	[»]
1KIK	NMR	-	A	64-119	[»]
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	7-34	[»]
1Q69	NMR	-	B	7-34	[»]
1QPC	X-ray	1.60	A	231-509	[»]
1QPD	X-ray	2.00	A	231-508	[»]
1QPE	X-ray	2.00	A	231-508	[»]
1QPJ	X-ray	2.20	A	231-508	[»]
1X27	X-ray	2.70	A/B/C/D/E/F	64-225	[»]
2IIM	X-ray	1.00	A	59-118	[»]
2OF2	X-ray	2.00	A	231-500	[»]
2OF4	X-ray	2.70	A	231-500	[»]
2OFU	X-ray	2.00	A	229-500	[»]
2OFV	X-ray	2.00	A/B	226-502	[»]
2OG8	X-ray	2.30	A/B	237-498	[»]
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	[»]
4D8K	X-ray	2.36	A	53-226	[»]

ProteinModelPortal

P06239.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-553N.

IntAct

P06239. 35 interactions.

MINT

MINT-110378.

PTM databases

PhosphoSite

P06239.

Polymorphism databases

DMDM

125474.

Proteomic databases

PaxDb

P06239.

PRIDE

P06239.

Protocols and materials databases

DNASU

3932.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000333070; ENSP00000328213; ENSG00000182866.
ENST00000336890; ENSP00000337825; ENSG00000182866.

GeneID

3932.

KEGG

hsa:3932.

UCSC

uc001bux.3. human.
uc001buz.3. human.

Organism-specific databases

CTD

3932.

GeneCards

GC01P032716.

H-InvDB

HIX0019954.

HGNC

HGNC:6524. LCK.

HPA

CAB003816.
HPA003494.

MIM

153390. gene.

neXtProt

NX_P06239.

Orphanet

280142. Severe combined immunodeficiency due to LCK deficiency.

PharmGKB

PA30307.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG008761.

KO

K05856.

OMA

GHTKVAI.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
nfkappabatypicalpathway. Atypical NF-kappaB pathway.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
glypican_1pathway. Glypican 1 network.
il12_2pathway. IL12-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il2_stat5pathway. IL2 signaling events mediated by STAT5.
il2_1pathway. IL2-mediated signaling events.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P06239.

Gene expression databases

ArrayExpress

P06239.

Bgee

P06239.

CleanEx

HS_LCK.

Genevestigator

P06239.

GermOnline

ENSG00000182866. Homo sapiens.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06239.

ChEMBL

CHEMBL258.

ChiTaRS

LCK. human.

DrugBank

DB01254. Dasatinib.

EvolutionaryTrace

P06239.

GenomeRNAi

3932.

NextBio

15441.

SOURCE

Search...

Entry information

Entry name

LCK_HUMAN

Accession

Primary (citable) accession number: P06239
Secondary accession number(s): D3DPP8 , P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 186 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.