LCK

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 tyrosine 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. Interacts with FYB2 (PubMed:27335501).8 Publications

Catalytic activityⁱ

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

Activity 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 key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	273	ATPPROSITE-ProRule annotation		1
Active siteⁱ	364	Proton acceptorPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	251 – 259	ATPPROSITE-ProRule annotation		9

GO - Molecular functionⁱ

ATPase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15671290
ATP binding Source: UniProtKB-KW
CD4 receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7486703
CD8 receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 2470098
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 17118402
- 24463463
kinase activity Source: Reactome
non-membrane spanning protein tyrosine kinase activity Source: GO_Central
phosphatidylinositol 3-kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7504174
phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
phosphotyrosine residue binding
Source: CAFA
Inferred from physical interactionⁱ
- 20624904
protein C-terminus binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16245368
protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 8618896
protein phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 22080863
protein serine/threonine phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 8506364
protein tyrosine kinase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 214242
SH2 domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7852312
- 8794306
T cell receptor binding
Source: CAFA
Inferred from physical interactionⁱ
- 8681956

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of cysteine-type endopeptidase activity involved in apoptotic process
Source: UniProtKB
Inferred from direct assayⁱ
- 16116473
B cell receptor signaling pathway Source: GO_Central
cell migration Source: GO_Central
cellular zinc ion homeostasis
Source: UniProtKB
Inferred from expression patternⁱ
- 11739864
hemopoiesis
Source: UniProtKB
Non-traceable author statementⁱ
- 12884910
innate immune response Source: GO_Central
leukocyte migration Source: Reactome
peptidyl-tyrosine autophosphorylation Source: GO_Central
peptidyl-tyrosine phosphorylation
Source: CAFA
Inferred from mutant phenotypeⁱ
- 8681956
platelet activation Source: Reactome
positive regulation of heterotypic cell-cell adhesion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 27400149
positive regulation of intrinsic apoptotic signaling pathway
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16116473
positive regulation of leukocyte cell-cell adhesion
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 27400149
positive regulation of protein kinase B signaling Source: Reactome
positive regulation of T cell activation
Source: UniProtKB
Inferred from direct assayⁱ
- 8943371
positive regulation of T cell receptor signaling pathway
Source: UniProtKB
Non-traceable author statementⁱ
- 12614355
protein phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 214242
regulation of cell proliferation Source: GO_Central
regulation of defense response to virus by virus Source: Reactome
regulation of lymphocyte activation
Source: UniProtKB
Non-traceable author statementⁱ
- 7852312
release of sequestered calcium ion into cytosol Source: UniProtKB
response to drug
Source: UniProtKB
Inferred from direct assayⁱ
- 16116473
T cell costimulation Source: Reactome
T cell differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 1579166
T cell receptor signaling pathway Source: Reactome
transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase, Tyrosine-protein kinase
Biological process	Host-virus interaction
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-114604 GPVI-mediated activation cascade R-HSA-1257604 PIP3 activates AKT signaling R-HSA-1433557 Signaling by SCF-KIT R-HSA-1433559 Regulation of KIT signaling R-HSA-164944 Nef and signal transduction R-HSA-167590 Nef Mediated CD4 Down-regulation R-HSA-202424 Downstream TCR signaling R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains R-HSA-202430 Translocation of ZAP-70 to Immunological synapse R-HSA-202433 Generation of second messenger molecules R-HSA-210990 PECAM1 interactions R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-2424491 DAP12 signaling R-HSA-389356 CD28 co-stimulation R-HSA-389357 CD28 dependent PI3K/Akt signaling R-HSA-389359 CD28 dependent Vav1 pathway R-HSA-389513 CTLA4 inhibitory signaling R-HSA-389948 PD-1 signaling R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-9020558 Interleukin-2 signaling
SignaLinkⁱ	P06239
SIGNORⁱ	P06239

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000182866.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6524 LCK
MIMⁱ	153390 gene
neXtProtⁱ	NX_P06239

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.

Immunodeficiency 22 (IMD22)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA primary immunodeficiency characterized by T-cell dysfunction. Affected individuals present with lymphopenia, recurrent infections, severe diarrhea, and failure to thrive.

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_071291	341	L → P in IMD22. 1 PublicationCorresponds to variant dbSNP:rs587777335EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	59	S → E: Allows interaction with SQSTM1. 1 Publication		1
Mutagenesisⁱ	154	R → K: No effect on interaction with SQSTM1. 1 Publication		1

Keywords - Diseaseⁱ

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3932
MalaCards human disease database More...MalaCardsⁱ	LCK
MIMⁱ	615758 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000182866
Orphanetⁱ	280142 Severe combined immunodeficiency due to LCK deficiency
PharmGKBⁱ	PA30307

Chemistry databases

ChEMBLⁱ	CHEMBL258
Drug and drug target database More...DrugBankⁱ	DB06925 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-N-[3-(TRIFLUOROMETHYL)PHENYL]BENZAMIDE DB01254 Dasatinib DB09079 Nintedanib DB04395 Phosphoaminophosphonic Acid-Adenylate Ester DB08901 Ponatinib DB02010 Staurosporine
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2053

Polymorphism and mutation databases

BioMutaⁱ	LCK
DMDMⁱ	125474

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000088124	2 – 509	Tyrosine-protein kinase LckAdd BLAST		508

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Lipidationⁱ	2	N-myristoyl glycineBy similarity	1
Lipidationⁱ	3	S-palmitoyl cysteineBy similarity	1
Lipidationⁱ	5	S-palmitoyl cysteineBy similarity	1
Modified residueⁱ	102	PhosphoserineCombined sources	1
Modified residueⁱ	159	PhosphothreonineCombined sources	1
Modified residueⁱ	162	PhosphoserineCombined sources	1
Modified residueⁱ	192	PhosphotyrosineBy similarity	1
Modified residueⁱ	194	PhosphoserineCombined sources	1
Modified residueⁱ	394	Phosphotyrosine; by autocatalysis1 Publication	1
Modified residueⁱ	505	Phosphotyrosine; by CSKCombined sources3 Publications	1

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.4 Publications

Myristoylation is required prior to palmitoylation.By similarity

Palmitoylation regulates subcellular location.By similarity

Keywords - PTMⁱ

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

EPDⁱ	P06239
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P06239
PaxDbⁱ	P06239
PeptideAtlas More...PeptideAtlasⁱ	P06239
PRIDEⁱ	P06239
ProteomicsDBⁱ	51874 51875 [P06239-2] 51876 [P06239-3]

PTM databases

iPTMnetⁱ	P06239
PhosphoSitePlusⁱ	P06239
SwissPalmⁱ	P06239

Expressionⁱ

Tissue specificityⁱ

Expressed specifically in lymphoid cells.

Gene expression databases

Bgeeⁱ	ENSG00000182866 Expressed in 144 organ(s), highest expression level in thymus
CleanExⁱ	HS_LCK
ExpressionAtlasⁱ	P06239 baseline and differential
Genevisibleⁱ	P06239 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB003816 HPA003494

HPAⁱ

CAB003816
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, FYB1 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. 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. Interacts with UNC119; this interaction plays a crucial role in activation of LCK. Interacts with CEACAM1 (via cytoplasmic domain); mediates CEACAM1 phosphorylation resulting in PTPN6 recruitment that dephosphorylates TCR stimulation-induced CD247 and ZAP70 (PubMed:18424730).10 Publications

(Microbial infection) Interacts with herpes simplex virus 1 UL46; this interaction activates LCK.1 Publication

(Microbial infection) Interacts with HIV-1 Nef through its SH3 domain.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-1348,EBI-1348
	P22575	7	EBI-1348,EBI-866709	From Saimiriine herpesvirus 2 (strain 488).
	Q9YJQ8	2	EBI-1348,EBI-7709835	From Ateline herpesvirus 3.
ADAM15	Q13444	3	EBI-1348,EBI-77818
AR	P10275	7	EBI-1348,EBI-608057
BCL3	P20749	3	EBI-1348,EBI-958997
CD4	P01730	2	EBI-1348,EBI-353826
CDKAL1	Q5VV42	3	EBI-1348,EBI-10194801
GAB1	Q13480	10	EBI-1348,EBI-517684
GATA3	P23771	3	EBI-1348,EBI-6664760
HSP90AB1	P08238	2	EBI-1348,EBI-352572
KHDRBS1	Q07666	5	EBI-1348,EBI-1364
KIT	P10721	8	EBI-1348,EBI-1379503
LAT	O43561	2	EBI-1348,EBI-1222766
LZTS2	Q9BRK4	3	EBI-1348,EBI-741037
MED28	Q9H204	4	EBI-1348,EBI-514199
MET	P08581	3	EBI-1348,EBI-1039152
NR3C1	P04150	3	EBI-1348,EBI-493507
PRKCQ	Q04759	2	EBI-1348,EBI-374762
PTK2	I6L996	3	EBI-13287659,EBI-10181089
PTPN22	Q9Y2R2	6	EBI-1348,EBI-1211241
PTPN6	P29350	5	EBI-1348,EBI-78260
PTPRC	P08575	7	EBI-1348,EBI-1341
SH2D2A	Q9NP31	12	EBI-1348,EBI-490630
SYK	P43405	7	EBI-1348,EBI-78302
THEMIS	Q8N1K5-1	3	EBI-1348,EBI-15102259
UBC	P0CG48	2	EBI-1348,EBI-3390054
ZAP70	P43403	2	EBI-1348,EBI-1211276

GO - Molecular functionⁱ

ATPase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15671290
CD4 receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7486703
CD8 receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 2470098
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 17118402
- 24463463
phosphatidylinositol 3-kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7504174
phosphotyrosine residue binding
Source: CAFA
Inferred from physical interactionⁱ
- 20624904
protein C-terminus binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16245368
protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 8618896
protein phosphatase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 22080863
SH2 domain binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 7852312
- 8794306
T cell receptor binding
Source: CAFA
Inferred from physical interactionⁱ
- 8681956

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110124, 89 interactors
CORUMⁱ	P06239
Database of interacting proteins More...DIPⁱ	DIP-553N
ELMⁱ	P06239
IntActⁱ	P06239, 86 interactors
Molecular INTeraction database More...MINTⁱ	P06239
STRINGⁱ	9606.ENSP00000337825

Chemistry databases

BindingDBⁱ

P06239

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	12 – 15	Combined sources	4
Beta strandⁱ	21 – 23	Combined sources	3
Beta strandⁱ	24 – 27	Combined sources	4
Turnⁱ	60 – 63	Combined sources	4
Beta strandⁱ	65 – 70	Combined sources	6
Beta strandⁱ	76 – 79	Combined sources	4
Beta strandⁱ	87 – 92	Combined sources	6
Beta strandⁱ	95 – 102	Combined sources	8
Turnⁱ	103 – 105	Combined sources	3
Beta strandⁱ	108 – 112	Combined sources	5
Helixⁱ	113 – 115	Combined sources	3
Beta strandⁱ	116 – 118	Combined sources	3
Beta strandⁱ	128 – 131	Combined sources	4
Helixⁱ	134 – 141	Combined sources	8
Beta strandⁱ	151 – 155	Combined sources	5
Beta strandⁱ	157 – 159	Combined sources	3
Beta strandⁱ	163 – 171	Combined sources	9
Turnⁱ	172 – 174	Combined sources	3
Beta strandⁱ	175 – 185	Combined sources	11
Turnⁱ	187 – 189	Combined sources	3
Beta strandⁱ	191 – 194	Combined sources	4
Beta strandⁱ	199 – 201	Combined sources	3
Helixⁱ	202 – 211	Combined sources	10
Beta strandⁱ	216 – 218	Combined sources	3
Turnⁱ	233 – 235	Combined sources	3
Beta strandⁱ	237 – 239	Combined sources	3
Helixⁱ	242 – 244	Combined sources	3
Beta strandⁱ	245 – 254	Combined sources	10
Beta strandⁱ	257 – 264	Combined sources	8
Turnⁱ	265 – 267	Combined sources	3
Beta strandⁱ	268 – 275	Combined sources	8
Turnⁱ	277 – 279	Combined sources	3
Helixⁱ	282 – 294	Combined sources	13
Beta strandⁱ	303 – 307	Combined sources	5
Beta strandⁱ	309 – 311	Combined sources	3
Beta strandⁱ	313 – 317	Combined sources	5
Helixⁱ	324 – 327	Combined sources	4
Helixⁱ	331 – 334	Combined sources	4
Helixⁱ	338 – 357	Combined sources	20
Helixⁱ	367 – 369	Combined sources	3
Beta strandⁱ	370 – 372	Combined sources	3
Beta strandⁱ	378 – 380	Combined sources	3
Helixⁱ	383 – 385	Combined sources	3
Helixⁱ	386 – 389	Combined sources	4
Beta strandⁱ	390 – 392	Combined sources	3
Beta strandⁱ	393 – 395	Combined sources	3
Turnⁱ	404 – 406	Combined sources	3
Helixⁱ	409 – 414	Combined sources	6
Helixⁱ	419 – 434	Combined sources	16
Turnⁱ	435 – 437	Combined sources	3
Helixⁱ	446 – 454	Combined sources	9
Helixⁱ	467 – 476	Combined sources	10
Helixⁱ	481 – 483	Combined sources	3
Helixⁱ	487 – 500	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	P06239
SMRⁱ	P06239
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P06239

EvolutionaryTraceⁱ

P06239

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	61 – 121	SH3PROSITE-ProRule annotationAdd BLAST	61
Domainⁱ	127 – 224	SH2PROSITE-ProRule annotationAdd BLAST	98
Domainⁱ	245 – 498	Protein kinasePROSITE-ProRule annotationAdd BLAST	254

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	2 – 72	Interactions with CD4 and CD8By similarityAdd BLAST		71
Regionⁱ	154 – 242	Interaction with PTPRH1 PublicationAdd BLAST		89

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation

Keywords - Domainⁱ

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGⁱ	KOG0197 Eukaryota COG0515 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118938
HOVERGENⁱ	HBG008761
InParanoidⁱ	P06239
KEGG Orthology (KO) More...KOⁱ	K05856
OMAⁱ	NPEDDWM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0D46
PhylomeDBⁱ	P06239
TreeFamⁱ	TF351634

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10362 SH2_Src_Lck, 1 hit cd12005 SH3_Lck, 1 hit
Gene3Dⁱ	3.30.505.10, 1 hit
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR035850 Lck_SH2 IPR035749 Lck_SH3 IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit PF00018 SH3_1, 1 hit
PRINTSⁱ	PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in 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

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 Add to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show all Align All

Isoform Long (identifier: P06239-1) [UniParc]FASTA Add 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

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

TEGQYQPQP

Length:509

Mass (Da):58,001

Last modified:January 23, 2007 - v6

Checksum:ⁱ44BFF0D43FFB420D

GO

Isoform Short (identifier: P06239-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT 
        60         70         80         90        100
YEGSNPPASP LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA 
       110        120        130        140        150
QSLTTGQEGF IPFNFVAKAN SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS 
       160        170        180        190        200
FLIRESESTA GSFSLSVRDF DQNQGEVVKH YKIRNLDNGG FYISPRITFP 
       210        220        230        240        250
GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV PRETLKLVER 
       260        270        280        290        300
LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 
       310        320        330        340        350
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQVRR 
       360 
LGRGAGQGNR PVT

Note: No experimental confirmation available.

Show »

Length:363

Mass (Da):40,866

Checksum:ⁱAC4AF1AB58D32577

GO

Isoform 3 (identifier: P06239-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT 
        60         70         80         90        100
YEGSNPPASP LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA 
       110        120        130        140        150
QSLTTGQEGF IPFNFVAKAN SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS 
       160        170        180        190        200
FLIRESESTA GSFSLSVRDF DQNQGEVVKH YKIRNLDNGG FYISPRITFP 
       210        220        230        240        250
GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV PRETLKLVER 
       260        270        280        290        300
LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL 
       310        320        330        340        350
VRLYAVVTQE PIYIITEYME NDTLLDSQLE EKGLGASPWG NLGQQLLLLP 
       360        370        380        390        400
TGSLVDFLKT PSGIKLTINK LLDMAAQIAE GMAFIEERNY IHRDLRAANI 
       410        420        430        440        450
LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK 
       460        470        480        490        500
SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY 
       510        520        530 
QLMRLCWKER PEDRPTFDYL RSVLEDFFTA TEGQYQPQP

Note: No experimental confirmation available.

Show »

Length:539

Mass (Da):61,190

Checksum:ⁱD1024F47D18B289C

GO

Computationally mapped potential isoform sequencesⁱ

There are 7 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

Q573B4	Q573B4_HUMAN	Tyrosine-protein kinase Tyrosine-protein kinase, EC 2.7.10.2	LCK	516	Annotation score:
E9PJ92	E9PJ92_HUMAN	Tyrosine-protein kinase Tyrosine-protein kinase, EC 2.7.10.2	LCK	319	Annotation score:
E9PAP0	E9PAP0_HUMAN	Tyrosine-protein kinase Lck Tyrosine-protein kinase Lck	LCK	285	Annotation score:
F8W6B9	F8W6B9_HUMAN	Tyrosine-protein kinase Lck Tyrosine-protein kinase Lck	LCK	137	Annotation score:
E9PKQ8	E9PKQ8_HUMAN	Tyrosine-protein kinase Lck Tyrosine-protein kinase Lck	LCK	200	Annotation score:
E9PQ10	E9PQ10_HUMAN	Tyrosine-protein kinase Lck Tyrosine-protein kinase Lck	LCK	149	Annotation score:
E9PI33	E9PI33_HUMAN	Tyrosine-protein kinase Lck Tyrosine-protein kinase Lck	LCK	167	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	29	P → R in AAA59502 (PubMed:3265417).Curated	1
Sequence conflictⁱ	35	T → R in AAA59502 (PubMed:3265417).Curated	1
Sequence conflictⁱ	87	Q → P in CAA31884 (PubMed:3265417).Curated	1
Sequence conflictⁱ	87	Q → P in AAA59502 (PubMed:3265417).Curated	1
Sequence conflictⁱ	206 – 211	VRHYTN → ASAITPI in CAA28691 (PubMed:3493153).Curated	6
Sequence conflictⁱ	254	G → A in AAA59502 (PubMed:3265417).Curated	1
Sequence conflictⁱ	258 – 267	EVWMGYYNGH → RCGWGTTTGT in CAA28691 (PubMed:3493153).Curated	10
Sequence conflictⁱ	282 – 286	PDAFL → AGRLP in CAA28691 (PubMed:3493153).Curated	5
Sequence conflictⁱ	375	T → A in CAA28165 (PubMed:3489486).Curated	1
Sequence conflictⁱ	472	L → H in CAA29667 (PubMed:2835736).Curated	1
Sequence conflictⁱ	504 – 509	QYQPQP → STA in CAA28691 (PubMed:3493153).Curated	6

Mass spectrometryⁱ

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

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_013463	28	V → L Found in leukemia. 1 Publication	1
Natural variantⁱVAR_051697	201	G → S. Corresponds to variant dbSNP:rs11567841Ensembl.	1
Natural variantⁱVAR_013464	232	P → PQKP in leukemia.	1
Natural variantⁱVAR_071291	341	L → P in IMD22. 1 PublicationCorresponds to variant dbSNP:rs587777335EnsemblClinVar.	1
Natural variantⁱVAR_013465	353	A → V Found in leukemia. 1 Publication	1
Natural variantⁱVAR_013466	447	P → L Found in leukemia. 1 Publication	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_016049	321	N → NDTLLDSQLEEKGLGASPWG NLGQQLLLLPT in isoform 3. 1 Publication	1
Alternative sequenceⁱVSP_005000	348 – 363	IAEGM…NYIHR → VRRLGRGAGQGNRPVT in isoform Short. 1 PublicationAdd BLAST	16
Alternative sequenceⁱVSP_005001	364 – 509	Missing in isoform Short. 1 PublicationAdd BLAST	146

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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 No translation available. 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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS359.1 [P06239-1]
PIRⁱ	JQ0152 OKHULK
NCBI Reference Sequences More...RefSeqⁱ	NP_001036236.1, NM_001042771.2 [P06239-1] NP_005347.3, NM_005356.4 [P06239-1]
UniGeneⁱ	Hs.470627

Genome annotation databases

Ensemblⁱ	ENST00000333070; ENSP00000328213; ENSG00000182866 [P06239-3] ENST00000336890; ENSP00000337825; ENSG00000182866 [P06239-1] ENST00000619559; ENSP00000477713; ENSG00000182866 [P06239-1]
GeneIDⁱ	3932
KEGGⁱ	hsa:3932
UCSC genome browser More...UCSCⁱ	uc001bux.3 human [P06239-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P06239	Tyrosine-protein kinase		PANTR		527	UniRef100_P06239
Tyrosine-protein kinase (Fragment)		HUMAN		509
Tyrosine-protein kinase		PANPA		509
Tyrosine-protein kinase		GORGO		509
Tyrosine-protein kinase		PANTR		509
P06239-3	Tyrosine-protein kinase		PANTR		539	UniRef100_H2PYK3
Tyrosine-protein kinase (Fragment)		HUMAN		539
Tyrosine-protein kinase Lck (Fragment)		HUMAN		137
UPI0007DBBB0C		PANTR		557

Protein	Similar proteins		Species	Score	Length	Source
P06239	Tyrosine-protein kinase Lck		AOTNA		509	UniRef90_P06239
Proto-oncogene tyrosine-protein kinase LCK		SAISC		509
Proto-oncogene tyrosine-protein kinase LCK		MOUSE		509
Proto-oncogene tyrosine-protein kinase LCK		RAT		509
Tyrosine-protein kinase		PANTR		527
+146
P06239-2	Tyrosine-protein kinase		TUPCH		444	UniRef90_P06239-2
P06239-3	Tyrosine-protein kinase		PANTR		539	UniRef90_H2PYK3
Tyrosine-protein kinase (Fragment)		HUMAN		539
Tyrosine-protein kinase		TARSY		540
Tyrosine-protein kinase		CERAT		540
Tyrosine-protein kinase		PAPAN		540
+11

Protein	Similar proteins		Species	Score	Length	Source
P06239	Tyrosine-protein kinase Fyn	)	HUMAN		537	UniRef50_P06241
Tyrosine-protein kinase fynb		DANRE		544
Tyrosine-protein kinase Fyn		RAT		537
Tyrosine-protein kinase Fyn		BOVIN		537
Tyrosine-protein kinase Fyn	)	MOUSE		537
+797
P06239-2	Tyrosine-protein kinase		TUPCH		444	UniRef50_P06239-2
Tyrosine-protein kinase		SCOMX		510
Tyrosine-protein kinase		TETNG		513
Tyrosine-protein kinase		PELSI		516
Tyrosine-protein kinase Lyn isoform 1		CAMFR		427
+134
P06239-3	Tyrosine-protein kinase		PANTR		539	UniRef50_H2PYK3
Tyrosine-protein kinase (Fragment)		HUMAN		539
Tyrosine-protein kinase		MACNE		540
Tyrosine-protein kinase		CERAT		540
Tyrosine-protein kinase		TARSY		540
+67

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Lck entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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 No translation available. 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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	5MTM	X-ray	2.40	A	118-231	[»]
	5MTN	X-ray	2.85	A	118-231	[»]
ProteinModelPortalⁱ	P06239
SMRⁱ	P06239
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110124, 89 interactors
CORUMⁱ	P06239
DIPⁱ	DIP-553N
ELMⁱ	P06239
IntActⁱ	P06239, 86 interactors
MINTⁱ	P06239
STRINGⁱ	9606.ENSP00000337825

Chemistry databases

BindingDBⁱ	P06239
ChEMBLⁱ	CHEMBL258
DrugBankⁱ	DB06925 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-N-[3-(TRIFLUOROMETHYL)PHENYL]BENZAMIDE DB01254 Dasatinib DB09079 Nintedanib DB04395 Phosphoaminophosphonic Acid-Adenylate Ester DB08901 Ponatinib DB02010 Staurosporine
GuidetoPHARMACOLOGYⁱ	2053

PTM databases

iPTMnetⁱ	P06239
PhosphoSitePlusⁱ	P06239
SwissPalmⁱ	P06239

Polymorphism and mutation databases

BioMutaⁱ	LCK
DMDMⁱ	125474

Proteomic databases

EPDⁱ	P06239
MaxQBⁱ	P06239
PaxDbⁱ	P06239
PeptideAtlasⁱ	P06239
PRIDEⁱ	P06239
ProteomicsDBⁱ	51874 51875 [P06239-2] 51876 [P06239-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	3932
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000333070; ENSP00000328213; ENSG00000182866 [P06239-3] ENST00000336890; ENSP00000337825; ENSG00000182866 [P06239-1] ENST00000619559; ENSP00000477713; ENSG00000182866 [P06239-1]
GeneIDⁱ	3932
KEGGⁱ	hsa:3932
UCSCⁱ	uc001bux.3 human [P06239-1]

Organism-specific databases

CTDⁱ	3932
DisGeNETⁱ	3932
EuPathDBⁱ	HostDB:ENSG00000182866.16
GeneCardsⁱ	LCK
H-InvDBⁱ	HIX0019954
HGNCⁱ	HGNC:6524 LCK
HPAⁱ	CAB003816 HPA003494
MalaCardsⁱ	LCK
MIMⁱ	153390 gene 615758 phenotype
neXtProtⁱ	NX_P06239
OpenTargetsⁱ	ENSG00000182866
Orphanetⁱ	280142 Severe combined immunodeficiency due to LCK deficiency
PharmGKBⁱ	PA30307
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0197 Eukaryota COG0515 LUCA
GeneTreeⁱ	ENSGT00760000118938
HOVERGENⁱ	HBG008761
InParanoidⁱ	P06239
KOⁱ	K05856
OMAⁱ	NPEDDWM
OrthoDBⁱ	EOG091G0D46
PhylomeDBⁱ	P06239
TreeFamⁱ	TF351634

Enzyme and pathway databases

BRENDAⁱ	2.7.10.2 2681
Reactomeⁱ	R-HSA-114604 GPVI-mediated activation cascade R-HSA-1257604 PIP3 activates AKT signaling R-HSA-1433557 Signaling by SCF-KIT R-HSA-1433559 Regulation of KIT signaling R-HSA-164944 Nef and signal transduction R-HSA-167590 Nef Mediated CD4 Down-regulation R-HSA-202424 Downstream TCR signaling R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains R-HSA-202430 Translocation of ZAP-70 to Immunological synapse R-HSA-202433 Generation of second messenger molecules R-HSA-210990 PECAM1 interactions R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-2424491 DAP12 signaling R-HSA-389356 CD28 co-stimulation R-HSA-389357 CD28 dependent PI3K/Akt signaling R-HSA-389359 CD28 dependent Vav1 pathway R-HSA-389513 CTLA4 inhibitory signaling R-HSA-389948 PD-1 signaling R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-9020558 Interleukin-2 signaling
SignaLinkⁱ	P06239
SIGNORⁱ	P06239

Miscellaneous databases

ChiTaRSⁱ	LCK human
EvolutionaryTraceⁱ	P06239
GeneWikiⁱ	Lck
GenomeRNAiⁱ	3932
Protein Ontology More...PROⁱ	PR:P06239
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000182866 Expressed in 144 organ(s), highest expression level in thymus
CleanExⁱ	HS_LCK
ExpressionAtlasⁱ	P06239 baseline and differential
Genevisibleⁱ	P06239 HS

Family and domain databases

CDDⁱ	cd10362 SH2_Src_Lck, 1 hit cd12005 SH3_Lck, 1 hit
Gene3Dⁱ	3.30.505.10, 1 hit
InterProⁱ	View protein in InterPro IPR011009 Kinase-like_dom_sf IPR035850 Lck_SH2 IPR035749 Lck_SH3 IPR000719 Prot_kinase_dom IPR017441 Protein_kinase_ATP_BS IPR001245 Ser-Thr/Tyr_kinase_cat_dom IPR000980 SH2 IPR036860 SH2_dom_sf IPR036028 SH3-like_dom_sf IPR001452 SH3_domain IPR008266 Tyr_kinase_AS IPR020635 Tyr_kinase_cat_dom
Pfamⁱ	View protein in Pfam PF07714 Pkinase_Tyr, 1 hit PF00017 SH2, 1 hit PF00018 SH3_1, 1 hit
PRINTSⁱ	PR00401 SH2DOMAIN PR00452 SH3DOMAIN PR00109 TYRKINASE
SMARTⁱ	View protein in SMART SM00252 SH2, 1 hit SM00326 SH3, 1 hit SM00219 TyrKc, 1 hit
SUPFAMⁱ	SSF50044 SSF50044, 1 hit SSF55550 SSF55550, 1 hit SSF56112 SSF56112, 1 hit
PROSITEⁱ	View protein in 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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LCK_HUMAN
Accessionⁱ	P06239Primary (citable) accession number: P06239 Secondary accession number(s): D3DPP8 Q9NYT8
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	October 10, 2018
	This is version 245 of the entry and version 6 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

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

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UniProtKB - P06239 (LCK_HUMAN)

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Tyrosine-protein kinase Lck

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Other locations

Cytoskeleton

Cytosol

Extracellular region or secreted

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Mass spectrometryⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ