LCK LCK proto-oncogene, Src family tyrosine kinase [Homo sapiens (human)] - Gene

Summary

Official Symbol: LCKprovided by HGNC
Official Full Name: LCK proto-oncogene, Src family tyrosine kinaseprovided by HGNC
Primary source: HGNC:HGNC:6524
See related: Ensembl:ENSG00000182866 MIM:153390; AllianceGenome:HGNC:6524
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: LSK; YT16; IMD22; p56lck; pp58lck
Summary: This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants encoding different isoforms have been described. [provided by RefSeq, Aug 2016]
Expression: Biased expression in lymph node (RPKM 46.5), appendix (RPKM 22.7) and 9 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1p35.2

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (32251265..32286165)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (32109169..32144081)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (32716866..32751766)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Combined Immunodeficiency Caused by a Novel Nonsense Mutation in LCK.
Title: Combined Immunodeficiency Caused by a Novel Nonsense Mutation in LCK.
A Novel Biallelic LCK Variant Resulting in Profound T-Cell Immune Deficiency and Review of the Literature.
Title: A Novel Biallelic LCK Variant Resulting in Profound T-Cell Immune Deficiency and Review of the Literature.
Identification of Breast Cancer LCK Proto-Oncogene as a Master Regulator of TNBC Neutrophil Enrichment and Polarization.
Title: Identification of Breast Cancer LCK Proto-Oncogene as a Master Regulator of TNBC Neutrophil Enrichment and Polarization.
LCK facilitates DNA damage repair by stabilizing RAD51 and BRCA1 in the nucleus of chemoresistant ovarian cancer.
Title: LCK facilitates DNA damage repair by stabilizing RAD51 and BRCA1 in the nucleus of chemoresistant ovarian cancer.
LCK, FOXC1 and hsa-miR-146a-5p as potential immune effector molecules associated with rheumatoid arthritis.
Title: LCK, FOXC1 and hsa-miR-146a-5p as potential immune effector molecules associated with rheumatoid arthritis.
A Cysteine Residue within the Kinase Domain of Zap70 Regulates Lck Activity and Proximal TCR Signaling.
Title: A Cysteine Residue within the Kinase Domain of Zap70 Regulates Lck Activity and Proximal TCR Signaling.
Role of Programmed Cell Death Protein-1 and Lymphocyte Specific Protein Tyrosine Kinase in the Aryl Hydrocarbon Receptor- Mediated Impairment of the IgM Response in Human CD5(+) Innate-Like B Cells.
Title: Role of Programmed Cell Death Protein-1 and Lymphocyte Specific Protein Tyrosine Kinase in the Aryl Hydrocarbon Receptor- Mediated Impairment of the IgM Response in Human CD5(+) Innate-Like B Cells.
Identification of lymphocyte cell-specific protein-tyrosine kinase (LCK) as a driver for invasion and migration of oral cancer by tumor heterogeneity exploitation.
Title: Identification of lymphocyte cell-specific protein-tyrosine kinase (LCK) as a driver for invasion and migration of oral cancer by tumor heterogeneity exploitation.
Cooperative Interaction of Nck and Lck Orchestrates Optimal TCR Signaling.
Title: Cooperative Interaction of Nck and Lck Orchestrates Optimal TCR Signaling.
A Novel, LAT/Lck Double Deficient T Cell Subline J.CaM1.7 for Combined Analysis of Early TCR Signaling.
Title: A Novel, LAT/Lck Double Deficient T Cell Subline J.CaM1.7 for Combined Analysis of Early TCR Signaling.

Submit: New GeneRIF Correction See all GeneRIFs (170)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Severe combined immunodeficiency due to LCK deficiency MedGen: C4014233 OMIM: 615758 GeneReviews: Not available	not available

Variation

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See Variation Viewer (GRCh37.p13)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	The ability of gp120 to inhibit SDF-1alpha-induced chemotaxis is mediated by the CD4 receptor and Lck signaling	PubMed
	env	Interaction of HIV-1 gp120 with CD4 leads to increased levels of phosphorylation of the src-family Lck and Fyn protein tyrosine kinases and enhancement of their activities	PubMed
	env	HIV-1 gp120 induces the dissociation of p56lck from CD4 and the downregulation of CD4 from the cellular surface	PubMed
	env	Binding of HIV-1 gp120 to CD4 induces p56lck activation and zeta-chain (TCR) associated protein kinase 70kDa desensitization independent of TCR tyrosine phosphorylation	PubMed
	env	Engagement of CD4 with HIV-1 gp120 inhibits Lck and F-actin recruitment into the immunological synapse	PubMed
	env	The protein tyrosine kinase p56lck plays an active role in transmitting an HIV-1 gp120-mediated signal that increases the oxidative state of cells and as a consequence amplifies TNF-mediated NF-kappa B DNA binding	PubMed
	env	HIV-1 gp120 induces an increase in tyrosine phosphorylation of two proteins, p56lck and phosphatidylinositol 3-kinase (PI 3-kinase) p85 alpha, that are physically complexed to the CD4 molecule	PubMed
	env	HIV-1 gp120 inhibits CD3-induced Lck activation and cellular tyrosine phosphorylation, particularly of phosphoinositide-specific phospholipase C-gamma-1	PubMed
	env	CD4-p56Lck interaction is required for HIV-1 gp120-induced nuclear translocation of NF-kappaB in HeLa cells	PubMed
	env	p56lck-positive cells are markedly more susceptible to syncytium formation than p56lck-negative cells, implying a regulatory role for p56lck in the syncytium formation mediated by HIV-1 gp120 envelope interaction with CD4	PubMed
	env	Binding of HIV-1 gp120 to CD4 molecules results in the association of Lck and Raf-1, which is abolished by preincubation of the virus with soluble CD4	PubMed
	env	Activation of the CD4-p56lck receptor signal transduction pathway by HIV-1 gp120 does not increase prostaglandin formation	PubMed
Envelope surface glycoprotein gp160, precursor	env	Interaction of HIV-1 gp160 with CD4 increases p56lck autophosphorylation and kinase activity	PubMed
	env	HIV-1 gp160 downregulates lymphocyte function-associated antigen-1 (LFA-1)-dependent adhesion between CD4+ T cells and B cells; this downregulation is shown to be p56lck-dependent	PubMed
Envelope transmembrane glycoprotein gp41	env	HIV-1 gp120 and gp41-induced cell killing is accompanied by tyrosine phosphorylation and activation of the CD4-associated p56(Lck) kinase, and by activation of a second member of the scr family of protein tyrosine kinases, p59(fyn) kinase	PubMed
Nef	nef	HIV-1 NL4-3 Nef recruits LCK (p56) into endosomes, which is dependent upon the CPG-motif of Nef	PubMed
	nef	HIV-1 Nef-induced relocalization of LCK is correlated with N-Ras activation at recycling endosome/TGN compartments	PubMed
	nef	HIV-1 Nef induces relocalization of LCK away from the plasma membrane to the recycling endosome and the trans-Golgi network, inhibiting recruitment of LCK to the immunological synapse	PubMed
	nef	HIV-1 Nef increases the association of the src family tyrosine kinase, Lck, and TCRzeta with rafts in human T cells, suggesting Nef primes resting T cells for activation by upregulating the levels of signaling molecules within rafts	PubMed
	nef	HIV-1 Nef efficiently interacts with Lck by coimmunoprecipitation and in vitro kinase assays; this interaction is reduced by an R71T mutation in the proline-rich motif of Nef	PubMed
	nef	The formation of Nef/LCK/PKCtheta complex activates the ERK MAPK signaling pathway	PubMed
	nef	HIV-1 Nef interferes with the activation of Lck and as a consequence of signaling via the IL-2 receptor	PubMed
	nef	Cooperation of the Lck SH2 and SH3 domains is required for HIV-1 Nef binding to Lck to a level similar to Nef binding to the Hck SH3 domain	PubMed
	nef	The HIV-1 Nef highly conserved valine-glycine-phenylalanine amino acid triplet (VGF) motif is essential for effects of Nef on actin dynamics and Lck localization	PubMed
	nef	Expression of SH3/SH2 ligand-uncoordinated 119 (UNC119) completely reverses the HIV-1 Nef-mediated inhibition of immunological synapse recruitment of LCK	PubMed
	nef	HIV-1 Nef-induced relocalization of LCK increases phosphorylated ERK1/2 induction in infected and trasduced primary T cells	PubMed
	nef	HIV-1 Nef induces intracellular accumulation of Lck and interferes with its recruitment to sites of TCR engagement. The accumulation of Lck requires the membrane attachment G2 and the SH3 binding motif AXXA of Nef	PubMed
	nef	Human T cells expressing herpes virus saimiri-Tip mediate restriction of late-stage replication of HIV-1 by disrupting Nef interaction with Lck in lipid rafts	PubMed
	nef	Formation of the Nef-associated kinase complex (NAKC) is sufficient to activate LCK and ERK1/2 and causes a strong Tat-dependent increase of HIV-1 transcription in T cells	PubMed
	nef	In the context of Nef-associated kinase complex (NAKC), hnRNP-K interacts with HIV-1 Nef and recruits LCK, PKCdelta, and PI-3 kinase. The proline-rich domain (amino-acids 289-315) of hnRNP-K is required for the recruitment of activated LCK18854243	PubMed
	nef	PKCtheta is a downstream effector of LCK and is recruited by HIV-1 Nef to form the Nef/LCK/PKCtheta complex, which promotes HIV transcription	PubMed
	nef	HIV-1 Nef-mediated increase of HIV transcription requires the Nef N terminus (amino acids 12-29) and LCK kinase activity by Nef activation	PubMed
	nef	Expression of p56(lck) in nonlymphoid CD4-expressing cells restores the ability of Nef in order to increase the internalization rate of CD4	PubMed
	nef	HIV-1 Nef increases the production of exosomes, which form at the plasma membrane and co-localizes with plasma membrane-associated proteins ICAM1, CD81, and Lck in Jurkat	PubMed
	nef	Amino acid residues 402-419 of the cytoplasmic tail of CD4 are required for association with Lck and also for the downregulation of CD4 induced by HIV-1 Nef, suggesting a potential interaction between Nef and Lck	PubMed
	nef	HIV-1 and SIV Nef can bind Lck SH2 domains, and their N-terminal 50 amino acid residues are sufficient for Src kinase binding and activation	PubMed
	nef	Assays with phage-displayed Nef from HIV-1 NL4-3 have been used to identify a series of guanidine alkaloid-based inhibitors of Nef interactions with p53, actin, and p56(lck)	PubMed
	nef	A highly conserved proline-rich repeat sequence in Nef between amino acids 69-78 directly binds to the SH2 and SH3 domains of Lck	PubMed
	nef	HIV-1 Nef enhances the phosphorylation of c-Cbl in CD4+ T cells, an effect that requires the Src tyrosine kinase Lck	PubMed
Pr55(Gag)	gag	The amplified luminescent proximity homogeneous assay (AlphaScreen) identifies the interaction of HIV-1 Gag with LCK	PubMed
	gag	Lck enhances HIV-1 Gag assembly and release in T cells. Lck palmitoylation sites at cysteine's 3 and 5 are required for the efficient virus production	PubMed
Tat	tat	Herpes virus saimiri-StpC synergizes with Tat during transcriptional activation of the HIV-1 LTR. This transcriptional synergy between StpC and Tat requires Lck and NF-kappaB consensus binding sequences	PubMed
	tat	Formation of the Nef-associated kinase complex (NAKC) is sufficient to activate LCK and ERK1/2 and causes a strong Tat-dependent increase of HIV-1 transcription in T cells	PubMed
	tat	HIV-1 Tat activates p56lck in Jurkat cells leading to the degradation of IkappaBalpha and activation of NFkappaB, AP-1, JNK, MAPKK, caspases, and apoptosis	PubMed
Vpu	vpu	HIV-1 Vpu affects the subcellular localization of LCK but with reduced efficacy compared to HIV-1 Nef	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

SHGC-12348 (e-PCR)
- UniSTS:63313

SHGC-74532 (e-PCR)
- UniSTS:43614

SHGC-74495 (e-PCR)
- UniSTS:33462

LCK_1394 (e-PCR)
- UniSTS:277447

LCK_v458 (e-PCR)
- UniSTS:277447

RH69098 (e-PCR)
- UniSTS:53719

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATPase binding	IPI Inferred from Physical Interaction more info	PubMed
enables CD4 receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables CD8 receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables SH2 domain binding	IPI Inferred from Physical Interaction more info	PubMed
enables T cell receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables histone H2AXY142 kinase activity	IEA Inferred from Electronic Annotation more info
enables histone H3Y41 kinase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables non-membrane spanning protein tyrosine kinase activity	IBA Inferred from Biological aspect of Ancestor more info
enables non-membrane spanning protein tyrosine kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables phosphatidylinositol 3-kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables phospholipase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables phospholipase binding	IPI Inferred from Physical Interaction more info	PubMed
enables phosphotyrosine residue binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein phosphatase binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein serine/threonine phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine kinase activity	EXP Inferred from Experiment more info	PubMed
enables protein tyrosine kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine kinase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein tyrosine kinase activity	TAS Traceable Author Statement more info
enables signaling receptor binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in B cell receptor signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in CD27 signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in Fc-gamma receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in T cell activation	IDA Inferred from Direct Assay more info	PubMed
involved_in T cell costimulation	TAS Traceable Author Statement more info
involved_in T cell differentiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in T cell differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in T cell receptor signaling pathway	IDA Inferred from Direct Assay more info	PubMed
involved_in T cell receptor signaling pathway	TAS Traceable Author Statement more info
involved_in cell surface receptor protein tyrosine kinase signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in hemopoiesis	NAS Non-traceable Author Statement more info	PubMed
involved_in intracellular signal transduction	IDA Inferred from Direct Assay more info	PubMed
involved_in intracellular zinc ion homeostasis	IEP Inferred from Expression Pattern more info	PubMed
involved_in leukocyte migration	TAS Traceable Author Statement more info
involved_in peptidyl-tyrosine autophosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in peptidyl-tyrosine phosphorylation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in platelet activation	TAS Traceable Author Statement more info
involved_in positive regulation of T cell activation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of T cell receptor signaling pathway	NAS Non-traceable Author Statement more info	PubMed
involved_in positive regulation of cysteine-type endopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of heterotypic cell-cell adhesion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of intrinsic apoptotic signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of leukocyte cell-cell adhesion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein phosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of lymphocyte activation	NAS Non-traceable Author Statement more info	PubMed
involved_in release of sequestered calcium ion into cytosol	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to xenobiotic stimulus	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	TAS Traceable Author Statement more info
located_in extracellular exosome	HDA more info	PubMed
located_in immunological synapse	IDA Inferred from Direct Assay more info	PubMed
located_in membrane raft	IDA Inferred from Direct Assay more info	PubMed
located_in pericentriolar material	IDA Inferred from Direct Assay more info	PubMed
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
is_active_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: tyrosine-protein kinase Lck

Names: T-lymphocyte specific protein tyrosine kinase p56lck; leukocyte C-terminal Src kinase; lymphocyte cell-specific protein-tyrosine kinase; p56(LSTRA) protein-tyrosine kinase; proto-oncogene tyrosine-protein kinase LCK; t cell-specific protein-tyrosine kinase

NP_001036236.1

EC 2.7.10.2

NP_001317397.1

EC 2.7.10.2

NP_005347.3

EC 2.7.10.2

XP_011539755.1

EC 2.7.10.2

XP_024302814.1

EC 2.7.10.2

XP_024302815.1

EC 2.7.10.2

XP_047276355.1

EC 2.7.10.2

XP_047276359.1

EC 2.7.10.2

XP_054192534.1

EC 2.7.10.2

XP_054192535.1

EC 2.7.10.2

XP_054192536.1

EC 2.7.10.2

XP_054192537.1

EC 2.7.10.2

XP_054192538.1

EC 2.7.10.2

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_023387.1 RefSeqGene

Range

5027..39927

Download

GenBank, FASTA, Sequence Viewer (Graphics), LRG_153

mRNA and Protein(s)

NM_001042771.3 → NP_001036236.1 tyrosine-protein kinase Lck isoform a

See identical proteins and their annotated locations for NP_001036236.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) is transcribed from the proximal type I promoter. Variants 1 and 2 encode the same isoform (a).

Source sequence(s)

AA747421, AF228313, DB122062, DB129997

Consensus CDS

CCDS359.1

UniProtKB/Swiss-Prot

D3DPP8, P06239, P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8

UniProtKB/TrEMBL

A0A0S2Z3Y8, B4DZS7

Related

ENSP00000328213.4, ENST00000333070.4

Conserved Domains (3) summary

cd10362
Location:123 → 223

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:65 → 118

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cd05067
Location:237 → 500

PTKc_Lck_Blk; Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk
NM_001330468.2 → NP_001317397.1 tyrosine-protein kinase Lck isoform b

Status: REVIEWED

Description

Transcript Variant: This variant (3) is transcribed from the distal type II promoter, contains a distinct 5' UTR, and lacks an alternate in-frame exon compared to variant 1. The resulting isoform (b) has the same N- and C-termini but is shorter compared to isoform a.

Source sequence(s)

AL109945, AL121991

Consensus CDS

CCDS90908.1

UniProtKB/TrEMBL

A0A0S2Z3Y4, B4DZS7, E9PJ92

Related

ENSP00000435605.2, ENST00000495610.7

Conserved Domains (3) summary

cd10362
Location:123 → 215

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:65 → 118

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cl21453
Location:212 → 449

PKc_like; Protein Kinases, catalytic domain
NM_005356.5 → NP_005347.3 tyrosine-protein kinase Lck isoform a

See identical proteins and their annotated locations for NP_005347.3

Status: REVIEWED

Description

Transcript Variant: This variant (2) is transcribed from the distal type II promoter and contains a distinct 5' UTR compared to variant 1. Variants 1 and 2 encode the same isoform (a).

Source sequence(s)

AA747421, AF228313, DA007906, X13529

Consensus CDS

CCDS359.1

UniProtKB/Swiss-Prot

D3DPP8, P06239, P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8

UniProtKB/TrEMBL

A0A0S2Z3Y8, B4DZS7

Related

ENSP00000337825.5, ENST00000336890.10

Conserved Domains (3) summary

cd10362
Location:123 → 223

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:65 → 118

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cd05067
Location:237 → 500

PTKc_Lck_Blk; Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000001.11 Reference GRCh38.p14 Primary Assembly

Range

32251265..32286165

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_024447046.1 → XP_024302814.1 tyrosine-protein kinase Lck isoform X1

UniProtKB/TrEMBL

B4DZS7, E9PKQ8

Related

ENSP00000431517.2, ENST00000482949.6

Conserved Domains (3) summary

cd10362
Location:181 → 281

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:123 → 176

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cd05067
Location:295 → 558

PTKc_Lck_Blk; Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk
XM_011541453.3 → XP_011539755.1 tyrosine-protein kinase Lck isoform X3

See identical proteins and their annotated locations for XP_011539755.1

UniProtKB/TrEMBL

B4DZS7, Q573B4

Conserved Domains (3) summary

cd10362
Location:181 → 273

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:123 → 176

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cl21453
Location:270 → 507

PKc_like; Protein Kinases, catalytic domain
XM_047420399.1 → XP_047276355.1 tyrosine-protein kinase Lck isoform X2
XM_024447047.2 → XP_024302815.1 tyrosine-protein kinase Lck isoform X1

UniProtKB/TrEMBL

B4DZS7, E9PKQ8

Conserved Domains (3) summary

cd10362
Location:181 → 281

SH2_Src_Lck; Src homology 2 (SH2) domain in lymphocyte cell kinase (Lck)

cd12005
Location:123 → 176

SH3_Lck; Src homology 3 domain of Lck Protein Tyrosine Kinase

cd05067
Location:295 → 558

PTKc_Lck_Blk; Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk
XM_047420403.1 → XP_047276359.1 tyrosine-protein kinase Lck isoform X4

UniProtKB/TrEMBL

A0A0S2Z3Y4, E9PJ92

Alternate T2T-CHM13v2.0

Genomic

NC_060925.1 Alternate T2T-CHM13v2.0

Range

32109169..32144081

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_054336559.1 → XP_054192534.1 tyrosine-protein kinase Lck isoform X1

UniProtKB/TrEMBL

E9PKQ8
XM_054336562.1 → XP_054192537.1 tyrosine-protein kinase Lck isoform X3

UniProtKB/TrEMBL

Q573B4
XM_054336561.1 → XP_054192536.1 tyrosine-protein kinase Lck isoform X2
XM_054336560.1 → XP_054192535.1 tyrosine-protein kinase Lck isoform X1

UniProtKB/TrEMBL

E9PKQ8
XM_054336563.1 → XP_054192538.1 tyrosine-protein kinase Lck isoform X4

UniProtKB/TrEMBL

A0A0S2Z3Y4, E9PJ92