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UniProtKB - P06239 (LCK_HUMAN)

Protein

Tyrosine-protein kinase Lck

Gene

LCK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei273ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei364Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi251 – 259ATPPROSITE-ProRule annotation9

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Transferase, Tyrosine-protein kinase
Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

More...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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P06239

SIGNOR Signaling Network Open Resource

More...SIGNORi		P06239

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LCK
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000182866.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:6524 LCK

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		153390 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P06239

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
See also OMIM:615758
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_071291341L → P in IMD22. 1 PublicationCorresponds to variant dbSNP:rs587777335EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59S → E: Allows interaction with SQSTM1. 1 Publication1
Mutagenesisi154R → K: No effect on interaction with SQSTM1. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		3932

MalaCards human disease database

More...MalaCardsi		LCK
MIMi615758 phenotype

Open Targets

More...OpenTargetsi		ENSG00000182866

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		280142 Severe combined immunodeficiency due to LCK deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30307

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...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

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		LCK

Domain mapping of disease mutations (DMDM)

More...DMDMi		125474

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000881242 – 509Tyrosine-protein kinase LckAdd BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycineBy similarity1
Lipidationi3S-palmitoyl cysteineBy similarity1
Lipidationi5S-palmitoyl cysteineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei102PhosphoserineCombined sources1
Modified residuei159PhosphothreonineCombined sources1
Modified residuei162PhosphoserineCombined sources1
Modified residuei192PhosphotyrosineBy similarity1
Modified residuei194PhosphoserineCombined sources1
Modified residuei394Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei505Phosphotyrosine; by CSKCombined sources3 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P06239

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06239

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P06239

PeptideAtlas

More...PeptideAtlasi		P06239

PRoteomics IDEntifications database

More...PRIDEi		P06239

ProteomicsDB human proteome resource

More...ProteomicsDBi		51874
51875 [P06239-2]
51876 [P06239-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06239

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P06239

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P06239

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed specifically in lymphoid cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000182866 Expressed in 144 organ(s), highest expression level in thymus

CleanEx database of gene expression profiles

More...CleanExi		HS_LCK

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P06239 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P06239 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB003816
HPA003494

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110124, 89 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P06239

Database of interacting proteins

More...DIPi		DIP-553N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P06239

Protein interaction database and analysis system

More...IntActi		P06239, 87 interactors

Molecular INTeraction database

More...MINTi		P06239

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000337825

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06239

<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

1509
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P06239

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06239

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06239

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 121SH3PROSITE-ProRule annotationAdd BLAST61
Domaini127 – 224SH2PROSITE-ProRule annotationAdd BLAST98
Domaini245 – 498Protein kinasePROSITE-ProRule annotationAdd BLAST254

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 72Interactions with CD4 and CD8By similarityAdd BLAST71
Regioni154 – 242Interaction with PTPRH1 PublicationAdd BLAST89

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<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

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

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000161163

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG008761

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06239

KEGG Orthology (KO)

More...KOi		K05856

Identification of Orthologs from Complete Genome Data

More...OMAi		EQNGEWW

Database of Orthologous Groups

More...OrthoDBi		EOG091G0D46

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06239

TreeFam database of animal gene trees

More...TreeFami		TF351634

Family and domain databases

Conserved Domains Database

More...CDDi		cd10362 SH2_Src_Lck, 1 hit
cd12005 SH3_Lck, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

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

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

« Hide
        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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i44BFF0D43FFB420D
GO
Isoform Short (identifier: P06239-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:363
Mass (Da):40,866
Checksum:iAC4AF1AB58D32577
GO
Isoform 3 (identifier: P06239-3) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:539
Mass (Da):61,190
Checksum:iD1024F47D18B289C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q573B4Q573B4_HUMAN
Tyrosine-protein kinase
LCK
516Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PJ92E9PJ92_HUMAN
Tyrosine-protein kinase
LCK
319Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PAP0E9PAP0_HUMAN
Tyrosine-protein kinase Lck
LCK
285Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8W6B9F8W6B9_HUMAN
Tyrosine-protein kinase Lck
LCK
137Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PKQ8E9PKQ8_HUMAN
Tyrosine-protein kinase Lck
LCK
200Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PQ10E9PQ10_HUMAN
Tyrosine-protein kinase Lck
LCK
149Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PI33E9PI33_HUMAN
Tyrosine-protein kinase Lck
LCK
167Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29P → R in AAA59502 (PubMed:3265417).Curated1
Sequence conflicti35T → R in AAA59502 (PubMed:3265417).Curated1
Sequence conflicti87Q → P in CAA31884 (PubMed:3265417).Curated1
Sequence conflicti87Q → P in AAA59502 (PubMed:3265417).Curated1
Sequence conflicti206 – 211VRHYTN → ASAITPI in CAA28691 (PubMed:3493153).Curated6
Sequence conflicti254G → A in AAA59502 (PubMed:3265417).Curated1
Sequence conflicti258 – 267EVWMGYYNGH → RCGWGTTTGT in CAA28691 (PubMed:3493153).Curated10
Sequence conflicti282 – 286PDAFL → AGRLP in CAA28691 (PubMed:3493153).Curated5
Sequence conflicti375T → A in CAA28165 (PubMed:3489486).Curated1
Sequence conflicti472L → H in CAA29667 (PubMed:2835736).Curated1
Sequence conflicti504 – 509QYQPQP → STA in CAA28691 (PubMed:3493153).Curated6

<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

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01346328V → L Found in leukemia. 1 Publication1
Natural variantiVAR_051697201G → S. Corresponds to variant dbSNP:rs11567841EnsemblClinVar.1
Natural variantiVAR_013464232P → PQKP in leukemia. 1
Natural variantiVAR_071291341L → P in IMD22. 1 PublicationCorresponds to variant dbSNP:rs587777335EnsemblClinVar.1
Natural variantiVAR_013465353A → V Found in leukemia. 1 Publication1
Natural variantiVAR_013466447P → L Found in leukemia. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_016049321N → NDTLLDSQLEEKGLGASPWG NLGQQLLLLPT in isoform 3. 1 Publication1
Alternative sequenceiVSP_005000348 – 363IAEGM…NYIHR → VRRLGRGAGQGNRPVT in isoform Short. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_005001364 – 509Missing in isoform Short. 1 PublicationAdd BLAST146

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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]

Protein sequence database of the Protein Information Resource

More...PIRi		JQ0152 OKHULK

NCBI Reference Sequences

More...RefSeqi		NP_001036236.1, NM_001042771.2 [P06239-1]
NP_005347.3, NM_005356.4 [P06239-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.470627

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000333070; ENSP00000328213; ENSG00000182866 [P06239-3]
ENST00000336890; ENSP00000337825; ENSG00000182866 [P06239-1]
ENST00000619559; ENSP00000477713; ENSG00000182866 [P06239-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3932

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3932

UCSC genome browser

More...UCSCi		uc001bux.3 human [P06239-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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
CCDSiCCDS359.1 [P06239-1]
PIRiJQ0152 OKHULK
RefSeqiNP_001036236.1, NM_001042771.2 [P06239-1]
NP_005347.3, NM_005356.4 [P06239-1]
UniGeneiHs.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 entryMethodResolution (Å)ChainPositionsPDBsum
1BHFX-ray1.80A119-226[»]
1BHHX-ray1.90A119-226[»]
B124-226[»]
1CWDX-ray2.25L127-222[»]
1CWEX-ray2.30A/C127-222[»]
1FBZX-ray2.40A/B123-226[»]
1H92NMR-A59-120[»]
1IJRX-ray2.20A124-226[»]
1KIKNMR-A64-120[»]
1LCJX-ray1.80A119-226[»]
1LCKX-ray2.50A53-226[»]
B502-509[»]
1LKKX-ray1.00A122-226[»]
1LKLX-ray1.80A123-226[»]
1Q68NMR-B7-35[»]
1Q69NMR-B7-35[»]
1QPCX-ray1.60A231-509[»]
1QPDX-ray2.00A231-509[»]
1QPEX-ray2.00A231-509[»]
1QPJX-ray2.20A231-509[»]
1X27X-ray2.70A/B/C/D/E/F64-226[»]
2IIMX-ray1.00A59-119[»]
2OF2X-ray2.00A231-501[»]
2OF4X-ray2.70A231-501[»]
2OFUX-ray2.00A229-501[»]
2OFVX-ray2.00A/B232-498[»]
2OG8X-ray2.30A/B237-499[»]
2PL0X-ray2.80A225-509[»]
2ZM1X-ray2.10A225-509[»]
2ZM4X-ray2.70A225-509[»]
2ZYBX-ray2.55A225-509[»]
3AC1X-ray1.99A225-509[»]
3AC2X-ray2.10A225-509[»]
3AC3X-ray2.55A225-509[»]
3AC4X-ray2.70A225-509[»]
3AC5X-ray2.50A225-509[»]
3AC8X-ray2.30A225-509[»]
3ACJX-ray2.20A225-509[»]
3ACKX-ray2.60A225-509[»]
3AD4X-ray2.20A225-509[»]
3AD5X-ray2.00A225-509[»]
3AD6X-ray2.15A225-509[»]
3B2WX-ray2.30A226-502[»]
3BRHX-ray2.20C/D391-397[»]
3BYMX-ray2.00A230-501[»]
3BYOX-ray2.00A231-501[»]
3BYSX-ray2.20A225-501[»]
3BYUX-ray2.30A225-501[»]
3KMMX-ray2.80A229-509[»]
3KXZX-ray2.37A225-509[»]
3LCKX-ray1.70A231-501[»]
3MPMX-ray1.95A237-501[»]
4C3FX-ray1.72A237-501[»]
4D8KX-ray2.36A53-226[»]
5MTMX-ray2.40A118-231[»]
5MTNX-ray2.85A118-231[»]
ProteinModelPortaliP06239
SMRiP06239
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110124, 89 interactors
CORUMiP06239
DIPiDIP-553N
ELMiP06239
IntActiP06239, 87 interactors
MINTiP06239
STRINGi9606.ENSP00000337825

Chemistry databases

BindingDBiP06239
ChEMBLiCHEMBL258
DrugBankiDB06925 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
GuidetoPHARMACOLOGYi2053

PTM databases

iPTMnetiP06239
PhosphoSitePlusiP06239
SwissPalmiP06239

Polymorphism and mutation databases

BioMutaiLCK
DMDMi125474

Proteomic databases

EPDiP06239
MaxQBiP06239
PaxDbiP06239
PeptideAtlasiP06239
PRIDEiP06239
ProteomicsDBi51874
51875 [P06239-2]
51876 [P06239-3]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3932
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333070; ENSP00000328213; ENSG00000182866 [P06239-3]
ENST00000336890; ENSP00000337825; ENSG00000182866 [P06239-1]
ENST00000619559; ENSP00000477713; ENSG00000182866 [P06239-1]
GeneIDi3932
KEGGihsa:3932
UCSCiuc001bux.3 human [P06239-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3932
DisGeNETi3932
EuPathDBiHostDB:ENSG00000182866.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		LCK

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0019954
HGNCiHGNC:6524 LCK
HPAiCAB003816
HPA003494
MalaCardsiLCK
MIMi153390 gene
615758 phenotype
neXtProtiNX_P06239
OpenTargetsiENSG00000182866
Orphaneti280142 Severe combined immunodeficiency due to LCK deficiency
PharmGKBiPA30307

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000161163
HOVERGENiHBG008761
InParanoidiP06239
KOiK05856
OMAiEQNGEWW
OrthoDBiEOG091G0D46
PhylomeDBiP06239
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-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
SignaLinkiP06239
SIGNORiP06239

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		LCK human
EvolutionaryTraceiP06239

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Lck

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		3932

Protein Ontology

More...PROi		PR:P06239

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000182866 Expressed in 144 organ(s), highest expression level in thymus
CleanExiHS_LCK
ExpressionAtlasiP06239 baseline and differential
GenevisibleiP06239 HS

Family and domain databases

CDDicd10362 SH2_Src_Lck, 1 hit
cd12005 SH3_Lck, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF07714 Pkinase_Tyr, 1 hit
PF00017 SH2, 1 hit
PF00018 SH3_1, 1 hit
PRINTSiPR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE
SMARTiView protein in SMART
SM00252 SH2, 1 hit
SM00326 SH3, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLCK_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06239
Secondary accession number(s): D3DPP8
, P07100, Q12850, Q13152, Q5TDH8, Q5TDH9, Q7RTZ3, Q96DW4, Q9NYT8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 247 of the entry and version 6 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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