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Protein

Tyrosine-protein kinase Lyn

Gene

LYN

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 transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation.19 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

Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Inhibited by Dasatinib, PP2, and SU6656.2 Publications

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 sitei275ATPPROSITE-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 sitei367Proton 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 bindingi253 – 261ATPPROSITE-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

GO - Biological processi

<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 processAdaptive immunity, Host-virus interaction, Immunity, Inflammatory response, Innate immunity
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.2 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114604 GPVI-mediated activation cascade
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1433559 Regulation of KIT signaling
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-210990 PECAM1 interactions
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-389356 CD28 co-stimulation
R-HSA-389513 CTLA4 inhibitory signaling
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-5621480 Dectin-2 family
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5690714 CD22 mediated BCR regulation
R-HSA-69231 Cyclin D associated events in G1
R-HSA-75892 Platelet Adhesion to exposed collagen
R-HSA-9006335 Signaling by Erythropoietin
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-912631 Regulation of signaling by CBL
R-HSA-982772 Growth hormone receptor signaling
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers

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

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SignaLinki
P07948

SIGNOR Signaling Network Open Resource

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SIGNORi
P07948

<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 Lyn (EC:2.7.10.2)
Alternative name(s):
Lck/Yes-related novel protein tyrosine kinase
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
<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:LYN
Synonyms:JTK8
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000254087.7

Human Gene Nomenclature Database

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HGNCi
HGNC:6735 LYN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
165120 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P07948

<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, Golgi apparatus, Membrane, Nucleus

<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

Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.

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>Mutagenesisi2G → A: Loss of localization to the cell membrane; when associated with A-3. 1 Publication1
Mutagenesisi3C → A: Loss of localization to the cell membrane; when associated with A-2. 1 Publication1
Mutagenesisi275K → A: Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3. 4 Publications1
Mutagenesisi275K → L or R: Loss of kinase activity. 4 Publications1
Mutagenesisi346D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. 1 Publication1
Mutagenesisi353E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. 1 Publication1
Mutagenesisi397Y → F: Strongly reduced kinase activity. 1 Publication1
Mutagenesisi498D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. 1 Publication1
Mutagenesisi499D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. 1 Publication1
Mutagenesisi508Y → F: Abolishes autoinhibition and thereby increases kinase activity. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
4067

Open Targets

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OpenTargetsi
ENSG00000254087

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30498

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3905

Drug and drug target database

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DrugBanki
DB06616 Bosutinib
DB09079 Nintedanib
DB08901 Ponatinib

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2060

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LYN

Domain mapping of disease mutations (DMDM)

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DMDMi
125480

<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 methionineiRemoved1 Publication
<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_00000881292 – 512Tyrosine-protein kinase LynAdd BLAST511

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 glycine1 Publication1 Publication1
Lipidationi3S-palmitoyl cysteine1 Publication1
<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 residuei11PhosphoserineCombined sources1
Modified residuei13PhosphoserineCombined sources1
Modified residuei193Phosphotyrosine1 Publication1
Modified residuei228PhosphoserineCombined sources1
Modified residuei306PhosphotyrosineCombined sources1
Modified residuei316PhosphotyrosineCombined sources1
Modified residuei397Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei460Phosphotyrosine1 Publication1
Modified residuei473PhosphotyrosineCombined sources1
Modified residuei508Phosphotyrosine; by autocatalysis, CSK and MATKCombined 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

Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent.2 Publications
Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.7 Publications

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P07948

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P07948

MaxQB - The MaxQuant DataBase

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MaxQBi
P07948

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

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PaxDbi
P07948

PeptideAtlas

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PeptideAtlasi
P07948

PRoteomics IDEntifications database

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PRIDEi
P07948

ProteomicsDB human proteome resource

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ProteomicsDBi
52045
52046 [P07948-2]

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
P07948

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P07948

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

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PhosphoSitePlusi
P07948

SwissPalm database of S-palmitoylation events

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SwissPalmi
P07948

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P07948

<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

Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000254087 Expressed in 204 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_LYN

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P07948 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P07948 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004492
HPA001231

<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

Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36. Interacts with LYN (By similarity).By similarity26 Publications
(Microbial infection) Interacts with Epstein-Barr virus LMP2A.1 Publication
(Microbial infection) Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip).2 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110245, 199 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P07948

Database of interacting proteins

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DIPi
DIP-1056N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P07948

Protein interaction database and analysis system

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IntActi
P07948, 72 interactors

Molecular INTeraction database

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MINTi
P07948

STRING: functional protein association networks

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STRINGi
9606.ENSP00000428924

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P07948

<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

1512
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
5XY1X-ray2.70A239-512[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P07948

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

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SMRi
P07948

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P07948

<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>Domaini63 – 123SH3PROSITE-ProRule annotationAdd BLAST61
Domaini129 – 226SH2PROSITE-ProRule annotationAdd BLAST98
Domaini247 – 501Protein kinasePROSITE-ProRule annotationAdd BLAST255

<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 protein kinase domain plays an important role in its localization in the cell membrane.1 Publication

<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

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eggNOGi
KOG0197 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158011

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233858

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG008761

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07948

KEGG Orthology (KO)

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KOi
K05854

Identification of Orthologs from Complete Genome Data

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OMAi
RFQAKDP

Database of Orthologous Groups

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OrthoDBi
539311at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P07948

TreeFam database of animal gene trees

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TreeFami
TF351634

Family and domain databases

Conserved Domains Database

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CDDi
cd10364 SH2_Src_Lyn, 1 hit
cd12004 SH3_Lyn, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR035852 Lyn_SH2
IPR035748 Lyn_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

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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

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PRINTSi
PR00401 SH2DOMAIN
PR00452 SH3DOMAIN
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50044 SSF50044, 1 hit
SSF55550 SSF55550, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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 (2+)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 2 <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 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P07948-1) [UniParc]FASTAAdd to basket
Also known as: LYN A, p56lyn

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
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL
60 70 80 90 100
LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW
110 120 130 140 150
KAKSLLTKKE GFIPSNYVAK LNTLETEEWF FKDITRKDAE RQLLAPGNSA
160 170 180 190 200
GAFLIRESET LKGSFSLSVR DFDPVHGDVI KHYKIRSLDN GGYYISPRIT
210 220 230 240 250
FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV
260 270 280 290 300
KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
310 320 330 340 350
KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ
360 370 380 390 400
IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR
410 420 430 440 450
EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA
460 470 480 490 500
DVMTALSQGY RMPRVENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF
510
YTATEGQYQQ QP
Length:512
Mass (Da):58,574
Last modified:January 23, 2007 - v3
<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:i408D3D461204E378
GO
Isoform 2 (identifier: P07948-2) [UniParc]FASTAAdd to basket
Also known as: LYN B, p53lyn

The sequence of this isoform differs from the canonical sequence as follows:
     23-43: Missing.

Show »
Length:491
Mass (Da):56,033
Checksum:iD74E4074D4B0C92A
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RJ37E5RJ37_HUMAN
Tyrosine-protein kinase Lyn
LYN
150Annotation 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>

Natural variant

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_041737385D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. 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_00500223 – 43Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M16038 mRNA Translation: AAA59540.1
M79321 mRNA Translation: AAB50019.1
BC075001 mRNA Translation: AAH75001.1
BC075002 mRNA Translation: AAH75002.1
BC126456 mRNA Translation: AAI26457.1
BC126458 mRNA Translation: AAI26459.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS47859.1 [P07948-2]
CCDS6162.1 [P07948-1]

Protein sequence database of the Protein Information Resource

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PIRi
A26719 TVHULY

NCBI Reference Sequences

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RefSeqi
NP_001104567.1, NM_001111097.2 [P07948-2]
NP_002341.1, NM_002350.3 [P07948-1]
XP_016868905.1, XM_017013416.1 [P07948-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.491767
Hs.545418

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000519728; ENSP00000428924; ENSG00000254087 [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087 [P07948-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
4067

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4067

UCSC genome browser

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UCSCi
uc003xsk.5 human [P07948-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16038 mRNA Translation: AAA59540.1
M79321 mRNA Translation: AAB50019.1
BC075001 mRNA Translation: AAH75001.1
BC075002 mRNA Translation: AAH75002.1
BC126456 mRNA Translation: AAI26457.1
BC126458 mRNA Translation: AAI26459.1
CCDSiCCDS47859.1 [P07948-2]
CCDS6162.1 [P07948-1]
PIRiA26719 TVHULY
RefSeqiNP_001104567.1, NM_001111097.2 [P07948-2]
NP_002341.1, NM_002350.3 [P07948-1]
XP_016868905.1, XM_017013416.1 [P07948-2]
UniGeneiHs.491767
Hs.545418

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
5XY1X-ray2.70A239-512[»]
ProteinModelPortaliP07948
SMRiP07948
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110245, 199 interactors
CORUMiP07948
DIPiDIP-1056N
ELMiP07948
IntActiP07948, 72 interactors
MINTiP07948
STRINGi9606.ENSP00000428924

Chemistry databases

BindingDBiP07948
ChEMBLiCHEMBL3905
DrugBankiDB06616 Bosutinib
DB09079 Nintedanib
DB08901 Ponatinib
GuidetoPHARMACOLOGYi2060

PTM databases

iPTMnetiP07948
PhosphoSitePlusiP07948
SwissPalmiP07948

Polymorphism and mutation databases

BioMutaiLYN
DMDMi125480

2D gel databases

REPRODUCTION-2DPAGEiP07948

Proteomic databases

EPDiP07948
jPOSTiP07948
MaxQBiP07948
PaxDbiP07948
PeptideAtlasiP07948
PRIDEiP07948
ProteomicsDBi52045
52046 [P07948-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4067
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000519728; ENSP00000428924; ENSG00000254087 [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087 [P07948-2]
GeneIDi4067
KEGGihsa:4067
UCSCiuc003xsk.5 human [P07948-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4067
DisGeNETi4067
EuPathDBiHostDB:ENSG00000254087.7

GeneCards: human genes, protein and diseases

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GeneCardsi
LYN
HGNCiHGNC:6735 LYN
HPAiCAB004492
HPA001231
MIMi165120 gene
neXtProtiNX_P07948
OpenTargetsiENSG00000254087
PharmGKBiPA30498

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158011
HOGENOMiHOG000233858
HOVERGENiHBG008761
InParanoidiP07948
KOiK05854
OMAiRFQAKDP
OrthoDBi539311at2759
PhylomeDBiP07948
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1433559 Regulation of KIT signaling
R-HSA-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-210990 PECAM1 interactions
R-HSA-2454202 Fc epsilon receptor (FCERI) signaling
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-2871809 FCERI mediated Ca+2 mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-389356 CD28 co-stimulation
R-HSA-389513 CTLA4 inhibitory signaling
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-5621480 Dectin-2 family
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5690714 CD22 mediated BCR regulation
R-HSA-69231 Cyclin D associated events in G1
R-HSA-75892 Platelet Adhesion to exposed collagen
R-HSA-9006335 Signaling by Erythropoietin
R-HSA-9027276 Erythropoietin activates Phosphoinositide-3-kinase (PI3K)
R-HSA-9027277 Erythropoietin activates Phospholipase C gamma (PLCG)
R-HSA-9027283 Erythropoietin activates STAT5
R-HSA-9027284 Erythropoietin activates RAS
R-HSA-912631 Regulation of signaling by CBL
R-HSA-982772 Growth hormone receptor signaling
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkiP07948
SIGNORiP07948

Miscellaneous databases

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

More...
ChiTaRSi
LYN human
EvolutionaryTraceiP07948

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
LYN

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

More...
GenomeRNAii
4067
PMAP-CutDBiP07948

Protein Ontology

More...
PROi
PR:P07948

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000254087 Expressed in 204 organ(s), highest expression level in blood
CleanExiHS_LYN
ExpressionAtlasiP07948 baseline and differential
GenevisibleiP07948 HS

Family and domain databases

CDDicd10364 SH2_Src_Lyn, 1 hit
cd12004 SH3_Lyn, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR035852 Lyn_SH2
IPR035748 Lyn_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 nameiLYN_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: P07948
Secondary accession number(s): A0AVQ5
<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: August 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 229 of the entry and version 3 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 and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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