Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P06241 (FYN_HUMAN)

Entry version 250 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tyrosine-protein kinase Fyn

Gene

FYN

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 a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).By similarity20 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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei299ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei390Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi277 – 285ATPPROSITE-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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionDevelopmental protein, Kinase, Transferase, Tyrosine-protein kinase
Biological processAdaptive immunity, Host-virus interaction, Immunity
LigandATP-binding, Manganese, Metal-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-1227986 Signaling by ERBB2
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-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-210990 PECAM1 interactions
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-2424491 DAP12 signaling
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-373753 Nephrin family interactions
R-HSA-375165 NCAM signaling for neurite out-growth
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-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928664 Ephrin signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-HSA-399956 CRMPs in Sema3A signaling
R-HSA-418885 DCC mediated attractive signaling [P06241-1]
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5621480 Dectin-2 family
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-75892 Platelet Adhesion to exposed collagen
R-HSA-8866376 Reelin signalling pathway
R-HSA-9032500 Activated NTRK2 signals through FYN [P06241-1]
R-HSA-9032759 NTRK2 activates RAC1 [P06241-1]
R-HSA-912631 Regulation of signaling by CBL
R-HSA-9607240 FLT3 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

More...SignaLinki		P06241

SIGNOR Signaling Network Open Resource

More...SIGNORi		P06241

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P06241 Predicted

<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 Fyn (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene Syn
Proto-oncogene c-Fyn
Src-like kinase
Short name:
SLK
p59-Fyn
<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:FYN
<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 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000010810.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:4037 FYN

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		137025 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P06241

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, 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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		2534

Open Targets

More...OpenTargetsi		ENSG00000010810

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28454

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P06241 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1841

Drug and drug target database

More...DrugBanki		DB01254 Dasatinib
DB12010 Fostamatinib
DB02078 Triglyme

DrugCentral

More...DrugCentrali		P06241

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2026

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FYN

Domain mapping of disease mutations (DMDM)

More...DMDMi		125370

<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_00000880992 – 537Tyrosine-protein kinase FynAdd BLAST536

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
Lipidationi3S-palmitoyl cysteineBy similarity1
Lipidationi6S-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 residuei12Phosphothreonine; by PKC1 Publication1
Modified residuei21PhosphoserineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei185PhosphotyrosineBy similarity1
Modified residuei420Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei531Phosphotyrosine; by CSKCombined sources1 Publication1

<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 at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus (PubMed:15537652). Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (PubMed:22080863). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).By similarity5 Publications
Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1792

Encyclopedia of Proteome Dynamics

More...EPDi		P06241

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P06241

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P06241

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06241

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

More...PaxDbi		P06241

PeptideAtlas

More...PeptideAtlasi		P06241

PRoteomics IDEntifications database

More...PRIDEi		P06241

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51877 [P06241-1]
51878 [P06241-2]
51879 [P06241-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06241

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

More...PhosphoSitePlusi		P06241

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P06241

<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

Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000010810 Expressed in 232 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P06241 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P06241 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB005034
CAB018387
HPA023887
HPA063770

<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 (via its SH3 domain) with PIK3R1 and PRMT8.

Interacts with FYB1, PAG1, and SH2D1A.

Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity.

Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity).

Interacts with TOM1L1 (phosphorylated form).

Interacts with KDR (tyrosine phosphorylated).

Interacts (via SH3 domain) with KLHL2 (via N-terminus) (By similarity).

Interacts with SH2D1A and SLAMF1.

Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates its activity.

Interacts with FASLG.

Interacts with RUNX3.

Interacts with KIT.

Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion.

Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation.

Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway.

Interacts with UNC119.

Interacts (via SH2 domain) with PTPRH (phosphorylated form) (By similarity).

Interacts with PTPRO (phosphorylated form) (By similarity).

Interacts with PTPRB (phosphorylated form) (By similarity).

Interacts with FYB2 (PubMed:27335501).

Interacts with DSCAM (By similarity).

Interacts with SKAP1 and FYB1; this interaction promotes the phosphorylation of CLNK (By similarity).

By similarity14 Publications

(Microbial infection) Interacts (via its SH3 domain) with hepatitis E virus/HEV protein ORF3.

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

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108810, 210 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P06241

Database of interacting proteins

More...DIPi		DIP-33876N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P06241

Protein interaction database and analysis system

More...IntActi		P06241, 311 interactors

Molecular INTeraction database

More...MINTi		P06241

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000346671

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P06241

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P06241 protein

<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

1537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P06241

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06241

<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>Domaini82 – 143SH3PROSITE-ProRule annotationAdd BLAST62
Domaini149 – 246SH2PROSITE-ProRule annotationAdd BLAST98
Domaini271 – 524Protein kinasePROSITE-ProRule annotationAdd BLAST254

<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		ENSGT00940000155462

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06241

KEGG Orthology (KO)

More...KOi		K05703

Identification of Orthologs from Complete Genome Data

More...OMAi		QCWHKEP

Database of Orthologous Groups

More...OrthoDBi		539311at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P06241

TreeFam database of animal gene trees

More...TreeFami		TF351634

Family and domain databases

Conserved Domains Database

More...CDDi		cd12006 SH3_Fyn_Yrk, 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
IPR035750 Fyn/Yrk_SH3
IPR011009 Kinase-like_dom_sf
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>. The information is filed in different subsections. The current subsections and their content are listed below:<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 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P06241-1) [UniParc]FASTAAdd to basket
Also known as: B

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY 
        60         70         80         90        100
NNFHAAGGQG LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD 
       110        120        130        140        150
LSFHKGEKFQ ILNSSEGDWW EARSLTTGET GYIPSNYVAP VDSIQAEEWY 
       160        170        180        190        200
FGKLGRKDAE RQLLSFGNPR GTFLIRESET TKGAYSLSIR DWDDMKGDHV 
       210        220        230        240        250
KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC RLVVPCHKGM 
       260        270        280        290        300
PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 
       310        320        330        340        350
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL 
       360        370        380        390        400
LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN 
       410        420        430        440        450
GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 
       460        470        480        490        500
SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI 
       510        520        530 
HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL
Length:537
Mass (Da):60,762
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:i4A1E443A4B5A0977
GO
Isoform 2 (identifier: P06241-2) [UniParc]FASTAAdd to basket
Also known as: T

The sequence of this isoform differs from the canonical sequence as follows:
     234-287: RAAGLCCRLV...GNGQFGEVWM → KADGLCFNLT...GQGCFAEVWL

Show »
Length:534
Mass (Da):60,141
Checksum:iFA082D40A24C2802
GO
Isoform 3 (identifier: P06241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     233-287: Missing.

Show »
Length:482
Mass (Da):54,513
Checksum:i055C3965AC5A9135
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 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RFS5E5RFS5_HUMAN
Tyrosine-protein kinase Fyn
FYN
232Annotation 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>
E5RIX5E5RIX5_HUMAN
Tyrosine-protein kinase Fyn
FYN
186Annotation 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>
E5RH71E5RH71_HUMAN
Tyrosine-protein kinase Fyn
FYN
175Annotation 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>
E5RFM0E5RFM0_HUMAN
Tyrosine-protein kinase Fyn
FYN
152Annotation 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>
E5RGT0E5RGT0_HUMAN
Tyrosine-protein kinase Fyn
FYN
153Annotation 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>
E5RI25E5RI25_HUMAN
Tyrosine-protein kinase Fyn
FYN
145Annotation 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>
E5RGM6E5RGM6_HUMAN
Tyrosine-protein kinase Fyn
FYN
139Annotation 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>
E5RFM4E5RFM4_HUMAN
Tyrosine-protein kinase Fyn
FYN
116Annotation 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>
E5RHF7E5RHF7_HUMAN
Tyrosine-protein kinase Fyn
FYN
118Annotation 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>
E5RK23E5RK23_HUMAN
Tyrosine-protein kinase Fyn
FYN
106Annotation 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>
There are more potential isoformsShow all

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 conflicti184A → S in AAA36615 (PubMed:3099169).Curated1
Sequence conflicti437A → R in AAA36615 (PubMed:3099169).Curated1
Sequence conflicti437A → R in AAB33113 (PubMed:7822789).Curated1

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_041704243V → L in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041705410G → R in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_014661445I → F. Corresponds to variant dbSNP:rs1801121Ensembl.1
Natural variantiVAR_041706506D → E1 PublicationCorresponds to variant dbSNP:rs28763975Ensembl.1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_024108233 – 287Missing in isoform 3. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_024110234 – 287RAAGL…GEVWM → KADGLCFNLTVIASSCTPQT SGLAKDAWEVARRSLCLEKK LGQGCFAEVWL in isoform 2. 1 PublicationAdd BLAST54

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
M14676 mRNA Translation: AAA36615.1
M14333 mRNA Translation: AAC08285.1
S74774 mRNA Translation: AAB33113.2
AB451293 mRNA Translation: BAG70107.1
AB451426 mRNA Translation: BAG70240.1
Z97989 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48278.1
CH471051 Genomic DNA Translation: EAW48279.1
CH471051 Genomic DNA Translation: EAW48281.1
CH471051 Genomic DNA Translation: EAW48282.1
CH471051 Genomic DNA Translation: EAW48283.1
BC032496 mRNA Translation: AAH32496.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5094.1 [P06241-1]
CCDS5095.1 [P06241-2]
CCDS5096.1 [P06241-3]

Protein sequence database of the Protein Information Resource

More...PIRi		A24314 TVHUSY

NCBI Reference Sequences

More...RefSeqi		NP_002028.1, NM_002037.5 [P06241-1]
NP_694592.1, NM_153047.3 [P06241-2]
NP_694593.1, NM_153048.3 [P06241-3]
XP_005266947.1, XM_005266890.3
XP_005266949.1, XM_005266892.3 [P06241-3]
XP_016866139.1, XM_017010650.1 [P06241-1]
XP_016866140.1, XM_017010651.1 [P06241-1]
XP_016866141.1, XM_017010652.1 [P06241-1]
XP_016866142.1, XM_017010653.1 [P06241-1]
XP_016866143.1, XM_017010654.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000229471; ENSP00000229471; ENSG00000010810 [P06241-3]
ENST00000354650; ENSP00000346671; ENSG00000010810 [P06241-1]
ENST00000368667; ENSP00000357656; ENSG00000010810 [P06241-1]
ENST00000368678; ENSP00000357667; ENSG00000010810 [P06241-2]
ENST00000368682; ENSP00000357671; ENSG00000010810 [P06241-2]
ENST00000538466; ENSP00000440646; ENSG00000010810 [P06241-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2534

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2534

UCSC genome browser

More...UCSCi		uc003pvh.3 human [P06241-1]

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
M14676 mRNA Translation: AAA36615.1
M14333 mRNA Translation: AAC08285.1
S74774 mRNA Translation: AAB33113.2
AB451293 mRNA Translation: BAG70107.1
AB451426 mRNA Translation: BAG70240.1
Z97989 Genomic DNA No translation available.
CH471051 Genomic DNA Translation: EAW48278.1
CH471051 Genomic DNA Translation: EAW48279.1
CH471051 Genomic DNA Translation: EAW48281.1
CH471051 Genomic DNA Translation: EAW48282.1
CH471051 Genomic DNA Translation: EAW48283.1
BC032496 mRNA Translation: AAH32496.1
CCDSiCCDS5094.1 [P06241-1]
CCDS5095.1 [P06241-2]
CCDS5096.1 [P06241-3]
PIRiA24314 TVHUSY
RefSeqiNP_002028.1, NM_002037.5 [P06241-1]
NP_694592.1, NM_153047.3 [P06241-2]
NP_694593.1, NM_153048.3 [P06241-3]
XP_005266947.1, XM_005266890.3
XP_005266949.1, XM_005266892.3 [P06241-3]
XP_016866139.1, XM_017010650.1 [P06241-1]
XP_016866140.1, XM_017010651.1 [P06241-1]
XP_016866141.1, XM_017010652.1 [P06241-1]
XP_016866142.1, XM_017010653.1 [P06241-1]
XP_016866143.1, XM_017010654.1

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
1A0NNMR-B80-148[»]
1AOTNMR-F143-248[»]
1AOUNMR-F143-248[»]
1AVZX-ray3.00C85-141[»]
1AZGNMR-B82-148[»]
1EFNX-ray2.50A/C86-143[»]
1FYNX-ray2.30A81-142[»]
1G83X-ray2.60A/B82-246[»]
1M27X-ray2.50C84-144[»]
1NYFNMR-A82-148[»]
1NYGNMR-A82-148[»]
1SHFX-ray1.90A/B84-142[»]
1ZBJNMR-A84-142[»]
2DQ7X-ray2.80X261-537[»]
2MQINMR-A148-248[»]
2MRJNMR-A148-248[»]
2MRKNMR-A149-248[»]
B528-537[»]
3H0FX-ray2.61A73-142[»]
3H0HX-ray1.76A73-142[»]
3H0IX-ray2.20A/B73-142[»]
3UA6X-ray1.85A/B81-143[»]
3UA7X-ray1.50A/B/C/D81-143[»]
4D8DX-ray2.52A/C84-141[»]
4EIKX-ray1.60A81-143[»]
4U17X-ray1.99A/B/C148-248[»]
4U1PX-ray1.40A148-248[»]
4ZNXX-ray2.10A/B/C/D84-141[»]
5ZAUNMR-A85-141[»]
6EDFX-ray1.40A83-146[»]
6IPYX-ray1.34A82-144[»]
6IPZX-ray1.58Z82-144[»]
SMRiP06241
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108810, 210 interactors
CORUMiP06241
DIPiDIP-33876N
ELMiP06241
IntActiP06241, 311 interactors
MINTiP06241
STRINGi9606.ENSP00000346671

Chemistry databases

BindingDBiP06241
ChEMBLiCHEMBL1841
DrugBankiDB01254 Dasatinib
DB12010 Fostamatinib
DB02078 Triglyme
DrugCentraliP06241
GuidetoPHARMACOLOGYi2026

Protein family/group databases

MoonDBiP06241 Predicted

PTM databases

iPTMnetiP06241
PhosphoSitePlusiP06241
SwissPalmiP06241

Polymorphism and mutation databases

BioMutaiFYN
DMDMi125370

Proteomic databases

CPTACiCPTAC-1792
EPDiP06241
jPOSTiP06241
MassIVEiP06241
MaxQBiP06241
PaxDbiP06241
PeptideAtlasiP06241
PRIDEiP06241
ProteomicsDBi51877 [P06241-1]
51878 [P06241-2]
51879 [P06241-3]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2534

Genome annotation databases

EnsembliENST00000229471; ENSP00000229471; ENSG00000010810 [P06241-3]
ENST00000354650; ENSP00000346671; ENSG00000010810 [P06241-1]
ENST00000368667; ENSP00000357656; ENSG00000010810 [P06241-1]
ENST00000368678; ENSP00000357667; ENSG00000010810 [P06241-2]
ENST00000368682; ENSP00000357671; ENSG00000010810 [P06241-2]
ENST00000538466; ENSP00000440646; ENSG00000010810 [P06241-2]
GeneIDi2534
KEGGihsa:2534
UCSCiuc003pvh.3 human [P06241-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2534
DisGeNETi2534
EuPathDBiHostDB:ENSG00000010810.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		FYN
HGNCiHGNC:4037 FYN
HPAiCAB005034
CAB018387
HPA023887
HPA063770
MIMi137025 gene
neXtProtiNX_P06241
OpenTargetsiENSG00000010810
PharmGKBiPA28454

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0197 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155462
InParanoidiP06241
KOiK05703
OMAiQCWHKEP
OrthoDBi539311at2759
PhylomeDBiP06241
TreeFamiTF351634

Enzyme and pathway databases

BRENDAi2.7.10.2 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1227986 Signaling by ERBB2
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-202733 Cell surface interactions at the vascular wall
R-HSA-2029481 FCGR activation
R-HSA-210990 PECAM1 interactions
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-2424491 DAP12 signaling
R-HSA-2682334 EPH-Ephrin signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-373753 Nephrin family interactions
R-HSA-375165 NCAM signaling for neurite out-growth
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-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-3928664 Ephrin signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-HSA-399956 CRMPs in Sema3A signaling
R-HSA-418885 DCC mediated attractive signaling [P06241-1]
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5621480 Dectin-2 family
R-HSA-5621575 CD209 (DC-SIGN) signaling
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-75892 Platelet Adhesion to exposed collagen
R-HSA-8866376 Reelin signalling pathway
R-HSA-9032500 Activated NTRK2 signals through FYN [P06241-1]
R-HSA-9032759 NTRK2 activates RAC1 [P06241-1]
R-HSA-912631 Regulation of signaling by CBL
R-HSA-9607240 FLT3 Signaling
R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers
SignaLinkiP06241
SIGNORiP06241

Miscellaneous databases

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

More...ChiTaRSi		FYN human
EvolutionaryTraceiP06241

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		FYN

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

More...GenomeRNAii		2534
PharosiP06241 Tclin

Protein Ontology

More...PROi		PR:P06241
RNActiP06241 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000010810 Expressed in 232 organ(s), highest expression level in corpus callosum
ExpressionAtlasiP06241 baseline and differential
GenevisibleiP06241 HS

Family and domain databases

CDDicd12006 SH3_Fyn_Yrk, 1 hit
Gene3Di3.30.505.10, 1 hit
InterProiView protein in InterPro
IPR035750 Fyn/Yrk_SH3
IPR011009 Kinase-like_dom_sf
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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiFYN_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: P06241
Secondary accession number(s): B5BU57
, E1P557, H0UI48, Q16248, Q5R3A6, Q5R3A7, Q8N5D7
<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 11, 2019
This is version 250 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 6
    Human chromosome 6: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again