LipidDB ID

LipidDB-9606-00585

Entry Name

UniProt Accession

P06241; B5BU57; E1P557; H0UI48; Q16248; Q5R3A6; Q5R3A7; Q8N5D7;

Theoretical PI

6.23

Molecular Weight

60761.9

Genbank Protein ID

AAA36615.1; AAC08285.1; AAB33113.2; BAG70107.1; BAG70240.1; CAI22300.1; CAI22301.1; EAW48278.1; EAW48279.1; EAW48281.1; EAW48282.1; EAW48283.1; AAH32496.1;

Genbank Nucleotide ID

M14676; M14333; S74774; AB451293; AB451426; Z97989; Z97989; CH471051; CH471051; CH471051; CH471051; CH471051; BC032496;

Protein Name

Tyrosine-protein kinase Fyn

Protein Synonyms/Alias

2.7.10.2; Proto-oncogene Syn; Proto-oncogene c-Fyn; Src-like kinase; SLK; p59-Fyn;

Gene Name

FYN

Gene Synonyms/Alias

Created Date

01-JAN-1988

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Alland L, Peseckis SM, Atherton RE, Berthiaume L, Resh MD. Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization. JBiol Chem. 1994 Jun 17;269(24):16701-5.[PMID:8206991]
[2] Sato I, Obata Y, Kasahara K, Nakayama Y, Fukumoto Y, Yamasaki T, Yokoyama KK, Saito T, Yamaguchi N. Differential trafficking of Src, Lyn, Yes and Fyn isspecified by the state of palmitoylation in the SH4 domain. J Cell Sci. 2009 Apr 1;122(Pt 7):965-75. doi: 10.1242/jcs.034843. Epub 2009 Mar 3.[PMID:19258394]

Functional Description

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, KIRREL 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. 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.

Sequence Annotation

Domain: 82 143 SH3.
Domain: 149 246 SH2.
Domain: 271 524 Protein kinase.
Nucleotide-binding: 277 285 ATP.
Active site: 390 390 Proton acceptor.
Binding site: 299 299 ATP.
Modified residue: 12 12 Phosphothreonine; by PKC.
Modified residue: 15 15 Phosphothreonine.
Modified residue: 21 21 Phosphoserine.
Modified residue: 25 25 Phosphoserine.
Modified residue: 185 185 Phosphotyrosine.
Modified residue: 213 213 Phosphotyrosine.
Modified residue: 214 214 Phosphotyrosine.
Modified residue: 257 257 Phosphoserine.
Modified residue: 420 420 Phosphotyrosine; by autocatalysis.
Modified residue: 440 440 Phosphotyrosine.
Modified residue: 512 512 Phosphothreonine.
Modified residue: 531 531 Phosphotyrosine; by CSK.

Protein Length

537 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005829; C:cytosol; TAS:Reactome
GO:0005768; C:endosome; IDA:HGNC
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:BHF-UCL
GO:0014069; C:postsynaptic density; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0046875; F:ephrin receptor binding; IPI:UniProtKB
GO:0001948; F:glycoprotein binding; IPI:BHF-UCL
GO:0070851; F:growth factor receptor binding; IPI:UniProtKB
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; NAS:UniProtKB
GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome
GO:0050798; P:activated T cell proliferation; IEA:Ensembl
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0006816; P:calcium ion transport; NAS:UniProtKB
GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl
GO:0048813; P:dendrite morphogenesis; IEA:Ensembl
GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl
GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome
GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0007631; P:feeding behavior; TAS:ProtInc
GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome
GO:0030900; P:forebrain development; IEA:Ensembl
GO:0045087; P:innate immune response; TAS:Reactome
GO:0035556; P:intracellular signal transduction; TAS:ProtInc
GO:0007612; P:learning; TAS:ProtInc
GO:0050900; P:leukocyte migration; TAS:Reactome
GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl
GO:0010629; P:negative regulation of gene expression; IEA:Ensembl
GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl
GO:0001764; P:neuron migration; IEA:Ensembl
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome
GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome
GO:0030168; P:platelet activation; TAS:Reactome
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl
GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl
GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl
GO:0046777; P:protein autophosphorylation; IEA:Ensembl
GO:0006468; P:protein phosphorylation; NAS:UniProtKB
GO:0008360; P:regulation of cell shape; IEA:Ensembl
GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome
GO:0042493; P:response to drug; IEA:Ensembl
GO:0045471; P:response to ethanol; IEA:Ensembl
GO:0031295; P:T cell costimulation; TAS:Reactome
GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB
GO:0016032; P:viral process; TAS:Reactome

Interpro

InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR000980; SH2
InterPro; IPR001452; SH3_domain
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom

Pfam

Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;

SMART

SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;

PROSITE

PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;

PRINTS

PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00452; SH3DOMAIN;
PRINTS; PR00109; TYRKINASE;