LipidDB ID

LipidDB-10090-00039

Entry Name

UniProt Accession

P39688; Q3TAT3; Q3U0T5; Q8K2A3;

Theoretical PI

6.23

Molecular Weight

60674.83

Genbank Protein ID

AAA37644.1; AAB09568.1; BAE33766.1; BAE42585.1; AAH32149.1; AAH92217.1;

Genbank Nucleotide ID

M27266; U70324; AK156584; AK171646; BC032149; BC092217;

Protein Name

Tyrosine-protein kinase Fyn

Protein Synonyms/Alias

2.7.10.2; Proto-oncogene c-Fyn; p59-Fyn;

Gene Name

Fyn

Gene Synonyms/Alias

Created Date

01-FEB-1995

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Reference

[1] Shenoy-Scaria AM, Gauen LK, Kwong J, Shaw AS, Lublin DM. Palmitylation of anamino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fynmediates interaction with glycosyl-phosphatidylinositol-anchored proteins. MolCell Biol. 1993 Oct;13(10):6385-92.[PMID:8413237]
[2] Koegl M, Zlatkine P, Ley SC, Courtneidge SA, Magee AI. Palmitoylation ofmultiple Src-family kinases at a homologous N-terminal motif. Biochem J. 1994 Nov1;303 ( Pt 3):749-53.[PMID:7980442]
[3] Wolven A, Okamura H, Rosenblatt Y, Resh MD. Palmitoylation of p59fyn isreversible and sufficient for plasma membrane association. Mol Biol Cell. 1997Jun;8(6):1159-73.[PMID:9201723]
[4] Timson Gauen LK, Linder ME, Shaw AS. Multiple features of the p59fyn srchomology 4 domain define a motif for immune-receptor tyrosine-based activationmotif (ITAM) binding and for plasma membrane localization. J Cell Biol. 1996Jun;133(5):1007-15.[PMID:8655574]

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 (By similarity).

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: 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; alternate.
Modified residue: 531 531 Phosphotyrosine; by CSK; alternate.

Protein Length

537 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005884; C:actin filament; IDA:MGI
GO:0071944; C:cell periphery; IDA:MGI
GO:0005829; C:cytosol; TAS:Reactome
GO:0005768; C:endosome; IDA:MGI
GO:0045121; C:membrane raft; IEA:Ensembl
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0014069; C:postsynaptic density; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0001664; F:G-protein coupled receptor binding; IPI:UniProt
GO:0044325; F:ion channel binding; IPI:BHF-UCL
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC
GO:0004672; F:protein kinase activity; IDA:MGI
GO:0004713; F:protein tyrosine kinase activity; IDA:MGI
GO:0015631; F:tubulin binding; IDA:MGI
GO:0050798; P:activated T cell proliferation; IMP:MGI
GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI
GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl
GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:MGI
GO:0048813; P:dendrite morphogenesis; IMP:MGI
GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI
GO:0030900; P:forebrain development; IMP:MGI
GO:0042552; P:myelination; TAS:MGI
GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl
GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL
GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI
GO:0001764; P:neuron migration; IMP:MGI
GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI
GO:0010976; P:positive regulation of neuron projection development; IGI:MGI
GO:1900182; P:positive regulation of protein localization to nucleus; IDA:MGI
GO:0046777; P:protein autophosphorylation; IDA:MGI
GO:0006468; P:protein phosphorylation; IMP:MGI
GO:0008360; P:regulation of cell shape; IDA:MGI
GO:0042493; P:response to drug; IEA:Ensembl
GO:0045471; P:response to ethanol; IGI:MGI
GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl

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;