Fyn
entrez
25150
canonical
uniprot
Q62844
canonical
ensembl
ENSRNOG00000000596
resolver
ensembl
ENSRNOG00055000725
resolver
ensembl
ENSRNOG00060007389
resolver
ensembl
ENSRNOG00065008840
resolver
ensp
ENSRNOP00000000733
resolver
ensp
ENSRNOP00000068458
resolver
ensp
ENSRNOP00000072210
resolver
ensp
ENSRNOP00000088889
resolver
ensp
ENSRNOP00055001005
resolver
ensp
ENSRNOP00060009164
resolver
ensp
ENSRNOP00065010550
resolver
enst
ENSRNOT00000000733
resolver
enst
ENSRNOT00000076859
resolver
enst
ENSRNOT00000118910
resolver
enst
ENSRNOT00055001252
resolver
enst
ENSRNOT00060012148
resolver
enst
ENSRNOT00065014115
resolver
genesymbol
Fyn
resolver
uniprot
A0A096MKC1
resolver
uniprot
A0A8I6A612
resolver
uniprot_entry
A0A096MKC1_RAT
resolver
uniprot_entry
A0A8I6A612_RAT
resolver
uniprot_entry
FYN_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site. {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MGCVQCKDKEAAKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL
uniprot
proteins
ec_number
2.7.10.2
uniprot
proteins
function
FUNCTION: 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 (PubMed:10366594). Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain (By similarity). Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions (By similarity). Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin) (By similarity). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT (By similarity). Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage (By similarity). 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 (By similarity). 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 (By similarity). Involved in reelin signaling by mediating phosphorylation of DAB1 following reelin (RELN)-binding to its receptor (By similarity). Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation (By similarity). Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation (By similarity). Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1 and PDCD1 (By similarity). Phosphorylation of PAG1 promotes interaction between PAG1 and CSK and recruitment of CSK to lipid rafts (By similarity). Phosphorylation of PDCD1 leads to the recruitment of PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules (By similarity). CSK maintains LCK and FYN in an inactive form (By similarity). Promotes CD28-induced phosphorylation of VAV1 (By similarity). In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). Can also promote CD244-mediated NK cell activation (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:10366594}.
uniprot
proteins
mass_dalton
60702
uniprot
proteins
mutagenesis
MUTAGEN 299; /note="K->M: Loss of kinase activity and reduction in oligodendrocyte process extension and myelin membrane formation."; /evidence="ECO:0000269|PubMed:10366594
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:P39688}.; PTM: Palmitoylated. Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location. {ECO:0000250|UniProtKB:P39688}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SRC subfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10366594
uniprot
proteins
pubmed
15715669
uniprot
proteins
pubmed
2062320
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000250|UniProtKB:P06241}. Perikaryon {ECO:0000269|PubMed:10366594}. Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:0000250|UniProtKB:P06241}.
uniprot
proteins