Fyn
entrez
14360
canonical
uniprot
P39688
canonical
ensembl
ENSMUSG00000019843
resolver
ensp
ENSMUSP00000057707
resolver
ensp
ENSMUSP00000097547
resolver
ensp
ENSMUSP00000114188
resolver
ensp
ENSMUSP00000115233
resolver
ensp
ENSMUSP00000118131
resolver
ensp
ENSMUSP00000282401
resolver
ensp
ENSMUSP00000282402
resolver
ensp
ENSMUSP00000282405
resolver
ensp
ENSMUSP00000282409
resolver
ensp
ENSMUSP00000282415
resolver
ensp
ENSMUSP00000282425
resolver
ensp
ENSMUSP00000344400
resolver
enst
ENSMUST00000136659
resolver
genesymbol
Fyn
resolver
uniprot
D3YZ57
resolver
uniprot
Q3TAT3
resolver
uniprot
Q3U0T5
resolver
uniprot
Q8K2A3
resolver
uniprot_entry
D3YZ57_MOUSE
resolver
uniprot_entry
FYN_MOUSE
resolver
uniprot_sec
Q3TAT3
resolver
uniprot_sec
Q3U0T5
resolver
uniprot_sec
Q8K2A3
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site. {ECO:0000269|PubMed:8441403}.
uniprot
proteins
amino_acid_sequence
MGCVQCKDKEAAKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL
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:12218089, PubMed:12526739, PubMed:12640114, PubMed:12681493, PubMed:14999081, PubMed:8007959). 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) (PubMed:12640114). 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 (PubMed:12526739). 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 (PubMed:12218089). Promotes CD28-induced phosphorylation of VAV1 (By similarity). In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (PubMed:12681493). Can also promote CD244-mediated NK cell activation (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12526739, ECO:0000269|PubMed:12640114, ECO:0000269|PubMed:12681493, ECO:0000269|PubMed:14999081, ECO:0000269|PubMed:8007959}.
uniprot
proteins
mass_dalton
60675
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes myristoylation and palmitoylation."; /evidence="ECO:0000269|PubMed:7980442"; MUTAGEN 3; /note="C->A: Abolishes palmitoylation and plasma membrane association; when associated with A-6."; /evidence="ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723"; MUTAGEN 3; /note="C->S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association."; /evidence="ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723"; MUTAGEN 6; /note="C->A: Abolishes palmitoylation and plasma membrane association; when associated with A-3."; /evidence="ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237"; MUTAGEN 6; /note="C->S: Abolishes palmitoylation and plasma membrane association; when associated with S-3."; /evidence="ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated at Tyr-420 (PubMed:8441403). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:8441403). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-15 and kinase activity, and promotes translocation from the cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (PubMed:22685302). {ECO:0000250|UniProtKB:P06241, ECO:0000269|PubMed:22685302, ECO:0000269|PubMed:8441403}.; PTM: Palmitoylated (PubMed:19956733, PubMed:7980442, PubMed:8413237, PubMed:9201723). Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location (PubMed:19956733, PubMed:7980442, PubMed:8413237, PubMed:9201723). {ECO:0000269|PubMed:19956733, ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237, ECO:0000269|PubMed:9201723}.; PTM: Myristoylation is required prior to palmitoylation. {ECO:0000269|PubMed:8655574}.
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
SRC subfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11711534
uniprot
proteins
pubmed
12218089
uniprot
proteins
pubmed
12526739
uniprot
proteins
pubmed
12640114
uniprot
proteins
pubmed
12681493
uniprot
proteins
pubmed
1361685
uniprot
proteins
pubmed
14645715
uniprot
proteins
pubmed
14999081
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16129412
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16966330
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19956733
uniprot
proteins
pubmed
20398064
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21872217
uniprot
proteins
pubmed
22685302
uniprot
proteins
pubmed
2488273
uniprot
proteins
pubmed
7681396
uniprot
proteins
pubmed
7980442
uniprot
proteins
pubmed
8007959
uniprot
proteins
pubmed
8168489
uniprot
proteins
pubmed
8413237
uniprot
proteins
pubmed
8441403
uniprot
proteins
pubmed
8655574
uniprot
proteins
pubmed
9201723
uniprot
proteins
pubmed
9312046
uniprot
proteins
pubmed
9895129
uniprot
proteins
sequence_length
537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:14645715}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (PubMed:14645715). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:0000250|UniProtKB:P06241, ECO:0000269|PubMed:14645715}.
uniprot
proteins