FYN
entrez
2534
canonical
uniprot
P06241
canonical
ensembl
ENSG00000010810
resolver
ensp
ENSP00000229471
resolver
ensp
ENSP00000346671
resolver
ensp
ENSP00000357656
resolver
ensp
ENSP00000357671
resolver
ensp
ENSP00000575592
resolver
ensp
ENSP00000575595
resolver
ensp
ENSP00000575596
resolver
ensp
ENSP00000575607
resolver
ensp
ENSP00000575608
resolver
ensp
ENSP00000582374
resolver
ensp
ENSP00000582377
resolver
ensp
ENSP00000636627
resolver
genesymbol
FYN
resolver
hgnc
HGNC:4037
resolver
uniprot
B5BU57
resolver
uniprot
E1P557
resolver
uniprot
H0UI48
resolver
uniprot
Q16248
resolver
uniprot
Q5R3A6
resolver
uniprot
Q5R3A7
resolver
uniprot
Q8N5D7
resolver
uniprot_entry
FYN_HUMAN
resolver
uniprot_sec
B5BU57
resolver
uniprot_sec
E1P557
resolver
uniprot_sec
H0UI48
resolver
uniprot_sec
Q16248
resolver
uniprot_sec
Q5R3A6
resolver
uniprot_sec
Q5R3A7
resolver
uniprot_sec
Q8N5D7
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:1699196}.
uniprot
proteins
amino_acid_sequence
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL
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:11536198, PubMed:15489916, PubMed:15557120, PubMed:16387660, PubMed:20100835, PubMed:7568038, PubMed:7822789). Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain (PubMed:15489916). Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions (PubMed:15489916). Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin) (PubMed:17194753). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT (PubMed:14707117, PubMed:15536091). Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage (PubMed:16841086). 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 (PubMed:14761972, PubMed:18258597, PubMed:19179337). 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 (PubMed:11162638, PubMed:12788081, PubMed:19652227). 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 (PubMed:22080863). Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation (PubMed:20028775). Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1 and PDCD1 (PubMed:18056706, PubMed:32184441). Phosphorylation of PAG1 promotes interaction between PAG1 and CSK and recruitment of CSK to lipid rafts (PubMed:18056706). Phosphorylation of PDCD1 leads to the recruitment of PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules (PubMed:32184441). CSK maintains LCK and FYN in an inactive form (By similarity). Promotes CD28-induced phosphorylation of VAV1 (PubMed:11005864). In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity). Can also promote CD244-mediated NK cell activation (PubMed:15713798). {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:11005864, ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198, ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117, ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091, ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:15713798, ECO:0000269|PubMed:16387660, ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753, ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597, ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227, ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:32184441, ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7822789, ECO:0000303|PubMed:15489916}.
uniprot
proteins
mass_dalton
60762
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 (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). {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:10196263, ECO:0000269|PubMed:1533589, ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:1699196, ECO:0000269|PubMed:22080863}.; 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
10196263
uniprot
proteins
pubmed
10498895
uniprot
proteins
pubmed
10790433
uniprot
proteins
pubmed
11005864
uniprot
proteins
pubmed
11162638
uniprot
proteins
pubmed
11518702
uniprot
proteins
pubmed
11536198
uniprot
proteins
pubmed
12218089
uniprot
proteins
pubmed
12545174
uniprot
proteins
pubmed
12788081
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14707117
uniprot
proteins
pubmed
14757743
uniprot
proteins
pubmed
14761972
uniprot
proteins
pubmed
1533589
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15489916
uniprot
proteins
pubmed
15536091
uniprot
proteins
pubmed
15537652
uniprot
proteins
pubmed
15557120
uniprot
proteins
pubmed
15713798
uniprot
proteins
pubmed
16387660
uniprot
proteins
pubmed
16841086
uniprot
proteins
pubmed
1699196
uniprot
proteins
pubmed
17194753
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17925405
uniprot
proteins
pubmed
18056706
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18258597
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19179337
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19652227
uniprot
proteins
pubmed
19807924
uniprot
proteins
pubmed
20028775
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20100835
uniprot
proteins
pubmed
22080863
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
27335501
uniprot
proteins
pubmed
3099169
uniprot
proteins
pubmed
32184441
uniprot
proteins
pubmed
3526330
uniprot
proteins
pubmed
7568038
uniprot
proteins
pubmed
7664083
uniprot
proteins
pubmed
7687536
uniprot
proteins
pubmed
7822789
uniprot
proteins
pubmed
8206991
uniprot
proteins
pubmed
8394019
uniprot
proteins
pubmed
8681387
uniprot
proteins
pubmed
8805554
uniprot
proteins
pubmed
8961927
uniprot
proteins
pubmed
9038210
uniprot
proteins
pubmed
9207119
uniprot
proteins
pubmed
9351806
uniprot
proteins
pubmed
9360983
uniprot
proteins
pubmed
9741627
uniprot
proteins
sequence_length
537
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:8206991}. Nucleus {ECO:0000269|PubMed:15537652}. Cell membrane {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:8206991}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (PubMed:12218089). Palmitoylation is crucial for proper trafficking (PubMed:8206991). {ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:8206991}.
uniprot
proteins