Search by BoMiProt ID - Bomi10174


Primary Information

BoMiProt ID Bomi10174
Protein Name Tyrosine-protein kinase Fyn/Proto-oncogene c-Fyn/p59-Fyn
Organism Bos taurus
Uniprot IdA0JNB0
Milk FractionWhey,Exosome,MFGM
Ref Sequence Id NP_001071440.1
Aminoacid Length 537
Molecular Weight 60718
Fasta Sequence https://www.uniprot.org/uniprot/A0JNB0.fasta
Gene Name FYN
Gene Id 527263
Protein Existence Status reviewed

Secondary Information

Protein Function non-receptor tyrosine kinase of the Src family,involved in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance.
Biochemical Properties Mn2+ as cofactor.Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site.N-terminal domain has a number of tyrosine residues which lie within consensus sequences for binding by various families of SH2 domains.contains both SH2 and SH3 domains that are critical to the various regulatory functions of the protein.
PTMs Phosphorylation,Myristoylation,Palmitoylation,Lipidation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A0JNB0|FYN_BOVIN Tyrosine-protein kinase Fyn OS=Bos taurus OX=9913 GN=FYN PE=2 SV=1 MGCVQCKDKEAT*12KLTEERDGS*21LNQSS*26GYRYGTDPTPQHYPSFGVTSIPNYNNFHGAGGQG LTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWW EARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESET TKGAY*185SLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCC RLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKT LKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGR ALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEY*420 TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVE RGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQY*531QPGENL
Predicted Disorder Regions 1-56, 528-535
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs 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.Ultraviolet B strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus.Phosphorylated on Ser residues by an isoform of PKC which is necessary for activation of Fyn in Keratinocytes.For full activity of Src Kinase activity,Tyr-419 within the activation loop of catalytic activity on Fyn must be autophosphorylated.Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.
Bibliography 1.Edwards JC, Kapadia S. Regulation of the bovine kidney microsomal chloride channel p64 by p59fyn, a Src family tyrosine kinase. J Biol Chem. 2000 Oct 13;275(41):31826-32. doi: 10.1074/jbc.M005275200. PMID: 10930415. 2.Crosby D, Poole AW. Physical and functional interaction between protein kinase C delta and Fyn tyrosine kinase in human platelets. J Biol Chem. 2003 Jul 4;278(27):24533-41. doi: 10.1074/jbc.M301847200. Epub 2003 Apr 29. PMID: 12721299.