Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Fyn (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Fyn a tyrosine kinase of the Src family. Implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Blocks axon outgrowth and attraction induced by NTN1 by phosphorylating its receptor DDC. Associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Three alternatively spliced isoforms have been described. Isoform 2 shows a greater ability to mobilize cytoplasmic calcium than isoform 1. Induced expression aids in cellular transformation and xenograft metastasis. In squamous cell carcinoma, Fyn transduces signals from EGFR and Src and is required for cell migration and invasiveness. Activity linked to migration in a murine melanoma model. Appears to block late stage development of neuroblastoma. Mouse knockout deficient in kindling response, a model for human epilepsy. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; EC 2.7.10.2; Protein kinase, tyrosine (non-receptor); Protein kinase, TK; TK group; Src family
Cellular Component: mitochondrion; intracellular membrane-bound organelle; membrane; cytoplasm; postsynaptic density; plasma membrane; nucleus; endosome; lipid raft
Molecular Function: tubulin binding; CD8 receptor binding; ephrin receptor binding; metal ion binding; nucleotide binding; non-membrane spanning protein tyrosine kinase activity; protein kinase activity; transferase activity; protein binding; G-protein-coupled receptor binding; peptide hormone receptor binding; protein-tyrosine kinase activity; transferase activity, transferring phosphorus-containing groups; protein complex binding; T cell receptor binding; phosphoinositide 3-kinase binding; kinase activity; glycoprotein binding; CD4 receptor binding; ATP binding; receptor binding
Biological Process: myelination; positive regulation of I-kappaB kinase/NF-kappaB cascade; peptidyl-tyrosine phosphorylation; immune system process; multicellular organismal development; dendrite morphogenesis; protein amino acid autophosphorylation; activated T cell proliferation; neuron migration; protein amino acid phosphorylation; T cell receptor signaling pathway; positive regulation of phosphoinositide 3-kinase cascade; detection of mechanical stimulus involved in sensory perception of pain; regulation of cell shape; response to ethanol; cell surface receptor linked signal transduction; forebrain development; negative regulation of neuron apoptosis; negative regulation of protein catabolic process; phosphorylation
Reference #:  P39688 (UniProtKB)
Alt. Names/Synonyms: AI448320; AW552119; Fyn; Fyn proto-oncogene; MGC115870; p59-Fyn; Proto-oncogene c-Fyn; proto-oncogene tyrosine-protein kinase Fyn; Src Kinase p59; Tyrosine-protein kinase Fyn
Gene Symbols: Fyn
Molecular weight: 60,675 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
CST Pathways:  Adherens Junction Dynamics  |  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs  |  Insulin Receptor Signaling  |  Tyrosine Kinases & Substrates
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Fyn

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Reactome  |  BioGPS  |  Scansite  |  KinBase  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
enzymatic activity, induced: Y420‑p
enzymatic activity, inhibited: Y28‑p, Y531‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
1 2 A12 QCKDKEAAKLTEERD
1 33 S21-p LTEERDGsLNQssGy
0 4 S25-p RDGsLNQssGyRYGT
0 3 S26-p DGsLNQssGyRYGTD
2 11 Y28-p sLNQssGyRYGTDPT
1 0 Y30 NQssGyRYGTDPTPQ
1 0 Y39 TDPTPQHYPSFGVTS
0 9 Y91-p VTLFVALyDYEARTE
0 4 Y150 SIQAEEWYFGKLGRK
1 288 Y185-p SETTKGAysLSIRDW
0 9 S186-p ETTKGAysLSIRDWD
1 1788 Y213-p RKLDNGGyyITTRAQ
1 668 Y214-p KLDNGGyyITTRAQF
0 2 S257-p MPRLTDLsVKTKDVW
0 4 S270 VWEIPRESLQLIKRL
0 1 T289 FGEVWMGTWNGNTKV
0 1 T294 MGTWNGNTKVAIKTL
0 1 T300 NTKVAIKTLKPGTMS
0 1 S307 TLKPGTMSPESFLEE
0 1 K320-m1 EEAQIMKkLkHDKLV
0 1 K322-m1 AQIMKkLkHDKLVQL
0 4 Y339-p VVSEEPIyIVTEYMS
0 1 S393-p YIHRDLRsANILVGN
0 1 K405 VGNGLICKIADFGLA
18 3057 Y420-p RLIEDNEytARQGAK
0 16 T421-p LIEDNEytARQGAKF
0 528 Y440-p TAPEAALyGRFTIKS
16 1034 Y531-p FTATEPQyQPGENL_
2101 : Phospho-Src Family (Tyr416) Antibody
6943 : Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb
  human

► Hide Isoforms
 
T12-p QCKDKEAtKLTEERD
S21-p LTEERDGsLNQssGy
S25-p RDGsLNQssGyRyGT
S26-p DGsLNQssGyRyGTD
Y28-p sLNQssGyRyGTDPT
Y30-p NQssGyRyGTDPTPQ
Y39-p TDPTPQHyPSFGVTS
Y91-p VTLFVALyDYEARTE
Y150 SIQAEEWYFGKLGRK
Y185-p SETTKGAysLSIRDW
S186-p ETTKGAysLSIRDWD
Y213-p RKLDNGGyyITTRAQ
Y214-p KLDNGGyyITTRAQF
S257-p MPRLTDLsVKTKDVW
S270 VWEIPRESLQLIKRL
T289-p FGEVWMGtWNGNtKV
T294-p MGtWNGNtKVAIKtL
T300-p NtKVAIKtLKPGTMs
S307-p tLKPGTMsPESFLEE
K320 EEAQIMKKLKHDKLV
K322 AQIMKKLKHDKLVQL
Y339-p VVSEEPIyIVTEYMN
S393 YIHRDLRSANILVGN
K405-ub VGNGLICkIADFGLA
Y420-p RLIEDNEytARQGAK
T421-p LIEDNEytARQGAKF
Y440-p TAPEAALyGRFTIKS
Y531-p FTATEPQyQPGENL_
2101 : Phospho-Src Family (Tyr416) Antibody
6943 : Phospho-Src Family (Tyr416) (D49G4) Rabbit mAb
  Fyn iso2  
T12 QCKDKEATKLTEERD
S21 LTEERDGSLNQSSGY
S25 RDGSLNQSSGYRYGT
S26 DGSLNQSSGYRYGTD
Y28 SLNQSSGYRYGTDPT
Y30 NQSSGYRYGTDPTPQ
Y39 TDPTPQHYPSFGVTS
Y91 VTLFVALYDYEARTE
Y150 SIQAEEWYFGKLGRK
Y185 SETTKGAYSLSIRDW
S186 ETTKGAYSLSIRDWD
Y213 RKLDNGGYYITTRAQ
Y214 KLDNGGYYITTRAQF
A257 TPQTSGLAKDAWEVA
S267-p AWEVARRsLCLEKKL
T286 FAEVWLGTWNGNTKV
T291 LGTWNGNTKVAIKTL
T297 NTKVAIKTLKPGTMS
S304 TLKPGTMSPESFLEE
K317 EEAQIMKKLKHDKLV
K319 AQIMKKLKHDKLVQL
Y336 VVSEEPIYIVTEYMN
S390 YIHRDLRSANILVGN
K402 VGNGLICKIADFGLA
Y417-p RLIEDNEyTARQGAK
T418 LIEDNEyTARQGAKF
Y437 TAPEAALYGRFTIKS
Y528-p FTATEPQyQPGENL_
  Fyn iso3  
T12 QCKDKEATKLTEERD
S21 LTEERDGSLNQSSGY
S25 RDGSLNQSSGYRYGT
S26 DGSLNQSSGYRYGTD
Y28 SLNQSSGYRYGTDPT
Y30 NQSSGYRYGTDPTPQ
Y39 TDPTPQHYPSFGVTS
Y91 VTLFVALYDYEARTE
Y150 SIQAEEWYFGKLGRK
Y185 SETTKGAYSLSIRDW
S186 ETTKGAYSLSIRDWD
Y213 RKLDNGGYYITTRAQ
Y214 KLDNGGYYITTRAQF
- gap
- gap
T234 LVQHYSGTWNGNTKV
T239 SGTWNGNTKVAIKTL
T245 NTKVAIKTLKPGTMS
S252 TLKPGTMSPESFLEE
K265 EEAQIMKKLKHDKLV
K267 AQIMKKLKHDKLVQL
Y284 VVSEEPIYIVTEYMN
S338 YIHRDLRSANILVGN
K350 VGNGLICKIADFGLA
Y365 RLIEDNEYTARQGAK
T366 LIEDNEYTARQGAKF
Y385 TAPEAALYGRFTIKS
Y476 FTATEPQYQPGENL_
  rat

 
A12 QCKDKEAAKLTEERD
S21-p LTEERDGsLNQSSGY
S25 RDGsLNQSSGYRYGT
S26 DGsLNQSSGYRYGTD
Y28 sLNQSSGYRYGTDPT
Y30 NQSSGYRYGTDPTPQ
Y39 TDPTPQHYPSFGVTS
Y91 VTLFVALYDYEARTE
Y150-p SIQAEEWyFGKLGRK
Y185-p SETTKGAysLSIRDW
S186-p ETTKGAysLSIRDWD
Y213-p RKLDNGGyyITTRAQ
Y214-p KLDNGGyyITTRAQF
S257 MPRLTDLSVKTKDVW
S270 VWEIPRESLQLIKRL
T289 FGEVWMGTWNGNTKV
T294 MGTWNGNTKVAIKTL
T300 NTKVAIKTLKPGTMS
S307 TLKPGTMSPESFLEE
K320 EEAQIMKKLKHDKLV
K322 AQIMKKLKHDKLVQL
Y339 VVSEEPIYIVTEYMN
S393 YIHRDLRSANILVGN
K405 VGNGLICKIADFGLA
Y420-p RLIEDNEyTARQGAK
T421 LIEDNEyTARQGAKF
Y440-p TAPEAALyGRFTIKS
Y531-p FTATEPQyQPGENL_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.