Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39688 (FYN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Fyn

EC=2.7.10.2
Alternative name(s):
Proto-oncogene c-Fyn
p59-Fyn
Gene names
Name:Fyn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. 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, KIRREL and TRPC6. 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. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1 By similarity. Ref.11 Ref.16 Ref.17 Ref.19

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Manganese.

Enzyme regulation

Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site. Ref.7

Subunit structure

Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts with TOM1L1 (phosphorylated form). Interacts with SH2D1A and SLAMF1. Interacts with and phosphorylates ITCH, down-regulating its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Interacts (via SH3 domain) with KLHL2 (via N-terminus) By similarity. Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Ref.6 Ref.10 Ref.13 Ref.15 Ref.21

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking By similarity. Ref.16 Ref.18

Tissue specificity

Isoform 1 is highly expressed in the brain, isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. Ref.5 Ref.11

Post-translational modification

Autophosphorylated at Tyr-420. 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 (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. Ref.7

Palmitoylation at Cys-3 and Cys-6 regulates subcellular location. Ref.8 Ref.9 Ref.14

Myristoylation is required prior to palmitoylation. Ref.8 Ref.9 Ref.14

Disruption phenotype

Mice have various neural defects, including defective long term potentiation, impaired spatial memory, hypomyelination, abnormal dendrite orientation and uncoordinated hippocampal structure. Ref.5 Ref.24

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

activated T cell proliferation

Inferred from mutant phenotype PubMed 1516132. Source: MGI

cell surface receptor signaling pathway

Inferred from direct assay PubMed 9177270. Source: MGI

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from mutant phenotype PubMed 12372285. Source: MGI

detection of mechanical stimulus involved in sensory perception of pain

Inferred from mutant phenotype PubMed 16190898. Source: MGI

forebrain development

Inferred from mutant phenotype PubMed 15073522. Source: MGI

myelination

Traceable author statement PubMed 11826099. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

negative regulation of gene expression

Inferred from mutant phenotype PubMed 20978343. Source: BHF-UCL

negative regulation of protein catabolic process

Inferred from mutant phenotype PubMed 16841086. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 15073522. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 10872802PubMed 17923684PubMed 8175795PubMed 8196616. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from genetic interaction PubMed 23169819. Source: MGI

positive regulation of neuron projection development

Inferred from genetic interaction PubMed 18354028. Source: MGI

positive regulation of protein localization to nucleus

Inferred from direct assay PubMed 20142099. Source: MGI

protein autophosphorylation

Inferred from direct assay PubMed 8175795. Source: MGI

protein phosphorylation

Inferred from mutant phenotype PubMed 16190898PubMed 9892651. Source: MGI

regulation of cell shape

Inferred from direct assay PubMed 11826099. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from genetic interaction PubMed 9381182. Source: MGI

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

endosome

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

G-protein coupled receptor binding

Inferred from physical interaction PubMed 23169819. Source: UniProt

ion channel binding

Inferred from physical interaction PubMed 12538589. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 10713104PubMed 7799925. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 11826099. Source: MGI

protein tyrosine kinase activity

Inferred from direct assay PubMed 10872802PubMed 16841086PubMed 17923684PubMed 20142099PubMed 8175795PubMed 8196616. Source: MGI

tubulin binding

Inferred from direct assay PubMed 11826099. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBLP226813EBI-524514,EBI-518228From a different organism.
Dynlt1P518073EBI-524514,EBI-642797
Irs1P355704EBI-524514,EBI-520230From a different organism.
Khdrbs1Q6074913EBI-524514,EBI-519077
PdgfrbP056223EBI-524514,EBI-1554855
PLXNA2O750513EBI-524514,EBI-308264From a different organism.
PTPRAP184332EBI-524514,EBI-2609645From a different organism.
Slamf1Q9QUM44EBI-524514,EBI-7910086
Sphk2Q9JIA72EBI-524514,EBI-985434

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39688-1)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P39688-2)

Also known as: T;

The sequence of this isoform differs from the canonical sequence as follows:
     234-236: RAA → KAD
     240-287: CRLVVPCHKG...GNGQFGEVWM → FNLTVVSSSC...GQGCFAEVWL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 537536Tyrosine-protein kinase Fyn
PRO_0000088100

Regions

Domain82 – 14362SH3
Domain149 – 24698SH2
Domain271 – 524254Protein kinase
Nucleotide binding277 – 2859ATP By similarity

Sites

Active site3901Proton acceptor By similarity
Binding site2991ATP By similarity

Amino acid modifications

Modified residue151Phosphothreonine By similarity
Modified residue211Phosphoserine Ref.23
Modified residue251Phosphoserine By similarity
Modified residue1851Phosphotyrosine Ref.22
Modified residue2131Phosphotyrosine By similarity
Modified residue2141Phosphotyrosine By similarity
Modified residue2571Phosphoserine By similarity
Modified residue4201Phosphotyrosine; by autocatalysis Ref.7
Modified residue4401Phosphotyrosine By similarity
Modified residue5121Phosphothreonine By similarity
Modified residue5311Phosphotyrosine; alternate Ref.7 Ref.22
Modified residue5311Phosphotyrosine; by CSK; alternate By similarity
Lipidation21N-myristoyl glycine Ref.12
Lipidation31S-palmitoyl cysteine Ref.8 Ref.9 Ref.14
Lipidation61S-palmitoyl cysteine Probable

Natural variations

Alternative sequence234 – 2363RAA → KAD in isoform 2.
VSP_024111
Alternative sequence240 – 28748CRLVV…GEVWM → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF AEVWL in isoform 2.
VSP_024112

Experimental info

Mutagenesis21G → A: Abolishes myristoylation and palmitoylation. Ref.9
Mutagenesis31C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. Ref.8 Ref.9 Ref.14
Mutagenesis31C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. Ref.8 Ref.9 Ref.14
Mutagenesis61C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. Ref.8 Ref.9
Mutagenesis61C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. Ref.8 Ref.9
Sequence conflict1791E → Q in AAA37644. Ref.1
Sequence conflict1791E → Q in AAB09568. Ref.2
Sequence conflict4321W → R in BAE42585. Ref.3

Secondary structure

............................. 537
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B) [UniParc].

Last modified April 3, 2013. Version 4.
Checksum: 99558702596DAEE0

FASTA53760,675
        10         20         30         40         50         60 
MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 

        70         80         90        100        110        120 
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 

       130        140        150        160        170        180 
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 

       190        200        210        220        230        240 
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 

       250        260        270        280        290        300 
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 

       310        320        330        340        350        360 
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR 

       370        380        390        400        410        420 
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 

       430        440        450        460        470        480 
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 

       490        500        510        520        530 
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL 

« Hide

Isoform 2 (T) [UniParc].

Checksum: 782C93B2003B7DCD
Show »

FASTA53460,059

References

« Hide 'large scale' references
[1]"Expression of a novel form of the fyn proto-oncogene in hematopoietic cells."
Cooke M.P., Perlmutter R.M.
New Biol. 1:66-74(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Two species of mRNAs for the fyn proto-oncogene are produced by an alternative polyadenylation."
Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.
Mol. Cells 8:746-749(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: T-cell.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: NOD.
Tissue: Spleen.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6 and FVB/N.
Tissue: Brain and Mammary tumor.
[5]"Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice."
Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., Kandel E.R.
Science 258:1903-1910(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]"Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor."
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F.
EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSF1R.
[7]"Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases."
Hurley T.R., Hyman R., Sefton B.M.
Mol. Cell. Biol. 13:1651-1656(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-420 AND TYR-531, ENZYME REGULATION.
[8]"Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins."
Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.
Mol. Cell. Biol. 13:6385-6392(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF CYS-3 AND CYS-6.
[9]"Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif."
Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.
Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-6.
[10]"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
Clark M.R., Johnson S.A., Cambier J.C.
EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD79A.
[11]"Unique catalytic properties dictate the enhanced function of p59fynT, the hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T cells."
Davidson D., Viallet J., Veillette A.
Mol. Cell. Biol. 14:4554-4564(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Multiple features of the p59fyn src homology 4 domain define a motif for immune-receptor tyrosine-based activation motif (ITAM) binding and for plasma membrane localization."
Gauen L.K.T., Linder M.E., Shaw A.S.
J. Cell Biol. 133:1007-1015(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[13]"Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling."
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.
EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSF1R.
[14]"Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association."
Wolven A., Okamura H., Rosenblatt Y., Resh M.D.
Mol. Biol. Cell 8:1159-1173(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF CYS-3.
[15]"'Srcasm: a novel Src activating and signaling molecule."
Seykora J.T., Mei L., Dotto G.P., Stein P.L.
J. Biol. Chem. 277:2812-2822(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOM1L1.
[16]"Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells."
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.
J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction."
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M.
Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CTNNB1.
[18]"Transmembrane phosphoprotein Cbp senses cell adhesion signaling mediated by Src family kinase in lipid rafts."
Shima T., Nada S., Okada M.
Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[19]"Phosphorylation of tau by fyn: implications for Alzheimer's disease."
Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K., Fang S.M., Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.
J. Neurosci. 24:2304-2312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[20]"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
Roskoski R. Jr.
Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[21]"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
Lamalice L., Houle F., Huot J.
J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDR.
[22]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[23]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Decreased dendritic spine density and abnormal spine morphology in Fyn knockout mice."
Babus L.W., Little E.M., Keenoy K.E., Minami S.S., Chen E., Song J.M., Caviness J., Koo S.Y., Pak D.T., Rebeck G.W., Turner R.S., Hoe H.S.
Brain Res. 1415:96-102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[25]"Crystal structure of a SH3 and SH2 domains of fyn protein (proto-concogene tyrosine-protein kinase fyn) from Mus musculus at 1.98 a resolution."
Joint center for structural genomics (JCSG)
Submitted (DEC-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 81-239.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27266 mRNA. Translation: AAA37644.1.
U70324 mRNA. Translation: AAB09568.1.
AK156584 mRNA. Translation: BAE33766.1.
AK171646 mRNA. Translation: BAE42585.1.
BC032149 mRNA. Translation: AAH32149.1.
BC092217 mRNA. Translation: AAH92217.1.
CCDSCCDS23788.1. [P39688-2]
CCDS48538.1. [P39688-1]
PIRA44991.
RefSeqNP_001116364.1. NM_001122892.1. [P39688-2]
NP_001116365.1. NM_001122893.1. [P39688-1]
NP_032080.2. NM_008054.2. [P39688-2]
XP_006512602.1. XM_006512539.1. [P39688-1]
XP_006512603.1. XM_006512540.1. [P39688-1]
UniGeneMm.4848.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UF4X-ray1.98A82-244[»]
ProteinModelPortalP39688.
SMRP39688. Positions 81-537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199773. 12 interactions.
DIPDIP-198N.
IntActP39688. 34 interactions.
MINTMINT-85422.

Chemistry

BindingDBP39688.
ChEMBLCHEMBL4517.

PTM databases

PhosphoSiteP39688.

Proteomic databases

PaxDbP39688.
PRIDEP39688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843. [P39688-2]
ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843. [P39688-1]
ENSMUST00000126486; ENSMUSP00000115233; ENSMUSG00000019843. [P39688-2]
ENSMUST00000135242; ENSMUSP00000117111; ENSMUSG00000019843. [P39688-2]
ENSMUST00000146287; ENSMUSP00000114188; ENSMUSG00000019843. [P39688-2]
GeneID14360.
KEGGmmu:14360.
UCSCuc007evx.2. mouse. [P39688-1]
uc007evy.2. mouse. [P39688-2]

Organism-specific databases

CTD2534.
MGIMGI:95602. Fyn.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00620000087702.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP39688.
KOK05703.
OMASHNSGYR.
TreeFamTF351634.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.
REACT_194409. Developmental Biology.

Gene expression databases

ArrayExpressP39688.
BgeeP39688.
CleanExMM_FYN.
GenevestigatorP39688.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFYN. mouse.
NextBio285821.
PROP39688.
SOURCESearch...

Entry information

Entry nameFYN_MOUSE
AccessionPrimary (citable) accession number: P39688
Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: April 3, 2013
Last modified: July 9, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot