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Reviewed, UniProtKB/Swiss-Prot P39688 (FYN_MOUSE)

Last modified February 9, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Proto-oncogene 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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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General annotation (Comments)

Function

Implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels, with isoform 2 showing the greater ability to mobilize cytoplasmic calcium in comparison to isoform 1. 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. Ref.10

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.6

Subunit structure

Interacts with PAG1 By similarity. Interacts with SH2D1A and SLAMF1 By similarity. Associates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase. Interacts with the FYN-binding protein (FYB). Interacts with phosphorylated TOM1L1. Interacts with CD79A upon activation of the B-cell antigen receptor which increases FYN activity. Interacts with SH2D1A and SLAMF1. Interacts (via SH3 domain) with PRMT8 By similarity. Ref.9 Ref.13

Subcellular location

Cell membrane. Note: Present and active in lipid rafts. Present in cell body and along the process of mature and developing oligodendroyctes. Ref.14 Ref.15

Tissue specificity

Isoform 1 is highly expressed in the brain, isoform 2 is expressed in cells of hemopoietic lineages, especially T lymphocytes. Ref.10 Ref.5

Post-translational modification

It is uncertain whether palmitoylation is on Cys-3 and/or Cys-6.

Myristoylation is required prior to palmitoylation.

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

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.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   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
Gene Ontology (GO)
   Biological processactivated T cell proliferation

Inferred from mutant phenotype. Source: MGI

detection of mechanical stimulus involved in sensory perception of pain

Inferred from mutant phenotype. Source: MGI

forebrain development

Inferred from mutant phenotype. Source: MGI

myelination

Traceable author statement. Source: MGI

neuron migration

Inferred from mutant phenotype. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from direct assay. Source: MGI

protein amino acid autophosphorylation

Inferred from direct assay. Source: MGI

regulation of cell shape

Inferred from direct assay. Source: MGI

response to ethanol

Inferred from genetic interaction. Source: MGI

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: EC

tubulin binding

Inferred from direct assay. Source: MGI

Complete GO annotation...

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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
     240-283: CRLVVPCHKG...IKRLGNGQFG → FNLTVVSSSC...EKKLGQGCFA

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 537536Proto-oncogene tyrosine-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
Modified residue251Phosphoserine By similarity
Modified residue1851Phosphotyrosine Ref.16
Modified residue2131Phosphotyrosine By similarity
Modified residue2141Phosphotyrosine By similarity
Modified residue2541Phosphothreonine Ref.18
Modified residue2571Phosphoserine Ref.18
Modified residue4201Phosphotyrosine; by autocatalysis Ref.6 Ref.17
Modified residue4401Phosphotyrosine By similarity
Modified residue5121Phosphothreonine By similarity
Modified residue5311Phosphotyrosine Ref.6 Ref.16
Lipidation21N-myristoyl glycine Ref.11
Lipidation31S-palmitoyl cysteine Ref.7 Ref.8 Ref.12
Lipidation61S-palmitoyl cysteine Probable

Natural variations

Alternative sequence234 – 2363RAA → KAD in isoform 2.
VSP_024111
Alternative sequence240 – 28344CRLVV…NGQFG → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF A in isoform 2.
VSP_024112

Experimental info

Mutagenesis21G → A: Abolishes myristoylation and palmitoylation. Ref.8
Mutagenesis31C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. Ref.7 Ref.8 Ref.12
Mutagenesis31C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. Ref.7 Ref.8 Ref.12
Mutagenesis61C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. Ref.7 Ref.8
Mutagenesis61C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. Ref.7 Ref.8
Sequence conflict1791Q → E in BAE42585. Ref.3
Sequence conflict1791Q → E in AAH92217. Ref.4
Sequence conflict1791Q → E in AAH32149. Ref.4
Sequence conflict2871L → M in BAE33766. Ref.3
Sequence conflict4321W → R in BAE42585. Ref.3

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Sequences

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

Last modified April 3, 2007. Version 3.
Checksum: 50B21D7FB58E2345

FASTA53760,656
        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 GTFLIRESQT 

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

       250        260        270        280        290        300 
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWLGTW 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).

Checksum: E0C0703F15A6641B
Show »

FASTA53460,058

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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: 2488273] [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: 9895129] [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: 16141072] [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: 15489334] [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: 1361685] [Abstract]
Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]"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: 8441403] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-531, AUTOPHOSPHORYLATION AT TYR-420, ENZYME REGULATION.
[7]"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: 8413237] [Abstract]
Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF CYS-3 AND CYS-6.
[8]"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: 7980442] [Abstract]
Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-6.
[9]"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: 8168489] [Abstract]
Cited for: INTERACTION WITH CD79A.
[10]"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: 8007959] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]"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: 8655574] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2.
[12]"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: 9201723] [Abstract]
Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF CYS-3.
[13]"'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: 11711534] [Abstract]
Cited for: INTERACTION WITH TOM1L1.
[14]"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: 12218089] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[15]"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: 14645715] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"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: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, MASS SPECTROMETRY.
Tissue: Brain.
[17]"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: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-420, MASS SPECTROMETRY.
Tissue: Macrophage.
[18]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-257, MASS SPECTROMETRY.
+Additional computationally mapped references.

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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.
IPIIPI00322097.
IPI00762435.
PIRA44991.
RefSeqNP_001116364.1.
NP_001116365.1.
NP_032080.2.
UniGeneMm.4848

3D structure databases

SMRP39688. Positions 81-142, 84-537.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-198N.
IntActP39688. 13 interactions.
STRINGP39688.

PTM databases

PhosphoSiteP39688.

Proteomic databases

PRIDEP39688.

Genome annotation databases

EnsemblENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843; Mus musculus. [Genome view]
ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843; Mus musculus. [Genome view]
GeneID14360.
KEGGmmu:14360.
UCSCuc007evz.1. mouse.

Organism-specific databases

CTD14360.
MGIMGI:95602. Fyn.

Phylogenomic databases

eggNOGroNOG12442.
HOGENOMHBG755340.
HOVERGENP39688.
InParanoidP39688.

Enzyme and pathway databases

BRENDA2.7.10.2. 244.

Gene expression databases

ArrayExpressP39688.
BgeeP39688.
CleanExMM_FYN.
GenevestigatorP39688.
GermOnlineENSMUSG00000019843. Mus musculus.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
IPR020745. Tyr_kinase_non-rcpt_Fyn.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PANTHERPTHR23256:SF256. Tyr_kinase_non-rcpt_Fyn. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
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 Resources

NextBio285821.
SOURCESearch...

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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, 2007
Last modified: February 9, 2010
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents