Reviewed, UniProtKB/Swiss-Prot P39688 (FYN_MOUSE)

Names and origin

Protein names

Recommended name:
    Proto-oncogene tyrosine-protein kinase Fyn
    EC=2.7.10.2
Alternative name(s):
    p59-Fyn

Gene names

Name:

Fyn

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Gene Ontology (GO)
Biological process	activated T cell proliferation Inferred from mutant phenotype. Source: MGI cell surface receptor linked signal transduction Inferred from direct assay. 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 component	cytosol Inferred from Experiment. Source: Reactome plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dynlt1	P51807	2	EBI-524514,EBI-642797
Hcls1	P49710	1	EBI-524514,EBI-924601
Khdrbs1	Q60749	4	EBI-524514,EBI-519077
MED28	Q9H204	1	EBI-524514,EBI-514199	From a different organism.
Med28	Q920D3	1	EBI-524514,EBI-309215
Snx26	Q80YF9	1	EBI-524514,EBI-1210140
Sphk2	Q9JIA7	2	EBI-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
     240-283: CRLVVPCHKG...IKRLGNGQFG → FNLTVVSSSC...EKKLGQGCFA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 537	536	Proto-oncogene tyrosine-protein kinase Fyn		PRO_0000088100
Regions
	Domain	82 – 143	62	SH3
	Domain	149 – 246	98	SH2
	Domain	271 – 524	254	Protein kinase
	Nucleotide binding	277 – 285	9	ATP By similarity
Sites
	Active site	390	1	Proton acceptor By similarity
	Binding site	299	1	ATP By similarity
Amino acid modifications
	Modified residue	21	1	Phosphoserine
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	185	1	Phosphotyrosine Ref.16
	Modified residue	213	1	Phosphotyrosine By similarity
	Modified residue	214	1	Phosphotyrosine By similarity
	Modified residue	254	1	Phosphothreonine Ref.18
	Modified residue	257	1	Phosphoserine Ref.18
	Modified residue	420	1	Phosphotyrosine; by autocatalysis Ref.6 Ref.17
	Modified residue	440	1	Phosphotyrosine By similarity
	Modified residue	531	1	Phosphotyrosine Ref.6 Ref.16
	Lipidation	2	1	N-myristoyl glycine
	Lipidation	3	1	S-palmitoyl cysteine Ref.7 Ref.8 Ref.12
	Lipidation	6	1	S-palmitoyl cysteine Probable
Natural variations
	Alternative sequence	234 – 236	3	RAA → KAD in isoform 2.		VSP_024111
	Alternative sequence	240 – 283	44	CRLVV…NGQFG → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF A in isoform 2.		VSP_024112
Experimental info
	Mutagenesis	2	1	G → A: Abolishes myristoylation and palmitoylation. Ref.8
	Mutagenesis	3	1	C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. Ref.7 Ref.8 Ref.12
	Mutagenesis	3	1	C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. Ref.7 Ref.8 Ref.12
	Mutagenesis	6	1	C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. Ref.7 Ref.8
	Mutagenesis	6	1	C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. Ref.7 Ref.8
	Sequence conflict	179	1	Q → E in BAE42585. Ref.3
	Sequence conflict	179	1	Q → E in AAH92217. Ref.4
	Sequence conflict	179	1	Q → E in AAH32149. Ref.4
	Sequence conflict	287	1	L → M in BAE33766. Ref.3
	Sequence conflict	432	1	W → R in BAE42585. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) [UniParc]. Last modified April 3, 2007. Version 3. Checksum: 50B21D7FB58E2345	FASTA	537	60,656
	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
	Isoform 2 (T). Checksum: E0C0703F15A6641B	FASTA	534	60,058
	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 YSEKADGLCF 250 260 270 280 290 300 NLTVVSSSCT PQTSGLAKDA WEVARDSLFL EKKLGQGCFA EVWLGTWNGN TKVAIKTLKP 310 320 330 340 350 360 GTMSPESFLE EAQIMKKLKH DKLVQLYAVV SEEPIYIVTE YMSKGSLLDF LKDGEGRALK 370 380 390 400 410 420 LPNLVDMAAQ VAAGMAYIER MNYIHRDLRS ANILVGNGLI CKIADFGLAR LIEDNEYTAR 430 440 450 460 470 480 QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR EVLEQVERGY 490 500 510 520 530 RMPCPQDCPI SLHELMIHCW KKDPEERPTF EYLQGFLEDY FTATEPQYQP GENL

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00322097. IPI00762435.
PIR	A44991.
RefSeq	NP_001116364.1. NP_001116365.1. NP_032080.2.
UniGene	Mm.4848
3D structure databases
HSSP	HSSP built from PDB template 1FYN based on UniProtKB P06241.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:198N.
IntAct	P39688. 13 interactions.
STRING	P39688.
PTM databases
PhosphoSite	P39688.
Proteomic databases
PRIDE	P39688.
Genome annotation databases
Ensembl	ENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843; Mus musculus. [Genome view] ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843; Mus musculus. [Genome view]
GeneID	14360.
KEGG	mmu:14360.
UCSC	uc007evx.1. mouse. uc007evy.1. mouse. uc007evz.1. mouse.
Organism-specific databases
CTD	14360.
MGI	MGI:95602. Fyn.
Phylogenomic databases
HOVERGEN	P39688.
Enzyme and pathway databases
BRENDA	2.7.10.2. 244.
Gene expression databases
ArrayExpress	P39688.
Bgee	P39688.
CleanEx	MM_FYN.
Genevestigator	P39688.
GermOnline	ENSMUSG00000019843. Mus musculus.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR000980. SH2. IPR001452. SH3_domain. IPR020473. SH3_region. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	PS00107. 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]
ProtoNet	Search...
Other Resources
NextBio	285821.
SOURCE	Search...

Entry information

Entry name

FYN_MOUSE

Accession

Primary (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:	October 13, 2009
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)