P06241 (FYN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fyn
EC=2.7.10.2

Alternative name(s):
Proto-oncogene Syn
Proto-oncogene c-Fyn
Src-like kinase
Short name=SLK
p59-Fyn

Gene names

Name:

FYN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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	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. Ref.3 Ref.12 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.33 Ref.35 Ref.38 Ref.39 Ref.44 Ref.45 Ref.48
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.
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 (via SH2 domain) with CSF1R (tyrosine phosphorylated) By similarity. Interacts with TOM1L1 (phosphorylated form). Interacts with KDR (tyrosine phosphorylated) By similarity. Interacts with SH2D1A and SLAMF1. Interacts (via its SH3 domain) with HEV ORF3 protein. Interacts with ITCH; the interaction phosphorylates ITCH and negatively regulates 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. Ref.10 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.31 Ref.34 Ref.43 Ref.48
Subcellular location	Cell membrane. Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking. Ref.23
Tissue specificity	Isoform 1 is highly expressed in the brain. Isoform 2 is expressed in cells of hemopoietic lineages, especially T lymphocytes. Ref.16
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 By similarity. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ref.8 Ref.9 Ref.12 Ref.16 Ref.19 Ref.20 Ref.24 Ref.25 Ref.26 Ref.28 Ref.30 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.44 Ref.45 Ref.46 Ref.47 Palmitoylation at Cys-3 and Cys-6 regulates subcellular location By similarity.
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 process	Adaptive immunity Host-virus interaction Immunity
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	T cell costimulation Traceable author statement. Source: Reactome T cell receptor signaling pathway Inferred from direct assay. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome calcium ion transport Non-traceable author statement Ref.3. Source: UniProtKB feeding behavior Traceable author statement. Source: ProtInc interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein kinase cascade Traceable author statement. Source: ProtInc learning Traceable author statement. Source: ProtInc leukocyte migration Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome regulation of defense response to virus by virus Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome endosome Inferred from direct assay. Source: HGNC plasma membrane Inferred from direct assay. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor binding Inferred from physical interaction Ref.17. Source: UniProtKB glycoprotein binding Inferred from physical interaction. Source: BHF-UCL metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Non-traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O92972	2	EBI-515315,EBI-710506	From a different organism.
	P27958	4	EBI-515315,EBI-706378	From a different organism.
	Q9WMX2	2	EBI-515315,EBI-710918	From a different organism.
ABL2	P42684	2	EBI-515315,EBI-1102694
ARHGAP32	A7KAX9	4	EBI-515315,EBI-308663
ARHGAP33	O14559	2	EBI-515315,EBI-1210010
ASAP1	Q9ULH1	2	EBI-515315,EBI-346622
COBRA1	Q8WX92	2	EBI-515315,EBI-347721
HTR6	P50406	7	EBI-515315,EBI-1182222
KHDRBS1	Q07666	3	EBI-515315,EBI-1364
MAP4K1	Q92918	2	EBI-515315,EBI-881
MED28	Q9H204	5	EBI-515315,EBI-514199
PRICKLE3	O43900	2	EBI-515315,EBI-1751761
PRKCD	Q05655	4	EBI-515315,EBI-704279
PRKCQ	Q04759	7	EBI-515315,EBI-374762
RAPGEF1	Q13905	2	EBI-515315,EBI-976876

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P06241-1)

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: P06241-2)

Also known as: T;

The sequence of this isoform differs from the canonical sequence as follows:
     234-287: RAAGLCCRLV...GNGQFGEVWM → KADGLCFNLT...GQGCFAEVWL

Isoform 3 (identifier: P06241-3)

The sequence of this isoform differs from the canonical sequence as follows:
     233-287: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 537

536

Tyrosine-protein kinase Fyn

PRO_0000088099

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

12

1

Phosphothreonine; by PKC By similarity

Modified residue

15

1

Phosphothreonine Ref.46

Modified residue

21

1

Phosphoserine Ref.36 Ref.37 Ref.40 Ref.41 Ref.42 Ref.46

Modified residue

25

1

Phosphoserine Ref.41

Modified residue

185

1

Phosphotyrosine By similarity

Modified residue

213

1

Phosphotyrosine Ref.32

Modified residue

214

1

Phosphotyrosine Ref.32

Modified residue

254

1

Phosphothreonine By similarity

Modified residue

257

1

Phosphoserine Ref.41

Modified residue

420

1

Phosphotyrosine; by autocatalysis Ref.32 Ref.36 Ref.40 Ref.47

Modified residue

440

1

Phosphotyrosine Ref.32

Modified residue

512

1

Phosphothreonine Ref.46

Modified residue

531

1

Phosphotyrosine; by CSK Ref.8 Ref.9 Ref.41 Ref.46

Lipidation

2

1

N-myristoyl glycine Ref.8

Lipidation

3

1

S-palmitoyl cysteine By similarity

Lipidation

6

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

233 – 287

55

Missing in isoform 3.

VSP_024108

Alternative sequence

234 – 287

54

RAAGL…GEVWM → KADGLCFNLTVIASSCTPQT SGLAKDAWEVARRSLCLEKK LGQGCFAEVWL in isoform 2.

VSP_024110

Natural variant

243

1

V → L in a lung squamous cell carcinoma sample; somatic mutation. Ref.56

VAR_041704

Natural variant

410

1

G → R in a metastatic melanoma sample; somatic mutation. Ref.56

VAR_041705

Natural variant

445

1

I → F.
Corresponds to variant rs1801121 [ dbSNP | Ensembl ].

VAR_014661

Natural variant

506

1

D → E. Ref.56
Corresponds to variant rs28763975 [ dbSNP | Ensembl ].

VAR_041706

Experimental info

Sequence conflict

184

1

A → S in AAA36615. Ref.1

Sequence conflict

437

1

A → R in AAA36615. Ref.1

Sequence conflict

437

1

A → R in AAB33113. Ref.3

Secondary structure

1

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537

Helix Strand Turn

Details...

Beta strand

86 – 91

6

Beta strand

97 – 100

4

Beta strand

108 – 113

6

Beta strand

117 – 124

8

Turn

125 – 127

3

Beta strand

130 – 134

5

Helix

135 – 137

3

Beta strand

138 – 140

3

Helix

144 – 146

3

Beta strand

147 – 150

4

Helix

156 – 164

9

Beta strand

173 – 177

5

Beta strand

179 – 181

3

Beta strand

185 – 192

8

Beta strand

194 – 196

3

Beta strand

198 – 207

10

Beta strand

220 – 223

4

Helix

224 – 233

10

Beta strand

238 – 240

3

Beta strand

263 – 265

3

Helix

268 – 270

3

Beta strand

271 – 278

8

Beta strand

285 – 290

6

Turn

291 – 293

3

Beta strand

294 – 299

6

Turn

303 – 305

3

Helix

308 – 318

11

Beta strand

329 – 333

5

Beta strand

335 – 337

3

Beta strand

339 – 343

5

Helix

350 – 354

5

Beta strand

355 – 357

3

Turn

358 – 360

3

Helix

364 – 383

20

Helix

393 – 395

3

Beta strand

396 – 399

4

Turn

400 – 402

3

Beta strand

403 – 406

4

Beta strand

416 – 418

3

Turn

430 – 432

3

Helix

435 – 438

4

Helix

445 – 460

16

Helix

472 – 481

10

Helix

496 – 502

7

Helix

507 – 509

3

Helix

513 – 521

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 4A1E443A4B5A0977	FASTA	537	60,762
	10 20 30 40 50 60 MGCVQCKDKE ATKLTEERDG 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 VTEYMNKGSL 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 PTFEYLQSFL EDYFTATEPQ YQPGENL
	Isoform 2 (T) [UniParc]. Checksum: FA082D40A24C2802	FASTA	534	60,141
	10 20 30 40 50 60 MGCVQCKDKE ATKLTEERDG 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 YSEKADGLCF 250 260 270 280 290 300 NLTVIASSCT PQTSGLAKDA WEVARRSLCL EKKLGQGCFA EVWLGTWNGN TKVAIKTLKP 310 320 330 340 350 360 GTMSPESFLE EAQIMKKLKH DKLVQLYAVV SEEPIYIVTE YMNKGSLLDF 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 EYLQSFLEDY FTATEPQYQP GENL
	Isoform 3 [UniParc]. Checksum: 055C3965AC5A9135	FASTA	482	54,513
	10 20 30 40 50 60 MGCVQCKDKE ATKLTEERDG 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 YSGTWNGNTK 250 260 270 280 290 300 VAIKTLKPGT MSPESFLEEA QIMKKLKHDK LVQLYAVVSE EPIYIVTEYM NKGSLLDFLK 310 320 330 340 350 360 DGEGRALKLP NLVDMAAQVA AGMAYIERMN YIHRDLRSAN ILVGNGLICK IADFGLARLI 370 380 390 400 410 420 EDNEYTARQG AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELVTKGRV PYPGMNNREV 430 440 450 460 470 480 LEQVERGYRM PCPQDCPISL HELMIHCWKK DPEERPTFEY LQSFLEDYFT ATEPQYQPGE NL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and oncogenic potential of a novel human src-like gene." Kawakami T., Pennington C.Y., Robbins K.C. Mol. Cell. Biol. 6:4195-4201(1986) [PubMed: 3099169] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family." Semba K., Nishizawa M., Miyajima N., Yoshida M.C., Sukegawa J., Yamanashi Y., Sasaki M., Yamamoto T., Toyoshima K. Proc. Natl. Acad. Sci. U.S.A. 83:5459-5463(1986) [PubMed: 3526330] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[3]	"Human p59fyn(T) regulates OKT3-induced calcium influx by a mechanism distinct from PIP2 hydrolysis in Jurkat T cells." Rigley K., Slocombe P., Proudfoot K., Wahid S., Mandair K., Bebbington C. J. Immunol. 154:1136-1145(1995) [PubMed: 7822789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION. Tissue: T-cell.
[4]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 3). Tissue: Blood.
[8]	"In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts." Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P. Oncogene 5:1313-1319(1990) [PubMed: 1699196] [Abstract] Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT TYR-531.
[9]	"Regulation of the p59fyn protein tyrosine kinase by the CD45 phosphotyrosine phosphatase." Mustelin T., Pessa-Morikawa T., Autero M., Gassmann M., Andersson L.C., Gahmberg C.G., Burn P. Eur. J. Immunol. 22:1173-1178(1992) [PubMed: 1533589] [Abstract] Cited for: DEPHOSPHORYLATION AT TYR-531 BY PTPRC.
[10]	"Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells." Prasad K.V., Janssen O., Kapeller R., Raab M., Cantley L.C., Rudd C.E. Proc. Natl. Acad. Sci. U.S.A. 90:7366-7370(1993) [PubMed: 8394019] [Abstract] Cited for: INTERACTION WITH PIK3R1.
[11]	"Dual myristylation and palmitylation of Src family member p59fyn affects subcellular localization." Alland L., Peseckis S.M., Atherton R.E., Berthiaume L., Resh M.D. J. Biol. Chem. 269:16701-16705(1994) [PubMed: 8206991] [Abstract] Cited for: PALMITOYLATION.
[12]	"p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: implications for T-cell costimulation." Raab M., Cai Y.C., Bunnell S.C., Heyeck S.D., Berg L.J., Rudd C.E. Proc. Natl. Acad. Sci. U.S.A. 92:8891-8895(1995) [PubMed: 7568038] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CD28.
[13]	"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes." Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H. J. Biol. Chem. 272:5915-5920(1997) [PubMed: 9038210] [Abstract] Cited for: INTERACTION WITH KIT.
[14]	"Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-containing leukocyte protein 76 and modulates interleukin 2 production." da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E. Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997) [PubMed: 9207119] [Abstract] Cited for: INTERACTION WITH FYB. Tissue: Tonsil.
[15]	"A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth." Wary K.K., Mariotti A., Zurzolo C., Giancotti F.G. Cell 94:625-634(1998) [PubMed: 9741627] [Abstract] Cited for: INTERACTION WITH CAV1.
[16]	"Altered expression of tyrosine kinases of the Src and Syk families in human T-cell leukemia virus type 1-infected T-cell lines." Weil R., Levraud J.P., Dodon M.D., Bessia C., Hazan U., Kourilsky P., Israel A. J. Virol. 73:3709-3717(1999) [PubMed: 10196263] [Abstract] Cited for: TISSUE SPECIFICITY, PHOSPHORYLATION, ALTERNATIVE SPLICING.
[17]	"Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity." Choi S., Park S. Oncogene 18:5413-5422(1999) [PubMed: 10498895] [Abstract] Cited for: INTERACTION WITH EPHA8.
[18]	"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation." Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B. J. Exp. Med. 191:1591-1604(2000) [PubMed: 10790433] [Abstract] Cited for: INTERACTION WITH PAG1.
[19]	"T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase." Huang J., Tilly D., Altman A., Sugie K., Grey H.M. Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000) [PubMed: 11005864] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF VAV1.
[20]	"Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125." Nakamura T., Yamashita H., Takahashi T., Nakamura S. Biochem. Biophys. Res. Commun. 280:1085-1092(2001) [PubMed: 11162638] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SNCA.
[21]	"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK." Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D. J. Biol. Chem. 276:42389-42400(2001) [PubMed: 11518702] [Abstract] Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
[22]	"Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation." Wolf R.M., Wilkes J.J., Chao M.V., Resh M.D. J. Neurobiol. 49:62-78(2001) [PubMed: 11536198] [Abstract] Cited for: FUNCTION.
[23]	"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.
[24]	"p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by Fyn." Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T. Biochem. Biophys. Res. Commun. 306:151-155(2003) [PubMed: 12788081] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ARHGAP32.
[25]	"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: 12640114] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CTNNB1.
[26]	"Regulation of TRPC6 channel activity by tyrosine phosphorylation." Hisatsune C., Kuroda Y., Nakamura K., Inoue T., Nakamura T., Michikawa T., Mizutani A., Mikoshiba K. J. Biol. Chem. 279:18887-18894(2004) [PubMed: 14761972] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TRPC6.
[27]	"Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone guidance." Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I., McFarlane S., Bloch-Gallego E., Lamarche-Vane N. J. Cell Biol. 167:687-698(2004) [PubMed: 15557120] [Abstract] Cited for: FUNCTION.
[28]	"Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein (WASp) tyrosine phosphorylation is required for coupling T cell antigen receptor engagement to WASp effector function and T cell activation." Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A. J. Exp. Med. 199:99-112(2004) [PubMed: 14707117] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF WAS.
[29]	"Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation." Palacios E.H., Weiss A. Oncogene 23:7990-8000(2004) [PubMed: 15489916] [Abstract] Cited for: REVIEW ON FUNCTION.
[30]	"Fyn phosphorylates human MAP-2c on tyrosine 67." Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B. J. Biol. Chem. 280:1962-1970(2005) [PubMed: 15536091] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAP2.
[31]	"Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation." Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C. Mol. Cell 21:135-141(2006) [PubMed: 16387660] [Abstract] Cited for: INTERACTION WITH ITCH, FUNCTION.
[32]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213; TYR-214; TYR-420 AND TYR-440, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[33]	"Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival." Tang X., Feng Y., Ye K. Cell Death Differ. 14:368-377(2007) [PubMed: 16841086] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF AGAP2.
[34]	"Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain." Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G. J. Biol. Chem. 282:36444-36453(2007) [PubMed: 17925405] [Abstract] Cited for: INTERACTION WITH PRMT8.
[35]	"Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA." Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P., Bustelo X.R., Garcia de Herreros A., Dunach M. Mol. Cell. Biol. 27:1745-1757(2007) [PubMed: 17194753] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CTNND1.
[36]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-420, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[37]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[38]	"Regulation of FynT function by dual domain docking on PAG/Cbp." Solheim S.A., Torgersen K.M., Tasken K., Berge T. J. Biol. Chem. 283:2773-2783(2008) [PubMed: 18056706] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PAG1.
[39]	"Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2." Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T., Hattori S. J. Biol. Chem. 283:9177-9186(2008) [PubMed: 18258597] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF KIRREL.
[40]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-420, MASS SPECTROMETRY. Tissue: Platelet.
[41]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-257 AND TYR-531, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[43]	"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening." Voss M., Lettau M., Janssen O. BMC Immunol. 10:53-53(2009) [PubMed: 19807924] [Abstract] Cited for: INTERACTION WITH FASLG.
[44]	"Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and activation of phospholipase C-{gamma}1." Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T., Ohsawa I., Ohta S., Hattori S. J. Biol. Chem. 284:8951-8962(2009) [PubMed: 19179337] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF NPHS1.
[45]	"Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation of collapsin response mediator protein 2 at tyrosine 32." Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y., Nakamura F., Goshima Y. J. Biol. Chem. 284:27393-27401(2009) [PubMed: 19652227] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DPYSL2.
[46]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15; SER-21; THR-512 AND TYR-531, MASS SPECTROMETRY.
[47]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-420, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[48]	"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm." Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C. J. Biol. Chem. 285:10122-10129(2010) [PubMed: 20100835] [Abstract] Cited for: FUNCTION, INTERACTION WITH RUNX3.
[49]	"Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin." Noble M.E.M., Musacchio A., Saraste M., Courtneidge S.A., Wierenga R.K. EMBO J. 12:2617-2624(1993) [PubMed: 7687536] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
[50]	"High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides." Musacchio A., Saraste M., Wilmanns M. Nat. Struct. Biol. 1:546-551(1994) [PubMed: 7664083] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-142.
[51]	"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase." Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C., Waterfield M.D., Campbell I.D., Ladbury J.E. Biochemistry 35:15646-15653(1996) [PubMed: 8961927] [Abstract] Cited for: STRUCTURE BY NMR.
[52]	"Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain." Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J. Cell 85:931-942(1996) [PubMed: 8681387] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 85-141 IN COMPLEX WITH NEF.
[53]	"Solution structure and peptide binding of the SH3 domain from human Fyn." Morton C.J., Pugh D.J.R., Brown E.L.J., Kahmann J.D., Renzoni D.A.C., Campbell I.D. Structure 4:705-714(1996) [PubMed: 8805554] [Abstract] Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
[54]	"The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity." Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D. Structure 5:1313-1323(1997) [PubMed: 9351806] [Abstract] Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
[55]	"SAP couples Fyn to SLAM immune receptors." Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J. Nat. Cell Biol. 5:155-160(2003) [PubMed: 12545174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1 AND SH2D1A.
[56]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-243; ARG-410 AND GLU-506.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14676 mRNA. Translation: AAA36615.1.
M14333 mRNA. Translation: AAC08285.1.
S74774 mRNA. Translation: AAB33113.2.
AB451293 mRNA. Translation: BAG70107.1.
AB451426 mRNA. Translation: BAG70240.1.
Z97989 Genomic DNA. Translation: CAI22300.1.
Z97989 Genomic DNA. Translation: CAI22301.1.
CH471051 Genomic DNA. Translation: EAW48278.1.
CH471051 Genomic DNA. Translation: EAW48281.1.
CH471051 Genomic DNA. Translation: EAW48282.1.
BC032496 mRNA. Translation: AAH32496.1.

IPI

IPI00166845.
IPI00219012.
IPI00640091.

PIR

TVHUSY. A24314.

RefSeq

NP_002028.1. NM_002037.5.
NP_694592.1. NM_153047.3.
NP_694593.1. NM_153048.3.

UniGene

Hs.390567.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A0N	NMR	-	B	82-148	[»]
1AOT	NMR	-	F	143-248	[»]
1AOU	NMR	-	F	143-248	[»]
1AVZ	X-ray	3.00	C	85-140	[»]
1AZG	NMR	-	B	82-148	[»]
1EFN	X-ray	2.50	A/C	86-143	[»]
1FYN	X-ray	2.30	A	81-142	[»]
1G83	X-ray	2.60	A/B	82-245	[»]
1M27	X-ray	2.50	C	84-144	[»]
1NYF	NMR	-	A	82-148	[»]
1NYG	NMR	-	A	82-148	[»]
1SHF	X-ray	1.90	A/B	84-142	[»]
1ZBJ	NMR	-	A	84-141	[»]
2DQ7	X-ray	2.80	X	261-536	[»]
3H0F	X-ray	2.61	A	73-142	[»]
3H0H	X-ray	1.76	A	73-142	[»]
3H0I	X-ray	2.20	A/B	73-142	[»]

ProteinModelPortal

P06241.

SMR

P06241. Positions 84-537.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33876N.

IntAct

P06241. 169 interactions.

MINT

MINT-93594.

STRING

P06241.

PTM databases

PhosphoSite

P06241.

Polymorphism databases

DMDM

125370.

Proteomic databases

PRIDE

P06241.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368667; ENSP00000357656; ENSG00000010810.
ENST00000368678; ENSP00000357667; ENSG00000010810.

GeneID

2534.

KEGG

hsa:2534.

UCSC

uc003pvh.1. human.
uc003pvi.1. human.
uc003pvj.1. human.

Organism-specific databases

CTD

2534.

GeneCards

GC06M111981.

H-InvDB

HIX0006144.

HGNC

HGNC:4037. FYN.

HPA

CAB005034.
CAB018387.
HPA023887.

MIM

137025. gene.

neXtProt

NX_P06241.

PharmGKB

PA28454.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084003.

HOGENOM

HBG755340.

HOVERGEN

HBG008761.

InParanoid

P06241.

OMA

TQSSGYR.

OrthoDB

EOG41ZF9H.

PhylomeDB

P06241.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

alphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinarevpathway. Ephrin A reverse signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
glypican_1pathway. Glypican 1 network.
il2_1pathway. IL2-mediated signaling events.
pdgfrbpathway. PDGFR-beta signaling pathway.
reelinpathway. Reelin signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
syndecan_3_pathway. Syndecan-3-mediated signaling events.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.
REACT_6185. HIV Infection.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P06241.

Bgee

P06241.

CleanEx

HS_FYN.

Genevestigator

P06241.

GermOnline

ENSG00000010810. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

KO

K05703.

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

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

DrugBank

DB01254. Dasatinib.

NextBio

9997.

PMAP-CutDB

P06241.

SOURCE

Search...

Entry information

Entry name

FYN_HUMAN

Accession

Primary (citable) accession number: P06241
Secondary accession number(s): B5BU57 , E1P557, Q16248, Q5R3A6, Q5R3A7, Q8N5D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 161 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.