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Reviewed, UniProtKB/Swiss-Prot P06241 (FYN_HUMAN)

Last modified February 9, 2010. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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
    Proto-oncogene Syn
    SLK
Gene names
Name: FYN
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.3 Ref.14

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

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 By similarity. Interacts with PAG1. Interacts (via SH3 domain) with PRMT8. Interacts with SH2D1A and SLAMF1. Interacts (via SH3 domain) with HEV ORF3 protein. Ref.11 Ref.12 Ref.16

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.13

Tissue specificity

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

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
   Biological processHost-virus interaction
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   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
Gene Ontology (GO)
   Biological processT cell receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

calcium ion transport Ref.3

Non-traceable author statement. Source: UniProtKB

feeding behavior

Traceable author statement. Source: ProtInc

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

learning

Traceable author statement. Source: ProtInc

protein kinase cascade

Traceable author statement. Source: ProtInc

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

endosome

Inferred from direct assay. Source: HGNC

plasma membrane

Inferred from direct assay. Source: HGNC

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycoprotein binding

Inferred from physical interaction. Source: UniProtKB

identical protein binding

Inferred from physical interaction. Source: IntAct

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity Ref.3

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-515315,EBI-515315
O929722EBI-515315,EBI-710506From a different organism.
P266601EBI-515315,EBI-706322From a different organism.
P279584EBI-515315,EBI-706378From a different organism.
Q9WMX22EBI-515315,EBI-710918From a different organism.
ABL1P005191EBI-515315,EBI-375543
ABL2P426841EBI-515315,EBI-1102694
AIREO439181EBI-515315,EBI-1753081
AKAP6Q130231EBI-515315,EBI-1056102
APOL5Q9BWW91EBI-515315,EBI-1753592
ARHGEF11O150851EBI-515315,EBI-311099
ASAP1Q9ULH11EBI-515315,EBI-346622
Asap1Q9QWY8-11EBI-515315,EBI-698517From a different organism.
Asap1Q9QWY8-21EBI-515315,EBI-698524From a different organism.
ASAP2O431501EBI-515315,EBI-310968
ASB16Q96NS51EBI-515315,EBI-1751918
BAZ2AQ9UIF91EBI-515315,EBI-934890
BCAR1P569451EBI-515315,EBI-702093
Bcar1Q637671EBI-515315,EBI-1176801From a different organism.
BMP8BP348201EBI-515315,EBI-1752660
BRCA2P515871EBI-515315,EBI-79792
BRPF3Q9ULD41EBI-515315,EBI-1753470
C6P136711EBI-515315,EBI-1753221
CACNA1FO608401EBI-515315,EBI-1757401
CASTP208101EBI-515315,EBI-1268770
CCKBRP322391EBI-515315,EBI-1753137
CCR10P460921EBI-515315,EBI-348022
CD2APQ9Y5K61EBI-515315,EBI-298152
CDC27P302601EBI-515315,EBI-994813
CDKL5O760391EBI-515315,EBI-1752465
CELSR3Q9NYQ71EBI-515315,EBI-308417
CENPAP494501EBI-515315,EBI-1751979
CHAF1AQ131111EBI-515315,EBI-1020839
CKAP5Q140081EBI-515315,EBI-310585
CNTFRP269921EBI-515315,EBI-743758
CNTNAP1P783571EBI-515315,EBI-1751903
COBRA1Q8WX921EBI-515315,EBI-347721
CSMD2Q7Z4081EBI-515315,EBI-1957312
CYP4F2P783291EBI-515315,EBI-1752413
DAB2P980821EBI-515315,EBI-1171238
DAG1Q141181EBI-515315,EBI-1755945
DDX41Q9UJV91EBI-515315,EBI-1046350
DKKL1Q9UK851EBI-515315,EBI-1753048
DLGAP1O144901EBI-515315,EBI-1753207
DLGAP2Q9P1A61EBI-515315,EBI-1753397
DLGAP3O958861EBI-515315,EBI-1752541
DLGAP4Q9Y2H01EBI-515315,EBI-722139
DLX4Q929881EBI-515315,EBI-1752755
DNASE1L2Q928741EBI-515315,EBI-1751995
DNM3Q9UQ161EBI-515315,EBI-1111783
DOCK1Q141851EBI-515315,EBI-446740
DOCK3Q8IZD91EBI-515315,EBI-1752361
DUSP15Q9H1R21EBI-515315,EBI-1752795
EPB41L3Q9Y2J21EBI-515315,EBI-310986
EPS15P425661EBI-515315,EBI-396684
EXTL3O439091EBI-515315,EBI-1754679
F2RL2O002541EBI-515315,EBI-1751853
FAM110AQ9BQ891EBI-515315,EBI-1752811
FANCAO153601EBI-515315,EBI-81570
FASLGP480231EBI-515315,EBI-495538
FCGR2BP319941EBI-515315,EBI-724784
FCGR2CP319951EBI-515315,EBI-1396036
FLNAP213331EBI-515315,EBI-350432
FLNCQ143151EBI-515315,EBI-489954
FOXF2Q129471EBI-515315,EBI-1752316
FYBO151171EBI-515315,EBI-1753267
GABBR1Q9UBS51EBI-515315,EBI-724156
GAD1Q992591EBI-515315,EBI-743184
GNSP155861EBI-515315,EBI-1752200
GP6Q9HCN61EBI-515315,EBI-515278
GPR45Q9Y5Y31EBI-515315,EBI-1751869
GPR63Q9BZJ61EBI-515315,EBI-1757612
GSTZ1O437081EBI-515315,EBI-748043
GTF3AQ926641EBI-515315,EBI-1752104
GUCY2DQ028461EBI-515315,EBI-1756902
HCN2Q9UL511EBI-515315,EBI-1751885
HCN4Q9Y3Q41EBI-515315,EBI-1753521
HDAC6Q9UBN71EBI-515315,EBI-301697
HEXAP068651EBI-515315,EBI-723519
HNRNPRO433901EBI-515315,EBI-713419
HOXC8P312731EBI-515315,EBI-1752118
HTR6P504067EBI-515315,EBI-1182222
IL3RAP269511EBI-515315,EBI-1757512
ISG20L2Q9H9L31EBI-515315,EBI-751335
KHDRBS1Q076662EBI-515315,EBI-1364
LATO435611EBI-515315,EBI-1222766
LRBAP508511EBI-515315,EBI-1052167
LTBP2Q147671EBI-515315,EBI-1546118
MAP4K1Q929181EBI-515315,EBI-881
MAP4K5Q9Y4K41EBI-515315,EBI-1279
MED14O602441EBI-515315,EBI-394489
MED28Q9H2043EBI-515315,EBI-514199
MEPEQ9NQ761EBI-515315,EBI-1753293
MKI67P460131EBI-515315,EBI-876367
MOSP005401EBI-515315,EBI-1757866
NBEAQ8NFP91EBI-515315,EBI-723014
NCKAP5O145131EBI-515315,EBI-1752508
NCKIPSDQ9NZQ31EBI-515315,EBI-957585
NEK8Q86SG61EBI-515315,EBI-1752987
NFASCO948561EBI-515315,EBI-1751948
NFS1Q9Y6971EBI-515315,EBI-1751791
NKX2-1P436991EBI-515315,EBI-1391923
NPVFQ9HCQ71EBI-515315,EBI-1753111
NR5A1Q132851EBI-515315,EBI-874629
ORC1LQ134151EBI-515315,EBI-374847
PAX3P237601EBI-515315,EBI-1167564
PAX7P237591EBI-515315,EBI-1042757
PDIA2Q130871EBI-515315,EBI-1752525
PKD1P981611EBI-515315,EBI-1752013
POLD1P283401EBI-515315,EBI-716569
PPP1R12AO149741EBI-515315,EBI-351726
PPP1R3DO956851EBI-515315,EBI-1045661
PRICKLE3O439001EBI-515315,EBI-1751761
PRKCDQ056553EBI-515315,EBI-704279
PRKCQQ047596EBI-515315,EBI-374762
PRXQ9BXM01EBI-515315,EBI-1753064
PTPN4P290741EBI-515315,EBI-710431
RAPGEF1Q139051EBI-515315,EBI-976876
RICSQ86YL63EBI-515315,EBI-1210177
RIMS1Q86UR51EBI-515315,EBI-1043236
RIMS2Q9UQ261EBI-515315,EBI-1756749
RIN3Q8TB241EBI-515315,EBI-1570523
RP1L1Q8IWN71EBI-515315,EBI-1757848
RPP38P783451EBI-515315,EBI-366493
RRASP103011EBI-515315,EBI-968703
RTN4Q9NQC31EBI-515315,EBI-715945
SCARF2Q96GP61EBI-515315,EBI-1752088
SEMA7AO753261EBI-515315,EBI-1753538
SEPN1Q9NZV51EBI-515315,EBI-1751965
SF3B4Q154271EBI-515315,EBI-348469
SHANK3Q9BYB01EBI-515315,EBI-1752330
SHROOM2Q137961EBI-515315,EBI-1644065
SLC24A1O607211EBI-515315,EBI-1753504
SNX12Q9UMY41EBI-515315,EBI-1752602
SNX17Q150361EBI-515315,EBI-1752620
SNX26O145591EBI-515315,EBI-1210010
SNX3O604931EBI-515315,EBI-727209
SNX8Q9Y5X21EBI-515315,EBI-1752557
SOS1Q078891EBI-515315,EBI-297487
SOS2Q078901EBI-515315,EBI-298181
SP1P080471EBI-515315,EBI-298336
SPHK1Q9NYA11EBI-515315,EBI-985303
Sphk1Q8CI151EBI-515315,EBI-985291From a different organism.
SPHK2Q9NRA01EBI-515315,EBI-985324
Sphk2Q9JIA71EBI-515315,EBI-985434From a different organism.
SUV39H2Q9H5I11EBI-515315,EBI-723127
SYNJ2O150561EBI-515315,EBI-310513
TCF9P163831EBI-515315,EBI-954074
TDRD1Q9BXT41EBI-515315,EBI-1757688
TGOLN2O434931EBI-515315,EBI-1752146
TMPOP421671EBI-515315,EBI-455283
TRAIPQ9BWF21EBI-515315,EBI-1756205
TRIM39Q9HCM91EBI-515315,EBI-739510
TSKSQ9UJT21EBI-515315,EBI-852101
TULP1O002941EBI-515315,EBI-1756778
TULP4Q9NRJ41EBI-515315,EBI-1753487
VPS13AQ96RL71EBI-515315,EBI-1752583
WBP7Q9UMN61EBI-515315,EBI-765774
WIPF1O435161EBI-515315,EBI-346356
WNK2Q9Y3S11EBI-515315,EBI-948521
XRCC1P188871EBI-515315,EBI-947466

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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:
     234-236: RAA → KAD
     240-283: CRLVVPCHKG...IKRLGNGQFG → FNLTVIASSC...EKKLGQGCFA
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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 537536Proto-oncogene tyrosine-protein kinase Fyn
PRO_0000088099

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 residue121Phosphothreonine; by PKC By similarity
Modified residue151Phosphothreonine
Modified residue211Phosphoserine Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Modified residue251Phosphoserine Ref.20
Modified residue1851Phosphotyrosine By similarity
Modified residue2131Phosphotyrosine Ref.15
Modified residue2141Phosphotyrosine Ref.15
Modified residue2541Phosphothreonine By similarity
Modified residue2571Phosphoserine Ref.20
Modified residue4201Phosphotyrosine; by autocatalysis Ref.17 Ref.19 Ref.15 Ref.23
Modified residue4401Phosphotyrosine Ref.15
Modified residue5121Phosphothreonine
Modified residue5311Phosphotyrosine Ref.20 Ref.8
Lipidation21N-myristoyl glycine Ref.8
Lipidation31S-palmitoyl cysteine By similarity
Lipidation61S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence233 – 28755Missing in isoform 3.
VSP_024108
Alternative sequence234 – 2363RAA → KAD in isoform 2.
VSP_024109
Alternative sequence240 – 28344CRLVV…NGQFG → FNLTVIASSCTPQTSGLAKD AWEVARRSLCLEKKLGQGCF A in isoform 2.
VSP_024110
Natural variant2431V → L in a lung squamous cell carcinoma sample; somatic mutation. Ref.31
VAR_041704
Natural variant4101G → R in a metastatic melanoma sample; somatic mutation. Ref.31
VAR_041705
Natural variant4451I → F: dbSNP rs1801121.
VAR_014661
Natural variant5061D → E: dbSNP rs28763975. Ref.31
VAR_041706

Experimental info

Sequence conflict1841A → S in AAA36615. Ref.1
Sequence conflict2871M → L in AAB33113. Ref.3
Sequence conflict2871M → L in CAI22301. Ref.4
Sequence conflict4371A → R in AAA36615. Ref.1
Sequence conflict4371A → R in AAB33113. Ref.3

Secondary structure

1 ................................................................................ 537
Helix Strand Turn

Details...

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Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 4A1E443A4B5A0977

FASTA53760,762
        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

« Hide

Isoform 2 (T).

Checksum: FA082D05A24C28B2
Show »

FASTA53460,159
Isoform 3.

Checksum: 055C3965AC5A9135
Show »

FASTA48254,513

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References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"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: BINDING OF SH3 DOMAIN TO PI 3-KINASE.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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. expand/collapse author list , 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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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: T-cell.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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. expand/collapse author list , 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.

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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.
BC032496 mRNA. Translation: AAH32496.1.
IPIIPI00166845.
IPI00219012.
IPI00640091.
PIRTVHUSY. A24314.
RefSeqNP_002028.1.
NP_694592.1.
NP_694593.1.
UniGeneHs.390567

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0NNMR-B82-148[»]
1AOTNMR-F143-248[»]
1AOUNMR-F143-248[»]
1AVZX-ray3.00C85-140[»]
1AZGNMR-B82-148[»]
1EFNX-ray2.50A/C86-143[»]
1FYNX-ray2.30A81-142[»]
1G83X-ray2.60A/B82-245[»]
1M27X-ray2.50C84-144[»]
1NYFNMR-A82-148[»]
1NYGNMR-A82-148[»]
1SHFX-ray1.90A/B84-142[»]
1ZBJNMR-A84-141[»]
2DQ7X-ray2.80X261-536[»]
SMRP06241. Positions 84-537.
ModBaseSearch...

Protein-protein interaction databases

IntActP06241. 165 interactions.
STRINGP06241.

PTM databases

PhosphoSiteP06241.

Proteomic databases

PRIDEP06241.

Genome annotation databases

EnsemblENST00000368667; ENSP00000357656; ENSG00000010810; Homo sapiens. [Genome view]
ENST00000368678; ENSP00000357667; ENSG00000010810; Homo sapiens. [Genome view]
GeneID2534.
KEGGhsa:2534.
UCSCuc003pvh.1. human.
uc003pvi.1. human.
uc003pvj.1. human.

Organism-specific databases

CTD2534.
GeneCardsGC06M112089.
H-InvDBHIX0006144.
HIX0076254.
HGNCHGNC:4037. FYN.
HPACAB005034.
CAB018387.
HPA023887.
MIM137025. gene.
PharmGKBPA28454.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG755340.
HOVERGENP06241.
InParanoidP06241.
OMATTIPNYN.
OrthoDBEOG9PP12J.
PhylomeDBP06241.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
Pathway_Interaction_DBalphasynuclein_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.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_18266. Axon guidance.
REACT_604. Hemostasis.
REACT_6185. HIV Infection.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP06241.
BgeeP06241.
CleanExHS_FYN.
GenevestigatorP06241.
GermOnlineENSG00000010810. Homo sapiens.

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

DrugBankDB01254. Dasatinib.
NextBio9997.
PMAP-CutDBP06241.
SOURCESearch...

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Entry information

Entry nameFYN_HUMAN
AccessionPrimary (citable) accession number: P06241
Secondary accession number(s): B5BU57 expand/collapse secondary AC list , Q16248, Q5R3A6, Q5R3A7, Q8N5D7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny 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.

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Index of Protein Data Bank (PDB) cross-references

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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