EKS-HOS-00371
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00371
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
TK/Src451.34.4E-135271520250
StatusReviewed
Ensembl ProteinENSP00000346671
UniProt AccessionP06241; B5BU57; E1P557; H0UI48; Q16248; Q5R3A6; Q5R3A7; Q8N5D7;
Protein NameTyrosine-protein kinase Fyn
Protein Synonyms/Alias Proto-oncogene Syn; Proto-oncogene c-Fyn; Src-like kinase; SLK; p59-Fyn;
Gene NameFYN
Gene Synonyms/Alias FYN;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000010810ENSP00000348295ENST00000356013
ENSG00000010810ENSP00000428493ENST00000524310
ENSG00000010810ENSP00000429992ENST00000523574
ENSG00000010810ENSP00000428042ENST00000521062
ENSG00000010810ENSP00000429813ENST00000518630
ENSG00000010810ENSP00000357671ENST00000368682
ENSG00000010810ENSP00000440646ENST00000538466
ENSG00000010810ENSP00000429590ENST00000462598
ENSG00000010810ENSP00000428695ENST00000518295
ENSG00000010810ENSP00000445439ENST00000544792
ENSG00000010810ENSP00000229470ENST00000229470
ENSG00000010810ENSP00000229471ENST00000229471
ENSG00000010810ENSP00000428045ENST00000523570
ENSG00000010810ENSP00000429294ENST00000520518
ENSG00000010810ENSP00000430455ENST00000487824
ENSG00000010810ENSP00000346671ENST00000354650
ENSG00000010810ENSP00000427993ENST00000462856
ENSG00000010810ENSP00000430364ENST00000523238
ENSG00000010810ENSP00000429866ENST00000517419
ENSG00000010810ENSP00000357656ENST00000368667
ENSG00000010810ENSP00000357667ENST00000368678
ENSG00000010810ENSP00000428983ENST00000484067
OrganismHomo sapiens
Functional DescriptionNon-receptor tyrosine-protein kinase that plays a rolein 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.
Protein Length537
Protein Sequence
(FASTA)
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 60
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 120
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 180
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 240
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 300
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR 360
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 420
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 480
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL 537
Nucleotide Sequence
(FASTA)
ATGGGCTGTG TGCAATGTAA GGATAAAGAA GCAACAAAAC TGACGGAGGA GAGGGACGGC 60
AGCCTGAACC AGAGCTCTGG GTACCGCTAT GGCACAGACC CCACCCCTCA GCACTACCCC 120
AGCTTCGGTG TGACCTCCAT CCCCAACTAC AACAACTTCC ACGCAGCCGG GGGCCAAGGA 180
CTCACCGTCT TTGGAGGTGT GAACTCTTCG TCTCATACGG GGACCTTGCG TACGAGAGGA 240
GGAACAGGAG TGACACTCTT TGTGGCCCTT TATGACTATG AAGCACGGAC AGAAGATGAC 300
CTGAGTTTTC ACAAAGGAGA AAAATTTCAA ATATTGAACA GCTCGGAAGG AGATTGGTGG 360
GAAGCCCGCT CCTTGACAAC TGGAGAGACA GGTTACATTC CCAGCAATTA TGTGGCTCCA 420
GTTGACTCTA TCCAGGCAGA AGAGTGGTAC TTTGGAAAAC TTGGCCGAAA AGATGCTGAG 480
CGACAGCTAT TGTCCTTTGG AAACCCAAGA GGTACCTTTC TTATCCGCGA GAGTGAAACC 540
ACCAAAGGTG CCTATTCACT TTCTATCCGT GATTGGGATG ATATGAAAGG AGACCATGTC 600
AAACATTATA AAATTCGCAA ACTTGACAAT GGTGGATACT ACATTACCAC CCGGGCCCAG 660
TTTGAAACAC TTCAGCAGCT TGTACAACAT TACTCAGAGA GAGCTGCAGG TCTCTGCTGC 720
CGCCTAGTAG TTCCCTGTCA CAAAGGGATG CCAAGGCTTA CCGATCTGTC TGTCAAAACC 780
AAAGATGTCT GGGAAATCCC TCGAGAATCC CTGCAGTTGA TCAAGAGACT GGGAAATGGG 840
CAGTTTGGGG AAGTATGGAT GGGTACCTGG AATGGAAACA CAAAAGTAGC CATAAAGACT 900
CTTAAACCAG GCACAATGTC CCCCGAATCA TTCCTTGAGG AAGCGCAGAT CATGAAGAAG 960
CTGAAGCACG ACAAGCTGGT CCAGCTCTAT GCAGTGGTGT CTGAGGAGCC CATCTACATC 1020
GTCACCGAGT ATATGAACAA AGGAAGTTTA CTGGATTTCT TAAAAGATGG AGAAGGAAGA 1080
GCTCTGAAAT TACCAAATCT TGTGGACATG GCAGCACAGG TGGCTGCAGG AATGGCTTAC 1140
ATCGAGCGCA TGAATTATAT CCATAGAGAT CTGCGATCAG CAAACATTCT AGTGGGGAAT 1200
GGACTCATAT GCAAGATTGC TGACTTCGGA TTGGCCCGAT TGATAGAAGA CAATGAGTAC 1260
ACAGCAAGAC AAGGTGCAAA GTTCCCCATC AAGTGGACGG CCCCCGAGGC AGCCCTGTAC 1320
GGGAGGTTCA CAATCAAGTC TGACGTGTGG TCTTTTGGAA TCTTACTCAC AGAGCTGGTC 1380
ACCAAAGGAA GAGTGCCATA CCCAGGCATG AACAACCGGG AGGTGCTGGA GCAGGTGGAG 1440
CGAGGCTACA GGATGCCCTG CCCGCAGGAC TGCCCCATCT CTCTGCATGA GCTCATGATC 1500
CACTGCTGGA AAAAGGACCC TGAAGAACGC CCCACTTTTG AGTACTTGCA GAGCTTCCTG 1560
GAAGACTACT TTACCGCGAC AGAGCCCCAG TACCAACCTG GTGAAAACCT GTAA 1614
Domain Profile
S: 1     lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly  60
         l+l+k+lG+GqfGevw+g+w+g++kva+ktlk+gt+spe+fleeaqi+kkl+h+klv+ly
Q: 271   LQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLY  330
         689*********************************************************
S: 61    avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr  120
         avvse ePiyivte+m+kGslldflk+ eg++lklp+lvd+aaqva+Gmay+e++n+ihr
Q: 331   AVVSE-EPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHR  389
         ****9.******************************************************
S: 121   dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv  180
         dl+++n+lvg+ l++k+adfGlarlied+eyta++gak+PikWtaPea+ +g+ftiksdv
Q: 390   DLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDV  449
         ************************************************************
S: 181   WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee  240
         WsfGillte+vtkG+vPypGm+n+evleqvergyr+p+p++cp +l+el+++cwkkdpee
Q: 450   WSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEE  509
         ************************************************************
S: 241   rPtfetlqevl  251
         rPtfe+lq++l
Q: 510   RPTFEYLQSFL  520
         ********986
Domain Sequence
(FASTA)
LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT LKPGTMSPES FLEEAQIMKK LKHDKLVQLY 60
AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR ALKLPNLVDM AAQVAAGMAY IERMNYIHRD 120
LRSANILVGN GLICKIADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 180
SFGILLTELV TKGRVPYPGM NNREVLEQVE RGYRMPCPQD CPISLHELMI HCWKKDPEER 240
PTFEYLQSFL 250
Keyword3D-structure; Adaptive immunity; Alternative splicing; ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Developmental protein; Host-virus interaction; Immunity; Kinase; Lipoprotein; Manganese; Membrane; Metal-binding; Myristate; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Choloepus hoffmanni"; ?>Danio rerio"; ?>Dasypus novemcinctus"; ?>Drosophila melanogaster"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Tupaia belangeri"; ?>Tursiops truncatus"; ?>Vicugna pacos"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00339
EKS-ANC-00354
EKS-BOT-00365
EKS-CAE-00300
EKS-CAJ-00369
EKS-CAF-00366
EKS-CAP-00398
EKS-CHH-00039
EKS-DAR-00744
EKS-DAN-00035
EKS-DRM-00174
EKS-EQC-00367
EKS-FEC-00353
EKS-GAM-00219
EKS-GAG-00309
EKS-GAA-00446
EKS-GOG-00358
EKS-ICT-00346
EKS-LAC-00380
EKS-LOA-00374
EKS-MAM-00365
EKS-MEG-00300
EKS-MOD-00354
EKS-MUM-00397
EKS-MUP-00359
EKS-MYL-00364
EKS-NOL-00335
EKS-ORN-00470
EKS-ORA-00320
EKS-ORC-00343
EKS-ORL-00432
EKS-OTG-00370
EKS-PAT-00345
EKS-PES-00325
EKS-POA-00355
EKS-PRC-00071
EKS-PTV-00093
EKS-RAN-00379
EKS-SAH-00336
EKS-SUS-00322
EKS-TAG-00440
EKS-TAR-00466
EKS-TEN-00462
EKS-TUB-00053
EKS-TUT-00097
EKS-VIP-00051
EKS-XET-00483
EKS-XIM-00460
Gene Ontology
GO:0005829; C:cytosol
GO:0005768; C:endosome
GO:0005739; C:mitochondrion
GO:0005886; C:plasma membrane
GO:0005524; F:ATP binding
GO:0046872; F:metal ion binding
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity
GO:0050798; P:activated T cell proliferation
GO:0007411; P:axon guidance
GO:0006816; P:calcium ion transport
GO:0071363; P:cellular response to growth factor stimulus
GO:0071375; P:cellular response to peptide hormone stimulus
GO:0048813; P:dendrite morphogenesis
GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain
GO:0007631; P:feeding behavior
GO:0030900; P:forebrain development
GO:0007243; P:intracellular protein kinase cascade
GO:0007612; P:learning
GO:0050900; P:leukocyte migration
GO:0010629; P:negative regulation of gene expression
GO:0042177; P:negative regulation of protein catabolic process
GO:0001764; P:neuron migration
GO:0018108; P:peptidyl-tyrosine phosphorylation
GO:0030168; P:platelet activation
GO:0046777; P:protein autophosphorylation
GO:0008360; P:regulation of cell shape
GO:0050690; P:regulation of defense response to virus by virus
GO:0042493; P:response to drug
GO:0045471; P:response to ethanol
GO:0031295; P:T cell costimulation
GO:0050852; P:T cell receptor signaling pathway
GO:0016032; P:viral reproduction
GO:0019048; P:virus-host interaction
KEGG
hsa:2534;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
IPR000980; SH2.
IPR001452; SH3_domain.
IPR008266; Tyr_kinase_AS.
IPR020635; Tyr_kinase_cat_dom.
Pfam
PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
SMARTs
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
Prosites
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
Prints
PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
Created Date20-Feb-2013