| Tag | Content |
|---|
| EKPD ID | EKS-RAN-00379 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TK/Src | 449.9 | 2.7E-135 | 271 | 519 | 249 |
|
| Status | Reviewed |
| Ensembl Protein | ENSRNOP00000000733 |
| UniProt Accession | Q62844; |
| Protein Name | Tyrosine-protein kinase Fyn |
| Protein Synonyms/Alias | Proto-oncogene c-Fyn; p59-Fyn; |
| Gene Name | Fyn |
| Gene Synonyms/Alias | Fyn; |
| Ensembl Information | |
| Organism | Rattus norvegicus |
| Functional Description | Non-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 (By similarity). |
| Protein Length | 537 |
Protein Sequence
(FASTA) | | MGCVQCKDKE AAKLTEERDG 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 PTFEYLQGFL EDYFTATEPQ YQPGENL 537 |
|
Nucleotide Sequence
(FASTA) | | ATGGGCTGTG TGCAATGTAA GGATAAAGAA GCAGCGAAAC TGACGGAGGA GAGGGACGGC 60 | | AGCCTGAACC AGAGCTCTGG GTACCGCTAT GGCACAGACC CCACCCCTCA GCACTACCCC 120 | | AGCTTCGGTG TGACCTCCAT CCCGAACTAC AACAACTTCC ACGCAGCCGG GGGCCAGGGA 180 | | CTCACGGTCT TTGGGGGTGT GAACTCCTCC TCTCACACCG GGACCCTGCG TACTAGAGGA 240 | | GGGACAGGAG TGACACTATT TGTGGCACTT TATGACTATG AAGCACGGAC AGAAGATGAC 300 | | CTGAGTTTTC ACAAAGGAGA AAAATTTCAA ATATTGAACA GCTCGGAAGG AGACTGGTGG 360 | | GAAGCCCGCT CCTTGACAAC TGGGGAAACT GGTTACATTC CTAGCAACTA CGTGGCTCCA 420 | | GTTGACTCCA TCCAGGCAGA AGAGTGGTAC TTTGGAAAAC TTGGCCGCAA GGATGCTGAG 480 | | AGACAGCTCC TGTCCTTTGG AAACCCAAGA GGTACCTTTC TTATCCGCGA GAGCGAAACC 540 | | ACCAAAGGTG CCTACTCCCT CTCCATCCGA GACTGGGACG ACATGAAGGG AGACCACGTC 600 | | AAACATTACA AAATCCGCAA GCTTGACAAC GGCGGGTACT ACATCACCAC GAGGGCCCAG 660 | | TTTGAGACCC TTCAGCAGCT TGTACAGCAT TACTCAGAGA GAGCCGCGGG TCTCTGCTGC 720 | | CGTCTAGTAG TTCCCTGTCA CAAAGGGATG CCAAGGCTTA CCGATCTGTC TGTCAAAACC 780 | | AAAGATGTCT GGGAAATCCC TCGAGAATCC CTGCAGTTGA TCAAGAGACT GGGAAATGGG 840 | | CAGTTTGGGG AAGTATGGAT GGGTACCTGG AATGGAAACA CAAAAGTAGC CATAAAGACT 900 | | CTTAAGCCAG GCACAATGTC CCCGGAATCC TTCCTGGAGG AAGCACAGAT CATGAAGAAG 960 | | CTGAAGCACG ACAAGCTGGT GCAGCTCTAT GCAGTTGTGT CCGAAGAGCC CATTTACATT 1020 | | GTCACGGAAT ACATGAACAA AGGAAGTTTG CTCGACTTCT TAAAAGACGG TGAAGGACGG 1080 | | GCTCTGAAAT TGCCAAACCT CGTGGACATG GCGGCACAGG TTGCTGCAGG AATGGCTTAC 1140 | | ATCGAACGCA TGAATTATAT CCACAGAGAT CTGCGGTCAG CTAACATTCT GGTGGGGAAC 1200 | | GGACTCATTT GCAAGATTGC TGACTTCGGA TTGGCCCGGT TGATTGAAGA CAATGAGTAC 1260 | | ACAGCCAGAC AAGGTGCAAA GTTTCCCATT AAGTGGACAG CCCCCGAAGC GGCCCTGTAT 1320 | | GGAAGGTTCA CAATCAAGTC TGACGTGTGG TCCTTTGGAA TCTTACTCAC AGAGCTGGTC 1380 | | ACCAAAGGCA GAGTGCCGTA CCCAGGCATG AACAACCGTG AGGTGCTGGA GCAGGTGGAG 1440 | | AGAGGCTACA GGATGCCCTG CCCGCAGGAC TGCCCGATCT CCCTGCACGA GCTCATGATC 1500 | | CACTGCTGGA AAAAGGATCC GGAGGAGCGC CCCACTTTCG AGTACTTGCA GGGCTTCCTG 1560 | | GAGGACTACT TTACCGCCAC AGAGCCCCAG TATCAGCCCG GTGAAAACCT GTGA 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 rPtfetlqev 250 | rPtfe+lq + | Q: 510 RPTFEYLQGF 519 | *******976 |
|
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 | | PTFEYLQGF 249 |
|
| Keyword | ATP-binding; Cell membrane; Complete proteome; Developmental protein; Kinase; Lipoprotein; Manganese; Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
| InterPros | |
| Pfam | |
| SMARTs | |
| Prosites | |
| Prints | |
| Created Date | 20-Feb-2013 |