| Tag | Content |
|---|
| EKPD ID | EKS-GAG-00310 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TK/Src | 447.5 | 1.3E-134 | 267 | 516 | 250 |
|
| Status | Reviewed |
| Ensembl Protein | ENSGALP00000006117 |
| UniProt Accession | P00523; Q90992; Q90993; Q91343; Q91345; Q92013; Q98915; |
| Protein Name | Proto-oncogene tyrosine-protein kinase Src |
| Protein Synonyms/Alias | Proto-oncogene c-Src; pp60c-src; p60-Src; |
| Gene Name | SRC |
| Gene Synonyms/Alias | SRC; |
| Ensembl Information | |
| Organism | Gallus gallus |
| Functional Description | Non-receptor protein tyrosine kinase which is activatedfollowing engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein- coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra- cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA- processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. |
| Protein Length | 533 |
Protein Sequence
(FASTA) | | MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL 60 | | FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL 120 | | AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT 180 | | KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR 240 | | LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG 300 | | TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL 360 | | PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ 420 | | GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR 480 | | MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL 533 |
|
Nucleotide Sequence
(FASTA) | | ATGGGGAGCA GCAAGAGCAA GCCCAAGGAC CCCAGCCAGC GCCGGCGCAG CCTGGAGCCA 60 | | CCCGACAGCA CCCACCACGG GGGATTCCCA GCCTCGCAGA CCCCCAACAA GACAGCAGCC 120 | | CCCGACACGC ACCGCACCCC CAGCCGCTCC TTTGGGACCG TGGCCACCGA GCCCAAGCTC 180 | | TTCGGGGGCT TCAACACTTC TGACACCGTC ACGTCGCCTC AGCGTGCCGG GGCACTGGCT 240 | | GGCGGCGTCA CCACTTTCGT GGCTCTCTAC GACTACGAGT CCCGGACTGA AACGGACTTG 300 | | TCCTTCAAGA AAGGAGAACG CCTGCAGATT GTCAACAACA CGGAAGGTGA CTGGTGGCTG 360 | | GCTCATTCCC TCACTACAGG ACAGACGGGC TACATCCCCA GTAACTATGT CGCGCCCTCA 420 | | GACTCCATCC AGGCTGAAGA GTGGTACTTT GGGAAGATCA CTCGTCGGGA GTCCGAGCGG 480 | | CTGCTGCTCA ACCCCGAAAA CCCCCGGGGA ACCTTCTTGG TCCGGGAGAG CGAGACGACA 540 | | AAAGGTGCCT ATTGCCTCTC CGTTTCTGAC TTTGACAACG CCAAGGGGCT CAATGTGAAG 600 | | CACTACAAGA TCCGCAAGCT GGACAGCGGC GGCTTCTACA TCACCTCACG CACACAGTTC 660 | | AGCAGCCTGC AGCAGCTGGT GGCCTACTAC TCCAAACACG CTGATGGCTT GTGCCACCGC 720 | | CTGACCAACG TCTGCCCCAC GTCCAAGCCC CAGACCCAGG GACTCGCCAA GGACGCGTGG 780 | | GAAATCCCCC GGGAGTCGCT GCGGCTGGAG GTGAAGCTGG GGCAGGGCTG CTTTGGAGAG 840 | | GTCTGGATGG GGACCTGGAA CGGCACCACC AGAGTGGCCA TAAAGACTCT GAAGCCCGGC 900 | | ACCATGTCCC CGGAGGCCTT CCTGCAGGAA GCCCAAGTGA TGAAGAAGCT CCGGCATGAG 960 | | AAGCTGGTTC AGCTGTACGC AGTGGTGTCG GAAGAGCCCA TCTACATCGT CACTGAGTAC 1020 | | ATGAGCAAGG GGAGCCTCCT GGATTTCCTG AAGGGAGAGA TGGGCAAGTA CCTGCGGCTG 1080 | | CCACAGCTCG TCGATATGGC TGCTCAGATT GCATCCGGCA TGGCCTATGT GGAGAGGATG 1140 | | AACTACGTGC ACCGAGACCT GCGGGCGGCC AACATCCTGG TGGGGGAGAA CCTGGTGTGC 1200 | | AAGGTGGCTG ACTTTGGGCT GGCACGCCTC ATCGAGGACA ACGAGTACAC AGCACGGCAA 1260 | | GGTGCCAAGT TCCCCATCAA GTGGACAGCC CCCGAGGCAG CCCTCTATGG CCGGTTCACC 1320 | | ATCAAGTCGG ATGTCTGGTC CTTCGGCATC CTGCTGACTG AGCTGACCAC CAAGGGCCGG 1380 | | GTGCCATACC CAGGGATGGT CAACAGGGAG GTGCTGGACC AGGTGGAGAG GGGCTACCGC 1440 | | ATGCCCTGCC CGCCCGAGTG CCCCGAGTCG CTGCATGACC TCATGTGCCA GTGCTGGCGG 1500 | | AAGGACCCTG AGGAGCGGCC CACTTTTGAG TACCTGCAGG CCTTCCTGGA GGACTACTTC 1560 | | ACCTCGACAG AGCCCCAGTA CCAGCCTGGA GAGAACCTAT AG 1602 |
|
| Domain Profile | S: 1 lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly 60 | l+l+ klG+G+fGevw+g+w+g+++va+ktlk+gt+speafl+eaq++kklrheklv+ly | Q: 267 LRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY 326 | 68999******************************************************* |
| S: 61 avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr 120 | avvse ePiyivte+m+kGslldflk e gk+l+lp+lvd+aaq+a+Gmay+e++n++hr | Q: 327 AVVSE-EPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHR 385 | ****9.****************************************************** |
| S: 121 dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv 180 | dl+a+n+lvge+lv+kvadfGlarlied+eyta++gak+PikWtaPea+ +g+ftiksdv | Q: 386 DLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDV 445 | ************************************************************ |
| S: 181 WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee 240 | WsfGillte++tkG+vPypGm n+evl+qvergyr+p+p ecpe+l++l+++cw+kdpee | Q: 446 WSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEE 505 | ************************************************************ |
| S: 241 rPtfetlqevl 251 | rPtfe+lq++l | Q: 506 RPTFEYLQAFL 516 | *******9876 |
|
Domain Sequence
(FASTA) | | LRLEVKLGQG CFGEVWMGTW NGTTRVAIKT LKPGTMSPEA FLQEAQVMKK LRHEKLVQLY 60 | | AVVSEEPIYI VTEYMSKGSL LDFLKGEMGK YLRLPQLVDM AAQIASGMAY VERMNYVHRD 120 | | LRAANILVGE NLVCKVADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 180 | | SFGILLTELT TKGRVPYPGM VNREVLDQVE RGYRMPCPPE CPESLHDLMC QCWRKDPEER 240 | | PTFEYLQAFL 250 |
|
| Keyword | 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Endosome; Immunity; Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; S-nitrosylation; 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 |