| Tag | Content |
|---|
| EKPD ID | EKS-MUM-00398 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TK/Src | 448.1 | 1.9E-134 | 269 | 518 | 250 |
|
| Status | Reviewed |
| Ensembl Protein | ENSMUSP00000029175 |
| UniProt Accession | P05480; Q2M4I4; |
| Protein Name | Neuronal 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 | Mus musculus |
| 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 such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin- 43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr- 1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta- arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. 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. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling.Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (By similarity). |
| Protein Length | 535 |
Protein Sequence
(FASTA) | | MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS AAFVPPAAEP 60 | | KLFGGFNSSD TVTSPQRAGP LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTEGDW 120 | | WLAHSLSTGQ TGYIPSNYVA PSDSIQAEEW YFGKITRRES ERLLLNAENP RGTFLVRESE 180 | | TTKGAYCLSV SDFDNAKGLN VKHYKIRKLD SGGFYITSRT QFNSLQQLVA YYSKHADGLC 240 | | HRLTTVCPTS KPQTQGLAKD AWEIPRESLR LEVKLGQGCF GEVWMGTWNG TTRVAIKTLK 300 | | PGTMSPEAFL QEAQVMKKLR HEKLVQLYAV VSEEPIYIVT EYMNKGSLLD FLKGETGKYL 360 | | RLPQLVDMSA QIASGMAYVE RMNYVHRDLR AANILVGENL VCKVADFGLA RLIEDNEYTA 420 | | RQGAKFPIKW TAPEAALYGR FTIKSDVWSF GILLTELTTK GRVPYPGMVN REVLDQVERG 480 | | YRMPCPPECP ESLHDLMCQC WRKEPEERPT FEYLQAFLED YFTSTEPQYQ PGENL 535 |
|
Nucleotide Sequence
(FASTA) | | ATGGGCAGCA ACAAGAGCAA GCCCAAGGAC GCCAGCCAGC GGCGCCGCAG CCTGGAGCCC 60 | | TCGGAAAACG TGCACGGGGC AGGGGGCGCC TTCCCGGCCT CACAGACACC GAGCAAGCCC 120 | | GCCTCCGCCG ACGGCCACCG CGGGCCCAGC GCCGCCTTCG TGCCGCCCGC GGCCGAGCCC 180 | | AAGCTCTTCG GAGGCTTCAA CTCCTCGGAC ACCGTCACCT CCCCGCAGAG GGCGGGGCCT 240 | | CTGGCAGGTG GGGTGACCAC CTTTGTGGCC CTCTATGACT ATGAGTCACG GACAGAGACT 300 | | GACCTGTCCT TCAAGAAAGG GGAGCGGCTG CAGATTGTCA ATAACACAGA GGGAGACTGG 360 | | TGGCTGGCAC ACTCGCTGAG CACGGGACAG ACCGGTTACA TCCCCAGCAA CTATGTGGCG 420 | | CCCTCCGACT CCATCCAGGC TGAGGAGTGG TACTTTGGCA AGATCACTAG ACGGGAATCA 480 | | GAGCGGCTGC TGCTCAACGC CGAGAACCCG AGAGGGACCT TCCTCGTGAG GGAGAGTGAG 540 | | ACCACAAAAG GTGCCTACTG CCTCTCTGTA TCCGACTTCG ACAATGCCAA GGGCCTAAAT 600 | | GTGAAACACT ACAAGATCCG CAAGCTGGAC AGCGGCGGTT TCTACATCAC CTCCCGCACC 660 | | CAGTTCAACA GCCTGCAGCA GCTCGTGGCT TACTACTCCA AACATGCTGA TGGCCTGTGT 720 | | CACCGCCTCA CTACCGTATG TCCCACATCC AAGCCTCAGA CCCAGGGATT GGCCAAGGAT 780 | | GCGTGGGAGA TCCCCCGGGA GTCCCTGCGG CTGGAGGTCA AGCTGGGCCA GGGTTGCTTC 840 | | GGAGAGGTGT GGATGGGGAC CTGGAACGGC ACCACGAGGG TTGCCATCAA AACTCTGAAG 900 | | CCAGGCACCA TGTCCCCAGA GGCCTTCCTG CAGGAGGCCC AAGTCATGAA GAAACTGAGG 960 | | CACGAGAAAC TGGTGCAGCT GTATGCTGTG GTGTCGGAAG AACCCATTTA CATTGTGACA 1020 | | GAGTACATGA ACAAGGGGAG TCTGCTGGAC TTTCTCAAGG GGGAAACGGG CAAATATTTG 1080 | | CGGCTACCCC AGCTGGTGGA CATGTCTGCT CAGATCGCTT CAGGCATGGC CTATGTGGAG 1140 | | CGGATGAACT ATGTGCACCG GGACCTTCGA GCCGCCAATA TCCTAGTAGG GGAGAACCTG 1200 | | GTGTGCAAAG TGGCCGACTT TGGGTTGGCC CGGCTCATAG AAGACAACGA ATACACAGCC 1260 | | CGGCAAGGTG CCAAATTCCC CATCAAGTGG ACCGCCCCTG AAGCTGCTCT GTACGGCAGG 1320 | | TTCACCATCA AGTCGGATGT GTGGTCCTTT GGGATTCTGC TGACCGAGCT CACCACTAAG 1380 | | GGAAGAGTGC CCTATCCTGG GATGGTGAAC CGTGAGGTTC TGGACCAGGT GGAGCGGGGC 1440 | | TACCGGATGC CTTGTCCCCC CGAGTGCCCC GAGTCCCTGC ATGACCTTAT GTGCCAGTGC 1500 | | TGGCGGAAGG AGCCCGAGGA GCGGCCCACC TTCGAGTACC TGCAGGCCTT CCTGGAAGAC 1560 | | TACTTTACGT CCACTGAGCC ACAGTACCAG CCCGGGGAGA ACCTATAG 1608 |
|
| Domain Profile | S: 1 lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly 60 | l+l+ klG+G+fGevw+g+w+g+++va+ktlk+gt+speafl+eaq++kklrheklv+ly | Q: 269 LRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY 328 | 68999******************************************************* |
| S: 61 avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr 120 | avvse ePiyivte+m+kGslldflk e+gk+l+lp+lvd++aq+a+Gmay+e++n++hr | Q: 329 AVVSE-EPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHR 387 | ****9.****************************************************** |
| S: 121 dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv 180 | dl+a+n+lvge+lv+kvadfGlarlied+eyta++gak+PikWtaPea+ +g+ftiksdv | Q: 388 DLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDV 447 | ************************************************************ |
| S: 181 WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee 240 | WsfGillte++tkG+vPypGm n+evl+qvergyr+p+p ecpe+l++l+++cw+k+pee | Q: 448 WSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEE 507 | ************************************************************ |
| S: 241 rPtfetlqevl 251 | rPtfe+lq++l | Q: 508 RPTFEYLQAFL 518 | *******9876 |
|
Domain Sequence
(FASTA) | | LRLEVKLGQG CFGEVWMGTW NGTTRVAIKT LKPGTMSPEA FLQEAQVMKK LRHEKLVQLY 60 | | AVVSEEPIYI VTEYMNKGSL LDFLKGETGK YLRLPQLVDM SAQIASGMAY VERMNYVHRD 120 | | LRAANILVGE NLVCKVADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 180 | | SFGILLTELT TKGRVPYPGM VNREVLDQVE RGYRMPCPPE CPESLHDLMC QCWRKEPEER 240 | | PTFEYLQAFL 250 |
|
| Keyword | ATP-binding; Cell adhesion; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; 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; Ubl conjugation. |
| Sequence Source | Ensembl |
| Orthology | |
| Gene Ontology | |
| KEGG | |
| InterPros | |
| Pfam | |
| SMARTs | |
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| Prints | |
| Created Date | 20-Feb-2013 |