| Tag | Content |
|---|
| EKPD ID | EKS-HOS-00372 |
| Classification | | Group/Family | Score | E-Value | Start | End | Domain Length |
|---|
| TK/Src | 448.4 | 3.2E-134 | 270 | 519 | 250 |
|
| Status | Reviewed |
| Ensembl Protein | ENSP00000350941 |
| UniProt Accession | P12931; E1P5V4; Q76P87; Q86VB9; Q9H5A8; |
| 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; SRC1; |
| Ensembl Information | |
| Organism | Homo sapiens |
| 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'. |
| Protein Length | 536 |
Protein Sequence
(FASTA) | | MGSNKSKPKD ASQRRRSLEP AENVHGAGGG AFPASQTPSK PASADGHRGP SAAFAPAAAE 60 | | PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE TDLSFKKGER LQIVNNTEGD 120 | | WWLAHSLSTG QTGYIPSNYV APSDSIQAEE WYFGKITRRE SERLLLNAEN PRGTFLVRES 180 | | ETTKGAYCLS VSDFDNAKGL NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL 240 | | CHRLTTVCPT SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL 300 | | KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMSKGSLL DFLKGETGKY 360 | | LRLPQLVDMA AQIASGMAYV ERMNYVHRDL RAANILVGEN LVCKVADFGL ARLIEDNEYT 420 | | ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELTT KGRVPYPGMV NREVLDQVER 480 | | GYRMPCPPEC PESLHDLMCQ CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL 536 |
|
Nucleotide Sequence
(FASTA) | | ATGGGTAGCA ACAAGAGCAA GCCCAAGGAT GCCAGCCAGC GGCGCCGCAG CCTGGAGCCC 60 | | GCCGAGAACG TGCACGGCGC TGGCGGGGGC GCTTTCCCCG CCTCGCAGAC CCCCAGCAAG 120 | | CCAGCCTCGG CCGACGGCCA CCGCGGCCCC AGCGCGGCCT TCGCCCCCGC GGCCGCCGAG 180 | | CCCAAGCTGT TCGGAGGCTT CAACTCCTCG GACACCGTCA CCTCCCCGCA GAGGGCGGGC 240 | | CCGCTGGCCG GTGGAGTGAC CACCTTTGTG GCCCTCTATG ACTATGAGTC TAGGACGGAG 300 | | ACAGACCTGT CCTTCAAGAA AGGCGAGCGG CTCCAGATTG TCAACAACAC AGAGGGAGAC 360 | | TGGTGGCTGG CCCACTCGCT CAGCACAGGA CAGACAGGCT ACATCCCCAG CAACTACGTG 420 | | GCGCCCTCCG ACTCCATCCA GGCTGAGGAG TGGTATTTTG GCAAGATCAC CAGACGGGAG 480 | | TCAGAGCGGT TACTGCTCAA TGCAGAGAAC CCGAGAGGGA CCTTCCTCGT GCGAGAAAGT 540 | | GAGACCACGA AAGGTGCCTA CTGCCTCTCA GTGTCTGACT TCGACAACGC CAAGGGCCTC 600 | | AACGTGAAGC ACTACAAGAT CCGCAAGCTG GACAGCGGCG GCTTCTACAT CACCTCCCGC 660 | | ACCCAGTTCA ACAGCCTGCA GCAGCTGGTG GCCTACTACT CCAAACACGC CGATGGCCTG 720 | | TGCCACCGCC TCACCACCGT GTGCCCCACG TCCAAGCCGC AGACTCAGGG CCTGGCCAAG 780 | | GATGCCTGGG AGATCCCTCG GGAGTCGCTG CGGCTGGAGG TCAAGCTGGG CCAGGGCTGC 840 | | TTTGGCGAGG TGTGGATGGG GACCTGGAAC GGTACCACCA GGGTGGCCAT CAAAACCCTG 900 | | AAGCCTGGCA CGATGTCTCC AGAGGCCTTC CTGCAGGAGG CCCAGGTCAT GAAGAAGCTG 960 | | AGGCATGAGA AGCTGGTGCA GTTGTATGCT GTGGTTTCAG AGGAGCCCAT TTACATCGTC 1020 | | ACGGAGTACA TGAGCAAGGG GAGTTTGCTG GACTTTCTCA AGGGGGAGAC AGGCAAGTAC 1080 | | CTGCGGCTGC CTCAGCTGGT GGACATGGCT GCTCAGATCG CCTCAGGCAT GGCGTACGTG 1140 | | GAGCGGATGA ACTACGTCCA CCGGGACCTT CGTGCAGCCA ACATCCTGGT GGGAGAGAAC 1200 | | CTGGTGTGCA AAGTGGCGGA CTTTGGGCTG GCTCGGCTCA TTGAAGACAA TGAGTACACG 1260 | | GCGCGGCAAG GTGCCAAATT CCCCATCAAG TGGACGGCTC CAGAAGCTGC CCTCTATGGC 1320 | | CGCTTCACCA TCAAGTCGGA CGTGTGGTCC TTCGGGATCC TGCTGACTGA GCTCACCACA 1380 | | AAGGGACGGG TGCCCTACCC TGGGATGGTG AACCGCGAGG TGCTGGACCA GGTGGAGCGG 1440 | | GGCTACCGGA TGCCCTGCCC GCCGGAGTGT CCCGAGTCCC TGCACGACCT CATGTGCCAG 1500 | | TGCTGGCGGA AGGAGCCTGA GGAGCGGCCC ACCTTCGAGT ACCTGCAGGC CTTCCTGGAG 1560 | | GACTACTTCA CGTCCACCGA GCCCCAGTAC CAGCCCGGGG AGAACCTCTA G 1611 |
|
| Domain Profile | S: 1 lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly 60 | l+l+ klG+G+fGevw+g+w+g+++va+ktlk+gt+speafl+eaq++kklrheklv+ly | Q: 270 LRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY 329 | 68999******************************************************* |
| S: 61 avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr 120 | avvse ePiyivte+m+kGslldflk e+gk+l+lp+lvd+aaq+a+Gmay+e++n++hr | Q: 330 AVVSE-EPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHR 388 | ****9.****************************************************** |
| S: 121 dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv 180 | dl+a+n+lvge+lv+kvadfGlarlied+eyta++gak+PikWtaPea+ +g+ftiksdv | Q: 389 DLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDV 448 | ************************************************************ |
| S: 181 WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee 240 | WsfGillte++tkG+vPypGm n+evl+qvergyr+p+p ecpe+l++l+++cw+k+pee | Q: 449 WSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEE 508 | ************************************************************ |
| S: 241 rPtfetlqevl 251 | rPtfe+lq++l | Q: 509 RPTFEYLQAFL 519 | *******9876 |
|
Domain Sequence
(FASTA) | | LRLEVKLGQG CFGEVWMGTW NGTTRVAIKT LKPGTMSPEA FLQEAQVMKK LRHEKLVQLY 60 | | AVVSEEPIYI VTEYMSKGSL LDFLKGETGK YLRLPQLVDM AAQIASGMAY VERMNYVHRD 120 | | LRAANILVGE NLVCKVADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 180 | | SFGILLTELT TKGRVPYPGM VNREVLDQVE RGYRMPCPPE CPESLHDLMC QCWRKEPEER 240 | | PTFEYLQAFL 250 |
|
| Keyword | 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Host-virus interaction; Immunity; Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; 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 | |
| Prosites | |
| Prints | |
| Created Date | 20-Feb-2013 |