EKS-DAR-00747
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-DAR-00747
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
TK/Src442.01.2E-132268516249
StatusReviewed
Ensembl ProteinENSDARP00000093618
UniProt AccessionQ1JPZ3; Q6EWH0;
Protein NameProto-oncogene tyrosine-protein kinase Src
Protein Synonyms/Alias Proto-oncogene c-Src; pp60c-src; p60-Src;
Gene Namesrc
Gene Synonyms/Alias src;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSDARG00000008107ENSDARP00000097596ENSDART00000112198
ENSDARG00000008107ENSDARP00000093618ENSDART00000102843
OrganismDanio rerio
Functional DescriptionNon-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 (By similarity).
Protein Length534
Protein Sequence
(FASTA)
MGGVKSKPKE LGQRSRSLDD GTGGHHHHTP NPTSFTPNRS PPVEGSRRGT QPNIINAEQA 60
LFGGVNSTTN SITSPNRIGI LGGVTTFVAL YDYESRTASD LSFRKGERLQ IVNNTEGDWW 120
LARSLTTGES GYIPSNYVAP SDSIQAEEWY FGKITRRDSE RLLLNLENRR GTFLVRESET 180
TKGAYCLSVL DYDNVKGLNV KHYKIRKLDS GGFYITSRTQ FSTLQQLVNH YRQHADGLCH 240
SLTDVCPVLK PPTQGLARDA WEIPRDSLRL DVKLGQGCFG EVWMGTWNGT TRVAIKTLKP 300
GTMSPEAFLQ EAQVMKKLRH EKLVQLYAVV SEEPIYIVTE YMGQGSLLDF LKGDMGKMLR 360
LPQLVDMASQ IASGMAYVER MNYVHRDLRA ANILVGDNLV CKVADFGLAR LIEDNEYTAR 420
QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELTTKG RVPYPGMVNR EVLDQVERGY 480
RMPCPAECPD SLHELMLTCW RKEPEERPTF EYLQGFLEDY FTSTEPQYQP GENL 534
Nucleotide Sequence
(FASTA)
ATGGGTGGAG TCAAGAGTAA ACCCAAAGAG CTGGGCCAGC GCTCGCGGAG TCTGGACGAC 60
GGCACCGGAG GACACCACCA CCACACCCCC AACCCCACCT CCTTCACCCC TAACCGCAGT 120
CCACCGGTGG AGGGGTCCCG GCGCGGCACA CAGCCCAACA TCATAAACGC GGAGCAGGCG 180
CTCTTTGGGG GAGTGAACTC CACCACCAAC AGCATCACAT CTCCTAATCG AATCGGCATA 240
TTAGGCGGCG TGACCACATT TGTGGCTCTG TATGACTACG AGTCACGAAC CGCCTCCGAT 300
TTGTCATTCA GGAAAGGAGA ACGACTCCAG ATTGTCAATA ACACGGAGGG TGACTGGTGG 360
CTAGCGCGAT CACTGACGAC AGGAGAGAGC GGATACATTC CCAGCAATTA CGTGGCACCG 420
TCTGACTCCA TCCAGGCTGA AGAATGGTAC TTCGGAAAAA TCACACGCAG AGACTCTGAG 480
CGACTGCTCT TGAATCTGGA GAACAGACGA GGAACTTTCC TGGTCAGAGA GAGCGAGACC 540
ACCAAAGGTG CCTACTGTCT CTCCGTCCTG GATTACGACA ACGTGAAGGG CCTGAATGTA 600
AAACATTATA AGATCCGCAA ACTGGACAGC GGTGGATTTT ACATCACGTC CCGCACACAG 660
TTCAGCACAT TACAGCAGCT GGTCAACCAC TACCGCCAGC ACGCAGACGG CCTGTGCCAC 720
TCCCTGACTG ACGTGTGTCC AGTGCTGAAG CCTCCGACTC AGGGTCTGGC ACGTGATGCC 780
TGGGAGATTC CTCGAGACTC GCTGAGACTG GATGTCAAGC TGGGCCAGGG CTGCTTCGGG 840
GAGGTCTGGA TGGGCACCTG GAACGGGACG ACACGTGTGG CCATCAAGAC TCTGAAGCCT 900
GGCACCATGT CTCCCGAAGC GTTCCTGCAG GAGGCGCAAG TGATGAAGAA GCTCCGGCAT 960
GAGAAGCTGG TGCAGCTTTA CGCCGTCGTC TCAGAGGAGC CCATTTACAT AGTCACTGAG 1020
TACATGGGTC AAGGAAGCCT GCTGGATTTC CTGAAAGGTG ACATGGGGAA AATGCTGCGT 1080
TTGCCTCAGC TCGTGGACAT GGCCTCTCAG ATCGCCTCAG GAATGGCATA CGTGGAGAGA 1140
ATGAACTATG TGCACAGGGA CCTCAGGGCT GCCAACATCC TGGTGGGCGA TAACCTGGTG 1200
TGTAAAGTGG CTGATTTCGG CCTCGCTCGA CTCATTGAGG ACAACGAATA CACCGCGAGA 1260
CAAGGAGCAA AGTTTCCTAT TAAGTGGACT GCACCGGAGG CAGCTCTGTA CGGACGCTTC 1320
ACCATCAAAT CTGACGTGTG GTCGTTTGGG ATTTTACTGA CGGAGCTCAC CACCAAAGGC 1380
AGGGTGCCTT ATCCAGGTAT GGTGAACCGC GAGGTGCTTG ACCAGGTGGA GCGTGGCTAC 1440
AGGATGCCCT GCCCGGCCGA ATGCCCTGAC TCCCTGCACG AGCTCATGCT GACCTGCTGG 1500
CGCAAAGAGC CCGAAGAGCG GCCCACATTC GAGTACCTGC AGGGTTTCCT GGAGGACTAC 1560
TTCACCTCCA CCGAACCACA ATACCAACCC GGAGAAAACC TCTAG 1605
Domain Profile
S: 1     lklvkklGeGqfGevwlgkwkgsvkvavktlkegtlspeafleeaqilkklrheklvkly  60
         l+l  klG+G+fGevw+g+w+g+++va+ktlk+gt+speafl+eaq++kklrheklv+ly
Q: 268   LRLDVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLY  327
         57889*******************************************************
S: 61    avvseeePiyivtelmakGslldflkeeegkklklpklvdlaaqvaeGmayleeknlihr  120
         avvse ePiyivte+m +Gslldflk + gk+l+lp+lvd+a+q+a+Gmay+e++n++hr
Q: 328   AVVSE-EPIYIVTEYMGQGSLLDFLKGDMGKMLRLPQLVDMASQIASGMAYVERMNYVHR  386
         ****9.******************************************************
S: 121   dlaarnvlvgeslvvkvadfGlarlieddeytakegaklPikWtaPeaiklgkftiksdv  180
         dl+a+n+lvg++lv+kvadfGlarlied+eyta++gak+PikWtaPea+ +g+ftiksdv
Q: 387   DLRAANILVGDNLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDV  446
         ************************************************************
S: 181   WsfGillteivtkGkvPypGmtneevleqvergyrlprpeecpeelyelllecwkkdpee  240
         WsfGillte++tkG+vPypGm n+evl+qvergyr+p+p+ecp++l+el+l+cw+k+pee
Q: 447   WSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPAECPDSLHELMLTCWRKEPEE  506
         ************************************************************
S: 241   rPtfetlqev  250
         rPtfe+lq +
Q: 507   RPTFEYLQGF  516
         *******976
Domain Sequence
(FASTA)
LRLDVKLGQG CFGEVWMGTW NGTTRVAIKT LKPGTMSPEA FLQEAQVMKK LRHEKLVQLY 60
AVVSEEPIYI VTEYMGQGSL LDFLKGDMGK MLRLPQLVDM ASQIASGMAY VERMNYVHRD 120
LRAANILVGD NLVCKVADFG LARLIEDNEY TARQGAKFPI KWTAPEAALY GRFTIKSDVW 180
SFGILLTELT TKGRVPYPGM VNREVLDQVE RGYRMPCPAE CPDSLHELML TCWRKEPEER 240
PTFEYLQGF 249
KeywordATP-binding; Cell adhesion; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; S-nitrosylation; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Ciona intestinalis"; ?>Ciona savignyi"; ?>Dipodomys ordii"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sus scrofa"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00340
EKS-ANC-00356
EKS-BOT-00366
EKS-CAJ-00371
EKS-CAF-00367
EKS-CAP-00399
EKS-CII-00206
EKS-CIS-00121
EKS-DIO-00054
EKS-EQC-00357
EKS-FEC-00354
EKS-GAM-00220
EKS-GAG-00310
EKS-GAA-00450
EKS-HOS-00372
EKS-ICT-00347
EKS-LAC-00383
EKS-LOA-00375
EKS-MAM-00366
EKS-MEG-00302
EKS-MIM-00048
EKS-MOD-00355
EKS-MUM-00398
EKS-MUP-00360
EKS-MYL-00367
EKS-NOL-00334
EKS-ORN-00476
EKS-ORC-00344
EKS-ORL-00436
EKS-OTG-00369
EKS-PAT-00346
EKS-PES-00326
EKS-POA-00356
EKS-RAN-00380
EKS-SAH-00337
EKS-SUS-00323
EKS-TAR-00470
EKS-TEN-00465
EKS-XET-00482
EKS-XIM-00463
Gene Ontology
GO:0005856; C:cytoskeleton
GO:0005743; C:mitochondrial inner membrane
GO:0005634; C:nucleus
GO:0005886; C:plasma membrane
GO:0005524; F:ATP binding
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity
GO:0007155; P:cell adhesion
GO:0007049; P:cell cycle
KEGG
dre:325084;
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