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UniProtKB/Swiss-Prot entry Q14247


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SRC8_HUMAN
Primary accession number Q14247
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 25, 2008 (Sequence version 2)
Annotations were last modified on    May 26, 2009 (Entry version 94)
Name and origin of the protein
Protein name Src substrate cortactin
Synonyms Amplaxin
Oncogene EMS1
Gene name
Name: CTTN
Synonyms: EMS1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=1532244 [NCBI, ExPASy, EBI, Israel, Japan]
Schuuring E.M.D., Verhoeven E., Mooi W.J., Michalides R.J.A.;
"Identification and cloning of two overexpressed genes, U21B31/PRAD1 and EMS1, within the amplified chromosome 11q13 region in human carcinomas.";
Oncogene 7:355-361(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8474448 [NCBI, ExPASy, EBI, Israel, Japan]
Schuuring E.M.D., Verhoeven E., Litvinov S., Michalides R.J.A.;
"The product of the EMS1 gene, amplified and overexpressed in human carcinomas, is homologous to a v-src substrate and is located in cell-substratum contact sites.";
Mol. Cell. Biol. 13:2891-2898(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04632; PubMed=16554811 [NCBI, ExPASy, EBI, Israel, Japan]
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene identification.";
Nature 440:497-500(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan]
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
[5]
INTERACTION WITH PLXDC2.
DOI=10.1158/0008-5472.CAN-04-2716; PubMed=15574754 [NCBI, ExPASy, EBI, Israel, Japan]
Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P., Shankara S., Nacht M., Teicher B., Stampfl J., Singh S., Vogelstein B., Kinzler K.W., St Croix B.;
"Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R.";
Cancer Res. 64:8507-8511(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334; TYR-446 AND TYR-453, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr050134h; PubMed=16212419 [NCBI, ExPASy, EBI, Israel, Japan]
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC).";
J. Proteome Res. 4:1661-1671(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215; TYR-446 AND TYR-453, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, AND MASS SPECTROMETRY.
DOI=10.1038/sj.emboj.7601384; PubMed=17053785 [NCBI, ExPASy, EBI, Israel, Japan]
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.;
"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling.";
EMBO J. 25:5058-5070(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-117; THR-399; THR-401; SER-405; SER-417 AND TYR-421, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; SER-418 AND TYR-421, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-405, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; THR-411; SER-417 AND SER-418, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[20]
STRUCTURE BY NMR OF 485-550.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the SH3 domain of human Src substrate cortactin.";
Submitted (NOV-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M98343; AAA58455.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP000487; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00029601; -.
PIR A48063; A48063.
RefSeq NP_005222.2; -.
UniGene Hs.596164
3D structure databases
PDB
1X69; NMR; -; A=485-550.[ExPASy / RCSB / EBI]
2D1X; X-ray; 1.90 A; A/B/C/D=490-550.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1X69; -.
2D1X; -.
ModBase Q14247.
Protein-protein interaction databases
IntAct Q14247; 4.
PTM databases
PhosphoSite Q14247; -.
Enzyme and pathway databases
Pathway_Interaction_DB fgf_pathway; FGF signaling pathway.
syndecan_3_pathway; Syndecan-3-mediated signaling events.
2D gel databases
OGP Q14247; -.
Organism-specific databases
GeneCards GC11P069922; -.
H-InvDB HIX0009895; -.
HGNC HGNC:3338; CTTN.
GenAtlas CTTN.
HPA CAB011235; -.
MIM 164765; gene. [NCBI / EBI]
PharmGKB PA27775; -.
Gene expression databases
ArrayExpress Q14247; -.
Bgee Q14247; -.
CleanEx HS_CTTN; -.
GermOnline ENSG00000085733; Homo sapiens.
Ontologies
GO
GO:0005938; Cellular component: cell cortex (inferred from sequence or structural similarity from UniProtKB).
GO:0005856; Cellular component: cytoskeleton (traceable author statement from ProtInc).
GO:0030027; Cellular component: lamellipodium (inferred from sequence or structural similarity from UniProtKB).
GO:0001726; Cellular component: ruffle (inferred from sequence or structural similarity from UniProtKB).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR015503; Cortactin.
IPR003134; Hs1_Cortactin.
IPR000108; Neu_cyt_fact_2.
IPR001452; SH3_domain.
Graphical view of domain structure.
PANTHER PTHR10829:SF4; Cortactin; 1.
Pfam PF02218; HS1_rep; 7.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00499; P67PHOX.
ProDom PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00326; SH3; 1.
SMART graphical view of domain structure.
PROSITE PS51090; CORTACTIN; 7.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q14247; -.
Genome annotation databases
Ensembl ENSG00000085733; Homo sapiens. [Contig view]
GeneID 2017; -.
KEGG hsa:2017; -.
Phylogenomic databases
HOVERGEN Q14247; -.
Other
SOURCE CTTN; Homo sapiens.
ProtoNet Q14247.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell projection; Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat; SH3 domain.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   550  550     Src substrate cortactin. PRO_0000072189
REPEAT   80   116  37     Cortactin 1. 
REPEAT   117   153  37     Cortactin 2. 
REPEAT   154   190  37     Cortactin 3. 
REPEAT   191   227  37     Cortactin 4. 
REPEAT   228   264  37     Cortactin 5. 
REPEAT   265   301  37     Cortactin 6. 
REPEAT   302   324  23     Cortactin 7; truncated. 
DOMAIN   492   550  59     SH3. 
MOD_RES   113   113        Phosphoserine. 
MOD_RES   117   117        Phosphoserine. 
MOD_RES   141   141        Phosphotyrosine. 
MOD_RES   215   215        Phosphotyrosine. 
MOD_RES   334   334        Phosphotyrosine. 
MOD_RES   399   399        Phosphothreonine. 
MOD_RES   401   401        Phosphothreonine. 
MOD_RES   405   405        Phosphoserine. 
MOD_RES   411   411        Phosphothreonine. 
MOD_RES   417   417        Phosphoserine. 
MOD_RES   418   418        Phosphoserine. 
MOD_RES   421   421        Phosphotyrosine. 
MOD_RES   446   446        Phosphotyrosine. 
MOD_RES   453   453        Phosphotyrosine. 
CONFLICT   495   495        I -> Y (in Ref. 1; AAA58455). 
STRAND   497   499  3      
STRAND   518   523  6      
STRAND   526   534  9      
STRAND   537   542  6      
HELIX   543   545  3      
STRAND   546   548  3      
Sequence information
Length: 550 AA [This is the length of the unprocessed precursor] Molecular weight: 61586 Da [This is the MW of the unprocessed precursor] CRC64: 7799326C2B4383BB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE 

        70         80         90        100        110        120 
NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV GHEYQSKLSK HCSQVDSVRG 

       130        140        150        160        170        180 
FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG 

       190        200        210        220        230        240 
KTEKHESQRD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT 

       250        260        270        280        290        300 
DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ 

       310        320        330        340        350        360 
DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI RANFENLAKE 

       370        380        390        400        410        420 
KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ TPPVSPAPQP TEERLPSSPV 

       430        440        450        460        470        480 
YEDAASFKAE LSYRGPVSGT EPEPVYSMEA ADYREASSQQ GLAYATEAVY ESAEAPGHYP 

       490        500        510        520        530        540 
AEDSTYDEYE NDLGITAVAL YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL 

       550 
FPANYVELRQ 

Q14247 in FASTA format

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