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Reviewed, UniProtKB/Swiss-Prot Q14247 (SRC8_HUMAN)

Last modified November 3, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Src substrate cortactin
Alternative name(s):
    Amplaxin
    Oncogene EMS1
Gene names
Name: CTTN
Synonyms: EMS1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May contribute to the organization of cell structure. The SH3 motif may function as a binding region to cytoskeleton. Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation.

Subunit structure

Interacts with SHANK2 and SHANK3 via its SH2 domain. Also interacts with FGD1 By similarity. Interacts with PLXDC2.

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Note: Associated with membrane ruffles and lamellipodia By similarity.

Sequence similarities

Contains 7 cortactin repeats.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

WIPF1O435161EBI-351886,EBI-346356

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Src substrate cortactin
PRO_0000072189

Regions

Repeat80 – 11637Cortactin 1
Repeat117 – 15337Cortactin 2
Repeat154 – 19037Cortactin 3
Repeat191 – 22737Cortactin 4
Repeat228 – 26437Cortactin 5
Repeat265 – 30137Cortactin 6
Repeat302 – 32423Cortactin 7; truncated
Domain492 – 55059SH3

Amino acid modifications

Modified residue871N6-acetyllysine Ref.21
Modified residue1131Phosphoserine Ref.14
Modified residue1171Phosphoserine Ref.14
Modified residue1411Phosphotyrosine Ref.13
Modified residue1541Phosphotyrosine Ref.20
Modified residue1981N6-acetyllysine Ref.21
Modified residue2151Phosphotyrosine Ref.9
Modified residue2181N6-acetyllysine Ref.21
Modified residue2351N6-acetyllysine Ref.21
Modified residue2721N6-acetyllysine Ref.21
Modified residue3041N6-acetyllysine Ref.21
Modified residue3091N6-acetyllysine Ref.21
Modified residue3341Phosphotyrosine Ref.7
Modified residue3991Phosphothreonine Ref.14 Ref.16 Ref.18
Modified residue4011Phosphothreonine Ref.14 Ref.16 Ref.18 Ref.6 Ref.12 Ref.15 Ref.17
Modified residue4051Phosphoserine Ref.14 Ref.16 Ref.18 Ref.6 Ref.12 Ref.15 Ref.17
Modified residue4111Phosphothreonine Ref.18
Modified residue4171Phosphoserine Ref.14 Ref.18
Modified residue4181Phosphoserine Ref.16 Ref.18 Ref.6 Ref.12 Ref.15 Ref.11
Modified residue4211Phosphotyrosine Ref.14 Ref.20 Ref.16 Ref.4
Modified residue4461Phosphotyrosine Ref.20 Ref.9 Ref.7 Ref.8 Ref.10
Modified residue4531Phosphotyrosine Ref.9 Ref.7

Experimental info

Sequence conflict4951I → Y in AAA58455. Ref.1

Secondary structure

........... 550
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14247-1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 7799326C2B4383BB

FASTA55061,586
        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 

« Hide

References

« Hide 'large scale' references
[1]"Identification and cloning of two overexpressed genes, U21B31/PRAD1 and EMS1, within the amplified chromosome 11q13 region in human carcinomas."
Schuuring E.M.D., Verhoeven E., Mooi W.J., Michalides R.J.A.
Oncogene 7:355-361(1992) [PubMed: 1532244] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"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."
Schuuring E.M.D., Verhoeven E., Litvinov S., Michalides R.J.A.
Mol. Cell. Biol. 13:2891-2898(1993) [PubMed: 8474448] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
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. expand/collapse author list , 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.
Nature 440:497-500(2006) [PubMed: 16554811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-421, MASS SPECTROMETRY.
[5]"Identification of a binding partner for the endothelial cell surface proteins TEM7 and TEM7R."
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.
Cancer Res. 64:8507-8511(2004) [PubMed: 15574754] [Abstract]
Cited for: INTERACTION WITH PLXDC2.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)."
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.
J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334; TYR-446 AND TYR-453, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-215; TYR-446 AND TYR-453, MASS SPECTROMETRY.
[10]"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling."
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z.
EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-446, MASS SPECTROMETRY.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, MASS SPECTROMETRY.
[14]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-117; THR-399; THR-401; SER-405; SER-417 AND TYR-421, MASS SPECTROMETRY.
[15]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND SER-418, MASS SPECTROMETRY.
[16]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; SER-418 AND TYR-421, MASS SPECTROMETRY.
Tissue: Platelet.
[17]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401 AND SER-405, MASS SPECTROMETRY.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405; THR-411; SER-417 AND SER-418, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154; TYR-421 AND TYR-446, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-218; LYS-235; LYS-272; LYS-304 AND LYS-309, MASS SPECTROMETRY.
[22]"Solution structures of the SH3 domain of human Src substrate cortactin."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 485-550.
+Additional computationally mapped references.

Web resources

Wikipedia

Cortactin entry

Cross-references

Sequence databases

M98343 mRNA. Translation: AAA58455.1.
AP000487 Genomic DNA. No translation available.
IPIIPI00029601.
PIRA48063.
RefSeqNP_005222.2.
UniGeneHs.596164

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ14247. 5 interactions.
STRINGQ14247.

PTM databases

PhosphoSiteQ14247.

2-D gel databases

OGPQ14247.

Proteomic databases

PRIDEQ14247.

Genome annotation databases

EnsemblENST00000301843; ENSP00000301843; ENSG00000085733; Homo sapiens. [Genome view]
ENST00000346329; ENSP00000317189; ENSG00000085733; Homo sapiens. [Genome view]
ENST00000376561; ENSP00000365745; ENSG00000085733; Homo sapiens. [Genome view]
ENST00000393747; ENSP00000377348; ENSG00000085733; Homo sapiens. [Genome view]
ENST00000415461; ENSP00000409014; ENSG00000085733; Homo sapiens. [Genome view]
GeneID2017.
KEGGhsa:2017.

Organism-specific databases

CTD2017.
GeneCardsGC11P069922.
H-InvDBHIX0009895.
HGNCHGNC:3338. CTTN.
HPACAB011235.
MIM164765. gene.
PharmGKBPA27775.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ14247.

Enzyme and pathway databases

Pathway_Interaction_DBfgf_pathway. FGF signaling pathway.
syndecan_3_pathway. Syndecan-3-mediated signaling events.

Gene expression databases

ArrayExpressQ14247.
BgeeQ14247.
CleanExHS_CTTN.
GenevestigatorQ14247.
GermOnlineENSG00000085733. Homo sapiens.

Family and domain databases

InterProIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR000108. Neu_cyt_fact_2.
IPR001452. SH3_domain.
IPR020473. SH3_region.
[Graphical view]
PANTHERPTHR10829:SF4. Cortactin. 1 hit.
PfamPF02218. HS1_rep. 7 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00499. P67PHOX.
PR00452. SH3DOMAIN.
ProDomPD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00326. SH3. 1 hit.
[Graphical view]
PROSITEPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameSRC8_HUMAN
AccessionPrimary (citable) accession number: Q14247
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: November 3, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents