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Q14247 (SRC8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the organization of the actin cytoskeleton and cell structure. In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Plays a role in the regulation of cell migration. Plays a role in the invasiveness of cancer cells, and the formation of metastases. Ref.27 Ref.31

Subunit structure

Interacts with SHANK2 and SHANK3 (via its SH3 domain). Also interacts with FGD1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2 By similarity. Interacts with PLXDC2 and SRCIN1. Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via Pro-rich region). Interacts with DNM2 and FER. Forms a complex made of ABL1 and MYLK. Interacts with CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts with CTTNBP2; this interaction may target CTTN at the cell cortex or dendritic spines. Ref.7 Ref.8 Ref.10 Ref.21 Ref.24 Ref.27 Ref.31

Subcellular location

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Note: Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers By similarity. In the presence of CTTNBP2, localizes at the cell cortex By similarity. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft By similarity. Ref.2 Ref.7 Ref.27 Ref.31

Domain

The SH3 motif may mediate binding to the cytoskeleton.

Post-translational modification

Phosphorylated by PKN2 at both serine and threonine residues in a GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and hence down-regulated CTTN ability to associates with filamentous actin By similarity. Phosphorylated by FER. Tyrosine phosphorylation in transformed cells may contribute to cellular growth regulation and transformation. Phosphorylated in response to FGR activation. Phosphorylation by SRC promotes MYLK binding. Ref.7 Ref.8 Ref.11

Sequence similarities

Contains 7 cortactin repeats.

Contains 1 SH3 domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ASAP1Q9ULH17EBI-351886,EBI-346622
Cbll1Q9JIY28EBI-351886,EBI-7644904From a different organism.
DNM2P505705EBI-351886,EBI-346547
HDAC6Q9UBN73EBI-351886,EBI-301697
Kcnma1Q084603EBI-351886,EBI-1633915From a different organism.
PTPN1P180312EBI-351886,EBI-968788
Srcin1Q9QWI6-22EBI-351886,EBI-775607From a different organism.
tirB7UM993EBI-351886,EBI-2504426From a different organism.
WASP427683EBI-351886,EBI-346375

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14247-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14247-2)

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.
     538-550: YGLFPANYVELRQ → FRELAFSCVR...CLGTWVPECP
Note: No experimental confirmation available.
Isoform 3 (identifier: Q14247-3)

The sequence of this isoform differs from the canonical sequence as follows:
     264-300: Missing.

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.23
Modified residue1241N6-acetyllysine By similarity
Modified residue1441N6-acetyllysine By similarity
Modified residue1611N6-acetyllysine By similarity
Modified residue1811N6-acetyllysine By similarity
Modified residue1981N6-acetyllysine Ref.23
Modified residue2351N6-acetyllysine Ref.23
Modified residue2721N6-acetyllysine Ref.23
Modified residue2951N6-acetyllysine By similarity
Modified residue3041N6-acetyllysine Ref.23
Modified residue3091N6-acetyllysine Ref.23
Modified residue3461N6-acetyllysine By similarity
Modified residue3991Phosphothreonine Ref.25
Modified residue4011Phosphothreonine Ref.25
Modified residue4051Phosphoserine Ref.9 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19 Ref.22 Ref.25
Modified residue4111Phosphothreonine Ref.19
Modified residue4171Phosphoserine Ref.19
Modified residue4181Phosphoserine Ref.14 Ref.19 Ref.22 Ref.25 Ref.28
Modified residue4211Phosphotyrosine; by SRC Ref.17 Ref.22
Modified residue4461Phosphotyrosine Ref.22
Modified residue4531Phosphotyrosine Ref.12
Modified residue4861Phosphotyrosine; by SRC Ref.11
Modified residue4891Phosphotyrosine; by SRC

Natural variations

Alternative sequence264 – 30037Missing in isoform 2 and isoform 3.
VSP_043120
Alternative sequence538 – 55013YGLFP…VELRQ → FRELAFSCVRVALVPIKCSR DLPGQARGLRSALWRVGRKD CPRRGASSRVSLLGRRGLGL MEVNPELSHPEHRSCHVRWE ICLCHTVTARRIRKLISFLR SREAGPVPSCSQVGGVSFQK VTWKCLGTWVPECP in isoform 2.
VSP_043121

Experimental info

Sequence conflict4951I → Y in AAA58455. Ref.1

Secondary structure

............. 550
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: 9F36B5AED4992281
Show »

FASTA63470,959
Isoform 3 [UniParc].

Checksum: 333C09D488528C40
Show »

FASTA51357,467

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
Tissue: Mammary gland.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Placenta and Testis.
[7]"Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER."
Kim L., Wong T.W.
J. Biol. Chem. 273:23542-23548(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FER, PHOSPHORYLATION OF CTTN, SUBCELLULAR LOCATION.
[8]"Novel interaction of cortactin with endothelial cell myosin light chain kinase."
Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.
Biochem. Biophys. Res. Commun. 298:511-519(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYLK, PHOSPHORYLATION BY SRC.
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXDC2.
[11]"The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-486.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND TYR-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[18]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; THR-411; SER-417 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity."
Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S., Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J., Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.
Neuron 61:85-100(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SRCIN1.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-418; TYR-421 AND TYR-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-235; LYS-272; LYS-304 AND LYS-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYLK AND ABL1.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405 AND SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"The immunoinhibitory adapter protein SRC homology domain 3 lymphocyte protein 2 (SLy2) regulates actin dynamics and B cell spreading."
von Holleben M., Gohla A., Janssen K.P., Iritani B.M., Beer-Hammer S.
J. Biol. Chem. 286:13489-13501(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SAMSN1.
[28]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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.
[31]"Targeting AMAP1 and cortactin binding bearing an atypical src homology 3/proline interface for prevention of breast cancer invasion and metastasis."
Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H., Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H., Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.
Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 490-550 IN COMPLEX WITH ASAP1, FUNCTION, INTERACTION WITH ASAP1 AND DNM2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Wikipedia

Cortactin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M98343 mRNA. Translation: AAA58455.1.
AK291097 mRNA. Translation: BAF83786.1.
AP000487 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74766.1.
CH471076 Genomic DNA. Translation: EAW74768.1.
BC008799 mRNA. Translation: AAH08799.1.
BC033889 mRNA. Translation: AAH33889.1.
PIRA48063.
RefSeqNP_001171669.1. NM_001184740.1.
NP_005222.2. NM_005231.3.
NP_612632.1. NM_138565.2.
UniGeneHs.596164.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X69NMR-A485-550[»]
2D1XX-ray1.90A/B/C/D490-550[»]
ProteinModelPortalQ14247.
SMRQ14247. Positions 490-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108332. 77 interactions.
IntActQ14247. 34 interactions.
MINTMINT-361929.
STRING9606.ENSP00000301843.

PTM databases

PhosphoSiteQ14247.

Polymorphism databases

DMDM215273892.

2D gel databases

OGPQ14247.

Proteomic databases

PaxDbQ14247.
PRIDEQ14247.

Protocols and materials databases

DNASU2017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301843; ENSP00000301843; ENSG00000085733. [Q14247-1]
ENST00000346329; ENSP00000317189; ENSG00000085733. [Q14247-3]
ENST00000376561; ENSP00000365745; ENSG00000085733. [Q14247-2]
GeneID2017.
KEGGhsa:2017.
UCSCuc001opu.3. human. [Q14247-2]
uc001opv.4. human. [Q14247-1]
uc001opw.4. human. [Q14247-3]

Organism-specific databases

CTD2017.
GeneCardsGC11P070244.
HGNCHGNC:3338. CTTN.
HPACAB011235.
MIM164765. gene.
neXtProtNX_Q14247.
PharmGKBPA27775.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG123488.
HOGENOMHOG000006523.
HOVERGENHBG005994.
KOK06106.
OMAHESQQDY.
OrthoDBEOG7V49ZC.
PhylomeDBQ14247.
TreeFamTF318935.

Gene expression databases

ArrayExpressQ14247.
BgeeQ14247.
CleanExHS_CTTN.
GenevestigatorQ14247.

Family and domain databases

InterProIPR015503. Cortactin.
IPR003134. Hs1_Cortactin.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR10829:SF4. PTHR10829:SF4. 1 hit.
PfamPF02218. HS1_rep. 7 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51090. CORTACTIN. 7 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTTN. human.
EvolutionaryTraceQ14247.
GeneWikiCortactin.
GenomeRNAi2017.
NextBio8171.
PROQ14247.
SOURCESearch...

Entry information

Entry nameSRC8_HUMAN
AccessionPrimary (citable) accession number: Q14247
Secondary accession number(s): Q8N707, Q96H99
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 11

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