SRC8_HUMAN
ID SRC8_HUMAN Reviewed; 550 AA.
AC Q14247; Q8N707; Q96H99;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Src substrate cortactin;
DE AltName: Full=Amplaxin;
DE AltName: Full=Oncogene EMS1;
GN Name=CTTN; Synonyms=EMS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=1532244;
RA Schuuring E.M.D., Verhoeven E., Mooi W.J., Michalides R.J.A.;
RT "Identification and cloning of two overexpressed genes, U21B31/PRAD1 and
RT EMS1, within the amplified chromosome 11q13 region in human carcinomas.";
RL Oncogene 7:355-361(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Mammary gland;
RX PubMed=8474448; DOI=10.1128/mcb.13.5.2891-2898.1993;
RA Schuuring E.M.D., Verhoeven E., Litvinov S., Michalides R.J.A.;
RT "The product of the EMS1 gene, amplified and overexpressed in human
RT carcinomas, is homologous to a v-src substrate and is located in cell-
RT substratum contact sites.";
RL Mol. Cell. Biol. 13:2891-2898(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH FER, PHOSPHORYLATION OF CTTN, AND SUBCELLULAR LOCATION.
RX PubMed=9722593; DOI=10.1074/jbc.273.36.23542;
RA Kim L., Wong T.W.;
RT "Growth factor-dependent phosphorylation of the actin-binding protein
RT cortactin is mediated by the cytoplasmic tyrosine kinase FER.";
RL J. Biol. Chem. 273:23542-23548(1998).
RN [8]
RP INTERACTION WITH MYLK, AND PHOSPHORYLATION BY SRC.
RX PubMed=12408982; DOI=10.1016/s0006-291x(02)02492-0;
RA Dudek S.M., Birukov K.G., Zhan X., Garcia J.G.N.;
RT "Novel interaction of cortactin with endothelial cell myosin light chain
RT kinase.";
RL Biochem. Biophys. Res. Commun. 298:511-519(2002).
RN [9]
RP INTERACTION WITH KCNA2, AND SUBCELLULAR LOCATION.
RX PubMed=12151401; DOI=10.1074/jbc.m205005200;
RA Hattan D., Nesti E., Cachero T.G., Morielli A.D.;
RT "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the
RT actin-binding protein cortactin.";
RL J. Biol. Chem. 277:38596-38606(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
RP INTERACTION WITH PLXDC2.
RX PubMed=15574754; DOI=10.1158/0008-5472.can-04-2716;
RA Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P., Shankara S.,
RA Nacht M., Teicher B., Stampfl J., Singh S., Vogelstein B., Kinzler K.W.,
RA St Croix B.;
RT "Identification of a binding partner for the endothelial cell surface
RT proteins TEM7 and TEM7R.";
RL Cancer Res. 64:8507-8511(2004).
RN [12]
RP PHOSPHORYLATION AT TYR-486.
RX PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
RA Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
RA Lowell C.A., Berton G.;
RT "The proto-oncogene Fgr regulates cell migration and this requires its
RT plasma membrane localization.";
RL Exp. Cell Res. 302:253-269(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND SER-418, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [17]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-486.
RX PubMed=17959782; DOI=10.1073/pnas.0703865104;
RA Williams M.R., Markey J.C., Doczi M.A., Morielli A.D.;
RT "An essential role for cortactin in the modulation of the potassium channel
RT Kv1.2.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:17412-17417(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405 AND TYR-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; THR-411; SER-417 AND
RP SER-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP INTERACTION WITH SRCIN1.
RX PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT plasticity.";
RL Neuron 61:85-100(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-418; TYR-421 AND
RP TYR-446, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-198; LYS-235; LYS-272;
RP LYS-304 AND LYS-309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP INTERACTION WITH MYLK AND ABL1, AND FUNCTION.
RX PubMed=20861316; DOI=10.1091/mbc.e09-10-0876;
RA Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E.,
RA Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E.,
RA Imam S.Z., Garcia J.G.N.;
RT "Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to
RT regulate endothelial barrier function.";
RL Mol. Biol. Cell 21:4042-4056(2010).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-399; THR-401; SER-405 AND
RP SER-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SAMSN1.
RX PubMed=21296879; DOI=10.1074/jbc.m110.155184;
RA von Holleben M., Gohla A., Janssen K.P., Iritani B.M., Beer-Hammer S.;
RT "The immunoinhibitory adapter protein SRC homology domain 3 lymphocyte
RT protein 2 (SLy2) regulates actin dynamics and B cell spreading.";
RL J. Biol. Chem. 286:13489-13501(2011).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP FUNCTION, AND INTERACTION WITH KCNH1.
RX PubMed=23144454; DOI=10.1074/jbc.m112.372540;
RA Herrmann S., Ninkovic M., Kohl T., Lorinczi E., Pardo L.A.;
RT "Cortactin controls surface expression of the voltage-gated potassium
RT channel K(V)10.1.";
RL J. Biol. Chem. 287:44151-44163(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261; THR-399; THR-401;
RP SER-405; SER-418; SER-426; SER-438 AND SER-447, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-261; THR-399;
RP THR-401; SER-405 AND SER-447, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-181 AND LYS-218, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-144; LYS-181 AND LYS-295, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [36]
RP STRUCTURE BY NMR OF 485-550.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the SH3 domain of human Src substrate cortactin.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [37]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 490-550 IN COMPLEX WITH ASAP1,
RP FUNCTION, INTERACTION WITH ASAP1 AND DNM2, AND SUBCELLULAR LOCATION.
RX PubMed=16636290; DOI=10.1073/pnas.0509166103;
RA Hashimoto S., Hirose M., Hashimoto A., Morishige M., Yamada A., Hosaka H.,
RA Akagi K., Ogawa E., Oneyama C., Agatsuma T., Okada M., Kobayashi H.,
RA Wada H., Nakano H., Ikegami T., Nakagawa A., Sabe H.;
RT "Targeting AMAP1 and cortactin binding bearing an atypical src homology
RT 3/proline interface for prevention of breast cancer invasion and
RT metastasis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7036-7041(2006).
CC -!- FUNCTION: Contributes to the organization of the actin cytoskeleton and
CC cell shape (PubMed:21296879). Plays a role in the formation of
CC lamellipodia and in cell migration. Plays a role in the regulation of
CC neuron morphology, axon growth and formation of neuronal growth cones
CC (By similarity). Through its interaction with CTTNBP2, involved in the
CC regulation of neuronal spine density (By similarity). Plays a role in
CC the invasiveness of cancer cells, and the formation of metastases
CC (PubMed:16636290). Plays a role in focal adhesion assembly and turnover
CC (By similarity). In complex with ABL1 and MYLK regulates cortical
CC actin-based cytoskeletal rearrangement critical to sphingosine 1-
CC phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement
CC (PubMed:20861316). Plays a role in intracellular protein transport and
CC endocytosis, and in modulating the levels of potassium channels present
CC at the cell membrane (PubMed:17959782). Plays a role in receptor-
CC mediated endocytosis via clathrin-coated pits (By similarity). Required
CC for stabilization of KCNH1 channels at the cell membrane
CC (PubMed:23144454). {ECO:0000250|UniProtKB:Q60598,
CC ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:16636290,
CC ECO:0000269|PubMed:17959782, ECO:0000269|PubMed:21296879,
CC ECO:0000269|PubMed:23144454}.
CC -!- SUBUNIT: Interacts with SHANK2 and SHANK3 (via its SH3 domain). Also
CC interacts with FGD1. Identified in a complex containing FGFR4, NCAM1,
CC CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ABL2 (By
CC similarity). Interacts with KCNA2 (via non-phosphorylated C-terminus)
CC (PubMed:12151401). Interacts with PLXDC2 and SRCIN1. Interacts with
CC SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with ASAP1 (via
CC Pro-rich region). Interacts (via SH3 domain) with DNM2 (By similarity).
CC Interacts with ACTN1 (By similarity). Interacts with FER
CC (PubMed:9722593). Forms a complex made of ABL1 and MYLK. Interacts with
CC CTTNBP2NL; this interaction may target CTTN to stress fibers. Interacts
CC with CTTNBP2; this interaction may target CTTN at the cell cortex or
CC dendritic spines. Interacts with KCNH1 (PubMed:23144454). Interacts
CC (via SH3 domain) with DIP2A (via N-terminus); the interaction enhances
CC CTTN acetylation and is required for proper synaptic transmission (By
CC similarity). {ECO:0000250|UniProtKB:Q60598,
CC ECO:0000250|UniProtKB:Q66HL2, ECO:0000269|PubMed:12151401,
CC ECO:0000269|PubMed:12408982, ECO:0000269|PubMed:15574754,
CC ECO:0000269|PubMed:16636290, ECO:0000269|PubMed:19146815,
CC ECO:0000269|PubMed:20861316, ECO:0000269|PubMed:21296879,
CC ECO:0000269|PubMed:23144454, ECO:0000269|PubMed:9722593}.
CC -!- INTERACTION:
CC Q14247; Q9ULH1: ASAP1; NbExp=7; IntAct=EBI-351886, EBI-346622;
CC Q14247; P50570: DNM2; NbExp=5; IntAct=EBI-351886, EBI-346547;
CC Q14247; P00533: EGFR; NbExp=4; IntAct=EBI-351886, EBI-297353;
CC Q14247; Q9UBN7: HDAC6; NbExp=4; IntAct=EBI-351886, EBI-301697;
CC Q14247; P18031: PTPN1; NbExp=2; IntAct=EBI-351886, EBI-968788;
CC Q14247; P42768: WAS; NbExp=3; IntAct=EBI-351886, EBI-346375;
CC Q14247; Q9JIY2: Cbll1; Xeno; NbExp=8; IntAct=EBI-351886, EBI-7644904;
CC Q14247; Q08460: Kcnma1; Xeno; NbExp=3; IntAct=EBI-351886, EBI-1633915;
CC Q14247; Q9QWI6-2: Srcin1; Xeno; NbExp=2; IntAct=EBI-351886, EBI-775607;
CC Q14247; B7UM99: tir; Xeno; NbExp=3; IntAct=EBI-351886, EBI-2504426;
CC Q14247-3; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-12748199, EBI-2859639;
CC Q14247-3; P32969: RPL9P9; NbExp=3; IntAct=EBI-12748199, EBI-358122;
CC Q14247-3; P78314-3: SH3BP2; NbExp=3; IntAct=EBI-12748199, EBI-12304031;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12151401}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:12151401}. Cell projection, ruffle. Cell
CC projection, dendrite {ECO:0000250}. Cell projection
CC {ECO:0000250|UniProtKB:Q66HL2}. Cell membrane
CC {ECO:0000305|PubMed:17959782}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection,
CC podosome {ECO:0000250|UniProtKB:Q01406}. Cell junction
CC {ECO:0000250|UniProtKB:Q66HL2}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q66HL2}. Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:Q66HL2}. Cell projection, dendritic spine
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12151401}.
CC Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions (By
CC similarity). Associated with membrane ruffles and lamellipodia. In the
CC presence of CTTNBP2NL, colocalizes with stress fibers (By similarity).
CC In the presence of CTTNBP2, localizes at the cell cortex (By
CC similarity). In response to neuronal activation by glutamate,
CC redistributes from dendritic spines to the dendritic shaft (By
CC similarity). Colocalizes with DNM2 at the basis of filopodia in
CC hippocampus neuron growth zones (By similarity).
CC {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14247-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14247-2; Sequence=VSP_043120, VSP_043121;
CC Name=3;
CC IsoId=Q14247-3; Sequence=VSP_043120;
CC -!- DOMAIN: The SH3 motif may mediate binding to the cytoskeleton.
CC {ECO:0000305}.
CC -!- PTM: Phosphorylated by PKN2 at both serine and threonine residues in a
CC GTP-bound Rac1-dependent manner in hyaluronan-induced astrocytes and
CC hence down-regulated CTTN ability to associates with filamentous actin
CC (By similarity). Phosphorylated on tyrosine residues in response to
CC CHRM1 activation (By similarity). Phosphorylated by PTK2/FAK1 in
CC response to cell adhesion (By similarity). Phosphorylated by FER.
CC Tyrosine phosphorylation in transformed cells may contribute to
CC cellular growth regulation and transformation. Phosphorylated in
CC response to FGR activation. Phosphorylation by SRC promotes MYLK
CC binding. {ECO:0000250, ECO:0000250|UniProtKB:Q66HL2,
CC ECO:0000269|PubMed:12408982, ECO:0000269|PubMed:15561106,
CC ECO:0000269|PubMed:9722593}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cortactin entry;
CC URL="https://en.wikipedia.org/wiki/Cortactin";
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DR EMBL; M98343; AAA58455.1; -; mRNA.
DR EMBL; AK291097; BAF83786.1; -; mRNA.
DR EMBL; AP000487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74766.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW74768.1; -; Genomic_DNA.
DR EMBL; BC008799; AAH08799.1; -; mRNA.
DR EMBL; BC033889; AAH33889.1; -; mRNA.
DR CCDS; CCDS41680.1; -. [Q14247-1]
DR CCDS; CCDS53676.1; -. [Q14247-2]
DR CCDS; CCDS8197.1; -. [Q14247-3]
DR PIR; A48063; A48063.
DR RefSeq; NP_001171669.1; NM_001184740.1. [Q14247-2]
DR RefSeq; NP_005222.2; NM_005231.3. [Q14247-1]
DR RefSeq; NP_612632.1; NM_138565.2. [Q14247-3]
DR PDB; 1X69; NMR; -; A=485-550.
DR PDB; 2D1X; X-ray; 1.90 A; A/B/C/D=490-550.
DR PDBsum; 1X69; -.
DR PDBsum; 2D1X; -.
DR AlphaFoldDB; Q14247; -.
DR BMRB; Q14247; -.
DR SMR; Q14247; -.
DR BioGRID; 108332; 280.
DR CORUM; Q14247; -.
DR DIP; DIP-33190N; -.
DR IntAct; Q14247; 102.
DR MINT; Q14247; -.
DR STRING; 9606.ENSP00000365745; -.
DR ChEMBL; CHEMBL4295820; -.
DR MoonDB; Q14247; Predicted.
DR GlyGen; Q14247; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q14247; -.
DR MetOSite; Q14247; -.
DR PhosphoSitePlus; Q14247; -.
DR SwissPalm; Q14247; -.
DR BioMuta; CTTN; -.
DR DMDM; 215273892; -.
DR OGP; Q14247; -.
DR CPTAC; CPTAC-345; -.
DR CPTAC; CPTAC-346; -.
DR CPTAC; CPTAC-963; -.
DR EPD; Q14247; -.
DR jPOST; Q14247; -.
DR MassIVE; Q14247; -.
DR MaxQB; Q14247; -.
DR PeptideAtlas; Q14247; -.
DR PRIDE; Q14247; -.
DR ProteomicsDB; 59947; -. [Q14247-1]
DR ProteomicsDB; 59948; -. [Q14247-2]
DR ProteomicsDB; 59949; -. [Q14247-3]
DR Antibodypedia; 4416; 975 antibodies from 45 providers.
DR DNASU; 2017; -.
DR Ensembl; ENST00000301843.13; ENSP00000301843.8; ENSG00000085733.16. [Q14247-1]
DR Ensembl; ENST00000346329.7; ENSP00000317189.4; ENSG00000085733.16. [Q14247-3]
DR Ensembl; ENST00000376561.7; ENSP00000365745.3; ENSG00000085733.16. [Q14247-2]
DR Ensembl; ENST00000671805.1; ENSP00000500756.1; ENSG00000288401.1. [Q14247-1]
DR Ensembl; ENST00000671849.1; ENSP00000499998.1; ENSG00000288401.1. [Q14247-2]
DR Ensembl; ENST00000672198.1; ENSP00000500927.1; ENSG00000288401.1. [Q14247-3]
DR GeneID; 2017; -.
DR KEGG; hsa:2017; -.
DR MANE-Select; ENST00000301843.13; ENSP00000301843.8; NM_005231.4; NP_005222.2.
DR UCSC; uc001opu.4; human. [Q14247-1]
DR CTD; 2017; -.
DR DisGeNET; 2017; -.
DR GeneCards; CTTN; -.
DR HGNC; HGNC:3338; CTTN.
DR HPA; ENSG00000085733; Low tissue specificity.
DR MIM; 164765; gene.
DR neXtProt; NX_Q14247; -.
DR OpenTargets; ENSG00000085733; -.
DR PharmGKB; PA27775; -.
DR VEuPathDB; HostDB:ENSG00000085733; -.
DR GeneTree; ENSGT00940000158565; -.
DR HOGENOM; CLU_019379_1_0_1; -.
DR InParanoid; Q14247; -.
DR OMA; PQKHASQ; -.
DR OrthoDB; 1243441at2759; -.
DR PhylomeDB; Q14247; -.
DR TreeFam; TF318935; -.
DR PathwayCommons; Q14247; -.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q14247; -.
DR SIGNOR; Q14247; -.
DR BioGRID-ORCS; 2017; 23 hits in 1078 CRISPR screens.
DR ChiTaRS; CTTN; human.
DR EvolutionaryTrace; Q14247; -.
DR GeneWiki; Cortactin; -.
DR GenomeRNAi; 2017; -.
DR Pharos; Q14247; Tbio.
DR PRO; PR:Q14247; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14247; protein.
DR Bgee; ENSG00000085733; Expressed in stromal cell of endometrium and 92 other tissues.
DR ExpressionAtlas; Q14247; baseline and differential.
DR Genevisible; Q14247; HS.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005522; F:profilin binding; IPI:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro.
DR GO; GO:0048870; P:cell motility; ISS:UniProtKB.
DR GO; GO:0097062; P:dendritic spine maintenance; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0097581; P:lamellipodium organization; ISS:UniProtKB.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:Ensembl.
DR GO; GO:0030516; P:regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl.
DR CDD; cd11959; SH3_Cortactin; 1.
DR InterPro; IPR015503; Cortactin.
DR InterPro; IPR035716; Cortactin_SH3.
DR InterPro; IPR003134; Hs1_Cortactin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829:SF15; PTHR10829:SF15; 3.
DR Pfam; PF02218; HS1_rep; 7.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51090; CORTACTIN; 7.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell membrane; Cell projection; Coated pit; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Isopeptide bond; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse;
KW Ubl conjugation.
FT CHAIN 1..550
FT /note="Src substrate cortactin"
FT /id="PRO_0000072189"
FT REPEAT 80..116
FT /note="Cortactin 1"
FT REPEAT 117..153
FT /note="Cortactin 2"
FT REPEAT 154..190
FT /note="Cortactin 3"
FT REPEAT 191..227
FT /note="Cortactin 4"
FT REPEAT 228..264
FT /note="Cortactin 5"
FT REPEAT 265..301
FT /note="Cortactin 6"
FT REPEAT 302..324
FT /note="Cortactin 7; truncated"
FT DOMAIN 492..550
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 348..401
FT /evidence="ECO:0000255"
FT COMPBIAS 355..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 119
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 181
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 295
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 314
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 346
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT MOD_RES 399
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 421
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 453
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 470
FT /note="Phosphotyrosine; by FAK1"
FT /evidence="ECO:0000250|UniProtKB:Q66HL2"
FT MOD_RES 486
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:15561106,
FT ECO:0000269|PubMed:17959782"
FT MOD_RES 489
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q60598"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 264..300
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043120"
FT VAR_SEQ 538..550
FT /note="YGLFPANYVELRQ -> FRELAFSCVRVALVPIKCSRDLPGQARGLRSALWR
FT VGRKDCPRRGASSRVSLLGRRGLGLMEVNPELSHPEHRSCHVRWEICLCHTVTARRIRK
FT LISFLRSREAGPVPSCSQVGGVSFQKVTWKCLGTWVPECP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043121"
FT CONFLICT 495
FT /note="I -> Y (in Ref. 1; AAA58455)"
FT /evidence="ECO:0000305"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:2D1X"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:1X69"
FT STRAND 518..523
FT /evidence="ECO:0007829|PDB:2D1X"
FT STRAND 526..534
FT /evidence="ECO:0007829|PDB:2D1X"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:2D1X"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:2D1X"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:2D1X"
SQ SEQUENCE 550 AA; 61586 MW; 7799326C2B4383BB CRC64;
MWKASAGHAV SIAQDDAGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE
NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDKSAV GHEYQSKLSK HCSQVDSVRG
FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG
KTEKHESQRD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT
DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSAAVGFDYK EKLAKHESQQ
DYSKGFGGKY GVQKDRMDKN ASTFEDVTQV SSAYQKTVPV EAVTSKTSNI RANFENLAKE
KEQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKTQ TPPVSPAPQP TEERLPSSPV
YEDAASFKAE LSYRGPVSGT EPEPVYSMEA ADYREASSQQ GLAYATEAVY ESAEAPGHYP
AEDSTYDEYE NDLGITAVAL YDYQAAGDDE ISFDPDDIIT NIEMIDDGWW RGVCKGRYGL
FPANYVELRQ
