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 27-MAR-2024, entry version 226. 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 IDENTIFICATION IN A COMPLEX WITH NEDD9 AND AURKA, INTERACTION WITH NEDD9, RP SUBCELLULAR LOCATION, AND ACETYLATION. RX PubMed=24574519; DOI=10.1158/1541-7786.mcr-13-0654; RA Kozyreva V.K., McLaughlin S.L., Livengood R.H., Calkins R.A., Kelley L.C., RA Rajulapati A., Ice R.J., Smolkin M.B., Weed S.A., Pugacheva E.N.; RT "NEDD9 regulates actin dynamics through cortactin deacetylation in an RT AURKA/HDAC6-dependent manner."; RL Mol. Cancer Res. 12:681-693(2014). RN [35] 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 [36] 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 [37] 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 [38] 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 focal adhesion assembly and turnover (By similarity). In complex with CC ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement CC critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell CC (EC) barrier enhancement (PubMed:20861316). Plays a role in CC intracellular protein transport and endocytosis, and in modulating the CC levels of potassium channels present at the cell membrane CC (PubMed:17959782). Plays a role in receptor-mediated endocytosis via CC clathrin-coated pits (By similarity). Required for stabilization of CC KCNH1 channels at the cell membrane (PubMed:23144454). Plays a role in CC the invasiveness of cancer cells, and the formation of metastases CC (PubMed:16636290). {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: Part of a complex composed of NEDD9, AURKA and CTTN; within CC the complex NEDD9 acts as a scaffold protein and is required for CC complex formation (PubMed:24574519). Interacts (via N-terminus) with CC NEDD9 (PubMed:24574519). Identified in a complex containing FGFR4, CC NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Forms a complex CC made of ABL1 and MYLK (PubMed:20861316). Interacts with SHANK2 and CC SHANK3 (via its SH3 domain). Interacts with FGD1. Interacts with ABL2 CC (By similarity). Interacts with KCNA2 (via non-phosphorylated C- CC terminus) (PubMed:12151401). Interacts with PLXDC2 and SRCIN1. CC Interacts with SAMSN1 (via SH3 domain). Interacts (via SH3 domain) with CC ASAP1 (via Pro-rich region). Interacts (via SH3 domain) with DNM2 (By CC similarity). Interacts with ACTN1 (By similarity). Interacts with FER CC (PubMed:9722593). Interacts with CTTNBP2NL; this interaction may target CC CTTN to stress fibers. Interacts with CTTNBP2; this interaction may CC target CTTN at the cell cortex or dendritic spines. Interacts with CC KCNH1 (PubMed:23144454). Interacts (via SH3 domain) with DIP2A (via N- CC terminus); the interaction enhances CTTN acetylation and is required CC for proper synaptic transmission (By similarity). CC {ECO:0000250|UniProtKB:Q60598, ECO:0000250|UniProtKB:Q66HL2, CC ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:12408982, CC ECO:0000269|PubMed:15574754, ECO:0000269|PubMed:16636290, CC ECO:0000269|PubMed:19146815, ECO:0000269|PubMed:20861316, CC ECO:0000269|PubMed:21296879, ECO:0000269|PubMed:23144454, CC ECO:0000269|PubMed:24574519, 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, ECO:0000269|PubMed:24574519}. Cell CC projection, ruffle. Cell projection, dendrite {ECO:0000250}. Cell CC projection {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 Endoplasmic reticulum {ECO:0000250|UniProtKB:Q01406}. Note=Colocalizes CC transiently with PTK2/FAK1 at focal adhesions (By similarity). CC Associated with membrane ruffles and lamellipodia. In the presence of CC CTTNBP2NL, colocalizes with stress fibers (By similarity). In the CC presence of CTTNBP2, localizes at the cell cortex (By similarity). In CC response to neuronal activation by glutamate, redistributes from CC dendritic spines to the dendritic shaft (By similarity). Colocalizes CC with DNM2 at the basis of filopodia in hippocampus neuron growth zones CC (By similarity). {ECO:0000250|UniProtKB:Q60598, CC 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 -!- PTM: Acetylated. {ECO:0000269|PubMed:24574519}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Cortactin entry; CC URL="https://en.wikipedia.org/wiki/Cortactin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 412. DR CORUM; Q14247; -. DR DIP; DIP-33190N; -. DR IntAct; Q14247; 107. DR MINT; Q14247; -. DR STRING; 9606.ENSP00000365745; -. DR ChEMBL; CHEMBL4295820; -. DR MoonDB; Q14247; Predicted. DR GlyCosmos; Q14247; 2 sites, 1 glycan. DR GlyGen; Q14247; 12 sites, 1 O-linked glycan (12 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 PaxDb; 9606-ENSP00000365745; -. DR PeptideAtlas; Q14247; -. DR ProteomicsDB; 59947; -. [Q14247-1] DR ProteomicsDB; 59948; -. [Q14247-2] DR ProteomicsDB; 59949; -. [Q14247-3] DR Pumba; Q14247; -. DR Antibodypedia; 4416; 1087 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 AGR; HGNC:3338; -. 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; KFDESWW; -. DR OrthoDB; 101008at2759; -. 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 1154 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 94 other cell types or tissues. DR ExpressionAtlas; Q14247; baseline and differential. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB. 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:0030139; C:endocytic vesicle; IBA:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; 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:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005522; F:profilin binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. 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:0030516; P:regulation of axon extension; ISS:UniProtKB. DR GO; GO:1901524; P:regulation of mitophagy; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IEA:Ensembl. DR CDD; cd11959; SH3_Cortactin; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. 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; CORTACTIN AND DREBRIN; 1. DR PANTHER; PTHR10829:SF15; SRC SUBSTRATE CORTACTIN; 1. DR Pfam; PF02218; HS1_rep; 7. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51090; CORTACTIN; 7. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q14247; HS. 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; Endoplasmic reticulum; Isopeptide bond; KW Membrane; Methylation; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Synapse; 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 //