EWS_HUMAN
ID EWS_HUMAN Reviewed; 656 AA.
AC Q01844; B0QYK1; Q5THL0; Q92635; Q96FE8; Q96MN4; Q96MX4; Q9BWA2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=RNA-binding protein EWS;
DE AltName: Full=EWS oncogene;
DE AltName: Full=Ewing sarcoma breakpoint region 1 protein;
GN Name=EWSR1; Synonyms=EWS;
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 EWS), INVOLVEMENT IN EWS, AND
RP CHROMOSOMAL TRANSLOCATION WITH FLI.
RC TISSUE=Fetal brain;
RX PubMed=1522903; DOI=10.1038/359162a0;
RA Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M.,
RA Kovar H., Joubert I., de Jong P., Rouleau G., Aurias A., Thomas G.;
RT "Gene fusion with an ETS DNA-binding domain caused by chromosome
RT translocation in human tumours.";
RL Nature 359:162-165(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8307570; DOI=10.1016/s0888-7543(05)80363-5;
RA Plougastel B., Zucman J., Peter M., Thomas G., Delattre O.;
RT "Genomic structure of the EWS gene and its relationship to EWSR1, a site of
RT tumor-associated chromosome translocation.";
RL Genomics 18:609-615(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Genomic sequence of the human EWS gene with the 5' flanking region.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS EWS; 3 AND 4).
RC TISSUE=Lymph, Muscle, Placenta, and Skin;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-345.
RX PubMed=8975699; DOI=10.1006/geno.1996.0625;
RA Zucman-Rossi J., Legoix P., Thomas G.;
RT "Identification of new members of the Gas2 and Ras families in the 22q12
RT chromosome region.";
RL Genomics 38:247-254(1996).
RN [10]
RP PROTEIN SEQUENCE OF 128-158; 233-247; 268-324; 334-364; 393-439; 447-518
RP AND 551-641, METHYLATION AT ARG-300; ARG-302; ARG-304; ARG-309; ARG-314;
RP ARG-317; ARG-321; ARG-455; ARG-464; ARG-471; ARG-490; ARG-494; ARG-500;
RP ARG-503; ARG-506; ARG-563; ARG-565; ARG-572; ARG-575; ARG-581; ARG-589;
RP ARG-592; ARG-596; ARG-600; ARG-603; ARG-607; ARG-615; ARG-633 AND ARG-636,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11278906; DOI=10.1074/jbc.m011446200;
RA Belyanskaya L.L., Gehrig P.M., Gehring H.;
RT "Exposure on cell surface and extensive arginine methylation of Ewing
RT sarcoma (EWS) protein.";
RL J. Biol. Chem. 276:18681-18687(2001).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 241-268.
RC TISSUE=Placenta;
RX PubMed=7542907; DOI=10.1002/gcc.2870130209;
RA Bhagirath T., Abe S., Nojima T., Yoshida M.C.;
RT "Molecular analysis of a t(11;22) translocation junction in a case of
RT Ewing's sarcoma.";
RL Genes Chromosomes Cancer 13:126-132(1995).
RN [12]
RP PROTEIN SEQUENCE OF 269-292; 393-404; 411-439; 491-500 AND 615-632,
RP METHYLATION AT ARG-494 AND ARG-615, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Zebisch A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [13]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-266.
RX PubMed=9341188; DOI=10.1074/jbc.272.43.27369;
RA Deloulme J.C., Prichard L., Delattre O., Storm D.R.;
RT "The prooncoprotein EWS binds calmodulin and is phosphorylated by protein
RT kinase C through an IQ domain.";
RL J. Biol. Chem. 272:27369-27377(1997).
RN [14]
RP CHROMOSOMAL TRANSLOCATION WITH ATF1.
RX PubMed=8401579; DOI=10.1038/ng0893-341;
RA Zucman J., Delattre O., Desmaze C., Epstein A.L., Stenman G., Speleman F.,
RA Fletchers C.D., Aurias A., Thomas G.;
RT "EWS and ATF-1 gene fusion induced by t(12;22) translocation in malignant
RT melanoma of soft parts.";
RL Nat. Genet. 4:341-345(1993).
RN [15]
RP ALTERNATIVE SPLICING, AND RNA-BINDING.
RX PubMed=8084618;
RA Ohno T., Ouchida M., Lee L., Gatalica Z., Rao V.N., Reddy E.S.P.;
RT "The EWS gene, involved in Ewing family of tumors, malignant melanoma of
RT soft parts and desmoplastic small round cell tumors, codes for an RNA
RT binding protein with novel regulatory domains.";
RL Oncogene 9:3087-3097(1994).
RN [16]
RP CHROMOSOMAL TRANSLOCATION WITH NR4A3.
RX PubMed=7539287; DOI=10.1002/gcc.2870120412;
RA Gill S., McManus A.P., Crew A.J., Benjamin H., Sheer D., Gusterson B.A.,
RA Pinkerton C.R., Patel K., Cooper C.S., Shipley J.M.;
RT "Fusion of the EWS gene to a DNA segment from 9q22-31 in a human myxoid
RT chondrosarcoma.";
RL Genes Chromosomes Cancer 12:307-310(1995).
RN [17]
RP CHROMOSOMAL TRANSLOCATION WITH ETV1.
RX PubMed=7700648;
RA Jeon I.-S., Davis J.N., Braun B.S., Sublett J.E., Roussel M.F., Denny C.T.,
RA Shapiro D.N.;
RT "A variant Ewing's sarcoma translocation (7;22) fuses the EWS gene to the
RT ETS gene ETV1.";
RL Oncogene 10:1229-1234(1995).
RN [18]
RP CHROMOSOMAL TRANSLOCATION WITH WT1.
RX PubMed=7862627; DOI=10.1073/pnas.92.4.1028;
RA Gerald W.L., Rosai J., Ladanyi M.;
RT "Characterization of the genomic breakpoint and chimeric transcripts in the
RT EWS-WT1 gene fusion of desmoplastic small round cell tumor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1028-1032(1995).
RN [19]
RP INVOLVEMENT IN EWS, AND CHROMOSOMAL TRANSLOCATION WITH FEV.
RX PubMed=9121764; DOI=10.1038/sj.onc.1200933;
RA Peter M., Couturier J., Pacquement H., Michon J., Thomas G., Magdelenat H.,
RA Delattre O.;
RT "A new member of the ETS family fused to EWS in Ewing tumors.";
RL Oncogene 14:1159-1164(1997).
RN [20]
RP INTERACTION WITH SF1.
RX PubMed=9660765; DOI=10.1074/jbc.273.29.18086;
RA Zhang D., Paley A.J., Childs G.;
RT "The transcriptional repressor ZFM1 interacts with and modulates the
RT ability of EWS to activate transcription.";
RL J. Biol. Chem. 273:18086-18091(1998).
RN [21]
RP CHARACTERIZATION.
RX PubMed=10767297; DOI=10.1074/jbc.m002961200;
RA Li K.K.C., Lee K.A.W.;
RT "Transcriptional activation by the Ewing's sarcoma (EWS) oncogene can be
RT cis-repressed by the EWS RNA-binding domain.";
RL J. Biol. Chem. 275:23053-23058(2000).
RN [22]
RP CHROMOSOMAL TRANSLOCATION WITH PATZ1.
RX PubMed=10949935; DOI=10.1038/sj.onc.1203762;
RA Mastrangelo T., Modena P., Tornielli S., Bullrich F., Testi A.,
RA Mezzelani A., Radice P., Azzarelli A., Pilotti S., Croce C., Pierotti M.,
RA Sozzi G.;
RT "A novel zinc finger gene is fused to EWS in small round cell tumor.";
RL Oncogene 19:3799-3804(2000).
RN [23]
RP CHROMOSOMAL TRANSLOCATION WITH ERG, CHROMOSOMAL TRANSLOCATION WITH FLI1,
RP AND INVOLVEMENT IN EWS.
RX PubMed=15044653; DOI=10.1056/nejmc032965;
RA Bielack S.S., Paulussen M., Koehler G.;
RT "A patient with two Ewing's sarcomas with distinct EWS fusion
RT transcripts.";
RL N. Engl. J. Med. 350:1364-1365(2004).
RN [24]
RP CHARACTERIZATION OF THE EWSR1-FEV FUSION PROTEIN.
RX PubMed=17172842; DOI=10.4161/cc.5.23.3505;
RA Braunreiter C.L., Hancock J.D., Coffin C.M., Boucher K.M., Lessnick S.L.;
RT "Expression of EWS-ETS fusions in NIH3T3 cells reveals significant
RT differences to Ewing's sarcoma.";
RL Cell Cycle 5:2753-2759(2006).
RN [25]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF
RP ARG-648; ARG-651; ARG-652; ASP-653; ARG-654; PRO-655 AND TYR-656.
RX PubMed=16965792; DOI=10.1016/j.jmb.2006.08.018;
RA Zakaryan R.P., Gehring H.;
RT "Identification and characterization of the nuclear localization/retention
RT signal in the EWS proto-oncoprotein.";
RL J. Mol. Biol. 363:27-38(2006).
RN [26]
RP INTERACTION WITH TDRD3.
RX PubMed=18632687; DOI=10.1093/hmg/ddn203;
RA Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.;
RT "TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic
RT stress granules.";
RL Hum. Mol. Genet. 17:3055-3074(2008).
RN [27]
RP METHYLATION AT ARG-490; ARG-572; ARG-596; ARG-603 AND ARG-607.
RX PubMed=18320585; DOI=10.1002/prot.22004;
RA Pahlich S., Zakaryan R.P., Gehring H.;
RT "Identification of proteins interacting with protein arginine
RT methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of
RT its methylation state.";
RL Proteins 72:1125-1137(2008).
RN [28]
RP 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 [29]
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 [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [31]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-471; ARG-486 AND ARG-615, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [32]
RP STRUCTURE BY NMR OF 353-453.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA recognition motif of Ewing sarcoma (EWS)
RT protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [33]
RP CHROMOSOMAL TRANSLOCATION WITH ATF1, AND INVOLVEMENT IN AFH.
RX PubMed=15884099; DOI=10.1002/gcc.20201;
RA Hallor K.H., Mertens F., Jin Y., Meis-Kindblom J.M., Kindblom L.-G.,
RA Behrendtz M., Kalen A., Mandahl N., Panagopoulos I.;
RT "Fusion of the EWSR1 and ATF1 genes without expression of the MITF-M
RT transcript in angiomatoid fibrous histiocytoma.";
RL Genes Chromosomes Cancer 44:97-102(2005).
RN [34]
RP CHROMOSOMAL TRANSLOCATION WITH CREB1, AND INVOLVEMENT IN AFH.
RX PubMed=17724745; DOI=10.1002/gcc.20491;
RA Antonescu C.R., Dal Cin P., Nafa K., Teot L.A., Surti U., Fletcher C.D.,
RA Ladanyi M.;
RT "EWSR1-CREB1 is the predominant gene fusion in angiomatoid fibrous
RT histiocytoma.";
RL Genes Chromosomes Cancer 46:1051-1060(2007).
CC -!- FUNCTION: Might normally function as a transcriptional repressor. EWS-
CC fusion-proteins (EFPS) may play a role in the tumorigenic process. They
CC may disturb gene expression by mimicking, or interfering with the
CC normal function of CTD-POLII within the transcription initiation
CC complex. They may also contribute to an aberrant activation of the
CC fusion protein target genes.
CC -!- SUBUNIT: Binds POLR2C, SF1, calmodulin and RNA. Interacts with
CC PTK2B/FAK2 and TDRD3. Binds calmodulin in the presence, but not in the
CC absence, of calcium ion. Forms a complex with REC8, PRDM9, SYCP3 and
CC SYCP1; complex formation is dependent of phosphorylated form of REC8
CC and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the
CC chromosomal axis through REC8 (By similarity).
CC {ECO:0000250|UniProtKB:Q61545, ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:9660765}.
CC -!- INTERACTION:
CC Q01844; Q8N5M1: ATPAF2; NbExp=7; IntAct=EBI-739737, EBI-1166928;
CC Q01844; P54252: ATXN3; NbExp=4; IntAct=EBI-739737, EBI-946046;
CC Q01844; Q09472: EP300; NbExp=2; IntAct=EBI-739737, EBI-447295;
CC Q01844; Q01844: EWSR1; NbExp=3; IntAct=EBI-739737, EBI-739737;
CC Q01844; P35637: FUS; NbExp=5; IntAct=EBI-739737, EBI-400434;
CC Q01844; Q92993: KAT5; NbExp=2; IntAct=EBI-739737, EBI-399080;
CC Q01844; Q8NDC0: MAPK1IP1L; NbExp=5; IntAct=EBI-739737, EBI-741424;
CC Q01844; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-739737, EBI-724639;
CC Q01844; O15162: PLSCR1; NbExp=4; IntAct=EBI-739737, EBI-740019;
CC Q01844; Q99873: PRMT1; NbExp=2; IntAct=EBI-739737, EBI-78738;
CC Q01844; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-739737, EBI-740924;
CC Q01844; Q9NS23-2: RASSF1; NbExp=3; IntAct=EBI-739737, EBI-438698;
CC Q01844; O95486: SEC24A; NbExp=3; IntAct=EBI-739737, EBI-749911;
CC Q01844; O94855: SEC24D; NbExp=3; IntAct=EBI-739737, EBI-748817;
CC Q01844; Q13485: SMAD4; NbExp=3; IntAct=EBI-739737, EBI-347263;
CC Q01844; Q9BWW4: SSBP3; NbExp=3; IntAct=EBI-739737, EBI-2902395;
CC Q01844; Q92734: TFG; NbExp=3; IntAct=EBI-739737, EBI-357061;
CC Q01844; Q13077: TRAF1; NbExp=3; IntAct=EBI-739737, EBI-359224;
CC Q01844; Q12933: TRAF2; NbExp=3; IntAct=EBI-739737, EBI-355744;
CC Q01844; P49910: ZNF165; NbExp=2; IntAct=EBI-739737, EBI-741694;
CC Q01844-3; P54252: ATXN3; NbExp=9; IntAct=EBI-25973273, EBI-946046;
CC Q01844-4; P54252: ATXN3; NbExp=3; IntAct=EBI-25896785, EBI-946046;
CC Q01844-4; P42858: HTT; NbExp=3; IntAct=EBI-25896785, EBI-466029;
CC Q01844-4; O76024: WFS1; NbExp=3; IntAct=EBI-25896785, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16965792}. Cytoplasm
CC {ECO:0000269|PubMed:16965792}. Cell membrane
CC {ECO:0000269|PubMed:16965792}. Note=Relocates from cytoplasm to
CC ribosomes upon PTK2B/FAK2 activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=EWS;
CC IsoId=Q01844-1; Sequence=Displayed;
CC Name=EWS-B;
CC IsoId=Q01844-2; Sequence=VSP_005793;
CC Name=3;
CC IsoId=Q01844-3; Sequence=VSP_043453;
CC Name=4;
CC IsoId=Q01844-4; Sequence=VSP_043452, VSP_043454;
CC Name=5;
CC IsoId=Q01844-5; Sequence=VSP_043451, VSP_043453;
CC Name=6;
CC IsoId=Q01844-6; Sequence=VSP_045412;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: EWS activation domain (EAD) functions as a potent activation
CC domain in EFPS. EWSR1 binds POLR2C but not POLR2E or POLR2G, whereas
CC the isolated EAD binds POLR2E and POLR2G but not POLR2C. Cis-linked
CC RNA-binding domain (RBD) can strongly and specifically repress trans-
CC activation by the EAD.
CC -!- PTM: Phosphorylated; calmodulin-binding inhibits phosphorylation of
CC Ser-266. {ECO:0000269|PubMed:9341188}.
CC -!- PTM: Highly methylated on arginine residues. Methylation is mediated by
CC PRMT1 and, at lower level by PRMT8. {ECO:0000269|PubMed:11278906,
CC ECO:0000269|PubMed:18320585, ECO:0000269|Ref.12}.
CC -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant,
CC metastatic, primitive small round cell tumor of bone and soft tissue
CC that affects children and adolescents. It belongs to the Ewing sarcoma
CC family of tumors, a group of morphologically heterogeneous neoplasms
CC that share the same cytogenetic features. They are considered neural
CC tumors derived from cells of the neural crest. Ewing sarcoma represents
CC the less differentiated form of the tumors.
CC {ECO:0000269|PubMed:15044653, ECO:0000269|PubMed:1522903,
CC ECO:0000269|PubMed:7700648, ECO:0000269|PubMed:9121764}. Note=The
CC protein represented in this entry is involved in disease pathogenesis.
CC Chromosomal aberrations involving EWSR1 are found in patients with
CC Ewing sarcoma. Translocation t(11;22)(q24;q12) with FLI1
CC (PubMed:1522903, PubMed:15044653). Translocation t(7;22)(p22;q12) with
CC ETV1 (PubMed:7700648). Translocation t(21;22)(q22;q21) with ERG
CC (PubMed:15044653). Translocation t(2;21;22)(q23;q22;q12) that forms a
CC EWSR1-FEV fusion protein with potential oncogenic activity
CC (PubMed:9121764). {ECO:0000269|PubMed:15044653,
CC ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648,
CC ECO:0000269|PubMed:9121764}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 has been found
CC in extraskeletal myxoid chondrosarcoma. Translocation t(9;22)(q22-
CC 31;q11-12) with NR4A3. {ECO:0000269|PubMed:7539287}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is associated
CC with desmoplastic small round cell tumor (DSRCT). Translocation
CC t(11;22)(p13;q12) with WT1. {ECO:0000269|PubMed:7862627}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is associated
CC with malignant melanoma of soft parts (MMSP). Translocation
CC t(12;22)(q13;q12) with ATF1. Malignant melanoma of soft parts, also
CC known as soft tissue clear cell sarcoma, is a rare tumor developing in
CC tendons and aponeuroses. {ECO:0000269|PubMed:8401579}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is associated
CC with small round cell sarcoma. Translocation t(11;22)(p36.1;q12) with
CC PATZ1. {ECO:0000269|PubMed:10949935}.
CC -!- DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A
CC distinct variant of malignant fibrous histiocytoma that typically
CC occurs in children and adolescents and is manifest by nodular
CC subcutaneous growth. Characteristic microscopic features include
CC lobulated sheets of histiocyte-like cells intimately associated with
CC areas of hemorrhage and cystic pseudovascular spaces, as well as a
CC striking cuffing of inflammatory cells, mimicking a lymph node
CC metastasis. {ECO:0000269|PubMed:15884099, ECO:0000269|PubMed:17724745}.
CC Note=The gene represented in this entry is involved in disease
CC pathogenesis. Chromosomal aberrations involving EWSR1 are found in
CC patients with angiomatoid fibrous histiocytoma. Translocation
CC t(12;22)(q13;q12) with ATF1 generates a chimeric EWSR1/ATF1 protein
CC (PubMed:15884099). Translocation t(2;22)(q33;q12) with CREB1 generates
CC a EWSR1/CREB1 fusion gene that is most common genetic abnormality in
CC this tumor type (PubMed:17724745). {ECO:0000269|PubMed:15884099,
CC ECO:0000269|PubMed:17724745}.
CC -!- DISEASE: Note=EFPS arise due to chromosomal translocations in which
CC EWSR1 is fused to a variety of cellular transcription factors. EFPS are
CC very potent transcriptional activators dependent on the EAD and a C-
CC terminal DNA-binding domain contributed by the fusion partner. The
CC spectrum of malignancies associated with EFPS are thought to arise via
CC EFP-induced transcriptional deregulation, with the tumor phenotype
CC specified by the EWSR1 fusion partner and cell type. Transcriptional
CC repression of the transforming growth factor beta type II receptor (TGF
CC beta RII) is an important target of the EWS-FLI1, EWS-ERG, or EWS-ETV1
CC oncogene. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EWSR1ID85.html";
CC ---------------------------------------------------------------------------
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DR EMBL; X66899; CAA47350.1; -; mRNA.
DR EMBL; X72990; CAA51489.1; -; Genomic_DNA.
DR EMBL; X72991; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72992; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72993; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72994; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72995; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72996; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72997; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72998; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X72999; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X73000; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X73001; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X73002; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X73003; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; X73004; CAA51489.1; JOINED; Genomic_DNA.
DR EMBL; Y07848; CAA69177.1; -; Genomic_DNA.
DR EMBL; CR456490; CAG30376.1; -; mRNA.
DR EMBL; AK056309; BAB71145.1; -; mRNA.
DR EMBL; AK056681; BAB71252.1; -; mRNA.
DR EMBL; AL031186; CAI18001.1; -; Genomic_DNA.
DR EMBL; AC000026; CAI18001.1; JOINED; Genomic_DNA.
DR EMBL; AC002059; CAI18001.1; JOINED; Genomic_DNA.
DR EMBL; AL031186; CAQ10937.1; -; Genomic_DNA.
DR EMBL; AC000026; CAQ10937.1; JOINED; Genomic_DNA.
DR EMBL; AC002059; CAQ10937.1; JOINED; Genomic_DNA.
DR EMBL; AL031186; CAQ10938.1; -; Genomic_DNA.
DR EMBL; AC000026; CAQ10938.1; JOINED; Genomic_DNA.
DR EMBL; AC002059; CAQ10938.1; JOINED; Genomic_DNA.
DR EMBL; AL031186; CAQ10940.1; -; Genomic_DNA.
DR EMBL; AC000026; CAQ10940.1; JOINED; Genomic_DNA.
DR EMBL; AC002059; CAQ10940.1; JOINED; Genomic_DNA.
DR EMBL; CH471095; EAW59780.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59781.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59785.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59786.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59787.1; -; Genomic_DNA.
DR EMBL; BC000527; AAH00527.1; -; mRNA.
DR EMBL; BC004817; AAH04817.1; -; mRNA.
DR EMBL; BC011048; AAH11048.1; -; mRNA.
DR EMBL; BC072442; AAH72442.1; -; mRNA.
DR EMBL; Y08806; CAA70044.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB016435; BAA31990.1; -; Genomic_DNA.
DR CCDS; CCDS13851.1; -. [Q01844-1]
DR CCDS; CCDS13852.2; -. [Q01844-5]
DR CCDS; CCDS54512.1; -. [Q01844-4]
DR CCDS; CCDS54513.1; -. [Q01844-3]
DR CCDS; CCDS54514.1; -. [Q01844-6]
DR PIR; A49358; A49358.
DR RefSeq; NP_001156757.1; NM_001163285.1. [Q01844-3]
DR RefSeq; NP_001156758.1; NM_001163286.1. [Q01844-6]
DR RefSeq; NP_001156759.1; NM_001163287.1. [Q01844-4]
DR RefSeq; NP_005234.1; NM_005243.3. [Q01844-1]
DR RefSeq; NP_053733.2; NM_013986.3. [Q01844-5]
DR PDB; 2CPE; NMR; -; A=353-453.
DR PDBsum; 2CPE; -.
DR AlphaFoldDB; Q01844; -.
DR BMRB; Q01844; -.
DR SMR; Q01844; -.
DR BioGRID; 108431; 781.
DR CORUM; Q01844; -.
DR DIP; DIP-34449N; -.
DR IntAct; Q01844; 212.
DR MINT; Q01844; -.
DR STRING; 9606.ENSP00000400142; -.
DR BindingDB; Q01844; -.
DR ChEMBL; CHEMBL3351202; -.
DR GlyGen; Q01844; 46 sites, 2 O-linked glycans (46 sites).
DR iPTMnet; Q01844; -.
DR MetOSite; Q01844; -.
DR PhosphoSitePlus; Q01844; -.
DR SwissPalm; Q01844; -.
DR BioMuta; EWSR1; -.
DR DMDM; 544261; -.
DR EPD; Q01844; -.
DR jPOST; Q01844; -.
DR MassIVE; Q01844; -.
DR MaxQB; Q01844; -.
DR PaxDb; Q01844; -.
DR PeptideAtlas; Q01844; -.
DR PRIDE; Q01844; -.
DR ProteomicsDB; 2658; -.
DR ProteomicsDB; 58004; -. [Q01844-1]
DR ProteomicsDB; 58005; -. [Q01844-2]
DR ProteomicsDB; 58006; -. [Q01844-3]
DR ProteomicsDB; 58007; -. [Q01844-4]
DR ProteomicsDB; 58008; -. [Q01844-5]
DR Antibodypedia; 3786; 577 antibodies from 41 providers.
DR DNASU; 2130; -.
DR Ensembl; ENST00000332035.10; ENSP00000331699.6; ENSG00000182944.18. [Q01844-6]
DR Ensembl; ENST00000333395.10; ENSP00000327456.6; ENSG00000182944.18. [Q01844-4]
DR Ensembl; ENST00000397938.7; ENSP00000381031.2; ENSG00000182944.18. [Q01844-1]
DR Ensembl; ENST00000406548.5; ENSP00000385726.1; ENSG00000182944.18. [Q01844-3]
DR Ensembl; ENST00000414183.6; ENSP00000400142.2; ENSG00000182944.18. [Q01844-5]
DR GeneID; 2130; -.
DR KEGG; hsa:2130; -.
DR MANE-Select; ENST00000397938.7; ENSP00000381031.2; NM_005243.4; NP_005234.1.
DR UCSC; uc003aes.5; human. [Q01844-1]
DR CTD; 2130; -.
DR DisGeNET; 2130; -.
DR GeneCards; EWSR1; -.
DR HGNC; HGNC:3508; EWSR1.
DR HPA; ENSG00000182944; Low tissue specificity.
DR MalaCards; EWSR1; -.
DR MIM; 133450; gene.
DR MIM; 612160; phenotype.
DR MIM; 612219; phenotype.
DR neXtProt; NX_Q01844; -.
DR OpenTargets; ENSG00000182944; -.
DR Orphanet; 83469; Desmoplastic small round cell tumor.
DR Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
DR Orphanet; 97338; Melanoma of soft tissue.
DR Orphanet; 319; Skeletal Ewing sarcoma.
DR PharmGKB; PA27921; -.
DR VEuPathDB; HostDB:ENSG00000182944; -.
DR eggNOG; KOG1995; Eukaryota.
DR GeneTree; ENSGT00940000154191; -.
DR HOGENOM; CLU_025609_1_1_1; -.
DR InParanoid; Q01844; -.
DR OMA; GPIRINR; -.
DR OrthoDB; 1539664at2759; -.
DR PhylomeDB; Q01844; -.
DR TreeFam; TF322599; -.
DR PathwayCommons; Q01844; -.
DR SignaLink; Q01844; -.
DR SIGNOR; Q01844; -.
DR BioGRID-ORCS; 2130; 672 hits in 1100 CRISPR screens.
DR ChiTaRS; EWSR1; human.
DR EvolutionaryTrace; Q01844; -.
DR GeneWiki; Ewing_sarcoma_breakpoint_region_1; -.
DR GenomeRNAi; 2130; -.
DR Pharos; Q01844; Tbio.
DR PRO; PR:Q01844; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q01844; protein.
DR Bgee; ENSG00000182944; Expressed in right uterine tube and 205 other tissues.
DR ExpressionAtlas; Q01844; baseline and differential.
DR Genevisible; Q01844; HS.
DR GO; GO:0015030; C:Cajal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR CDD; cd12533; RRM_EWS; 1.
DR DisProt; DP00632; -.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034869; EWS_RRM.
DR InterPro; IPR033109; EWSR1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034870; TET_fam.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23238; PTHR23238; 1.
DR PANTHER; PTHR23238:SF3; PTHR23238:SF3; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
KW Cell membrane; Chromosomal rearrangement; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..656
FT /note="RNA-binding protein EWS"
FT /id="PRO_0000081586"
FT REPEAT 8..16
FT /note="1"
FT REPEAT 17..27
FT /note="2"
FT REPEAT 28..34
FT /note="3"
FT REPEAT 35..42
FT /note="4"
FT REPEAT 43..50
FT /note="5"
FT REPEAT 51..59
FT /note="6"
FT REPEAT 60..68
FT /note="7"
FT REPEAT 69..75
FT /note="8"
FT REPEAT 76..84
FT /note="9"
FT REPEAT 85..91
FT /note="10"
FT REPEAT 92..110
FT /note="11"
FT REPEAT 111..116
FT /note="12"
FT REPEAT 117..125
FT /note="13"
FT REPEAT 126..156
FT /note="14"
FT REPEAT 157..163
FT /note="15"
FT REPEAT 164..170
FT /note="16"
FT REPEAT 171..177
FT /note="17"
FT REPEAT 178..188
FT /note="18"
FT REPEAT 189..193
FT /note="19"
FT REPEAT 194..201
FT /note="20"
FT REPEAT 202..206
FT /note="21"
FT REPEAT 207..212
FT /note="22"
FT REPEAT 213..218
FT /note="23"
FT REPEAT 219..224
FT /note="24"
FT REPEAT 225..230
FT /note="25"
FT REPEAT 231..238
FT /note="26"
FT REPEAT 239..245
FT /note="27"
FT REPEAT 246..252
FT /note="28"
FT REPEAT 253..259
FT /note="29"
FT DOMAIN 256..285
FT /note="IQ"
FT REPEAT 260..276
FT /note="30"
FT REPEAT 277..285
FT /note="31"
FT DOMAIN 361..447
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 518..549
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 1..285
FT /note="EAD (Gln/Pro/Thr-rich)"
FT REGION 8..285
FT /note="31 X approximate tandem repeats"
FT REGION 123..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 639..656
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16965792"
FT COMPBIAS 133..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 265
FT /note="Breakpoint for translocation to form chimeric
FT EWSR1/ATF1 protein"
FT SITE 348..349
FT /note="Breakpoint for insertion to form EWSR1-FEV fusion
FT protein"
FT MOD_RES 266
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 300
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 302
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 304
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 309
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 314
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 317
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 321
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61545"
FT MOD_RES 455
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 464
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 471
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 471
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0007744|PubMed:24129315"
FT MOD_RES 486
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 490
FT /note="Asymmetric dimethylarginine; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 494
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906, ECO:0000269|Ref.12"
FT MOD_RES 500
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 503
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 506
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 506
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61545"
FT MOD_RES 563
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 565
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 572
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 572
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 575
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 581
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 589
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 592
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 596
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 596
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 600
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 603
FT /note="Asymmetric dimethylarginine; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 607
FT /note="Asymmetric dimethylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 607
FT /note="Omega-N-methylarginine; alternate; by PRMT8"
FT /evidence="ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585"
FT MOD_RES 615
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:11278906, ECO:0000269|Ref.12"
FT MOD_RES 615
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 633
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT MOD_RES 636
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:11278906"
FT VAR_SEQ 74
FT /note="P -> PTVEGTS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043451"
FT VAR_SEQ 136..191
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045412"
FT VAR_SEQ 266..338
FT /note="Missing (in isoform EWS-B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005793"
FT VAR_SEQ 326..354
FT /note="SAGERGGFNKPGGPMDEGPDLDLGPPVDP -> LQSESLVYTSILKKYPYSV
FT LSRQHNEKWD (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043452"
FT VAR_SEQ 326
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15461802, ECO:0000303|PubMed:15489334"
FT /id="VSP_043453"
FT VAR_SEQ 355..656
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043454"
FT MUTAGEN 648
FT /note="R->A: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 648
FT /note="R->K: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 651
FT /note="R->A: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 652
FT /note="R->A: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 652
FT /note="R->K: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 653
FT /note="D->A: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 654
FT /note="R->A: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 655
FT /note="P->A: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:16965792"
FT MUTAGEN 656
FT /note="Y->A: Cytoplasmic localization."
FT /evidence="ECO:0000269|PubMed:16965792"
FT CONFLICT 224
FT /note="S -> G (in Ref. 5; BAB71252)"
FT /evidence="ECO:0000305"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:2CPE"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:2CPE"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:2CPE"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2CPE"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:2CPE"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:2CPE"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:2CPE"
FT HELIX 420..430
FT /evidence="ECO:0007829|PDB:2CPE"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:2CPE"
SQ SEQUENCE 656 AA; 68478 MW; 0DA02CEE146720BB CRC64;
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV SYTQAQTTAT
YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT TTATVTTTQA SYAAQSAYGT
QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP
MQPVTAPPSY PPTSYSSTQP TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY
PPQTGSYSQA PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSMSGPDNR
GRGRGGFDRG GMSRGGRGGG RGGMGSAGER GGFNKPGGPM DEGPDLDLGP PVDPDEDSDN
SAIYVQGLND SVTLDDLADF FKQCGVVKMN KRTGQPMIHI YLDKETGKPK GDATVSYEDP
PTAKAAVEWF DGKDFQGSKL KVSLARKKPP MNSMRGGLPP REGRGMPPPL RGGPGGPGGP
GGPMGRMGGR GGDRGGFPPR GPRGSRGNPS GGGNVQHRAG DWQCPNPGCG NQNFAWRTEC
NQCKAPKPEG FLPPPFPPPG GDRGRGGPGG MRGGRGGLMD RGGPGGMFRG GRGGDRGGFR
GGRGMDRGGF GGGRRGGPGG PPGPLMEQMG GRRGGRGGPG KMDKGEHRQE RRDRPY
