MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=RNA-binding protein EWS; AltName: Full=EWS oncogene; AltName: Full=Ewing sarcoma breakpoint region 1 protein; |
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| MyHits synonyms | EWS_HUMAN , Q01844 , B0QYK1 , Q5THL0 , Q92635 , Q96FE8 , Q96MN4 , Q96MX4 , Q9BWA2 , 0DA02CEE146720BB |
 Legends: 1, SITE Breakpoint for translocation to form chimeric EWSR1/ATF1 protein; 2, Phosphoserine; by PKC. {ECO:0000250}; 3, Asymmetric dimethylarginine. {ECO:0000269|PubMed:11278906}; 4, N6-acetyllysine. {ECO:0000250|UniProtKB:Q61545}; 5, Asymmetric dimethylarginine; alternate. {ECO:0000269|PubMed:11278906}; 6, Omega-N-methylarginine; alternate. {ECO:0000244|PubMed:24129315, ECO:0000269|PubMed:11278906}; 7, Omega-N-methylarginine. {ECO:0000244|PubMed:24129315}; 8, Asymmetric dimethylarginine; by PRMT8. {ECO:0000269|PubMed:11278906, ECO:0000269|PubMed:18320585}; 9, Asymmetric dimethylarginine. {ECO:0000269|PubMed:11278906, ECO:0000269|Ref.12}; 10, Omega-N-methylarginine; alternate. {ECO:0000250|UniProtKB:Q61545}; 11, Asymmetric dimethylarginine; alternate; by PRMT8. {ECO:0000269|PubMed:11278906, ECO:0000269|PubMed:18320585}; 12, Omega-N-methylarginine; alternate; by PRMT8. {ECO:0000269|PubMed:11278906, ECO:0000269|PubMed:18320585}; 13, Asymmetric dimethylarginine; alternate. {ECO:0000269|PubMed:11278906, ECO:0000269|Ref.12}; 14, Omega-N-methylarginine; alternate. {ECO:0000244|PubMed:24129315}; 15, VAR_SEQ P -> PTVEGTS (in isoform 5). {ECO:0000303|PubMed:14702039}; 16, VAR_SEQ Missing (in isoform 3 and isoform 5). {ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15461802, ECO:0000303|PubMed:15489334}; 17, MUTAGEN R->A: Cytoplasmic localization. {ECO:0000269|PubMed:16965792}; 18, MUTAGEN R->K: No effect on nuclear targeting. {ECO:0000269|PubMed:16965792}; 19, MUTAGEN R->A: No effect on nuclear targeting. {ECO:0000269|PubMed:16965792}; 20, MUTAGEN D->A: No effect on nuclear targeting. {ECO:0000269|PubMed:16965792}; 21, MUTAGEN P->A: Cytoplasmic localization. {ECO:0000269|PubMed:16965792}; 22, MUTAGEN Y->A: Cytoplasmic localization. {ECO:0000269|PubMed:16965792}; 23, CONFLICT S -> G (in Ref. 5; BAB71252). {ECO:0000305}; 24, REPEAT 1; 25, REPEAT 2; 26, REPEAT 3; 27, REPEAT 4; 28, REPEAT 5; 29, REPEAT 6; 30, REPEAT 7; 31, REPEAT 8; 32, REPEAT 9; 33, REPEAT 10; 34, REPEAT 11; 35, REPEAT 12; 36, REPEAT 13; 37, REPEAT 14; 38, REPEAT 15; 39, REPEAT 16; 40, REPEAT 17; 41, REPEAT 18; 42, REPEAT 19; 43, REPEAT 20; 44, REPEAT 21; 45, REPEAT 22; 46, REPEAT 23; 47, REPEAT 24; 48, REPEAT 25; 49, REPEAT 26; 50, REPEAT 27; 51, REPEAT 28; 52, REPEAT 29; 53, REPEAT 30; 54, REPEAT 31; 55, RRM. {ECO:0000255|PROSITE- ProRule:PRU00176}; 56, ZN_FING RanBP2-type. {ECO:0000255|PROSITE- ProRule:PRU00322}; 57, MOTIF Nuclear localization signal. {ECO:0000269|PubMed:16965792}; 58, COMPBIAS Arg/Gly/Pro-rich; 59, SITE Breakpoint for insertion to form EWSR1- FEV fusion protein; 60, VAR_SEQ Missing (in isoform 6). {ECO:0000303|PubMed:14702039}; 61, VAR_SEQ Missing (in isoform EWS-B). {ECO:0000305}; 62, VAR_SEQ SAGERGGFNKPGGPMDEGPDLDLGPPVDP -> LQSESLVY TSILKKYPYSVLSRQHNEKWD (in isoform 4). {ECO:0000303|PubMed:15489334}; 63, VAR_SEQ Missing (in isoform 4). {ECO:0000303|PubMed:15489334}; 64, ipfam:zf-RanBP [T]; 65, iprf:ZF_RANBP2_2 [T]; 66, ismart:RRM [T]; 67, ipfam:RRM_1 [T]; 68, ipat:ZF_RANBP2_1 [T]; 69, ismart:ZnF_RBZ [T]; 70, STRAND {ECO:0000244|PDB:2CPE}; 71, HELIX {ECO:0000244|PDB:2CPE}; 72, TURN {ECO:0000244|PDB:2CPE}.
| |
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 18-JAN-2017, entry version 196.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT site of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA 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.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA 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.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT 22q12 chromosome region.";
RL Genomics 38:247-254(1996).
RN [10]
RP PROTEIN SEQUENCE OF 128-158; 233-247; 268-324; 334-364; 393-439;
RP 447-518 AND 551-641, METHYLATION AT ARG-300; ARG-302; ARG-304;
RP ARG-309; ARG-314; ARG-317; ARG-321; ARG-455; ARG-464; ARG-471;
RP ARG-490; ARG-494; ARG-500; ARG-503; ARG-506; ARG-563; ARG-565;
RP ARG-572; ARG-575; ARG-581; ARG-589; ARG-592; ARG-596; ARG-600;
RP ARG-603; ARG-607; ARG-615; ARG-633 AND ARG-636, AND IDENTIFICATION BY
RP 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
RT protein 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.,
RA Speleman F., Fletchers C.D., Aurias A., Thomas G.;
RT "EWS and ATF-1 gene fusion induced by t(12;22) translocation in
RT malignant 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
RT of soft parts and desmoplastic small round cell tumors, codes for an
RT RNA 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.,
RA Gusterson B.A., 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
RT myxoid 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.,
RA Denny C.T., Shapiro D.N.;
RT "A variant Ewing's sarcoma translocation (7;22) fuses the EWS gene to
RT the 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
RT in the 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.,
RA Magdelenat H., 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
RT be 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.,
RA Pierotti M., 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
RP FLI1, 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.,
RA 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
RT localization/retention 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
RT cytoplasmic 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
RT of 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-471; ARG-486 AND ARG-615,
RP AND 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.,
RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA Vemulapalli V., 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
RT (EWS) 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.,
RA Fletcher C.D., 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.
CC EWS-fusion-proteins (EFPS) may play a role in the tumorigenic
CC process. They may disturb gene expression by mimicking, or
CC interfering with the normal function of CTD-POLII within the
CC transcription initiation complex. They may also contribute to an
CC aberrant activation of the 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
CC the absence, of calcium ion. {ECO:0000269|PubMed:18632687,
CC ECO:0000269|PubMed:9660765}.
CC -!- INTERACTION:
CC Self; NbExp=3; IntAct=EBI-739737, EBI-739737;
CC Q8N5M1:ATPAF2; NbExp=3; IntAct=EBI-739737, EBI-1166928;
CC P35637:FUS; NbExp=5; IntAct=EBI-739737, EBI-400434;
CC Q8NDC0:MAPK1IP1L; NbExp=5; IntAct=EBI-739737, EBI-741424;
CC Q9UBV8:PEF1; NbExp=3; IntAct=EBI-739737, EBI-724639;
CC O15162:PLSCR1; NbExp=4; IntAct=EBI-739737, EBI-740019;
CC Q99873:PRMT1; NbExp=2; IntAct=EBI-739737, EBI-78738;
CC Q9NZ81:PRR13; NbExp=3; IntAct=EBI-739737, EBI-740924;
CC Q9NS23-2:RASSF1; NbExp=3; IntAct=EBI-739737, EBI-438698;
CC O95486:SEC24A; NbExp=3; IntAct=EBI-739737, EBI-749911;
CC O94855:SEC24D; NbExp=3; IntAct=EBI-739737, EBI-748817;
CC Q9BWW4:SSBP3; NbExp=3; IntAct=EBI-739737, EBI-2902395;
CC Q92734:TFG; NbExp=3; IntAct=EBI-739737, EBI-357061;
CC Q13077:TRAF1; NbExp=3; IntAct=EBI-739737, EBI-359224;
CC Q12933:TRAF2; NbExp=3; IntAct=EBI-739737, EBI-355744;
CC P49910:ZNF165; NbExp=2; IntAct=EBI-739737, EBI-741694;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16965792}.
CC Cytoplasm {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 Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q01844-3; Sequence=VSP_043453;
CC Name=4;
CC IsoId=Q01844-4; Sequence=VSP_043452, VSP_043454;
CC Note=No experimental confirmation available.;
CC Name=5;
CC IsoId=Q01844-5; Sequence=VSP_043451, VSP_043453;
CC Note=No experimental confirmation available.;
CC Name=6;
CC IsoId=Q01844-6; Sequence=VSP_045412;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: EWS activation domain (EAD) functions as a potent
CC activation domain in EFPS. EWSR1 binds POLR2C but not POLR2E or
CC POLR2G, whereas the isolated EAD binds POLR2E and POLR2G but not
CC POLR2C. Cis-linked RNA-binding domain (RBD) can strongly and
CC specifically repress trans-activation by the EAD.
CC -!- PTM: Phosphorylated; calmodulin-binding inhibits phosphorylation
CC of Ser-266. {ECO:0000269|PubMed:9341188}.
CC -!- PTM: Highly methylated on arginine residues. Methylation is
CC mediated by PRMT1 and, at lower level by PRMT8.
CC {ECO:0000269|PubMed:11278906, ECO:0000269|PubMed:18320585,
CC 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
CC tissue that affects children and adolescents. It belongs to the
CC Ewing sarcoma family of tumors, a group of morphologically
CC heterogeneous neoplasms that share the same cytogenetic features.
CC They are considered neural tumors derived from cells of the neural
CC crest. Ewing sarcoma represents the less differentiated form of
CC the tumors. {ECO:0000269|PubMed:15044653,
CC ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648,
CC ECO:0000269|PubMed:9121764}. Note=The protein represented in this
CC entry is involved in disease pathogenesis. Chromosomal aberrations
CC involving EWSR1 are found in patients with Ewing sarcoma.
CC Translocation t(11;22)(q24;q12) with FLI1 (PubMed:1522903,
CC PubMed:15044653). Translocation t(7;22)(p22;q12) with ETV1
CC (PubMed:7700648). Translocation t(21;22)(q22;q21) with ERG
CC (PubMed:15044653). Translocation t(2;21;22)(q23;q22;q12) that
CC forms a 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
CC found in extraskeletal myxoid chondrosarcoma. Translocation
CC t(9;22)(q22-31;q11-12) with NR4A3. {ECO:0000269|PubMed:7539287}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is
CC associated with desmoplastic small round cell tumor (DSRCT).
CC Translocation t(11;22)(p13;q12) with WT1.
CC {ECO:0000269|PubMed:7862627}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is
CC associated with malignant melanoma of soft parts (MMSP).
CC Translocation t(12;22)(q13;q12) with ATF1. Malignant melanoma of
CC soft parts, also known as soft tissue clear cell sarcoma, is a
CC rare tumor developing in tendons and aponeuroses.
CC {ECO:0000269|PubMed:8401579}.
CC -!- DISEASE: Note=A chromosomal aberration involving EWSR1 is
CC associated with small round cell sarcoma. Translocation
CC t(11;22)(p36.1;q12) with 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
CC with areas of hemorrhage and cystic pseudovascular spaces, as well
CC as a striking cuffing of inflammatory cells, mimicking a lymph
CC node metastasis. {ECO:0000269|PubMed:15884099,
CC ECO:0000269|PubMed:17724745}. Note=The gene represented in this
CC entry is involved in disease pathogenesis. Chromosomal aberrations
CC involving EWSR1 are found in patients with angiomatoid fibrous
CC histiocytoma. Translocation t(12;22)(q13;q12) with ATF1 generates
CC a chimeric EWSR1/ATF1 protein (PubMed:15884099). Translocation
CC t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene
CC that is most common genetic abnormality in this tumor type
CC (PubMed:17724745). {ECO:0000269|PubMed:15884099,
CC ECO:0000269|PubMed:17724745}.
CC -!- DISEASE: Note=EFPS arise due to chromosomal translocations in
CC which EWSR1 is fused to a variety of cellular transcription
CC factors. EFPS are very potent transcriptional activators dependent
CC on the EAD and a C-terminal DNA-binding domain contributed by the
CC fusion partner. The spectrum of malignancies associated with EFPS
CC are thought to arise via EFP-induced transcriptional deregulation,
CC with the tumor phenotype specified by the EWSR1 fusion partner and
CC cell type. Transcriptional repression of the transforming growth
CC factor beta type II receptor (TGF beta RII) is an important target
CC of the EWS-FLI1, EWS-ERG, or EWS-ETV1 oncogene. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RRM TET family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 IQ domain. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC {ECO:0000255|PROSITE-ProRule:PRU00322}.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00176}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EWSR1ID85.html";
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 UniGene; Hs.374477; -.
DR PDB; 2CPE; NMR; -; A=353-453.
DR PDBsum; 2CPE; -.
DR DisProt; DP00632; -.
DR ProteinModelPortal; Q01844; -.
DR SMR; Q01844; -.
DR BioGrid; 108431; 648.
DR DIP; DIP-34449N; -.
DR IntAct; Q01844; 150.
DR MINT; MINT-4992203; -.
DR STRING; 9606.ENSP00000400142; -.
DR iPTMnet; Q01844; -.
DR PhosphoSitePlus; Q01844; -.
DR SwissPalm; Q01844; -.
DR BioMuta; EWSR1; -.
DR DMDM; 544261; -.
DR EPD; Q01844; -.
DR MaxQB; Q01844; -.
DR PaxDb; Q01844; -.
DR PeptideAtlas; Q01844; -.
DR PRIDE; Q01844; -.
DR DNASU; 2130; -.
DR Ensembl; ENST00000332035; ENSP00000331699; ENSG00000182944. [Q01844-6]
DR Ensembl; ENST00000333395; ENSP00000327456; ENSG00000182944. [Q01844-4]
DR Ensembl; ENST00000397938; ENSP00000381031; ENSG00000182944. [Q01844-1]
DR Ensembl; ENST00000406548; ENSP00000385726; ENSG00000182944. [Q01844-3]
DR Ensembl; ENST00000414183; ENSP00000400142; ENSG00000182944. [Q01844-5]
DR GeneID; 2130; -.
DR KEGG; hsa:2130; -.
DR UCSC; uc003aes.5; human. [Q01844-1]
DR CTD; 2130; -.
DR DisGeNET; 2130; -.
DR GeneCards; EWSR1; -.
DR HGNC; HGNC:3508; EWSR1.
DR HPA; CAB004230; -.
DR HPA; HPA051771; -.
DR HPA; HPA062953; -.
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; 319; Ewing sarcoma.
DR Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
DR Orphanet; 97338; Melanoma of soft parts.
DR PharmGKB; PA27921; -.
DR eggNOG; KOG1995; Eukaryota.
DR eggNOG; ENOG4111Q2F; LUCA.
DR GeneTree; ENSGT00530000063105; -.
DR HOGENOM; HOG000038010; -.
DR HOVERGEN; HBG000970; -.
DR InParanoid; Q01844; -.
DR KO; K13209; -.
DR OMA; NEREMGR; -.
DR OrthoDB; EOG091G0U8W; -.
DR PhylomeDB; Q01844; -.
DR TreeFam; TF322599; -.
DR BioCyc; ZFISH:G66-31013-MONOMER; -.
DR SIGNOR; Q01844; -.
DR ChiTaRS; EWSR1; human.
DR EvolutionaryTrace; Q01844; -.
DR GeneWiki; Ewing_sarcoma_breakpoint_region_1; -.
DR GenomeRNAi; 2130; -.
DR PRO; PR:Q01844; -.
DR Proteomes; UP000005640; Chromosome 22.
DR Bgee; ENSG00000182944; -.
DR CleanEx; HS_EWSR1; -.
DR ExpressionAtlas; Q01844; baseline and differential.
DR Genevisible; Q01844; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1060.10; -; 1.
DR InterPro; IPR033109; EWSR1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR23238:SF3; PTHR23238:SF3; 2.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 656 RNA-binding protein EWS.
FT /FTId=PRO_0000081586.
FT REPEAT 8 16 1.
FT REPEAT 17 27 2.
FT REPEAT 28 34 3.
FT REPEAT 35 42 4.
FT REPEAT 43 50 5.
FT REPEAT 51 59 6.
FT REPEAT 60 68 7.
FT REPEAT 69 75 8.
FT REPEAT 76 84 9.
FT REPEAT 85 91 10.
FT REPEAT 92 110 11.
FT REPEAT 111 116 12.
FT REPEAT 117 125 13.
FT REPEAT 126 156 14.
FT REPEAT 157 163 15.
FT REPEAT 164 170 16.
FT REPEAT 171 177 17.
FT REPEAT 178 188 18.
FT REPEAT 189 193 19.
FT REPEAT 194 201 20.
FT REPEAT 202 206 21.
FT REPEAT 207 212 22.
FT REPEAT 213 218 23.
FT REPEAT 219 224 24.
FT REPEAT 225 230 25.
FT REPEAT 231 238 26.
FT REPEAT 239 245 27.
FT REPEAT 246 252 28.
FT REPEAT 253 259 29.
FT DOMAIN 256 285 IQ.
FT REPEAT 260 276 30.
FT REPEAT 277 285 31.
FT DOMAIN 361 447 RRM. {ECO:0000255|PROSITE-
FT ProRule:PRU00176}.
FT ZN_FING 518 549 RanBP2-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00322}.
FT REGION 1 285 EAD (Gln/Pro/Thr-rich).
FT REGION 8 285 31 X approximate tandem repeats.
FT MOTIF 639 656 Nuclear localization signal.
FT {ECO:0000269|PubMed:16965792}.
FT COMPBIAS 300 340 Arg/Gly/Pro-rich.
FT COMPBIAS 454 513 Arg/Gly/Pro-rich.
FT COMPBIAS 559 640 Arg/Gly/Pro-rich.
FT SITE 265 265 Breakpoint for translocation to form
FT chimeric EWSR1/ATF1 protein.
FT SITE 348 349 Breakpoint for insertion to form EWSR1-
FT FEV fusion protein.
FT MOD_RES 266 266 Phosphoserine; by PKC. {ECO:0000250}.
FT MOD_RES 300 300 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 302 302 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 304 304 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 309 309 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 314 314 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 317 317 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 321 321 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 439 439 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:Q61545}.
FT MOD_RES 455 455 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 464 464 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 471 471 Asymmetric dimethylarginine; alternate.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 471 471 Omega-N-methylarginine; alternate.
FT {ECO:0000244|PubMed:24129315,
FT ECO:0000269|PubMed:11278906}.
FT MOD_RES 486 486 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 490 490 Asymmetric dimethylarginine; by PRMT8.
FT {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 494 494 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906,
FT ECO:0000269|Ref.12}.
FT MOD_RES 500 500 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 503 503 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 506 506 Asymmetric dimethylarginine; alternate.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 506 506 Omega-N-methylarginine; alternate.
FT {ECO:0000250|UniProtKB:Q61545}.
FT MOD_RES 563 563 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 565 565 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 572 572 Asymmetric dimethylarginine; alternate;
FT by PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 572 572 Omega-N-methylarginine; alternate; by
FT PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 575 575 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 581 581 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 589 589 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 592 592 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 596 596 Asymmetric dimethylarginine; alternate;
FT by PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 596 596 Omega-N-methylarginine; alternate; by
FT PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 600 600 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 603 603 Asymmetric dimethylarginine; by PRMT8.
FT {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 607 607 Asymmetric dimethylarginine; alternate;
FT by PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 607 607 Omega-N-methylarginine; alternate; by
FT PRMT8. {ECO:0000269|PubMed:11278906,
FT ECO:0000269|PubMed:18320585}.
FT MOD_RES 615 615 Asymmetric dimethylarginine; alternate.
FT {ECO:0000269|PubMed:11278906,
FT ECO:0000269|Ref.12}.
FT MOD_RES 615 615 Omega-N-methylarginine; alternate.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 633 633 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT MOD_RES 636 636 Asymmetric dimethylarginine.
FT {ECO:0000269|PubMed:11278906}.
FT VAR_SEQ 74 74 P -> PTVEGTS (in isoform 5).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_043451.
FT VAR_SEQ 136 191 Missing (in isoform 6).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_045412.
FT VAR_SEQ 266 338 Missing (in isoform EWS-B).
FT {ECO:0000305}.
FT /FTId=VSP_005793.
FT VAR_SEQ 326 354 SAGERGGFNKPGGPMDEGPDLDLGPPVDP -> LQSESLVY
FT TSILKKYPYSVLSRQHNEKWD (in isoform 4).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_043452.
FT VAR_SEQ 326 326 Missing (in isoform 3 and isoform 5).
FT {ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15461802,
FT ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_043453.
FT VAR_SEQ 355 656 Missing (in isoform 4).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_043454.
FT MUTAGEN 648 648 R->A: Cytoplasmic localization.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 648 648 R->K: No effect on nuclear targeting.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 651 651 R->A: No effect on nuclear targeting.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 652 652 R->A: Cytoplasmic localization.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 652 652 R->K: No effect on nuclear targeting.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 653 653 D->A: No effect on nuclear targeting.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 654 654 R->A: No effect on nuclear targeting.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 655 655 P->A: Cytoplasmic localization.
FT {ECO:0000269|PubMed:16965792}.
FT MUTAGEN 656 656 Y->A: Cytoplasmic localization.
FT {ECO:0000269|PubMed:16965792}.
FT CONFLICT 224 224 S -> G (in Ref. 5; BAB71252).
FT {ECO:0000305}.
FT STRAND 362 366 {ECO:0000244|PDB:2CPE}.
FT HELIX 374 381 {ECO:0000244|PDB:2CPE}.
FT TURN 382 384 {ECO:0000244|PDB:2CPE}.
FT STRAND 391 393 {ECO:0000244|PDB:2CPE}.
FT STRAND 396 399 {ECO:0000244|PDB:2CPE}.
FT TURN 404 406 {ECO:0000244|PDB:2CPE}.
FT STRAND 411 419 {ECO:0000244|PDB:2CPE}.
FT HELIX 420 430 {ECO:0000244|PDB:2CPE}.
FT STRAND 441 443 {ECO:0000244|PDB:2CPE}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 518 548 ipfam:zf-RanBP [T]
FT MYHIT 361 447 iprf:RRM [T]
FT MYHIT 518 549 iprf:ZF_RANBP2_2 [T]
FT MYHIT 362 443 ismart:RRM [T]
FT MYHIT 363 441 ipfam:RRM_1 [T]
FT MYHIT 522 543 ipat:ZF_RANBP2_1 [T]
FT MYHIT 520 546 ismart:ZnF_RBZ [T]
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
//
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