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Q01844 (EWS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 168. Feed History...

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

Names and origin

Protein namesRecommended name:
RNA-binding protein EWS
Alternative name(s):
EWS oncogene
Ewing sarcoma breakpoint region 1 protein
Gene names
Name:EWSR1
Synonyms:EWS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Might normally function as a transcriptionnal repressor. EWS-fusion-proteins (EFPS) may play a role in the tumorigenic process. They may disturb gene expression by mimicking, or interfering with the normal function of CTD-POLII within the transcription initiation complex. They may also contribute to an aberrant activation of the fusion protein target genes.

Subunit structure

Binds POLR2C, SF1, calmodulin and RNA. Interacts with PTK2B/FAK2 and TDRD3. Binds calmodulin in the presence, but not in the absence, of calcium ion. Ref.16 Ref.20

Subcellular location

Nucleus. Cytoplasm. Cell membrane. Note: Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation. Ref.19

Tissue specificity

Ubiquitous.

Domain

EWS activation domain (EAD) functions as a potent activation domain in EFPS. EWSR1 binds POLR2C but not POLR2E or POLR2G, whereas the isolated EAD binds POLR2E and POLR2G but not POLR2C. Cis-linked RNA-binding domain (RBD) can strongly and specifically repress trans-activation by the EAD.

Post-translational modification

Phosphorylated; calmodulin-binding inhibits phosphorylation of Ser-266. Ref.13

Highly methylated on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8. Ref.10 Ref.12 Ref.21

Involvement in disease

Ewing sarcoma (ES) [MIM:612219]: A highly malignant, metastatic, primitive small round cell tumor of bone and soft tissue that affects children and adolescents. It belongs to the Ewing sarcoma family of tumors, a group of morphologically heterogeneous neoplasms that share the same cytogenetic features. They are considered neural tumors derived from cells of the neural crest. Ewing sarcoma represents the less differentiated form of the tumors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Chromosomal aberrations involving EWSR1 are found in patients with Ewing sarcoma. Translocation t(11;22)(q24;q12) with FLI1; translocation t(7;22)(p22;q12) with ETV1; translocation t(21;22)(q22;q12) with ERG; translocation t(9;22)(q22-31;q11-12) with NR4A3. Translocation t(2;21;22)(q23;q22;q12) that forms a EWSR1-FEV fusion protein with potential oncogenic activity.

A chromosomal aberration involving EWSR1 is associated with desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with WT1.

A chromosomal aberration involving EWSR1 is associated with malignant melanoma of soft parts (MMSP). Translocation t(12;22)(q13;q12) with ATF-1. Malignant melanoma of soft parts, also known as soft tissue clear cell sarcoma, is a rare tumor developing in tendons and aponeuroses.

A chromosomal aberration involving EWSR1 is associated with small round cell sarcoma. Translocation t(11;22)(p36.1;q12) with PATZ1.

Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A distinct variant of malignant fibrous histiocytoma that typically occurs in children and adolescents and is manifest by nodular subcutaneous growth. Characteristic microscopic features include lobulated sheets of histiocyte-like cells intimately associated with areas of hemorrhage and cystic pseudovascular spaces, as well as a striking cuffing of inflammatory cells, mimicking a lymph node metastasis.
Note: The disease may be caused by mutations affecting the gene represented in this entry. Chromosomal aberrations involving EWSR1 are found in patients with angiomatoid fibrous histiocytoma. Translocation t(12;22)(q13;q12) with ATF1 generates a chimeric EWSR1/ATF1 protein. Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type.

EFPS arise due to chromosomal translocations in which EWSR1 is fused to a variety of cellular transcription factors. EFPS are very potent transcriptional activators dependent on the EAD and a C-terminal DNA-binding domain contributed by the fusion partner. The spectrum of malignancies associated with EFPS are thought to arise via EFP-induced transcriptional deregulation, with the tumor phenotype specified by the EWSR1 fusion partner and cell type. Transcriptional repression of the transforming growth factor beta type II receptor (TGF beta RII) is an important target of the EWS-FLI1, EWS-ERG, or EWS-ETV1 oncogene.

Sequence similarities

Belongs to the RRM TET family.

Contains 1 IQ domain.

Contains 1 RanBP2-type zinc finger.

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence CAA70044.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform EWS (identifier: Q01844-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform EWS-B (identifier: Q01844-2)

The sequence of this isoform differs from the canonical sequence as follows:
     266-338: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q01844-3)

The sequence of this isoform differs from the canonical sequence as follows:
     326-326: Missing.
Isoform 4 (identifier: Q01844-4)

The sequence of this isoform differs from the canonical sequence as follows:
     326-354: SAGERGGFNKPGGPMDEGPDLDLGPPVDP → LQSESLVYTSILKKYPYSVLSRQHNEKWD
     355-656: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q01844-5)

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: P → PTVEGTS
     326-326: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: Q01844-6)

The sequence of this isoform differs from the canonical sequence as follows:
     136-191: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656RNA-binding protein EWS
PRO_0000081586

Regions

Repeat8 – 1691
Repeat17 – 27112
Repeat28 – 3473
Repeat35 – 4284
Repeat43 – 5085
Repeat51 – 5996
Repeat60 – 6897
Repeat69 – 7578
Repeat76 – 8499
Repeat85 – 91710
Repeat92 – 1101911
Repeat111 – 116612
Repeat117 – 125913
Repeat126 – 1563114
Repeat157 – 163715
Repeat164 – 170716
Repeat171 – 177717
Repeat178 – 1881118
Repeat189 – 193519
Repeat194 – 201820
Repeat202 – 206521
Repeat207 – 212622
Repeat213 – 218623
Repeat219 – 224624
Repeat225 – 230625
Repeat231 – 238826
Repeat239 – 245727
Repeat246 – 252728
Repeat253 – 259729
Domain256 – 28530IQ
Repeat260 – 2761730
Repeat277 – 285931
Domain361 – 44787RRM
Zinc finger518 – 54932RanBP2-type
Region1 – 285285EAD (Gln/Pro/Thr-rich)
Region8 – 28527831 X approximate tandem repeats
Motif639 – 65618Nuclear localization signal Ref.19
Compositional bias300 – 34041Arg/Gly/Pro-rich
Compositional bias454 – 51360Arg/Gly/Pro-rich
Compositional bias559 – 64082Arg/Gly/Pro-rich

Sites

Site2651Breakpoint for translocation to form chimeric EWSR1/ATF1 protein
Site348 – 3492Breakpoint for insertion to form EWSR1-FEV fusion protein

Amino acid modifications

Modified residue2661Phosphoserine; by PKC By similarity
Modified residue3001Asymmetric dimethylarginine Ref.10
Modified residue3021Asymmetric dimethylarginine Ref.10
Modified residue3041Asymmetric dimethylarginine Ref.10
Modified residue3091Asymmetric dimethylarginine Ref.10
Modified residue3141Asymmetric dimethylarginine Ref.10
Modified residue3171Asymmetric dimethylarginine Ref.10
Modified residue3211Asymmetric dimethylarginine Ref.10
Modified residue4391N6-acetyllysine By similarity
Modified residue4551Asymmetric dimethylarginine Ref.10
Modified residue4641Asymmetric dimethylarginine Ref.10
Modified residue4711Asymmetric dimethylarginine; alternate Ref.10
Modified residue4711Omega-N-methylarginine; alternate Ref.10
Modified residue4901Asymmetric dimethylarginine; by PRMT8 Ref.10 Ref.21
Modified residue4941Asymmetric dimethylarginine Ref.10 Ref.12
Modified residue5001Asymmetric dimethylarginine Ref.10
Modified residue5031Asymmetric dimethylarginine Ref.10
Modified residue5061Asymmetric dimethylarginine Ref.10
Modified residue5631Asymmetric dimethylarginine Ref.10
Modified residue5651Asymmetric dimethylarginine Ref.10
Modified residue5721Asymmetric dimethylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue5721Omega-N-methylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue5751Asymmetric dimethylarginine Ref.10
Modified residue5811Asymmetric dimethylarginine Ref.10
Modified residue5891Asymmetric dimethylarginine Ref.10
Modified residue5921Asymmetric dimethylarginine Ref.10
Modified residue5961Asymmetric dimethylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue5961Omega-N-methylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue6001Asymmetric dimethylarginine Ref.10
Modified residue6031Asymmetric dimethylarginine; by PRMT8 Ref.10 Ref.21
Modified residue6071Asymmetric dimethylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue6071Omega-N-methylarginine; alternate; by PRMT8 Ref.10 Ref.21
Modified residue6151Asymmetric dimethylarginine Ref.10 Ref.12
Modified residue6331Asymmetric dimethylarginine Ref.10
Modified residue6361Asymmetric dimethylarginine Ref.10

Natural variations

Alternative sequence741P → PTVEGTS in isoform 5.
VSP_043451
Alternative sequence136 – 19156Missing in isoform 6.
VSP_045412
Alternative sequence266 – 33873Missing in isoform EWS-B.
VSP_005793
Alternative sequence326 – 35429SAGER…PPVDP → LQSESLVYTSILKKYPYSVL SRQHNEKWD in isoform 4.
VSP_043452
Alternative sequence3261Missing in isoform 3 and isoform 5.
VSP_043453
Alternative sequence355 – 656302Missing in isoform 4.
VSP_043454

Experimental info

Mutagenesis6481R → A: Cytoplasmic localization. Ref.19
Mutagenesis6481R → K: No effect on nuclear targeting. Ref.19
Mutagenesis6511R → A: No effect on nuclear targeting. Ref.19
Mutagenesis6521R → A: Cytoplasmic localization. Ref.19
Mutagenesis6521R → K: No effect on nuclear targeting. Ref.19
Mutagenesis6531D → A: No effect on nuclear targeting. Ref.19
Mutagenesis6541R → A: No effect on nuclear targeting. Ref.19
Mutagenesis6551P → A: Cytoplasmic localization. Ref.19
Mutagenesis6561Y → A: Cytoplasmic localization. Ref.19
Sequence conflict2241S → G in BAB71252. Ref.5

Secondary structure

................. 656
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform EWS [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0DA02CEE146720BB

FASTA65668,478
        10         20         30         40         50         60 
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV SYTQAQTTAT 

        70         80         90        100        110        120 
YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT TTATVTTTQA SYAAQSAYGT 

       130        140        150        160        170        180 
QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP 

       190        200        210        220        230        240 
MQPVTAPPSY PPTSYSSTQP TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY 

       250        260        270        280        290        300 
PPQTGSYSQA PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSMSGPDNR 

       310        320        330        340        350        360 
GRGRGGFDRG GMSRGGRGGG RGGMGSAGER GGFNKPGGPM DEGPDLDLGP PVDPDEDSDN 

       370        380        390        400        410        420 
SAIYVQGLND SVTLDDLADF FKQCGVVKMN KRTGQPMIHI YLDKETGKPK GDATVSYEDP 

       430        440        450        460        470        480 
PTAKAAVEWF DGKDFQGSKL KVSLARKKPP MNSMRGGLPP REGRGMPPPL RGGPGGPGGP 

       490        500        510        520        530        540 
GGPMGRMGGR GGDRGGFPPR GPRGSRGNPS GGGNVQHRAG DWQCPNPGCG NQNFAWRTEC 

       550        560        570        580        590        600 
NQCKAPKPEG FLPPPFPPPG GDRGRGGPGG MRGGRGGLMD RGGPGGMFRG GRGGDRGGFR 

       610        620        630        640        650 
GGRGMDRGGF GGGRRGGPGG PPGPLMEQMG GRRGGRGGPG KMDKGEHRQE RRDRPY 

« Hide

Isoform EWS-B [UniParc].

Checksum: 1B011799A0B290ED
Show »

FASTA58361,217
Isoform 3 [UniParc].

Checksum: B539ED1E98C601ED
Show »

FASTA65568,391
Isoform 4 [UniParc].

Checksum: AE4B8FCDF458390B
Show »

FASTA35437,620
Isoform 5 [UniParc].

Checksum: 5F84F52FDCD51269
Show »

FASTA66168,966
Isoform 6 [UniParc].

Checksum: B3D01637474FFFB0
Show »

FASTA60062,508

References

« Hide 'large scale' references
[1]"Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours."
Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M., Kovar H., Joubert I., de Jong P., Rouleau G., Aurias A., Thomas G.
Nature 359:162-165(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EWS).
Tissue: Fetal brain.
[2]"Genomic structure of the EWS gene and its relationship to EWSR1, a site of tumor-associated chromosome translocation."
Plougastel B., Zucman J., Peter M., Thomas G., Delattre O.
Genomics 18:609-615(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic sequence of the human EWS gene with the 5' flanking region."
Zucman-Rossi J., Legoix P., Thomas G.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS EWS; 3 AND 4).
Tissue: Lymph, Muscle, Placenta and Skin.
[9]"Identification of new members of the Gas2 and Ras families in the 22q12 chromosome region."
Zucman-Rossi J., Legoix P., Thomas G.
Genomics 38:247-254(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-345.
[10]"Exposure on cell surface and extensive arginine methylation of Ewing sarcoma (EWS) protein."
Belyanskaya L.L., Gehrig P.M., Gehring H.
J. Biol. Chem. 276:18681-18687(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 128-158; 233-247; 268-324; 334-364; 393-439; 447-518 AND 551-641, METHYLATION AT ARG-300; ARG-302; ARG-304; ARG-309; ARG-314; ARG-317; ARG-321; ARG-455; ARG-464; ARG-471; ARG-490; ARG-494; ARG-500; ARG-503; ARG-506; ARG-563; ARG-565; ARG-572; ARG-575; ARG-581; ARG-589; ARG-592; ARG-596; ARG-600; ARG-603; ARG-607; ARG-615; ARG-633 AND ARG-636, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Molecular analysis of a t(11;22) translocation junction in a case of Ewing's sarcoma."
Bhagirath T., Abe S., Nojima T., Yoshida M.C.
Genes Chromosomes Cancer 13:126-132(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 241-268.
Tissue: Placenta.
[12]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Zebisch A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 269-292; 393-404; 411-439; 491-500 AND 615-632, METHYLATION AT ARG-494 AND ARG-615, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[13]"The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain."
Deloulme J.C., Prichard L., Delattre O., Storm D.R.
J. Biol. Chem. 272:27369-27377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-266.
[14]"The EWS gene, involved in Ewing family of tumors, malignant melanoma of soft parts and desmoplastic small round cell tumors, codes for an RNA binding protein with novel regulatory domains."
Ohno T., Ouchida M., Lee L., Gatalica Z., Rao V.N., Reddy E.S.P.
Oncogene 9:3087-3097(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, RNA-BINDING.
[15]"A new member of the ETS family fused to EWS in Ewing tumors."
Peter M., Couturier J., Pacquement H., Michon J., Thomas G., Magdelenat H., Delattre O.
Oncogene 14:1159-1164(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH FEV.
[16]"The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription."
Zhang D., Paley A.J., Childs G.
J. Biol. Chem. 273:18086-18091(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SF1.
[17]"Transcriptional activation by the Ewing's sarcoma (EWS) oncogene can be cis-repressed by the EWS RNA-binding domain."
Li K.K.C., Lee K.A.W.
J. Biol. Chem. 275:23053-23058(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[18]"Expression of EWS-ETS fusions in NIH3T3 cells reveals significant differences to Ewing's sarcoma."
Braunreiter C.L., Hancock J.D., Coffin C.M., Boucher K.M., Lessnick S.L.
Cell Cycle 5:2753-2759(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EWSR1-FEV FUSION PROTEIN.
[19]"Identification and characterization of the nuclear localization/retention signal in the EWS proto-oncoprotein."
Zakaryan R.P., Gehring H.
J. Mol. Biol. 363:27-38(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF ARG-648; ARG-651; ARG-652; ASP-653; ARG-654; PRO-655 AND TYR-656.
[20]"TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules."
Goulet I., Boisvenue S., Mokas S., Mazroui R., Cote J.
Hum. Mol. Genet. 17:3055-3074(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TDRD3.
[21]"Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state."
Pahlich S., Zakaryan R.P., Gehring H.
Proteins 72:1125-1137(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-490; ARG-572; ARG-596; ARG-603 AND ARG-607.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Solution structure of the RNA recognition motif of Ewing sarcoma (EWS) protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 353-453.
[24]"Fusion of the EWSR1 and ATF1 genes without expression of the MITF-M transcript in angiomatoid fibrous histiocytoma."
Hallor K.H., Mertens F., Jin Y., Meis-Kindblom J.M., Kindblom L.-G., Behrendtz M., Kalen A., Mandahl N., Panagopoulos I.
Genes Chromosomes Cancer 44:97-102(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH ATF1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
[25]"EWSR1-CREB1 is the predominant gene fusion in angiomatoid fibrous histiocytoma."
Antonescu C.R., Dal Cin P., Nafa K., Teot L.A., Surti U., Fletcher C.D., Ladanyi M.
Genes Chromosomes Cancer 46:1051-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH CREB1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66899 mRNA. Translation: CAA47350.1.
X72990 expand/collapse EMBL AC list , X72991, X72992, X72993, X72994, X72995, X72996, X72997, X72998, X72999, X73000, X73001, X73002, X73003, X73004 Genomic DNA. Translation: CAA51489.1.
Y07848 Genomic DNA. Translation: CAA69177.1.
CR456490 mRNA. Translation: CAG30376.1.
AK056309 mRNA. Translation: BAB71145.1.
AK056681 mRNA. Translation: BAB71252.1.
AL031186, AC000026, AC002059 Genomic DNA. Translation: CAI18001.1.
AL031186, AC000026, AC002059 Genomic DNA. Translation: CAQ10937.1.
AL031186, AC000026, AC002059 Genomic DNA. Translation: CAQ10938.1.
AL031186, AC000026, AC002059 Genomic DNA. Translation: CAQ10940.1.
CH471095 Genomic DNA. Translation: EAW59780.1.
CH471095 Genomic DNA. Translation: EAW59781.1.
CH471095 Genomic DNA. Translation: EAW59785.1.
CH471095 Genomic DNA. Translation: EAW59786.1.
CH471095 Genomic DNA. Translation: EAW59787.1.
BC000527 mRNA. Translation: AAH00527.1.
BC004817 mRNA. Translation: AAH04817.1.
BC011048 mRNA. Translation: AAH11048.1.
BC072442 mRNA. Translation: AAH72442.1.
Y08806 Genomic DNA. Translation: CAA70044.1. Different initiation.
AB016435 Genomic DNA. Translation: BAA31990.1.
PIRA49358.
RefSeqNP_001156757.1. NM_001163285.1.
NP_001156758.1. NM_001163286.1.
NP_001156759.1. NM_001163287.1.
NP_005234.1. NM_005243.3.
NP_053733.2. NM_013986.3.
UniGeneHs.374477.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPENMR-A353-453[»]
DisProtDP00632.
ProteinModelPortalQ01844.
SMRQ01844. Positions 349-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108431. 215 interactions.
DIPDIP-34449N.
IntActQ01844. 133 interactions.
MINTMINT-4992203.
STRING9606.ENSP00000381031.

PTM databases

PhosphoSiteQ01844.

Polymorphism databases

DMDM544261.

Proteomic databases

PaxDbQ01844.
PRIDEQ01844.

Protocols and materials databases

DNASU2130.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332035; ENSP00000331699; ENSG00000182944. [Q01844-6]
ENST00000333395; ENSP00000327456; ENSG00000182944. [Q01844-4]
ENST00000397938; ENSP00000381031; ENSG00000182944. [Q01844-1]
ENST00000406548; ENSP00000385726; ENSG00000182944. [Q01844-3]
ENST00000414183; ENSP00000400142; ENSG00000182944. [Q01844-5]
GeneID2130.
KEGGhsa:2130.
UCSCuc003aes.4. human. [Q01844-4]
uc003aet.3. human. [Q01844-1]
uc003aev.3. human. [Q01844-5]
uc003aew.3. human.
uc003aex.3. human. [Q01844-3]

Organism-specific databases

CTD2130.
GeneCardsGC22P029663.
HGNCHGNC:3508. EWSR1.
HPACAB004230.
MIM133450. gene.
612160. phenotype.
612219. phenotype.
neXtProtNX_Q01844.
Orphanet83469. Desmoplastic small round cell tumor.
319. Ewing sarcoma.
370334. Extraskeletal Ewing sarcoma.
209916. Extraskeletal myxoid chondrosarcoma.
97338. Melanoma of soft part.
PharmGKBPA27921.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240581.
HOGENOMHOG000038010.
HOVERGENHBG000970.
KOK13209.
OMARDGMMGR.
OrthoDBEOG7DZ8N7.
PhylomeDBQ01844.
TreeFamTF322599.

Gene expression databases

ArrayExpressQ01844.
BgeeQ01844.
CleanExHS_EWSR1.
GenevestigatorQ01844.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEWSR1. human.
EvolutionaryTraceQ01844.
GeneWikiEwing_sarcoma_breakpoint_region_1.
GenomeRNAi2130.
NextBio8605.
PROQ01844.
SOURCESearch...

Entry information

Entry nameEWS_HUMAN
AccessionPrimary (citable) accession number: Q01844
Secondary accession number(s): B0QYK1 expand/collapse secondary AC list , Q5THL0, Q92635, Q96FE8, Q96MN4, Q96MX4, Q9BWA2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM