Reviewed, UniProtKB/Swiss-Prot Q01844 (EWS_HUMAN)

Names and origin

Protein names

Recommended name:
    RNA-binding protein EWS
Alternative name(s):
    EWS oncogene
    Ewing sarcoma breakpoint region 1 protein

Gene names

Name:	EWSR1
Synonyms:	EWS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	656 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Might normally function as a 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. Ref.12 Ref.16
Subcellular location	Nucleus. Cytoplasm. Cell membrane. Note: Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation.
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.9 Highly methyalted on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8.
Involvement in disease	Chromosomal aberrations involving EWSR1 are a cause of Ewing sarcoma [MIM:133450]. 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. Chromosomal aberrations involving EWSR1 are associated with angiomatoid fibrous histiocytoma (AFH) [MIM:612160]. 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.
Miscellaneous	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. Binds calmodulin in the presence, but not in the absence, of calcium ion.
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Repeat Zinc-finger
Ligand	Calmodulin-binding Metal-binding RNA-binding Zinc
Molecular function	Repressor
PTM	Methylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	RNA binding Ref.10 Traceable author statement. Source: ProtInc calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGDIA	P52565	1	EBI-739737,EBI-712693
CD2BP2	O95400	1	EBI-739737,EBI-768015
GSK3B	P49841	1	EBI-739737,EBI-373586
ILK	Q13418	1	EBI-739737,EBI-747644
NDRG1	Q92597	1	EBI-739737,EBI-716486
PUF60	Q9UHX1	1	EBI-739737,EBI-1053259
RASSF1	Q9NS23-2	1	EBI-739737,EBI-438698
SMNDC1	O75940	1	EBI-739737,EBI-1052641
ZNF165	P49910	1	EBI-739737,EBI-741694

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 656

656

RNA-binding protein EWS

PRO_0000081586

Regions

Repeat

8 – 16

9

1

Repeat

17 – 27

11

2

Repeat

28 – 34

7

3

Repeat

35 – 42

8

4

Repeat

43 – 50

8

5

Repeat

51 – 59

9

6

Repeat

60 – 68

9

7

Repeat

69 – 75

7

8

Repeat

76 – 84

9

9

Repeat

85 – 91

7

10

Repeat

92 – 110

19

11

Repeat

111 – 116

6

12

Repeat

117 – 125

9

13

Repeat

126 – 156

31

14

Repeat

157 – 163

7

15

Repeat

164 – 170

7

16

Repeat

171 – 177

7

17

Repeat

178 – 188

11

18

Repeat

189 – 193

5

19

Repeat

194 – 201

8

20

Repeat

202 – 206

5

21

Repeat

207 – 212

6

22

Repeat

213 – 218

6

23

Repeat

219 – 224

6

24

Repeat

225 – 230

6

25

Repeat

231 – 238

8

26

Repeat

239 – 245

7

27

Repeat

246 – 252

7

28

Repeat

253 – 259

7

29

Domain

256 – 285

30

IQ

Repeat

260 – 276

17

30

Repeat

277 – 285

9

31

Domain

361 – 447

87

RRM

Zinc finger

518 – 549

32

RanBP2-type

Region

1 – 285

285

EAD (Gln/Pro/Thr-rich)

Region

8 – 285

278

31 X approximate tandem repeats

Compositional bias

300 – 340

41

Arg/Gly/Pro-rich

Compositional bias

454 – 513

60

Arg/Gly/Pro-rich

Compositional bias

559 – 640

82

Arg/Gly/Pro-rich

Sites

Site

265

1

Breakpoint for translocation to form chimeric EWSR1/ATF1 protein

Site

348 – 349

2

Breakpoint for insertion to form EWSR1-FEV fusion protein

Amino acid modifications

Modified residue

266

1

Phosphoserine; by PKC By similarity

Modified residue

300

1

Asymmetric dimethylarginine Ref.6

Modified residue

302

1

Asymmetric dimethylarginine Ref.6

Modified residue

304

1

Asymmetric dimethylarginine Ref.6

Modified residue

309

1

Asymmetric dimethylarginine Ref.6

Modified residue

314

1

Asymmetric dimethylarginine Ref.6

Modified residue

317

1

Asymmetric dimethylarginine Ref.6

Modified residue

321

1

Asymmetric dimethylarginine Ref.6

Modified residue

455

1

Asymmetric dimethylarginine Ref.6

Modified residue

464

1

Asymmetric dimethylarginine Ref.6

Modified residue

471

1

Asymmetric dimethylarginine; alternate Ref.6 Ref.14

Modified residue

471

1

Omega-N-methylarginine; alternate Ref.6 Ref.14

Modified residue

490

1

Asymmetric dimethylarginine; by PRMT8

Modified residue

494

1

Asymmetric dimethylarginine Ref.6 Ref.8

Modified residue

500

1

Asymmetric dimethylarginine Ref.6

Modified residue

503

1

Asymmetric dimethylarginine Ref.6 Ref.14

Modified residue

506

1

Asymmetric dimethylarginine Ref.6 Ref.14

Modified residue

563

1

Asymmetric dimethylarginine Ref.6

Modified residue

565

1

Asymmetric dimethylarginine Ref.6

Modified residue

572

1

Asymmetric dimethylarginine; alternate; by PRMT8

Modified residue

572

1

Omega-N-methylarginine; alternate; by PRMT8

Modified residue

575

1

Asymmetric dimethylarginine Ref.6

Modified residue

581

1

Asymmetric dimethylarginine Ref.6

Modified residue

589

1

Asymmetric dimethylarginine Ref.6

Modified residue

592

1

Asymmetric dimethylarginine Ref.6

Modified residue

596

1

Asymmetric dimethylarginine; alternate; by PRMT8

Modified residue

596

1

Omega-N-methylarginine; alternate; by PRMT8

Modified residue

600

1

Asymmetric dimethylarginine Ref.6

Modified residue

603

1

Asymmetric dimethylarginine; by PRMT8

Modified residue

607

1

Asymmetric dimethylarginine; alternate; by PRMT8

Modified residue

607

1

Omega-N-methylarginine; alternate; by PRMT8

Modified residue

615

1

Asymmetric dimethylarginine Ref.6 Ref.14 Ref.8

Modified residue

633

1

Asymmetric dimethylarginine Ref.6 Ref.14

Modified residue

636

1

Asymmetric dimethylarginine Ref.6 Ref.14

Natural variations

Alternative sequence

266 – 338

73

Missing in isoform EWS-B.

VSP_005793

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

656

Helix Strand Turn

Details...

Beta strand

362 – 366

5

Helix

374 – 381

8

Turn

382 – 384

3

Beta strand

391 – 393

3

Beta strand

396 – 399

4

Turn

404 – 406

3

Beta strand

411 – 419

9

Helix

420 – 430

11

Beta strand

441 – 443

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform EWS [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 0DA02CEE146720BB	FASTA	656	68,478
	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
	Isoform EWS-B. Checksum: 1B011799A0B290ED	FASTA	583	61,217
	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 YGQQSPMDEG PDLDLGPPVD PDEDSDNSAI YVQGLNDSVT 310 320 330 340 350 360 LDDLADFFKQ CGVVKMNKRT GQPMIHIYLD KETGKPKGDA TVSYEDPPTA KAAVEWFDGK 370 380 390 400 410 420 DFQGSKLKVS LARKKPPMNS MRGGLPPREG RGMPPPLRGG PGGPGGPGGP MGRMGGRGGD 430 440 450 460 470 480 RGGFPPRGPR GSRGNPSGGG NVQHRAGDWQ CPNPGCGNQN FAWRTECNQC KAPKPEGFLP 490 500 510 520 530 540 PPFPPPGGDR GRGGPGGMRG GRGGLMDRGG PGGMFRGGRG GDRGGFRGGR GMDRGGFGGG 550 560 570 580 RRGGPGGPPG PLMEQMGGRR GGRGGPGKMD KGEHRQERRD RPY

References

	« Hide 'large scale' referencesShow '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: 1522903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 8307570] [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]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	"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: 8975699] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-345.
[6]	"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: 11278906] [Abstract] Cited for: PROTEIN SEQUENCE OF 128-158; 233-247; 268-324; 334-364; 393-439; 447-518 AND 551-641, METHYLATION AT ARGININES, MASS SPECTROMETRY.
[7]	"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: 7542907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 241-268. Tissue: Placenta.
[8]	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, MASS SPECTROMETRY. Tissue: Colon carcinoma and Ovarian carcinoma.
[9]	"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: 9341188] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-266.
[10]	"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: 8084618] [Abstract] Cited for: ALTERNATIVE SPLICING, RNA-BINDING.
[11]	"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: 9121764] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FEV.
[12]	"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: 9660765] [Abstract] Cited for: INTERACTION WITH SF1.
[13]	"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: 10767297] [Abstract] Cited for: CHARACTERIZATION.
[14]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-471; ARG-503; ARG-506; ARG-615; ARG-633 AND ARG-636, MASS SPECTROMETRY.
[15]	"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: 17172842] [Abstract] Cited for: CHARACTERIZATION OF THE EWSR1-FEV FUSION PROTEIN.
[16]	"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: 18632687] [Abstract] Cited for: INTERACTION WITH TDRD3.
[17]	"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: 18320585] [Abstract] Cited for: METHYLATION AT ARG-490; ARG-572; ARG-596; ARG-603 AND ARG-607.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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.
[20]	"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: 15884099] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ATF1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
[21]	"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: 17724745] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CREB1, ASSOCIATION WITH ANGIOMATOID FIBROUS HISTIOCYTOMA.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

X66899 mRNA. Translation: CAA47350.1.
X72990 , 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.
BC004817 mRNA. Translation: AAH04817.1.
Y08806 Genomic DNA. Translation: CAA70044.1. Different initiation.
AB016435 Genomic DNA. Translation: BAA31990.1.

IPI

IPI00293254.
IPI00872855.

PIR

A49358.

RefSeq

NP_005234.1.

UniGene

Hs.374477

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CPE	NMR	-	A	353-453	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01844. 113 interactions.

PTM databases

PhosphoSite

Q01844.

Proteomic databases

PRIDE

Q01844.

Genome annotation databases

Ensembl

ENSG00000182944. Homo sapiens. [Contig view]

GeneID

2130.

KEGG

hsa:2130.

Organism-specific databases

GeneCards

GC22P027988.

H-InvDB

HIX0016349.

HGNC

HGNC:3508. EWSR1.

HPA

CAB004230.

MIM

133450. gene.
612160. phenotype.

Orphanet

83469. Desmoplastic small round cell tumor.
319. Ewing sarcoma.

PharmGKB

PA27921.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q01844.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

Gene expression databases

ArrayExpress

Q01844.

Bgee

Q01844.

CleanEx

HS_EWSR1.

GermOnline

ENSG00000182944. Homo sapiens.

Family and domain databases

InterPro

IPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
IPR018942. Seminal_vesicle_protein_repeat.
IPR001876. Znf_RanBP2.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF00076. RRM_1. 1 hit.
PF10578. SVS_QK. 2 hits.
PF00641. zf-RanBP. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS50096. IQ. False negative.
PS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8605.

SOURCE

Search...

Entry information

Entry name

EWS_HUMAN

Accession

Primary (citable) accession number: Q01844
Secondary accession number(s): Q92635

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)