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Protein

RNA-binding protein EWS

Gene

EWSR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Might normally function as a transcriptional 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei348 – 349Breakpoint for insertion to form EWSR1-FEV fusion protein2

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri518 – 549RanBP2-typePROSITE-ProRule annotationAdd BLAST32

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Calmodulin-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-31013-MONOMER.
SIGNORiQ01844.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein EWS
Alternative name(s):
EWS oncogene
Ewing sarcoma breakpoint region 1 protein
Gene namesi
Name:EWSR1
Synonyms:EWS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:3508. EWSR1.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cell membrane 1 Publication

  • Note: Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ewing sarcoma (ES)4 Publications
The protein represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving EWSR1 are found in patients with Ewing sarcoma. Translocation t(11;22)(q24;q12) with FLI1 (PubMed:1522903, PubMed:15044653). Translocation t(7;22)(p22;q12) with ETV1 (PubMed:7700648). Translocation t(21;22)(q22;q21) with ERG (PubMed:15044653). Translocation t(2;21;22)(q23;q22;q12) that forms a EWSR1-FEV fusion protein with potential oncogenic activity (PubMed:9121764).4 Publications
Disease descriptionA 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.
See also OMIM:612219

A chromosomal aberration involving EWSR1 has been found in extraskeletal myxoid chondrosarcoma. Translocation t(9;22)(q22-31;q11-12) with NR4A3.

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 ATF1. 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)2 Publications
The gene represented in this entry is involved in disease pathogenesis. 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 (PubMed:15884099). Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type (PubMed:17724745).2 Publications
Disease descriptionA 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.
See also OMIM:612160

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi648R → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi648R → K: No effect on nuclear targeting. 1 Publication1
Mutagenesisi651R → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi652R → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi652R → K: No effect on nuclear targeting. 1 Publication1
Mutagenesisi653D → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi654R → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi655P → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi656Y → A: Cytoplasmic localization. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei265Breakpoint for translocation to form chimeric EWSR1/ATF1 protein1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi2130.
MalaCardsiEWSR1.
MIMi612160. phenotype.
612219. phenotype.
OpenTargetsiENSG00000182944.
Orphaneti83469. Desmoplastic small round cell tumor.
319. Ewing sarcoma.
370334. Extraskeletal Ewing sarcoma.
209916. Extraskeletal myxoid chondrosarcoma.
97338. Melanoma of soft parts.
PharmGKBiPA27921.

Polymorphism and mutation databases

BioMutaiEWSR1.
DMDMi544261.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000815861 – 656RNA-binding protein EWSAdd BLAST656

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266Phosphoserine; by PKCBy similarity1
Modified residuei300Asymmetric dimethylarginine1 Publication1
Modified residuei302Asymmetric dimethylarginine1 Publication1
Modified residuei304Asymmetric dimethylarginine1 Publication1
Modified residuei309Asymmetric dimethylarginine1 Publication1
Modified residuei314Asymmetric dimethylarginine1 Publication1
Modified residuei317Asymmetric dimethylarginine1 Publication1
Modified residuei321Asymmetric dimethylarginine1 Publication1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei455Asymmetric dimethylarginine1 Publication1
Modified residuei464Asymmetric dimethylarginine1 Publication1
Modified residuei471Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei471Omega-N-methylarginine; alternateCombined sources1 Publication1
Modified residuei486Omega-N-methylarginineCombined sources1
Modified residuei490Asymmetric dimethylarginine; by PRMT82 Publications1
Modified residuei494Asymmetric dimethylarginine2 Publications1
Modified residuei500Asymmetric dimethylarginine1 Publication1
Modified residuei503Asymmetric dimethylarginine1 Publication1
Modified residuei506Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei506Omega-N-methylarginine; alternateBy similarity1
Modified residuei563Asymmetric dimethylarginine1 Publication1
Modified residuei565Asymmetric dimethylarginine1 Publication1
Modified residuei572Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei572Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei575Asymmetric dimethylarginine1 Publication1
Modified residuei581Asymmetric dimethylarginine1 Publication1
Modified residuei589Asymmetric dimethylarginine1 Publication1
Modified residuei592Asymmetric dimethylarginine1 Publication1
Modified residuei596Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei596Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei600Asymmetric dimethylarginine1 Publication1
Modified residuei603Asymmetric dimethylarginine; by PRMT82 Publications1
Modified residuei607Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei607Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei615Asymmetric dimethylarginine; alternate2 Publications1
Modified residuei615Omega-N-methylarginine; alternateCombined sources1
Modified residuei633Asymmetric dimethylarginine1 Publication1
Modified residuei636Asymmetric dimethylarginine1 Publication1

Post-translational modificationi

Phosphorylated; calmodulin-binding inhibits phosphorylation of Ser-266.1 Publication
Highly methylated on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8.3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ01844.
MaxQBiQ01844.
PaxDbiQ01844.
PeptideAtlasiQ01844.
PRIDEiQ01844.

PTM databases

iPTMnetiQ01844.
PhosphoSitePlusiQ01844.
SwissPalmiQ01844.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000182944.
CleanExiHS_EWSR1.
ExpressionAtlasiQ01844. baseline and differential.
GenevisibleiQ01844. HS.

Organism-specific databases

HPAiCAB004230.
HPA051771.
HPA062953.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-739737,EBI-739737
ATPAF2Q8N5M13EBI-739737,EBI-1166928
FUSP356375EBI-739737,EBI-400434
MAPK1IP1LQ8NDC05EBI-739737,EBI-741424
PEF1Q9UBV83EBI-739737,EBI-724639
PLSCR1O151624EBI-739737,EBI-740019
PRMT1Q998732EBI-739737,EBI-78738
PRR13Q9NZ813EBI-739737,EBI-740924
RASSF1Q9NS23-23EBI-739737,EBI-438698
SEC24AO954863EBI-739737,EBI-749911
SEC24DO948553EBI-739737,EBI-748817
SSBP3Q9BWW43EBI-739737,EBI-2902395
TFGQ927343EBI-739737,EBI-357061
TRAF1Q130773EBI-739737,EBI-359224
TRAF2Q129333EBI-739737,EBI-355744
ZNF165P499102EBI-739737,EBI-741694

Protein-protein interaction databases

BioGridi108431. 648 interactors.
DIPiDIP-34449N.
IntActiQ01844. 150 interactors.
MINTiMINT-4992203.
STRINGi9606.ENSP00000400142.

Structurei

Secondary structure

1656
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi362 – 366Combined sources5
Helixi374 – 381Combined sources8
Turni382 – 384Combined sources3
Beta strandi391 – 393Combined sources3
Beta strandi396 – 399Combined sources4
Turni404 – 406Combined sources3
Beta strandi411 – 419Combined sources9
Helixi420 – 430Combined sources11
Beta strandi441 – 443Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CPENMR-A353-453[»]
DisProtiDP00632.
ProteinModelPortaliQ01844.
SMRiQ01844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01844.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati8 – 1619
Repeati17 – 272Add BLAST11
Repeati28 – 3437
Repeati35 – 4248
Repeati43 – 5058
Repeati51 – 5969
Repeati60 – 6879
Repeati69 – 7587
Repeati76 – 8499
Repeati85 – 91107
Repeati92 – 11011Add BLAST19
Repeati111 – 116126
Repeati117 – 125139
Repeati126 – 15614Add BLAST31
Repeati157 – 163157
Repeati164 – 170167
Repeati171 – 177177
Repeati178 – 18818Add BLAST11
Repeati189 – 193195
Repeati194 – 201208
Repeati202 – 206215
Repeati207 – 212226
Repeati213 – 218236
Repeati219 – 224246
Repeati225 – 230256
Repeati231 – 238268
Repeati239 – 245277
Repeati246 – 252287
Repeati253 – 259297
Domaini256 – 285IQAdd BLAST30
Repeati260 – 27630Add BLAST17
Repeati277 – 285319
Domaini361 – 447RRMPROSITE-ProRule annotationAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 285EAD (Gln/Pro/Thr-rich)Add BLAST285
Regioni8 – 28531 X approximate tandem repeatsAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi639 – 656Nuclear localization signal1 PublicationAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi300 – 340Arg/Gly/Pro-richAdd BLAST41
Compositional biasi454 – 513Arg/Gly/Pro-richAdd BLAST60
Compositional biasi559 – 640Arg/Gly/Pro-richAdd BLAST82

Domaini

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.

Sequence similaritiesi

Belongs to the RRM TET family.Curated
Contains 1 IQ domain.Curated
Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri518 – 549RanBP2-typePROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1995. Eukaryota.
ENOG4111Q2F. LUCA.
GeneTreeiENSGT00530000063105.
HOGENOMiHOG000038010.
HOVERGENiHBG000970.
InParanoidiQ01844.
KOiK13209.
OMAiNEREMGR.
OrthoDBiEOG091G0U8W.
PhylomeDBiQ01844.
TreeFamiTF322599.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProiIPR033109. EWSR1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PANTHERiPTHR23238:SF3. PTHR23238:SF3. 2 hits.
PfamiPF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform EWS (identifier: Q01844-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV
60 70 80 90 100
SYTQAQTTAT YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT
110 120 130 140 150
TTATVTTTQA SYAAQSAYGT QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ
160 170 180 190 200
PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP MQPVTAPPSY PPTSYSSTQP
210 220 230 240 250
TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY PPQTGSYSQA
260 270 280 290 300
PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSMSGPDNR
310 320 330 340 350
GRGRGGFDRG GMSRGGRGGG RGGMGSAGER GGFNKPGGPM DEGPDLDLGP
360 370 380 390 400
PVDPDEDSDN SAIYVQGLND SVTLDDLADF FKQCGVVKMN KRTGQPMIHI
410 420 430 440 450
YLDKETGKPK GDATVSYEDP PTAKAAVEWF DGKDFQGSKL KVSLARKKPP
460 470 480 490 500
MNSMRGGLPP REGRGMPPPL RGGPGGPGGP GGPMGRMGGR GGDRGGFPPR
510 520 530 540 550
GPRGSRGNPS GGGNVQHRAG DWQCPNPGCG NQNFAWRTEC NQCKAPKPEG
560 570 580 590 600
FLPPPFPPPG GDRGRGGPGG MRGGRGGLMD RGGPGGMFRG GRGGDRGGFR
610 620 630 640 650
GGRGMDRGGF GGGRRGGPGG PPGPLMEQMG GRRGGRGGPG KMDKGEHRQE

RRDRPY
Length:656
Mass (Da):68,478
Last modified:June 1, 1994 - v1
Checksum:i0DA02CEE146720BB
GO
Isoform EWS-B (identifier: Q01844-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-338: Missing.

Note: No experimental confirmation available.
Show »
Length:583
Mass (Da):61,217
Checksum:i1B011799A0B290ED
GO
Isoform 3 (identifier: Q01844-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-326: Missing.

Show »
Length:655
Mass (Da):68,391
Checksum:iB539ED1E98C601ED
GO
Isoform 4 (identifier: Q01844-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-354: SAGERGGFNKPGGPMDEGPDLDLGPPVDP → LQSESLVYTSILKKYPYSVLSRQHNEKWD
     355-656: Missing.

Note: No experimental confirmation available.
Show »
Length:354
Mass (Da):37,620
Checksum:iAE4B8FCDF458390B
GO
Isoform 5 (identifier: Q01844-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: P → PTVEGTS
     326-326: Missing.

Note: No experimental confirmation available.
Show »
Length:661
Mass (Da):68,966
Checksum:i5F84F52FDCD51269
GO
Isoform 6 (identifier: Q01844-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-191: Missing.

Note: No experimental confirmation available.
Show »
Length:600
Mass (Da):62,508
Checksum:iB3D01637474FFFB0
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti224S → G in BAB71252 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04345174P → PTVEGTS in isoform 5. 1 Publication1
Alternative sequenceiVSP_045412136 – 191Missing in isoform 6. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_005793266 – 338Missing in isoform EWS-B. CuratedAdd BLAST73
Alternative sequenceiVSP_043452326 – 354SAGER…PPVDP → LQSESLVYTSILKKYPYSVL SRQHNEKWD in isoform 4. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_043453326Missing in isoform 3 and isoform 5. 3 Publications1
Alternative sequenceiVSP_043454355 – 656Missing in isoform 4. 1 PublicationAdd BLAST302

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
CCDSiCCDS13851.1. [Q01844-1]
CCDS13852.2. [Q01844-5]
CCDS54512.1. [Q01844-4]
CCDS54513.1. [Q01844-3]
CCDS54514.1. [Q01844-6]
PIRiA49358.
RefSeqiNP_001156757.1. NM_001163285.1. [Q01844-3]
NP_001156758.1. NM_001163286.1. [Q01844-6]
NP_001156759.1. NM_001163287.1. [Q01844-4]
NP_005234.1. NM_005243.3. [Q01844-1]
NP_053733.2. NM_013986.3. [Q01844-5]
UniGeneiHs.374477.

Genome annotation databases

EnsembliENST00000332035; ENSP00000331699; ENSG00000182944. [Q01844-6]
ENST00000333395; ENSP00000327456; ENSG00000182944. [Q01844-4]
ENST00000397938; ENSP00000381031; ENSG00000182944. [Q01844-1]
ENST00000406548; ENSP00000385726; ENSG00000182944. [Q01844-3]
ENST00000414183; ENSP00000400142; ENSG00000182944. [Q01844-5]
GeneIDi2130.
KEGGihsa:2130.
UCSCiuc003aes.5. human. [Q01844-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
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.
CCDSiCCDS13851.1. [Q01844-1]
CCDS13852.2. [Q01844-5]
CCDS54512.1. [Q01844-4]
CCDS54513.1. [Q01844-3]
CCDS54514.1. [Q01844-6]
PIRiA49358.
RefSeqiNP_001156757.1. NM_001163285.1. [Q01844-3]
NP_001156758.1. NM_001163286.1. [Q01844-6]
NP_001156759.1. NM_001163287.1. [Q01844-4]
NP_005234.1. NM_005243.3. [Q01844-1]
NP_053733.2. NM_013986.3. [Q01844-5]
UniGeneiHs.374477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CPENMR-A353-453[»]
DisProtiDP00632.
ProteinModelPortaliQ01844.
SMRiQ01844.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108431. 648 interactors.
DIPiDIP-34449N.
IntActiQ01844. 150 interactors.
MINTiMINT-4992203.
STRINGi9606.ENSP00000400142.

PTM databases

iPTMnetiQ01844.
PhosphoSitePlusiQ01844.
SwissPalmiQ01844.

Polymorphism and mutation databases

BioMutaiEWSR1.
DMDMi544261.

Proteomic databases

EPDiQ01844.
MaxQBiQ01844.
PaxDbiQ01844.
PeptideAtlasiQ01844.
PRIDEiQ01844.

Protocols and materials databases

DNASUi2130.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332035; ENSP00000331699; ENSG00000182944. [Q01844-6]
ENST00000333395; ENSP00000327456; ENSG00000182944. [Q01844-4]
ENST00000397938; ENSP00000381031; ENSG00000182944. [Q01844-1]
ENST00000406548; ENSP00000385726; ENSG00000182944. [Q01844-3]
ENST00000414183; ENSP00000400142; ENSG00000182944. [Q01844-5]
GeneIDi2130.
KEGGihsa:2130.
UCSCiuc003aes.5. human. [Q01844-1]

Organism-specific databases

CTDi2130.
DisGeNETi2130.
GeneCardsiEWSR1.
HGNCiHGNC:3508. EWSR1.
HPAiCAB004230.
HPA051771.
HPA062953.
MalaCardsiEWSR1.
MIMi133450. gene.
612160. phenotype.
612219. phenotype.
neXtProtiNX_Q01844.
OpenTargetsiENSG00000182944.
Orphaneti83469. Desmoplastic small round cell tumor.
319. Ewing sarcoma.
370334. Extraskeletal Ewing sarcoma.
209916. Extraskeletal myxoid chondrosarcoma.
97338. Melanoma of soft parts.
PharmGKBiPA27921.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1995. Eukaryota.
ENOG4111Q2F. LUCA.
GeneTreeiENSGT00530000063105.
HOGENOMiHOG000038010.
HOVERGENiHBG000970.
InParanoidiQ01844.
KOiK13209.
OMAiNEREMGR.
OrthoDBiEOG091G0U8W.
PhylomeDBiQ01844.
TreeFamiTF322599.

Enzyme and pathway databases

BioCyciZFISH:G66-31013-MONOMER.
SIGNORiQ01844.

Miscellaneous databases

ChiTaRSiEWSR1. human.
EvolutionaryTraceiQ01844.
GeneWikiiEwing_sarcoma_breakpoint_region_1.
GenomeRNAii2130.
PROiQ01844.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000182944.
CleanExiHS_EWSR1.
ExpressionAtlasiQ01844. baseline and differential.
GenevisibleiQ01844. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProiIPR033109. EWSR1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PANTHERiPTHR23238:SF3. PTHR23238:SF3. 2 hits.
PfamiPF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF90209. SSF90209. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEWS_HUMAN
AccessioniPrimary (citable) accession number: Q01844
Secondary accession number(s): B0QYK1
, Q5THL0, Q92635, Q96FE8, Q96MN4, Q96MX4, Q9BWA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 195 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.