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Q01844

- EWS_HUMAN

UniProt

Q01844 - EWS_HUMAN

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Protein

RNA-binding protein EWS

Gene

EWSR1

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

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei265 – 2651Breakpoint for translocation to form chimeric EWSR1/ATF1 protein
Sitei348 – 3492Breakpoint for insertion to form EWSR1-FEV fusion protein

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri518 – 54932RanBP2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. RNA binding Source: ProtInc
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. regulation of transcription, DNA-templated Source: UniProtKB-KW
  2. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

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
ProteomesiUP000005640: 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

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi648 – 6481R → A: Cytoplasmic localization. 1 Publication
Mutagenesisi648 – 6481R → K: No effect on nuclear targeting. 1 Publication
Mutagenesisi651 – 6511R → A: No effect on nuclear targeting. 1 Publication
Mutagenesisi652 – 6521R → A: Cytoplasmic localization. 1 Publication
Mutagenesisi652 – 6521R → K: No effect on nuclear targeting. 1 Publication
Mutagenesisi653 – 6531D → A: No effect on nuclear targeting. 1 Publication
Mutagenesisi654 – 6541R → A: No effect on nuclear targeting. 1 Publication
Mutagenesisi655 – 6551P → A: Cytoplasmic localization. 1 Publication
Mutagenesisi656 – 6561Y → A: Cytoplasmic localization. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656656RNA-binding protein EWSPRO_0000081586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661Phosphoserine; by PKCBy similarity
Modified residuei300 – 3001Asymmetric dimethylarginine1 Publication
Modified residuei302 – 3021Asymmetric dimethylarginine1 Publication
Modified residuei304 – 3041Asymmetric dimethylarginine1 Publication
Modified residuei309 – 3091Asymmetric dimethylarginine1 Publication
Modified residuei314 – 3141Asymmetric dimethylarginine1 Publication
Modified residuei317 – 3171Asymmetric dimethylarginine1 Publication
Modified residuei321 – 3211Asymmetric dimethylarginine1 Publication
Modified residuei439 – 4391N6-acetyllysineBy similarity
Modified residuei455 – 4551Asymmetric dimethylarginine1 Publication
Modified residuei464 – 4641Asymmetric dimethylarginine1 Publication
Modified residuei471 – 4711Asymmetric dimethylarginine; alternate1 Publication
Modified residuei471 – 4711Omega-N-methylarginine; alternate1 Publication
Modified residuei490 – 4901Asymmetric dimethylarginine; by PRMT82 Publications
Modified residuei494 – 4941Asymmetric dimethylarginine2 Publications
Modified residuei500 – 5001Asymmetric dimethylarginine1 Publication
Modified residuei503 – 5031Asymmetric dimethylarginine1 Publication
Modified residuei506 – 5061Asymmetric dimethylarginine1 Publication
Modified residuei563 – 5631Asymmetric dimethylarginine1 Publication
Modified residuei565 – 5651Asymmetric dimethylarginine1 Publication
Modified residuei572 – 5721Asymmetric dimethylarginine; alternate; by PRMT82 Publications
Modified residuei572 – 5721Omega-N-methylarginine; alternate; by PRMT82 Publications
Modified residuei575 – 5751Asymmetric dimethylarginine1 Publication
Modified residuei581 – 5811Asymmetric dimethylarginine1 Publication
Modified residuei589 – 5891Asymmetric dimethylarginine1 Publication
Modified residuei592 – 5921Asymmetric dimethylarginine1 Publication
Modified residuei596 – 5961Asymmetric dimethylarginine; alternate; by PRMT82 Publications
Modified residuei596 – 5961Omega-N-methylarginine; alternate; by PRMT82 Publications
Modified residuei600 – 6001Asymmetric dimethylarginine1 Publication
Modified residuei603 – 6031Asymmetric dimethylarginine; by PRMT82 Publications
Modified residuei607 – 6071Asymmetric dimethylarginine; alternate; by PRMT82 Publications
Modified residuei607 – 6071Omega-N-methylarginine; alternate; by PRMT82 Publications
Modified residuei615 – 6151Asymmetric dimethylarginine2 Publications
Modified residuei633 – 6331Asymmetric dimethylarginine1 Publication
Modified residuei636 – 6361Asymmetric dimethylarginine1 Publication

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

MaxQBiQ01844.
PaxDbiQ01844.
PRIDEiQ01844.

PTM databases

PhosphoSiteiQ01844.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ01844.
CleanExiHS_EWSR1.
ExpressionAtlasiQ01844. baseline and differential.
GenevestigatoriQ01844.

Organism-specific databases

HPAiCAB004230.

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
FUSP356375EBI-739737,EBI-400434
PRMT1Q998732EBI-739737,EBI-78738
RASSF1Q9NS23-23EBI-739737,EBI-438698
ZNF165P499102EBI-739737,EBI-741694

Protein-protein interaction databases

BioGridi108431. 210 interactions.
DIPiDIP-34449N.
IntActiQ01844. 135 interactions.
MINTiMINT-4992203.
STRINGi9606.ENSP00000381031.

Structurei

Secondary structure

1
656
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi362 – 3665Combined sources
Helixi374 – 3818Combined sources
Turni382 – 3843Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi396 – 3994Combined sources
Turni404 – 4063Combined sources
Beta strandi411 – 4199Combined sources
Helixi420 – 43011Combined sources
Beta strandi441 – 4433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPENMR-A353-453[»]
DisProtiDP00632.
ProteinModelPortaliQ01844.
SMRiQ01844. Positions 349-453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01844.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 1691
Repeati17 – 27112Add
BLAST
Repeati28 – 3473
Repeati35 – 4284
Repeati43 – 5085
Repeati51 – 5996
Repeati60 – 6897
Repeati69 – 7578
Repeati76 – 8499
Repeati85 – 91710
Repeati92 – 1101911Add
BLAST
Repeati111 – 116612
Repeati117 – 125913
Repeati126 – 1563114Add
BLAST
Repeati157 – 163715
Repeati164 – 170716
Repeati171 – 177717
Repeati178 – 1881118Add
BLAST
Repeati189 – 193519
Repeati194 – 201820
Repeati202 – 206521
Repeati207 – 212622
Repeati213 – 218623
Repeati219 – 224624
Repeati225 – 230625
Repeati231 – 238826
Repeati239 – 245727
Repeati246 – 252728
Repeati253 – 259729
Domaini256 – 28530IQAdd
BLAST
Repeati260 – 2761730Add
BLAST
Repeati277 – 285931
Domaini361 – 44787RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 285285EAD (Gln/Pro/Thr-rich)Add
BLAST
Regioni8 – 28527831 X approximate tandem repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi639 – 65618Nuclear localization signal1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi300 – 34041Arg/Gly/Pro-richAdd
BLAST
Compositional biasi454 – 51360Arg/Gly/Pro-richAdd
BLAST
Compositional biasi559 – 64082Arg/Gly/Pro-richAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri518 – 54932RanBP2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG240581.
GeneTreeiENSGT00530000063105.
HOGENOMiHOG000038010.
HOVERGENiHBG000970.
InParanoidiQ01844.
KOiK13209.
OMAiRDGMMGR.
OrthoDBiEOG7DZ8N7.
PhylomeDBiQ01844.
TreeFamiTF322599.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamiPF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
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. Align

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 CAA70044.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241S → G in BAB71252. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 741P → PTVEGTS in isoform 5. 1 PublicationVSP_043451
Alternative sequencei136 – 19156Missing in isoform 6. 1 PublicationVSP_045412Add
BLAST
Alternative sequencei266 – 33873Missing in isoform EWS-B. CuratedVSP_005793Add
BLAST
Alternative sequencei326 – 35429SAGER…PPVDP → LQSESLVYTSILKKYPYSVL SRQHNEKWD in isoform 4. 1 PublicationVSP_043452Add
BLAST
Alternative sequencei326 – 3261Missing in isoform 3 and isoform 5. 3 PublicationsVSP_043453
Alternative sequencei355 – 656302Missing in isoform 4. 1 PublicationVSP_043454Add
BLAST

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.4. human. [Q01844-4]
uc003aet.3. human. [Q01844-1]
uc003aev.3. human. [Q01844-5]
uc003aew.3. human.
uc003aex.3. human. [Q01844-3]

Polymorphism databases

DMDMi544261.

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 .
CCDSi CCDS13851.1. [Q01844-1 ]
CCDS13852.2. [Q01844-5 ]
CCDS54512.1. [Q01844-4 ]
CCDS54513.1. [Q01844-3 ]
CCDS54514.1. [Q01844-6 ]
PIRi A49358.
RefSeqi NP_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 ]
UniGenei Hs.374477.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CPE NMR - A 353-453 [» ]
DisProti DP00632.
ProteinModelPortali Q01844.
SMRi Q01844. Positions 349-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108431. 210 interactions.
DIPi DIP-34449N.
IntActi Q01844. 135 interactions.
MINTi MINT-4992203.
STRINGi 9606.ENSP00000381031.

PTM databases

PhosphoSitei Q01844.

Polymorphism databases

DMDMi 544261.

Proteomic databases

MaxQBi Q01844.
PaxDbi Q01844.
PRIDEi Q01844.

Protocols and materials databases

DNASUi 2130.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332035 ; ENSP00000331699 ; ENSG00000182944 . [Q01844-6 ]
ENST00000333395 ; ENSP00000327456 ; ENSG00000182944 . [Q01844-4 ]
ENST00000397938 ; ENSP00000381031 ; ENSG00000182944 . [Q01844-1 ]
ENST00000406548 ; ENSP00000385726 ; ENSG00000182944 . [Q01844-3 ]
ENST00000414183 ; ENSP00000400142 ; ENSG00000182944 . [Q01844-5 ]
GeneIDi 2130.
KEGGi hsa:2130.
UCSCi uc003aes.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

CTDi 2130.
GeneCardsi GC22P029663.
HGNCi HGNC:3508. EWSR1.
HPAi CAB004230.
MIMi 133450. gene.
612160. phenotype.
612219. phenotype.
neXtProti NX_Q01844.
Orphaneti 83469. Desmoplastic small round cell tumor.
319. Ewing sarcoma.
370334. Extraskeletal Ewing sarcoma.
209916. Extraskeletal myxoid chondrosarcoma.
97338. Melanoma of soft parts.
PharmGKBi PA27921.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240581.
GeneTreei ENSGT00530000063105.
HOGENOMi HOG000038010.
HOVERGENi HBG000970.
InParanoidi Q01844.
KOi K13209.
OMAi RDGMMGR.
OrthoDBi EOG7DZ8N7.
PhylomeDBi Q01844.
TreeFami TF322599.

Miscellaneous databases

ChiTaRSi EWSR1. human.
EvolutionaryTracei Q01844.
GeneWikii Ewing_sarcoma_breakpoint_region_1.
GenomeRNAii 2130.
NextBioi 8605.
PROi Q01844.
SOURCEi Search...

Gene expression databases

Bgeei Q01844.
CleanExi HS_EWSR1.
ExpressionAtlasi Q01844. baseline and differential.
Genevestigatori Q01844.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
4.10.1060.10. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view ]
Pfami PF00641. zf-RanBP. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. 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. 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.

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 26, 2014
This is version 175 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

External Data

Dasty 3