Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01844

- EWS_HUMAN

UniProt

Q01844 - EWS_HUMAN

Protein

RNA-binding protein EWS

Gene

EWSR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: UniProtKB
    5. RNA binding Source: ProtInc
    6. zinc ion binding Source: InterPro

    GO - Biological processi

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

    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-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiQ01844.
    BgeeiQ01844.
    CleanExiHS_EWSR1.
    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. 209 interactions.
    DIPiDIP-34449N.
    IntActiQ01844. 133 interactions.
    MINTiMINT-4992203.
    STRINGi9606.ENSP00000381031.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000038010.
    HOVERGENiHBG000970.
    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

    MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV    50
    SYTQAQTTAT YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT 100
    TTATVTTTQA SYAAQSAYGT QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ 150
    PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP MQPVTAPPSY PPTSYSSTQP 200
    TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY PPQTGSYSQA 250
    PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSMSGPDNR 300
    GRGRGGFDRG GMSRGGRGGG RGGMGSAGER GGFNKPGGPM DEGPDLDLGP 350
    PVDPDEDSDN SAIYVQGLND SVTLDDLADF FKQCGVVKMN KRTGQPMIHI 400
    YLDKETGKPK GDATVSYEDP PTAKAAVEWF DGKDFQGSKL KVSLARKKPP 450
    MNSMRGGLPP REGRGMPPPL RGGPGGPGGP GGPMGRMGGR GGDRGGFPPR 500
    GPRGSRGNPS GGGNVQHRAG DWQCPNPGCG NQNFAWRTEC NQCKAPKPEG 550
    FLPPPFPPPG GDRGRGGPGG MRGGRGGLMD RGGPGGMFRG GRGGDRGGFR 600
    GGRGMDRGGF GGGRRGGPGG PPGPLMEQMG GRRGGRGGPG KMDKGEHRQE 650
    RRDRPY 656
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 209 interactions.
    DIPi DIP-34449N.
    IntActi Q01844. 133 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.
    HOGENOMi HOG000038010.
    HOVERGENi HBG000970.
    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

    ArrayExpressi Q01844.
    Bgeei Q01844.
    CleanExi HS_EWSR1.
    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

    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: October 1, 2014
    This is version 173 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