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)

Q61545

- EWS_MOUSE

UniProt

Q61545 - EWS_MOUSE

Protein

RNA-binding protein EWS

Gene

Ewsr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Might function as a transcriptionnal repressor.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri517 – 54832RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. protein binding Source: IntAct
    3. RNA binding Source: UniProtKB-KW
    4. 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
    Gene namesi
    Name:Ewsr1
    Synonyms:Ews, Ewsh
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:99960. Ewsr1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 655655RNA-binding protein EWSPRO_0000081587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei266 – 2661Phosphoserine; by PKCBy similarity
    Modified residuei300 – 3001Asymmetric dimethylarginineBy similarity
    Modified residuei302 – 3021Asymmetric dimethylarginineBy similarity
    Modified residuei304 – 3041Asymmetric dimethylarginineBy similarity
    Modified residuei309 – 3091Asymmetric dimethylarginineBy similarity
    Modified residuei314 – 3141Asymmetric dimethylarginineBy similarity
    Modified residuei317 – 3171Asymmetric dimethylarginineBy similarity
    Modified residuei321 – 3211Asymmetric dimethylarginineBy similarity
    Modified residuei438 – 4381N6-acetyllysine1 Publication
    Modified residuei454 – 4541Asymmetric dimethylarginineBy similarity
    Modified residuei463 – 4631Asymmetric dimethylarginineBy similarity
    Modified residuei470 – 4701Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei470 – 4701Omega-N-methylarginine; alternateBy similarity
    Modified residuei489 – 4891Asymmetric dimethylarginine; by PRMT8By similarity
    Modified residuei493 – 4931Asymmetric dimethylarginineBy similarity
    Modified residuei499 – 4991Asymmetric dimethylarginineBy similarity
    Modified residuei502 – 5021Asymmetric dimethylarginineBy similarity
    Modified residuei505 – 5051Asymmetric dimethylarginineBy similarity
    Modified residuei562 – 5621Asymmetric dimethylarginineBy similarity
    Modified residuei564 – 5641Asymmetric dimethylarginineBy similarity
    Modified residuei571 – 5711Asymmetric dimethylarginine; alternate; by PRMT8By similarity
    Modified residuei571 – 5711Omega-N-methylarginine; alternate; by PRMT8By similarity
    Modified residuei574 – 5741Asymmetric dimethylarginineBy similarity
    Modified residuei580 – 5801Asymmetric dimethylarginineBy similarity
    Modified residuei588 – 5881Asymmetric dimethylarginineBy similarity
    Modified residuei591 – 5911Asymmetric dimethylarginineBy similarity
    Modified residuei595 – 5951Asymmetric dimethylarginine; alternate; by PRMT8By similarity
    Modified residuei595 – 5951Omega-N-methylarginine; alternate; by PRMT8By similarity
    Modified residuei599 – 5991Asymmetric dimethylarginineBy similarity
    Modified residuei602 – 6021Asymmetric dimethylarginine; by PRMT8By similarity
    Modified residuei606 – 6061Asymmetric dimethylarginine; alternate; by PRMT8By similarity
    Modified residuei606 – 6061Omega-N-methylarginine; alternate; by PRMT8By similarity
    Modified residuei614 – 6141Asymmetric dimethylarginineBy similarity
    Modified residuei632 – 6321Asymmetric dimethylarginineBy similarity
    Modified residuei635 – 6351Asymmetric dimethylarginineBy similarity

    Post-translational modificationi

    Phosphorylated; calmodulin-binding inhibits phosphorylation of Ser-266.By similarity
    Highly methylated on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61545.
    PaxDbiQ61545.
    PRIDEiQ61545.

    PTM databases

    PhosphoSiteiQ61545.

    Expressioni

    Gene expression databases

    BgeeiQ61545.
    CleanExiMM_EWSR1.
    GenevestigatoriQ61545.

    Interactioni

    Subunit structurei

    Binds RNA, POLR2C, SF1 and calmodulin. Interacts with PTK2B and TDRD3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Pou5f1P2026313EBI-1606991,EBI-1606219

    Protein-protein interaction databases

    BioGridi199551. 57 interactions.
    IntActiQ61545. 6 interactions.
    MINTiMINT-4126745.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61545.
    SMRiQ61545. Positions 352-452.
    ModBaseiSearch...
    MobiDBiSearch...

    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
    Domaini360 – 44687RRMPROSITE-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
    Motifi638 – 65518Nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi300 – 33940Arg/Gly/Pro-richAdd
    BLAST
    Compositional biasi453 – 51260Arg/Gly/Pro-richAdd
    BLAST
    Compositional biasi558 – 63982Arg/Gly/Pro-richAdd
    BLAST

    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 fingeri517 – 54832RanBP2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG240581.
    GeneTreeiENSGT00530000063105.
    HOVERGENiHBG000970.
    KOiK13209.
    OrthoDBiEOG7DZ8N7.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q61545-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV    50
    SYTQAQTTAT YGQTAYATSY GQPPTGYSTP TAPQAYSQPV QGYGTGTYDS 100
    TTATVTTTQA SYAAQTAYGT QPAYPTYGQQ PTATAPTRPQ DGNKPAETSQ 150
    PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP MQPVTAPPSY PPTSYSSSQP 200
    TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY PPQTGSYSQA 250
    PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSLSGPDNR 300
    GRGRGGFDRG GMSRGGRGGG RGGLGAGERG GFNKPGGPMD EGPDLDLGLP 350
    IDPDEDSDNS AIYVQGLNDN VTLDDLADFF KQCGVVKMNK RTGQPMIHIY 400
    LDKETGKPKG DATVSYEDPP TAKAAVEWFD GKDFQGSKLK VSLARKKPPM 450
    NSMRGGMPPR EGRGMPPPLR GGPGGPGGPG GPMGRMGGRG GDRGGFPPRG 500
    PRGSRGNPSG GGNVQHRAGD WQCPNPGCGN QNFAWRTECN QCKAPKPEGF 550
    LPPPFPPPGG DRGRGGPGGM RGGRGGLMDR GGPGGMFRGG RGGDRGGFRG 600
    GRGMDRGGFG GGRRGGPGGP PGPLMEQMGG RRGGRGGPGK MDKGEHRQER 650
    RDRPY 655
    Length:655
    Mass (Da):68,462
    Last modified:July 27, 2011 - v2
    Checksum:i10C7F06A921668F3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971T → A in CAA55815. (PubMed:7829090)Curated
    Sequence conflicti116 – 1161T → S in CAA55815. (PubMed:7829090)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79233 mRNA. Translation: CAA55815.1.
    AK019460 mRNA. Translation: BAB31732.1.
    AK151625 mRNA. Translation: BAE30560.1.
    AL645845 Genomic DNA. Translation: CAI25231.1.
    CH466574 Genomic DNA. Translation: EDL40519.1.
    CCDSiCCDS24396.1.
    PIRiA55726.
    RefSeqiNP_031994.2. NM_007968.3.
    UniGeneiMm.142822.

    Genome annotation databases

    EnsembliENSMUST00000079949; ENSMUSP00000078867; ENSMUSG00000009079.
    GeneIDi14030.
    KEGGimmu:14030.
    UCSCiuc007hvw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79233 mRNA. Translation: CAA55815.1 .
    AK019460 mRNA. Translation: BAB31732.1 .
    AK151625 mRNA. Translation: BAE30560.1 .
    AL645845 Genomic DNA. Translation: CAI25231.1 .
    CH466574 Genomic DNA. Translation: EDL40519.1 .
    CCDSi CCDS24396.1.
    PIRi A55726.
    RefSeqi NP_031994.2. NM_007968.3.
    UniGenei Mm.142822.

    3D structure databases

    ProteinModelPortali Q61545.
    SMRi Q61545. Positions 352-452.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199551. 57 interactions.
    IntActi Q61545. 6 interactions.
    MINTi MINT-4126745.

    PTM databases

    PhosphoSitei Q61545.

    Proteomic databases

    MaxQBi Q61545.
    PaxDbi Q61545.
    PRIDEi Q61545.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079949 ; ENSMUSP00000078867 ; ENSMUSG00000009079 .
    GeneIDi 14030.
    KEGGi mmu:14030.
    UCSCi uc007hvw.1. mouse.

    Organism-specific databases

    CTDi 2130.
    MGIi MGI:99960. Ewsr1.

    Phylogenomic databases

    eggNOGi NOG240581.
    GeneTreei ENSGT00530000063105.
    HOVERGENi HBG000970.
    KOi K13209.
    OrthoDBi EOG7DZ8N7.
    TreeFami TF322599.

    Miscellaneous databases

    NextBioi 284964.
    PROi Q61545.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61545.
    CleanExi MM_EWSR1.
    Genevestigatori Q61545.

    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. "Cloning and chromosome localization of the mouse Ews gene."
      Plougastel B., Mattei M.-G., Thomas G., Delattre O.
      Genomics 23:278-281(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Placenta.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiEWS_MOUSE
    AccessioniPrimary (citable) accession number: Q61545
    Secondary accession number(s): Q9D2P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds calmodulin in the presence, but not in the absence, of calcium ion.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3