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Protein

RNA-binding protein EWS

Gene

Ewsr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. poly(A) RNA binding Source: Ensembl
  3. 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
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
Complete GO annotation...

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.
ExpressionAtlasiQ61545. baseline and differential.
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.
InParanoidiQ61545.
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

        10         20         30         40         50
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV
60 70 80 90 100
SYTQAQTTAT YGQTAYATSY GQPPTGYSTP TAPQAYSQPV QGYGTGTYDS
110 120 130 140 150
TTATVTTTQA SYAAQTAYGT QPAYPTYGQQ PTATAPTRPQ DGNKPAETSQ
160 170 180 190 200
PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP MQPVTAPPSY PPTSYSSSQP
210 220 230 240 250
TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY PPQTGSYSQA
260 270 280 290 300
PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSLSGPDNR
310 320 330 340 350
GRGRGGFDRG GMSRGGRGGG RGGLGAGERG GFNKPGGPMD EGPDLDLGLP
360 370 380 390 400
IDPDEDSDNS AIYVQGLNDN VTLDDLADFF KQCGVVKMNK RTGQPMIHIY
410 420 430 440 450
LDKETGKPKG DATVSYEDPP TAKAAVEWFD GKDFQGSKLK VSLARKKPPM
460 470 480 490 500
NSMRGGMPPR EGRGMPPPLR GGPGGPGGPG GPMGRMGGRG GDRGGFPPRG
510 520 530 540 550
PRGSRGNPSG GGNVQHRAGD WQCPNPGCGN QNFAWRTECN QCKAPKPEGF
560 570 580 590 600
LPPPFPPPGG DRGRGGPGGM RGGRGGLMDR GGPGGMFRGG RGGDRGGFRG
610 620 630 640 650
GRGMDRGGFG GGRRGGPGGP PGPLMEQMGG RRGGRGGPGK MDKGEHRQER

RDRPY
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ61545.

Proteomic databases

MaxQBiQ61545.
PaxDbiQ61545.
PRIDEiQ61545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2130.
MGIiMGI:99960. Ewsr1.

Phylogenomic databases

eggNOGiNOG240581.
GeneTreeiENSGT00530000063105.
HOVERGENiHBG000970.
InParanoidiQ61545.
KOiK13209.
OrthoDBiEOG7DZ8N7.
TreeFamiTF322599.

Miscellaneous databases

NextBioi284964.
PROiQ61545.
SOURCEiSearch...

Gene expression databases

BgeeiQ61545.
CleanExiMM_EWSR1.
ExpressionAtlasiQ61545. baseline and differential.
GenevestigatoriQ61545.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 142 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

Similar proteinsi

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