Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RNA-binding protein EWS

Gene

Ewsr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Might function as a transcriptional repressor.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri517 – 548RanBP2-typePROSITE-ProRule annotationAdd BLAST32

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

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
Proteomesi
  • UP000000589 Componenti: 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

  • cytoplasm Source: UniProtKB-SubCell
  • nucleolus Source: Ensembl
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000815871 – 655RNA-binding protein EWSAdd BLAST655

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266Phosphoserine; by PKCBy similarity1
Modified residuei300Asymmetric dimethylarginineBy similarity1
Modified residuei302Asymmetric dimethylarginineBy similarity1
Modified residuei304Asymmetric dimethylarginineBy similarity1
Modified residuei309Asymmetric dimethylarginineBy similarity1
Modified residuei314Asymmetric dimethylarginineBy similarity1
Modified residuei317Asymmetric dimethylarginineBy similarity1
Modified residuei321Asymmetric dimethylarginineBy similarity1
Modified residuei438N6-acetyllysineCombined sources1
Modified residuei454Asymmetric dimethylarginineBy similarity1
Modified residuei463Asymmetric dimethylarginineBy similarity1
Modified residuei470Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei470Omega-N-methylarginine; alternateCombined sources1
Modified residuei485Omega-N-methylarginineCombined sources1
Modified residuei489Asymmetric dimethylarginine; by PRMT8By similarity1
Modified residuei493Asymmetric dimethylarginineBy similarity1
Modified residuei499Asymmetric dimethylarginineBy similarity1
Modified residuei502Asymmetric dimethylarginineCombined sources1
Modified residuei505Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei505Omega-N-methylarginine; alternateCombined sources1
Modified residuei562Asymmetric dimethylarginineBy similarity1
Modified residuei564Asymmetric dimethylarginineBy similarity1
Modified residuei571Asymmetric dimethylarginine; alternate; by PRMT8By similarity1
Modified residuei571Omega-N-methylarginine; alternate; by PRMT8By similarity1
Modified residuei574Asymmetric dimethylarginineBy similarity1
Modified residuei580Asymmetric dimethylarginineBy similarity1
Modified residuei588Asymmetric dimethylarginineBy similarity1
Modified residuei591Asymmetric dimethylarginineBy similarity1
Modified residuei595Asymmetric dimethylarginine; alternate; by PRMT8By similarity1
Modified residuei595Omega-N-methylarginine; alternate; by PRMT8By similarity1
Modified residuei599Asymmetric dimethylarginineBy similarity1
Modified residuei602Asymmetric dimethylarginine; by PRMT8By similarity1
Modified residuei606Asymmetric dimethylarginine; alternate; by PRMT8By similarity1
Modified residuei606Omega-N-methylarginine; alternate; by PRMT8By similarity1
Modified residuei614Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei614Omega-N-methylarginine; alternateCombined sources1
Modified residuei632Asymmetric dimethylarginineBy similarity1
Modified residuei635Asymmetric dimethylarginineBy similarity1

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

EPDiQ61545.
MaxQBiQ61545.
PaxDbiQ61545.
PRIDEiQ61545.

PTM databases

iPTMnetiQ61545.
PhosphoSitePlusiQ61545.

Expressioni

Gene expression databases

BgeeiENSMUSG00000009079.
CleanExiMM_EWSR1.
ExpressionAtlasiQ61545. baseline and differential.
GenevisibleiQ61545. MM.

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. 65 interactors.
IntActiQ61545. 13 interactors.
MINTiMINT-4126745.
STRINGi10090.ENSMUSP00000078867.

Structurei

3D structure databases

ProteinModelPortaliQ61545.
SMRiQ61545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati8 – 1619
Repeati17 – 272Add BLAST11
Repeati28 – 3437
Repeati35 – 4248
Repeati43 – 5058
Repeati51 – 5969
Repeati60 – 6879
Repeati69 – 7587
Repeati76 – 8499
Repeati85 – 91107
Repeati92 – 11011Add BLAST19
Repeati111 – 116126
Repeati117 – 125139
Repeati126 – 15614Add BLAST31
Repeati157 – 163157
Repeati164 – 170167
Repeati171 – 177177
Repeati178 – 18818Add BLAST11
Repeati189 – 193195
Repeati194 – 201208
Repeati202 – 206215
Repeati207 – 212226
Repeati213 – 218236
Repeati219 – 224246
Repeati225 – 230256
Repeati231 – 238268
Repeati239 – 245277
Repeati246 – 252287
Repeati253 – 259297
Domaini256 – 285IQAdd BLAST30
Repeati260 – 27630Add BLAST17
Repeati277 – 285319
Domaini360 – 446RRMPROSITE-ProRule annotationAdd BLAST87

Region

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi638 – 655Nuclear localization signalBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi300 – 339Arg/Gly/Pro-richAdd BLAST40
Compositional biasi453 – 512Arg/Gly/Pro-richAdd BLAST60
Compositional biasi558 – 639Arg/Gly/Pro-richAdd BLAST82

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri517 – 548RanBP2-typePROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1995. Eukaryota.
ENOG4111Q2F. LUCA.
GeneTreeiENSGT00530000063105.
HOVERGENiHBG000970.
InParanoidiQ61545.
KOiK13209.
TreeFamiTF322599.

Family and domain databases

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

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)DescriptionActionsGraphical viewLength
Sequence conflicti97T → A in CAA55815 (PubMed:7829090).Curated1
Sequence conflicti116T → S in CAA55815 (PubMed:7829090).Curated1

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.2. 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199551. 65 interactors.
IntActiQ61545. 13 interactors.
MINTiMINT-4126745.
STRINGi10090.ENSMUSP00000078867.

PTM databases

iPTMnetiQ61545.
PhosphoSitePlusiQ61545.

Proteomic databases

EPDiQ61545.
MaxQBiQ61545.
PaxDbiQ61545.
PRIDEiQ61545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079949; ENSMUSP00000078867; ENSMUSG00000009079.
GeneIDi14030.
KEGGimmu:14030.
UCSCiuc007hvw.2. mouse.

Organism-specific databases

CTDi2130.
MGIiMGI:99960. Ewsr1.

Phylogenomic databases

eggNOGiKOG1995. Eukaryota.
ENOG4111Q2F. LUCA.
GeneTreeiENSGT00530000063105.
HOVERGENiHBG000970.
InParanoidiQ61545.
KOiK13209.
TreeFamiTF322599.

Miscellaneous databases

PROiQ61545.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009079.
CleanExiMM_EWSR1.
ExpressionAtlasiQ61545. baseline and differential.
GenevisibleiQ61545. MM.

Family and domain databases

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

Entry informationi

Entry nameiEWS_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: November 2, 2016
This is version 158 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

Similar proteinsi

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