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Q61545 (EWS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding protein EWS
Gene names
Name:Ewsr1
Synonyms:Ews, Ewsh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Might function as a transcriptionnal repressor By similarity.

Subunit structure

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

Subcellular location

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

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the RRM TET family.

Contains 1 IQ domain.

Contains 1 RanBP2-type zinc finger.

Contains 1 RRM (RNA recognition motif) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pou5f1P2026313EBI-1606991,EBI-1606219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655RNA-binding protein EWS
PRO_0000081587

Regions

Repeat8 – 1691
Repeat17 – 27112
Repeat28 – 3473
Repeat35 – 4284
Repeat43 – 5085
Repeat51 – 5996
Repeat60 – 6897
Repeat69 – 7578
Repeat76 – 8499
Repeat85 – 91710
Repeat92 – 1101911
Repeat111 – 116612
Repeat117 – 125913
Repeat126 – 1563114
Repeat157 – 163715
Repeat164 – 170716
Repeat171 – 177717
Repeat178 – 1881118
Repeat189 – 193519
Repeat194 – 201820
Repeat202 – 206521
Repeat207 – 212622
Repeat213 – 218623
Repeat219 – 224624
Repeat225 – 230625
Repeat231 – 238826
Repeat239 – 245727
Repeat246 – 252728
Repeat253 – 259729
Domain256 – 28530IQ
Repeat260 – 2761730
Repeat277 – 285931
Domain360 – 44687RRM
Zinc finger517 – 54832RanBP2-type
Region1 – 285285EAD (Gln/Pro/Thr-rich)
Region8 – 28527831 X approximate tandem repeats
Motif638 – 65518Nuclear localization signal By similarity
Compositional bias300 – 33940Arg/Gly/Pro-rich
Compositional bias453 – 51260Arg/Gly/Pro-rich
Compositional bias558 – 63982Arg/Gly/Pro-rich

Amino acid modifications

Modified residue2661Phosphoserine; by PKC By similarity
Modified residue3001Asymmetric dimethylarginine By similarity
Modified residue3021Asymmetric dimethylarginine By similarity
Modified residue3041Asymmetric dimethylarginine By similarity
Modified residue3091Asymmetric dimethylarginine By similarity
Modified residue3141Asymmetric dimethylarginine By similarity
Modified residue3171Asymmetric dimethylarginine By similarity
Modified residue3211Asymmetric dimethylarginine By similarity
Modified residue4541Asymmetric dimethylarginine By similarity
Modified residue4631Asymmetric dimethylarginine By similarity
Modified residue4701Asymmetric dimethylarginine; alternate By similarity
Modified residue4701Omega-N-methylarginine; alternate By similarity
Modified residue4891Asymmetric dimethylarginine; by PRMT8 By similarity
Modified residue4931Asymmetric dimethylarginine By similarity
Modified residue4991Asymmetric dimethylarginine By similarity
Modified residue5021Asymmetric dimethylarginine By similarity
Modified residue5051Asymmetric dimethylarginine By similarity
Modified residue5621Asymmetric dimethylarginine By similarity
Modified residue5641Asymmetric dimethylarginine By similarity
Modified residue5711Asymmetric dimethylarginine; alternate; by PRMT8 By similarity
Modified residue5711Omega-N-methylarginine; alternate; by PRMT8 By similarity
Modified residue5741Asymmetric dimethylarginine By similarity
Modified residue5801Asymmetric dimethylarginine By similarity
Modified residue5881Asymmetric dimethylarginine By similarity
Modified residue5911Asymmetric dimethylarginine By similarity
Modified residue5951Asymmetric dimethylarginine; alternate; by PRMT8 By similarity
Modified residue5951Omega-N-methylarginine; alternate; by PRMT8 By similarity
Modified residue5991Asymmetric dimethylarginine By similarity
Modified residue6021Asymmetric dimethylarginine; by PRMT8 By similarity
Modified residue6061Asymmetric dimethylarginine; alternate; by PRMT8 By similarity
Modified residue6061Omega-N-methylarginine; alternate; by PRMT8 By similarity
Modified residue6141Asymmetric dimethylarginine By similarity
Modified residue6321Asymmetric dimethylarginine By similarity
Modified residue6351Asymmetric dimethylarginine By similarity

Experimental info

Sequence conflict971T → A in CAA55815. Ref.1
Sequence conflict1161T → S in CAA55815. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61545 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 10C7F06A921668F3

FASTA65568,462
        10         20         30         40         50         60 
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV SYTQAQTTAT 

        70         80         90        100        110        120 
YGQTAYATSY GQPPTGYSTP TAPQAYSQPV QGYGTGTYDS TTATVTTTQA SYAAQTAYGT 

       130        140        150        160        170        180 
QPAYPTYGQQ PTATAPTRPQ DGNKPAETSQ PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP 

       190        200        210        220        230        240 
MQPVTAPPSY PPTSYSSSQP TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY 

       250        260        270        280        290        300 
PPQTGSYSQA PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSLSGPDNR 

       310        320        330        340        350        360 
GRGRGGFDRG GMSRGGRGGG RGGLGAGERG GFNKPGGPMD EGPDLDLGLP IDPDEDSDNS 

       370        380        390        400        410        420 
AIYVQGLNDN VTLDDLADFF KQCGVVKMNK RTGQPMIHIY LDKETGKPKG DATVSYEDPP 

       430        440        450        460        470        480 
TAKAAVEWFD GKDFQGSKLK VSLARKKPPM NSMRGGMPPR EGRGMPPPLR GGPGGPGGPG 

       490        500        510        520        530        540 
GPMGRMGGRG GDRGGFPPRG PRGSRGNPSG GGNVQHRAGD WQCPNPGCGN QNFAWRTECN 

       550        560        570        580        590        600 
QCKAPKPEGF LPPPFPPPGG DRGRGGPGGM RGGRGGLMDR GGPGGMFRGG RGGDRGGFRG 

       610        620        630        640        650 
GRGMDRGGFG GGRRGGPGGP PGPLMEQMGG RRGGRGGPGK MDKGEHRQER RDRPY

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00742310.
PIRA55726.
RefSeqNP_031994.2. NM_007968.2.
UniGeneMm.142822.

3D structure databases

ProteinModelPortalQ61545.
SMRQ61545. Positions 352-452.
ModBaseSearch...

Protein-protein interaction databases

IntActQ61545. 4 interactions.

PTM databases

PhosphoSiteQ61545.

Proteomic databases

PaxDbQ61545.
PRIDEQ61545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079949; ENSMUSP00000078867; ENSMUSG00000009079.
GeneID14030.
KEGGmmu:14030.

Organism-specific databases

CTD2130.
MGIMGI:99960. Ewsr1.

Phylogenomic databases

eggNOGNOG240581.
GeneTreeENSGT00530000063105.
HOVERGENHBG000970.
KOK13209.
OrthoDBEOG42NJ15.

Gene expression databases

ArrayExpressQ61545.
BgeeQ61545.
CleanExMM_EWSR1.
GenevestigatorQ61545.
GermOnlineENSMUSG00000009079. Mus musculus.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001876. Znf_RanBP2.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
PROSITEPS50096. IQ. False negative.
PS50102. RRM. 1 hit.
PS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284964.
SOURCESearch...

Entry information

Entry nameEWS_MOUSE
AccessionPrimary (citable) accession number: Q61545
Secondary accession number(s): Q9D2P0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents