Skip Header

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

UniProtKB - Q01844 (EWS_HUMAN)

Entry version 221 (16 Oct 2019)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

RNA-binding protein EWS

Gene

EWSR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Might normally function as a transcriptional 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)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei348 – 349Breakpoint for insertion to form EWSR1-FEV fusion protein2

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri518 – 549RanBP2-typePROSITE-ProRule annotationAdd BLAST32

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Repressor, RNA-binding
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q01844

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RNA-binding protein EWS
Alternative name(s):
EWS oncogene
Ewing sarcoma breakpoint region 1 protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EWSR1
Synonyms:EWS
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3508 EWSR1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		133450 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q01844

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Ewing sarcoma (ES)4 Publications
The protein represented in this entry is involved in disease pathogenesis. Chromosomal aberrations involving EWSR1 are found in patients with Ewing sarcoma. Translocation t(11;22)(q24;q12) with FLI1 (PubMed:1522903, PubMed:15044653). Translocation t(7;22)(p22;q12) with ETV1 (PubMed:7700648). Translocation t(21;22)(q22;q21) with ERG (PubMed:15044653). Translocation t(2;21;22)(q23;q22;q12) that forms a EWSR1-FEV fusion protein with potential oncogenic activity (PubMed:9121764).4 Publications
Disease descriptionA 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.
Related information in OMIM
A chromosomal aberration involving EWSR1 has been found in extraskeletal myxoid chondrosarcoma. Translocation t(9;22)(q22-31;q11-12) with NR4A3.1 Publication
A chromosomal aberration involving EWSR1 is associated with desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with WT1.1 Publication
A chromosomal aberration involving EWSR1 is associated with malignant melanoma of soft parts (MMSP). Translocation t(12;22)(q13;q12) with ATF1. Malignant melanoma of soft parts, also known as soft tissue clear cell sarcoma, is a rare tumor developing in tendons and aponeuroses.1 Publication
A chromosomal aberration involving EWSR1 is associated with small round cell sarcoma. Translocation t(11;22)(p36.1;q12) with PATZ1.1 Publication
Angiomatoid fibrous histiocytoma (AFH)2 Publications
The gene represented in this entry is involved in disease pathogenesis. 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 (PubMed:15884099). Translocation t(2;22)(q33;q12) with CREB1 generates a EWSR1/CREB1 fusion gene that is most common genetic abnormality in this tumor type (PubMed:17724745).2 Publications
Disease descriptionA 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.
Related information in OMIM
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.Curated

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi648R → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi648R → K: No effect on nuclear targeting. 1 Publication1
Mutagenesisi651R → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi652R → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi652R → K: No effect on nuclear targeting. 1 Publication1
Mutagenesisi653D → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi654R → A: No effect on nuclear targeting. 1 Publication1
Mutagenesisi655P → A: Cytoplasmic localization. 1 Publication1
Mutagenesisi656Y → A: Cytoplasmic localization. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei265Breakpoint for translocation to form chimeric EWSR1/ATF1 protein1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		2130

MalaCards human disease database

More...MalaCardsi		EWSR1
MIMi612160 phenotype
612219 phenotype

Open Targets

More...OpenTargetsi		ENSG00000182944

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		83469 Desmoplastic small round cell tumor
319 Ewing sarcoma
370334 Extraskeletal Ewing sarcoma
209916 Extraskeletal myxoid chondrosarcoma
97338 Melanoma of soft tissue

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27921

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q01844

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		EWSR1

Domain mapping of disease mutations (DMDM)

More...DMDMi		544261

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000815861 – 656RNA-binding protein EWSAdd BLAST656

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei266Phosphoserine; by PKCBy similarity1
Modified residuei300Asymmetric dimethylarginine1 Publication1
Modified residuei302Asymmetric dimethylarginine1 Publication1
Modified residuei304Asymmetric dimethylarginine1 Publication1
Modified residuei309Asymmetric dimethylarginine1 Publication1
Modified residuei314Asymmetric dimethylarginine1 Publication1
Modified residuei317Asymmetric dimethylarginine1 Publication1
Modified residuei321Asymmetric dimethylarginine1 Publication1
Modified residuei439N6-acetyllysineBy similarity1
Modified residuei455Asymmetric dimethylarginine1 Publication1
Modified residuei464Asymmetric dimethylarginine1 Publication1
Modified residuei471Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei471Omega-N-methylarginine; alternateCombined sources1 Publication1
Modified residuei486Omega-N-methylarginineCombined sources1
Modified residuei490Asymmetric dimethylarginine; by PRMT82 Publications1
Modified residuei494Asymmetric dimethylarginine2 Publications1
Modified residuei500Asymmetric dimethylarginine1 Publication1
Modified residuei503Asymmetric dimethylarginine1 Publication1
Modified residuei506Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei506Omega-N-methylarginine; alternateBy similarity1
Modified residuei563Asymmetric dimethylarginine1 Publication1
Modified residuei565Asymmetric dimethylarginine1 Publication1
Modified residuei572Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei572Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei575Asymmetric dimethylarginine1 Publication1
Modified residuei581Asymmetric dimethylarginine1 Publication1
Modified residuei589Asymmetric dimethylarginine1 Publication1
Modified residuei592Asymmetric dimethylarginine1 Publication1
Modified residuei596Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei596Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei600Asymmetric dimethylarginine1 Publication1
Modified residuei603Asymmetric dimethylarginine; by PRMT82 Publications1
Modified residuei607Asymmetric dimethylarginine; alternate; by PRMT82 Publications1
Modified residuei607Omega-N-methylarginine; alternate; by PRMT82 Publications1
Modified residuei615Asymmetric dimethylarginine; alternate2 Publications1
Modified residuei615Omega-N-methylarginine; alternateCombined sources1
Modified residuei633Asymmetric dimethylarginine1 Publication1
Modified residuei636Asymmetric dimethylarginine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		Q01844

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q01844

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q01844

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q01844

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q01844

PeptideAtlas

More...PeptideAtlasi		Q01844

PRoteomics IDEntifications database

More...PRIDEi		Q01844

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		2658
58004 [Q01844-1]
58005 [Q01844-2]
58006 [Q01844-3]
58007 [Q01844-4]
58008 [Q01844-5]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q01844

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q01844

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q01844

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000182944 Expressed in 234 organ(s), highest expression level in testis

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q01844 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q01844 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB004230
HPA051771
HPA062953

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Forms a complex with REC8, PRDM9, SYCP3 and SYCP1; complex formation is dependent of phosphorylated form of REC8 and requires PRDM9 bound to hotspot DNA; EWSR1 joins PRDM9 with the chromosomal axis through REC8 (By similarity).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108431, 686 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q01844

Database of interacting proteins

More...DIPi		DIP-34449N

Protein interaction database and analysis system

More...IntActi		Q01844, 170 interactors

Molecular INTeraction database

More...MINTi		Q01844

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000400142

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1656
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q01844

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q01844

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini256 – 285IQAdd BLAST30
Repeati260 – 27630Add BLAST17
Repeati277 – 285319
Domaini361 – 447RRMPROSITE-ProRule annotationAdd BLAST87

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 285EAD (Gln/Pro/Thr-rich)Add BLAST285
Regioni8 – 28531 X approximate tandem repeatsAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi639 – 656Nuclear localization signal1 PublicationAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi300 – 340Arg/Gly/Pro-richAdd BLAST41
Compositional biasi454 – 513Arg/Gly/Pro-richAdd BLAST60
Compositional biasi559 – 640Arg/Gly/Pro-richAdd BLAST82

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RRM TET family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri518 – 549RanBP2-typePROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1995 Eukaryota
ENOG4111Q2F LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154191

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000038010

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q01844

KEGG Orthology (KO)

More...KOi		K13209

Identification of Orthologs from Complete Genome Data

More...OMAi		DMRDHRQ

Database of Orthologous Groups

More...OrthoDBi		1568974at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q01844

TreeFam database of animal gene trees

More...TreeFami		TF322599

Family and domain databases

Conserved Domains Database

More...CDDi		cd12533 RRM_EWS, 1 hit

Database of protein disorder

More...DisProti		DP00632

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.70.330, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034869 EWS_RRM
IPR033109 EWSR1
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR034870 TET_fam
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf

The PANTHER Classification System

More...PANTHERi		PTHR23238 PTHR23238, 1 hit
PTHR23238:SF3 PTHR23238:SF3, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00076 RRM_1, 1 hit
PF00641 zf-RanBP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00360 RRM, 1 hit
SM00547 ZnF_RBZ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54928 SSF54928, 1 hit
SSF90209 SSF90209, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50102 RRM, 1 hit
PS01358 ZF_RANBP2_1, 1 hit
PS50199 ZF_RANBP2_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform EWS (identifier: Q01844-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV 
        60         70         80         90        100
SYTQAQTTAT YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT 
       110        120        130        140        150
TTATVTTTQA SYAAQSAYGT QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ 
       160        170        180        190        200
PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP MQPVTAPPSY PPTSYSSTQP 
       210        220        230        240        250
TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY PPQTGSYSQA 
       260        270        280        290        300
PSQYSQQSSS YGQQSSFRQD HPSSMGVYGQ ESGGFSGPGE NRSMSGPDNR 
       310        320        330        340        350
GRGRGGFDRG GMSRGGRGGG RGGMGSAGER GGFNKPGGPM DEGPDLDLGP 
       360        370        380        390        400
PVDPDEDSDN SAIYVQGLND SVTLDDLADF FKQCGVVKMN KRTGQPMIHI 
       410        420        430        440        450
YLDKETGKPK GDATVSYEDP PTAKAAVEWF DGKDFQGSKL KVSLARKKPP 
       460        470        480        490        500
MNSMRGGLPP REGRGMPPPL RGGPGGPGGP GGPMGRMGGR GGDRGGFPPR 
       510        520        530        540        550
GPRGSRGNPS GGGNVQHRAG DWQCPNPGCG NQNFAWRTEC NQCKAPKPEG 
       560        570        580        590        600
FLPPPFPPPG GDRGRGGPGG MRGGRGGLMD RGGPGGMFRG GRGGDRGGFR 
       610        620        630        640        650
GGRGMDRGGF GGGRRGGPGG PPGPLMEQMG GRRGGRGGPG KMDKGEHRQE 

RRDRPY
Length:656
Mass (Da):68,478
Last modified:June 1, 1994 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B0QYK0B0QYK0_HUMAN
RNA-binding protein EWS
EWSR1
618Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9JGE3C9JGE3_HUMAN
EWS RNA-binding protein variant 6
EWSR1
620Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0D9SFL3A0A0D9SFL3_HUMAN
RNA-binding protein EWS
EWSR1
584Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7BY36H7BY36_HUMAN
RNA-binding protein EWS
EWSR1
308Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYJ7B0QYJ7_HUMAN
RNA-binding protein EWS
EWSR1
233Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WC90F8WC90_HUMAN
RNA-binding protein EWS
EWSR1
292Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYJ3B0QYJ3_HUMAN
RNA-binding protein EWS
EWSR1
156Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYJ4B0QYJ4_HUMAN
RNA-binding protein EWS
EWSR1
166Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYJ6B0QYJ6_HUMAN
RNA-binding protein EWS
EWSR1
180Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QYJ5B0QYJ5_HUMAN
RNA-binding protein EWS
EWSR1
77Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA70044 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti224S → G in BAB71252 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04345174P → PTVEGTS in isoform 5. 1 Publication1
Alternative sequenceiVSP_045412136 – 191Missing in isoform 6. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_005793266 – 338Missing in isoform EWS-B. CuratedAdd BLAST73
Alternative sequenceiVSP_043452326 – 354SAGER…PPVDP → LQSESLVYTSILKKYPYSVL SRQHNEKWD in isoform 4. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_043453326Missing in isoform 3 and isoform 5. 3 Publications1
Alternative sequenceiVSP_043454355 – 656Missing in isoform 4. 1 PublicationAdd BLAST302

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13851.1 [Q01844-1]
CCDS13852.2 [Q01844-5]
CCDS54512.1 [Q01844-4]
CCDS54513.1 [Q01844-3]
CCDS54514.1 [Q01844-6]

Protein sequence database of the Protein Information Resource

More...PIRi		A49358

NCBI Reference Sequences

More...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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...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]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2130

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2130

UCSC genome browser

More...UCSCi		uc003aes.5 human [Q01844-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CPENMR-A353-453[»]
SMRiQ01844
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi108431, 686 interactors
CORUMiQ01844
DIPiDIP-34449N
IntActiQ01844, 170 interactors
MINTiQ01844
STRINGi9606.ENSP00000400142

PTM databases

iPTMnetiQ01844
PhosphoSitePlusiQ01844
SwissPalmiQ01844

Polymorphism and mutation databases

BioMutaiEWSR1
DMDMi544261

Proteomic databases

EPDiQ01844
jPOSTiQ01844
MassIVEiQ01844
MaxQBiQ01844
PaxDbiQ01844
PeptideAtlasiQ01844
PRIDEiQ01844
ProteomicsDBi2658
58004 [Q01844-1]
58005 [Q01844-2]
58006 [Q01844-3]
58007 [Q01844-4]
58008 [Q01844-5]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2130

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.5 human [Q01844-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2130
DisGeNETi2130

GeneCards: human genes, protein and diseases

More...GeneCardsi		EWSR1
HGNCiHGNC:3508 EWSR1
HPAiCAB004230
HPA051771
HPA062953
MalaCardsiEWSR1
MIMi133450 gene
612160 phenotype
612219 phenotype
neXtProtiNX_Q01844
OpenTargetsiENSG00000182944
Orphaneti83469 Desmoplastic small round cell tumor
319 Ewing sarcoma
370334 Extraskeletal Ewing sarcoma
209916 Extraskeletal myxoid chondrosarcoma
97338 Melanoma of soft tissue
PharmGKBiPA27921

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1995 Eukaryota
ENOG4111Q2F LUCA
GeneTreeiENSGT00940000154191
HOGENOMiHOG000038010
InParanoidiQ01844
KOiK13209
OMAiDMRDHRQ
OrthoDBi1568974at2759
PhylomeDBiQ01844
TreeFamiTF322599

Enzyme and pathway databases

SIGNORiQ01844

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		EWSR1 human
EvolutionaryTraceiQ01844

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Ewing_sarcoma_breakpoint_region_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2130
PharosiQ01844

Protein Ontology

More...PROi		PR:Q01844

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000182944 Expressed in 234 organ(s), highest expression level in testis
ExpressionAtlasiQ01844 baseline and differential
GenevisibleiQ01844 HS

Family and domain databases

CDDicd12533 RRM_EWS, 1 hit
DisProtiDP00632
Gene3Di3.30.70.330, 1 hit
InterProiView protein in InterPro
IPR034869 EWS_RRM
IPR033109 EWSR1
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR034870 TET_fam
IPR001876 Znf_RanBP2
IPR036443 Znf_RanBP2_sf
PANTHERiPTHR23238 PTHR23238, 1 hit
PTHR23238:SF3 PTHR23238:SF3, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 1 hit
PF00641 zf-RanBP, 1 hit
SMARTiView protein in SMART
SM00360 RRM, 1 hit
SM00547 ZnF_RBZ, 1 hit
SUPFAMiSSF54928 SSF54928, 1 hit
SSF90209 SSF90209, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 1 hit
PS01358 ZF_RANBP2_1, 1 hit
PS50199 ZF_RANBP2_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEWS_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01844
Secondary accession number(s): B0QYK1
, Q5THL0, Q92635, Q96FE8, Q96MN4, Q96MX4, Q9BWA2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 16, 2019
This is version 221 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again