EWSR1
entrez
2130
canonical
uniprot
Q01844
canonical
ensembl
ENSG00000182944
resolver
ensp
ENSP00000327456
resolver
ensp
ENSP00000331699
resolver
ensp
ENSP00000381031
resolver
ensp
ENSP00000385726
resolver
ensp
ENSP00000400142
resolver
ensp
ENSP00000412670
resolver
ensp
ENSP00000486709
resolver
ensp
ENSP00000559530
resolver
ensp
ENSP00000559531
resolver
ensp
ENSP00000559533
resolver
ensp
ENSP00000559535
resolver
ensp
ENSP00000559537
resolver
ensp
ENSP00000559538
resolver
ensp
ENSP00000559539
resolver
ensp
ENSP00000559545
resolver
ensp
ENSP00000559548
resolver
ensp
ENSP00000559549
resolver
ensp
ENSP00000559550
resolver
ensp
ENSP00000559552
resolver
ensp
ENSP00000559561
resolver
ensp
ENSP00000559571
resolver
ensp
ENSP00000559573
resolver
ensp
ENSP00000595380
resolver
ensp
ENSP00000595382
resolver
ensp
ENSP00000595385
resolver
ensp
ENSP00000595392
resolver
ensp
ENSP00000630034
resolver
ensp
ENSP00000630039
resolver
ensp
ENSP00000630044
resolver
ensp
ENSP00000630045
resolver
ensp
ENSP00000630049
resolver
enst
ENST00000629659
resolver
genesymbol
EWSR1
resolver
genesymbol_syn
EWS
resolver
hgnc
HGNC:3508
resolver
uniprot
A0A0D9SFL3
resolver
uniprot
B0QYK1
resolver
uniprot
Q5THL0
resolver
uniprot
Q92635
resolver
uniprot
Q96FE8
resolver
uniprot
Q96MN4
resolver
uniprot
Q96MX4
resolver
uniprot
Q9BWA2
resolver
uniprot_entry
A0A0D9SFL3_HUMAN
resolver
uniprot_entry
EWS_HUMAN
resolver
uniprot_sec
B0QYK1
resolver
uniprot_sec
Q5THL0
resolver
uniprot_sec
Q92635
resolver
uniprot_sec
Q96FE8
resolver
uniprot_sec
Q96MN4
resolver
uniprot_sec
Q96MX4
resolver
uniprot_sec
Q9BWA2
resolver
amino_acid_sequence
MASTDYSTYSQAAAQQGYSAYTAQPTQGYAQTTQAYGQQSYGTYGQPTDVSYTQAQTTATYGQTAYATSYGQPPTGYTTPTAPQAYSQPVQGYGTGAYDTTTATVTTTQASYAAQSAYGTQPAYPAYGQQPAATAPTRPQDGNKPTETSQPQSSTGGYNQPSLGYGQSNYSYPQVPGSYPMQPVTAPPSYPPTSYSSTQPTSYDQSSYSQQNTYGQPSSYGQQSSYGQQSSYGQQPPTSYPPQTGSYSQAPSQYSQQSSSYGQQSSFRQDHPSSMGVYGQESGGFSGPGENRSMSGPDNRGRGRGGFDRGGMSRGGRGGGRGGMGSAGERGGFNKPGGPMDEGPDLDLGPPVDPDEDSDNSAIYVQGLNDSVTLDDLADFFKQCGVVKMNKRTGQPMIHIYLDKETGKPKGDATVSYEDPPTAKAAVEWFDGKDFQGSKLKVSLARKKPPMNSMRGGLPPREGRGMPPPLRGGPGGPGGPGGPMGRMGGRGGDRGGFPPRGPRGSRGNPSGGGNVQHRAGDWQCPNPGCGNQNFAWRTECNQCKAPKPEGFLPPPFPPPGGDRGRGGPGGMRGGRGGLMDRGGPGGMFRGGRGGDRGGFRGGRGMDRGGFGGGRRGGPGGPPGPLMEQMGGRRGGRGGPGKMDKGEHRQERRDRPY
uniprot
proteins
disease_involvement
DISEASE: Ewing sarcoma (ES) [MIM:612219]: A 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. {ECO:0000269|PubMed:15044653, ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648, ECO:0000269|PubMed:9121764}. Note=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:15044653, PubMed:1522903). 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). {ECO:0000269|PubMed:15044653, ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:7700648, ECO:0000269|PubMed:9121764}.; DISEASE: Note=A chromosomal aberration involving EWSR1 has been found in extraskeletal myxoid chondrosarcoma. Translocation t(9;22)(q22-31;q11-12) with NR4A3. {ECO:0000269|PubMed:7539287}.; DISEASE: Note=A chromosomal aberration involving EWSR1 is associated with desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with WT1. {ECO:0000269|PubMed:7862627}.; DISEASE: Note=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. {ECO:0000269|PubMed:8401579}.; DISEASE: Note=A chromosomal aberration involving EWSR1 is associated with small round cell sarcoma. Translocation t(11;22)(p36.1;q12) with PATZ1. {ECO:0000269|PubMed:10949935}.; DISEASE: Angiomatoid fibrous histiocytoma (AFH) [MIM:612160]: A 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. {ECO:0000269|PubMed:15884099, ECO:0000269|PubMed:17724745}. Note=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). {ECO:0000269|PubMed:15884099, ECO:0000269|PubMed:17724745}.; DISEASE: Note=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. {ECO:0000305}.
uniprot
proteins
function
FUNCTION: Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Might normally function as a transcriptional repressor (PubMed:10767297). 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. {ECO:0000269|PubMed:10767297, ECO:0000269|PubMed:21256132}.
uniprot
proteins
mass_dalton
68478
uniprot
proteins
mutagenesis
MUTAGEN 648; /note="R->A: Cytoplasmic localization."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 648; /note="R->K: No effect on nuclear targeting."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 651; /note="R->A: No effect on nuclear targeting."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 652; /note="R->A: Cytoplasmic localization."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 652; /note="R->K: No effect on nuclear targeting."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 653; /note="D->A: No effect on nuclear targeting."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 654; /note="R->A: No effect on nuclear targeting."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 655; /note="P->A: Cytoplasmic localization."; /evidence="ECO:0000269|PubMed:16965792"; MUTAGEN 656; /note="Y->A: Cytoplasmic localization."; /evidence="ECO:0000269|PubMed:16965792
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; calmodulin-binding inhibits phosphorylation of Ser-266. {ECO:0000269|PubMed:9341188}.; PTM: Highly methylated on arginine residues. Methylation is mediated by PRMT1 and, at lower level by PRMT8. {ECO:0000269|PubMed:11278906, ECO:0000269|PubMed:18320585, ECO:0000269|Ref.12}.
uniprot
proteins
protein_family
RRM TET family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10767297
uniprot
proteins
pubmed
10949935
uniprot
proteins
pubmed
11278906
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15044653
uniprot
proteins
pubmed
1522903
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15884099
uniprot
proteins
pubmed
16965792
uniprot
proteins
pubmed
17172842
uniprot
proteins
pubmed
17724745
uniprot
proteins
pubmed
18320585
uniprot
proteins
pubmed
18632687
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21256132
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7539287
uniprot
proteins
pubmed
7542907
uniprot
proteins
pubmed
7700648
uniprot
proteins
pubmed
7862627
uniprot
proteins
pubmed
8084618
uniprot
proteins
pubmed
8307570
uniprot
proteins
pubmed
8401579
uniprot
proteins
pubmed
8975699
uniprot
proteins
pubmed
9121764
uniprot
proteins
pubmed
9341188
uniprot
proteins
pubmed
9660765
uniprot
proteins
sequence_length
656
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16965792}. Cytoplasm {ECO:0000269|PubMed:16965792}. Cell membrane {ECO:0000269|PubMed:16965792}. Note=Relocates from cytoplasm to ribosomes upon PTK2B/FAK2 activation.
uniprot
proteins