Tag | Content |
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CPLM ID | CPLM-010892 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | RNA-binding protein EWS |
Protein Synonyms/Alias | EWS oncogene; Ewing sarcoma breakpoint region 1 protein |
Gene Name | EWSR1 |
Gene Synonyms/Alias | EWS |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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351 | YEDPPTAKAAVEWFD | ubiquitination | [1] |
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Reference | [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | Might normally function as a transcriptionnal 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. |
Sequence Annotation | REPEAT 8 16 1. REPEAT 17 27 2. REPEAT 28 34 3. REPEAT 35 42 4. REPEAT 43 50 5. REPEAT 51 59 6. REPEAT 60 68 7. REPEAT 69 75 8. REPEAT 76 84 9. REPEAT 85 91 10. REPEAT 92 110 11. REPEAT 111 116 12. REPEAT 117 125 13. REPEAT 126 156 14. REPEAT 157 163 15. REPEAT 164 170 16. REPEAT 171 177 17. REPEAT 178 188 18. REPEAT 189 193 19. REPEAT 194 201 20. REPEAT 202 206 21. REPEAT 207 212 22. REPEAT 213 218 23. REPEAT 219 224 24. REPEAT 225 230 25. REPEAT 231 238 26. REPEAT 239 245 27. REPEAT 246 252 28. REPEAT 253 259 29. DOMAIN 256 285 IQ. REPEAT 260 276 30. REPEAT 277 285 31. DOMAIN 361 447 RRM. ZN_FING 518 549 RanBP2-type. REGION 1 285 EAD (Gln/Pro/Thr-rich). REGION 8 285 31 X approximate tandem repeats. MOTIF 639 656 Nuclear localization signal. MOD_RES 266 266 Phosphoserine; by PKC (By similarity). MOD_RES 300 300 Asymmetric dimethylarginine. MOD_RES 302 302 Asymmetric dimethylarginine. MOD_RES 304 304 Asymmetric dimethylarginine. MOD_RES 309 309 Asymmetric dimethylarginine. MOD_RES 314 314 Asymmetric dimethylarginine. MOD_RES 317 317 Asymmetric dimethylarginine. MOD_RES 321 321 Asymmetric dimethylarginine. MOD_RES 455 455 Asymmetric dimethylarginine. MOD_RES 464 464 Asymmetric dimethylarginine. MOD_RES 471 471 Asymmetric dimethylarginine; alternate. MOD_RES 471 471 Omega-N-methylarginine; alternate. MOD_RES 490 490 Asymmetric dimethylarginine; by PRMT8. MOD_RES 494 494 Asymmetric dimethylarginine. MOD_RES 500 500 Asymmetric dimethylarginine. MOD_RES 503 503 Asymmetric dimethylarginine. MOD_RES 506 506 Asymmetric dimethylarginine. MOD_RES 563 563 Asymmetric dimethylarginine. MOD_RES 565 565 Asymmetric dimethylarginine. MOD_RES 572 572 Asymmetric dimethylarginine; alternate; MOD_RES 572 572 Omega-N-methylarginine; alternate; by MOD_RES 575 575 Asymmetric dimethylarginine. MOD_RES 581 581 Asymmetric dimethylarginine. MOD_RES 589 589 Asymmetric dimethylarginine. MOD_RES 592 592 Asymmetric dimethylarginine. MOD_RES 596 596 Asymmetric dimethylarginine; alternate; MOD_RES 596 596 Omega-N-methylarginine; alternate; by MOD_RES 600 600 Asymmetric dimethylarginine. MOD_RES 603 603 Asymmetric dimethylarginine; by PRMT8. MOD_RES 607 607 Asymmetric dimethylarginine; alternate; MOD_RES 607 607 Omega-N-methylarginine; alternate; by MOD_RES 615 615 Asymmetric dimethylarginine. MOD_RES 633 633 Asymmetric dimethylarginine. MOD_RES 636 636 Asymmetric dimethylarginine. |
Keyword | 3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane; Chromosomal rearrangement; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Metal-binding; Methylation; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Repressor; RNA-binding; Transcription; Transcription regulation; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 656 AA |
Protein Sequence | MASTDYSTYS QAAAQQGYSA YTAQPTQGYA QTTQAYGQQS YGTYGQPTDV SYTQAQTTAT 60 YGQTAYATSY GQPPTGYTTP TAPQAYSQPV QGYGTGAYDT TTATVTTTQA SYAAQSAYGT 120 QPAYPAYGQQ PAATAPTRPQ DGNKPTETSQ PQSSTGGYNQ PSLGYGQSNY SYPQVPGSYP 180 MQPVTAPPSY PPTSYSSTQP TSYDQSSYSQ QNTYGQPSSY GQQSSYGQQS SYGQQPPTSY 240 PPQTGSYSQA PSQYSQQSSS YGQQSPMDEG PDLDLGPPVD PDEDSDNSAI YVQGLNDSVT 300 LDDLADFFKQ CGVVKMNKRT GQPMIHIYLD KETGKPKGDA TVSYEDPPTA KAAVEWFDGK 360 DFQGSKLKVS LARKKPPMNS MRGGLPPREG RGMPPPLRGG PGGPGGPGGP MGRMGGRGGD 420 RGGFPPRGPR GSRGNPSGGG NVQHRAGDWQ CPNPGCGNQN FAWRTECNQC KAPKPEGFLP 480 PPFPPPGGDR GRGGPGGMRG GRGGLMDRGG PGGMFRGGRG GDRGGFRGGR GMDRGGFGGG 540 RRGGPGGPPG PLMEQMGGRR GGRGGPGKMD KGEHRQERRD RPY 583 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0000166; F:nucleotide binding; IEA:InterPro. GO:0003723; F:RNA binding; TAS:ProtInc. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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