CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
351YEDPPTAKAAVEWFDubiquitination[1]
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. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR001876; Znf_RanBP2. 
Pfam
 PF00641; zf-RanBP 
SMART
 SM00360; RRM
 SM00547; ZnF_RBZ 
PROSITE
 PS50096; IQ
 PS50102; RRM
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS