CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001652
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polypyrimidine tract-binding protein 3 
Protein Synonyms/Alias
 Regulator of differentiation 1; Rod1 
Gene Name
 PTBP3 
Gene Synonyms/Alias
 ROD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
98VTNLLMLKGKSQAFLubiquitination[1]
143YSNHRELKTDNLPNQubiquitination[2]
263TLRIDFSKLTSLNVKubiquitination[1]
270KLTSLNVKYNNDKSRubiquitination[1]
455QEDQGLTKDFSNSPLubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U). 
Sequence Annotation
 DOMAIN 59 143 RRM 1.
 DOMAIN 182 258 RRM 2.
 DOMAIN 358 432 RRM 3.
 DOMAIN 475 550 RRM 4.
 MOD_RES 423 423 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Differentiation; Erythrocyte maturation; mRNA processing; mRNA splicing; Reference proteome; Repeat; Repressor; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 552 AA 
Protein Sequence
MDASPSPFSL PKKLNELSAR RGSDELLSSG IINGPFTMNS STPSTANGND SKKFKRDRPP 60
CSPSRVLHLR KIPCDVTEAE IISLGLPFGK VTNLLMLKGK SQAFLEMASE EAAVTMVNYY 120
TPITPHLRSQ PVYIQYSNHR ELKTDNLPNQ ARAQAALQAV SAVQSGSLAL SGGPSNEGTV 180
LPGQSPVLRI IIENLFYPVT LEVLHQIFSK FGTVLKIITF TKNNQFQALL QYADPVNAHY 240
AKMALDGQNI YNACCTLRID FSKLTSLNVK YNNDKSRDFT RLDLPTGDGQ PSLEPPMAAA 300
FGAPGIISSP YAGAAGFAPA IGFPQATGLS VPAVPGALGP LTITSSAVTG RMAIPGASGI 360
PGNSVLLVTN LNPDLITPHG LFILFGVYGD VHRVKIMFNK KENALVQMAD ANQAQLAMNH 420
LSGQRLYGKV LRATLSKHQA VQLPREGQED QGLTKDFSNS PLHRFKKPGS KNFQNIFPPS 480
ATLHLSNIPP SVTVDDLKNL FIEAGCSVKA FKFFQKDRKM ALIQLGSVEE AIQALIELHN 540
HDLGENHHLR VSFSKSTI 558 
Gene Ontology
 GO:0005634; C:nucleus; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0033119; P:negative regulation of RNA splicing; IDA:UniProtKB.
 GO:0045595; P:regulation of cell differentiation; IEA:Compara.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
Interpro
 IPR006536; HnRNP-L_PTB.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS