CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001651
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
16ANGNDSKKFKRDRPPubiquitination[1]
34SRVLHLRKIPCDVTEubiquitination[1]
106YSNHRELKTDNLPNQubiquitination[1]
392SGQRLYGKVLRATLSubiquitination[1]
418QEDQGLTKDFSNSPLubiquitination[1, 2]
434RFKKPGSKNFQNIFPubiquitination[1]
472IEAGCSVKAFKFFQKubiquitination[1]
475GCSVKAFKFFQKDRKubiquitination[1]
479KAFKFFQKDRKMALIubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] 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
 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
MNSSTPSTAN GNDSKKFKRD RPPCSPSRVL HLRKIPCDVT EAEIISLGLP FGKVTNLLML 60
KGKSQAFLEM ASEEAAVTMV NYYTPITPHL RSQPVYIQYS NHRELKTDNL PNQARAQAAL 120
QAVSAVQSGS LALSGGPSNE GTVLPGQSPV LRIIIENLFY PVTLEVLHQI FSKFGTVLKI 180
ITFTKNNQFQ ALLQYADPVN AHYAKMALDG QNIYNACCTL RIDFSKLTSL NVKYNNDKSR 240
DFTRLDLPTG DGQPSLEPPM AAAFGAPGII SSPYAGAAGF APAIGFPQAT GLSVPAVPGA 300
LGPLTITSSA VTGRMAIPGA SGIPGNSVLL VTNLNPDLIT PHGLFILFGV YGDVHRVKIM 360
FNKKENALVQ MADANQAQLA MNHLSGQRLY GKVLRATLSK HQAVQLPREG QEDQGLTKDF 420
SNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSVTVDDL KNLFIEAGCS VKAFKFFQKD 480
RKMALIQLGS VEEAIQALIE LHNHDLGENH HLRVSFSKST I 521 
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