CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005518
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Polypyrimidine tract-binding protein 1 
Protein Synonyms/Alias
 PTB; 57 kDa RNA-binding protein PPTB-1; Heterogeneous nuclear ribonucleoprotein I; hnRNP I 
Gene Name
 PTBP1 
Gene Synonyms/Alias
 PTB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
65SRVIHIRKLPIDVTEubiquitination[1]
259TLRIDFSKLTSLNVKubiquitination[1]
266KLTSLNVKYNNDKSRubiquitination[1]
429PIRITLSKHQNVQLPubiquitination[1]
501SSNGGVVKGFKFFQKubiquitination[1]
547HLRVSFSKSTI****ubiquitination[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
 Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. 
Sequence Annotation
 DOMAIN 59 143 RRM 1.
 DOMAIN 184 260 RRM 2.
 DOMAIN 337 411 RRM 3.
 DOMAIN 454 529 RRM 4.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 138 138 Phosphothreonine.
 MOD_RES 141 141 Phosphoserine.
 MOD_RES 433 433 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Complete proteome; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 531 AA 
Protein Sequence
MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV 60
IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV 120
LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ 180
SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS 240
LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFASP 300
YAGAGFPPTF AIPQAAGLSV PNVHGALAPL AIPSAAAAAA AAGRIAIPGL AGAGNSVLLV 360
SNLNPERVTP QSLFILFGVY GDVQRVKILF NKKENALVQM ADGNQAQLAM SHLNGHKLHG 420
KPIRITLSKH QNVQLPREGQ EDQGLTKDYG NSPLHRFKKP GSKNFQNIFP PSATLHLSNI 480
PPSVSEEDLK VLFSSNGGVV KGFKFFQKDR KMALIQMGSV EEAVQALIDL HNHDLGENHH 540
LRVSFSKSTI 550 
Gene Ontology
 GO:0005730; C:nucleolus; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008187; F:poly-pyrimidine tract binding; TAS:ProtInc.
 GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
 GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
 GO:0051148; P:negative regulation of muscle cell differentiation; IDA:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. 
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