UniProt Accession

 PTBP1_MOUSE; P17225 

Genbank Protein ID

 X52101 

Genbank Nucleotide ID

 CAA36321.1 

Protein Name

 Polypyrimidine tract-binding protein 1 

Protein Synonyms/Alias

 PTB; Heterogeneous nuclear ribonucleoprotein I; hnRNP I 

Gene Name

 Ptbp1 

Gene Synonyms/Alias

 Ptb 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
217	LKIITFTKNNQFQAL	ubiquitination	[1]
258	TLRIDFSKLTSLNVK	ubiquitination	[1, 2]
265	KLTSLNVKYNNDKSR	ubiquitination	[1]
366	YGDVQRVKILFNKKE	acetylation	[3]
478	SSNGGVVKGFKFFQK	acetylation	[3]
478	SSNGGVVKGFKFFQK	ubiquitination	[4]
481	GGVVKGFKFFQKDRK	acetylation	[3]
481	GGVVKGFKFFQKDRK	ubiquitination	[4]

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]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 

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 58 142 RRM 1.
 DOMAIN 183 259 RRM 2.
 DOMAIN 335 386 RRM 3.
 DOMAIN 450 525 RRM 4.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 16 16 Phosphoserine (By similarity).
 MOD_RES 137 137 Phosphothreonine (By similarity).
 MOD_RES 140 140 Phosphoserine (By similarity).
 MOD_RES 430 430 Phosphoserine (By similarity).  

Keyword

 Acetylation; Activator; 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

 527 AA 

Protein Sequence

Gene Ontology

 GO:0005634; C:nucleus; IDA:MGI.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0051148; P:negative regulation of muscle cell differentiation; ISS:UniProtKB.
 GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 

Interpro

 IPR006536; HnRNP-L_PTB.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 

Pfam

  

SMART

 SM00360; RRM 

PROSITE

 PS50102; RRM 

PRINTS