UniProt Accession

 PTBP1_HUMAN; P26599; Q9BUQ0 

Genbank Protein ID

 X62006; X65371; X65372; X60648; X66975; BT006819; AC006273; CH471242; BC002397; BC004383; BC013694 

Genbank Nucleotide ID

 CAA43973.1; CAA46443.1; CAA46444.1; CAA43056.1; CAA47386.1; AAP35465.1; AAC99798.1; EAW61154.1; AAH02397.1; AAH04383.1; AAH13694.1 

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
13	PDIAVGTKRGSDELF	ubiquitination	[1, 2]
65	SRVIHIRKLPIDVTE	ubiquitination	[3, 4]
92	VTNLLMLKGKNQAFI	ubiquitination	[4]
94	NLLMLKGKNQAFIEM	ubiquitination	[3]
134	YIQFSNHKELKTDSS	ubiquitination	[5]
218	LKIITFTKNNQFQAL	ubiquitination	[3, 5]
259	TLRIDFSKLTSLNVK	ubiquitination	[3, 6]
266	KLTSLNVKYNNDKSR	ubiquitination	[3]
368	YGDVQRVKILFNKKE	ubiquitination	[5]
410	PIRITLSKHQNVQLP	ubiquitination	[4, 5]
428	QEDQGLTKDYGNSPL	ubiquitination	[4, 5]
482	SSNGGVVKGFKFFQK	ubiquitination	[2, 3, 4, 5]
485	GGVVKGFKFFQKDRK	ubiquitination	[5]
528	HLRVSFSKSTI****	ubiquitination	[2, 3, 6]

Reference

 [1] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] 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]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

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

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