UniProt Accession

 PABP1_MOUSE; P29341; Q99L36 

Genbank Protein ID

 X65553; AK044829; AK133196; AK159703; AK159733; AK160968; AK161123; AK161671; AK168466; CH466541; BC003870; BC011207; BC023145; BC046233 

Genbank Nucleotide ID

 CAA46522.1; BAC32110.1; BAE21553.1; BAE35302.1; BAE35327.1; BAE36120.1; BAE36203.1; BAE36522.1; BAE40360.1; EDL08818.1; AAH03870.1; AAH11207.1; AAH23145.1; AAH46233.1 

Protein Name

 Polyadenylate-binding protein 1 

Protein Synonyms/Alias

 PABP-1; Poly(A)-binding protein 1 

Gene Name

 Pabpc1 

Gene Synonyms/Alias

 Pabp1 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
78	TMNFDVIKGKPVRIM	acetylation	[1]
78	TMNFDVIKGKPVRIM	ubiquitination	[2]
80	NFDVIKGKPVRIMWS	acetylation	[1]
95	QRDPSLRKSGVGNIF	ubiquitination	[2]
104	GVGNIFIKNLDKSID	acetylation	[3, 4]
104	GVGNIFIKNLDKSID	ubiquitination	[2]
108	IFIKNLDKSIDNKAL	ubiquitination	[2]
138	VCDENGSKGYGFVHF	ubiquitination	[2]
157	AAERAIEKMNGMLLN	ubiquitination	[2]
188	AELGARAKEFTNVYI	ubiquitination	[2]
196	EFTNVYIKNFGEDMD	ubiquitination	[2]
213	RLKELFGKFGPALSV	acetylation	[5]
213	RLKELFGKFGPALSV	ubiquitination	[2]
231	TDESGKSKGFGFVSF	ubiquitination	[2]
259	NGKELNGKQIYVGRA	ubiquitination	[2]
284	KRKFEQMKQDRITRY	ubiquitination	[2]
299	QGVNLYVKNLDDGID	acetylation	[4]
299	QGVNLYVKNLDDGID	ubiquitination	[2]
312	IDDERLRKEFSPFGT	ubiquitination	[2]
333	MMEGGRSKGFGFVCF	ubiquitination	[2]
348	SSPEEATKAVTEMNG	ubiquitination	[2]
361	NGRIVATKPLYVALA	acetylation	[3, 5]
361	NGRIVATKPLYVALA	succinylation	[5]
361	NGRIVATKPLYVALA	ubiquitination	[2]
512	VRTVPQYKYAAGVRN	acetylation	[5]
512	VRTVPQYKYAAGVRN	ubiquitination	[2]
620	VLQAHQAKEAAQKAV	ubiquitination	[2]

Reference

 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] 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]
 [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 investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 

Functional Description

 Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre- mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (By similarity). 

Sequence Annotation

 DOMAIN 11 89 RRM 1.
 DOMAIN 99 175 RRM 2.
 DOMAIN 191 268 RRM 3.
 DOMAIN 294 370 RRM 4.
 DOMAIN 542 619 PABC.
 REGION 166 289 CSDE1-binding (By similarity).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 116 116 Phosphotyrosine.
 MOD_RES 299 299 N6-methyllysine (By similarity).
 MOD_RES 315 315 Phosphoserine (By similarity).
 MOD_RES 455 455 Omega-N-methylated arginine; by CARM1 (By
 MOD_RES 460 460 Omega-N-methylated arginine; by CARM1 (By
 MOD_RES 493 493 Dimethylated arginine; alternate (By
 MOD_RES 493 493 Omega-N-methylarginine; alternate (By
 MOD_RES 512 512 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Methylation; mRNA processing; mRNA splicing; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spliceosome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 636 AA 

Protein Sequence

Gene Ontology

 GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008143; F:poly(A) RNA binding; ISS:UniProtKB.
 GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
 GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
 GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 

Interpro

 IPR012677; Nucleotide-bd_a/b_plait.
 IPR006515; PABP_1234.
 IPR002004; PABP_HYD.
 IPR000504; RRM_dom. 

Pfam

 PF00658; PABP
 PF00076; RRM_1 

SMART

 SM00517; PolyA
 SM00360; RRM 

PROSITE

 PS51309; PABC
 PS50102; RRM 

PRINTS