UniProt Accession

 PABP1_HUMAN; P11940; Q15097; Q93004 

Genbank Protein ID

 Y00345; U68104; U68093; U68094; U68095; U68097; U68098; U68099; U68100; U68101; U68102; U68103; AP001205; BC015958; BC023520; Z48501 

Genbank Nucleotide ID

 CAA68428.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAD08718.1; AAH15958.1; AAH23520.1; CAA88401.1 

Protein Name

 Polyadenylate-binding protein 1 

Protein Synonyms/Alias

 PABP-1; Poly(A)-binding protein 1 

Gene Name

 PABPC1 

Gene Synonyms/Alias

 PAB1; PABP1; PABPC2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
78	TMNFDVIKGKPVRIM	ubiquitination	[1, 2, 3, 4, 5]
80	NFDVIKGKPVRIMWS	ubiquitination	[1, 4, 5]
95	QRDPSLRKSGVGNIF	acetylation	[6]
95	QRDPSLRKSGVGNIF	ubiquitination	[2, 4]
104	GVGNIFIKNLDKSID	acetylation	[7]
104	GVGNIFIKNLDKSID	ubiquitination	[1, 2, 3, 4, 5]
108	IFIKNLDKSIDNKAL	ubiquitination	[1, 2, 4, 5, 8]
113	LDKSIDNKALYDTFS	ubiquitination	[2, 4]
129	FGNILSCKVVCDENG	ubiquitination	[2]
138	VCDENGSKGYGFVHF	ubiquitination	[4]
157	AAERAIEKMNGMLLN	ubiquitination	[1, 2, 3, 4, 5]
167	GMLLNDRKVFVGRFK	ubiquitination	[2, 4]
188	AELGARAKEFTNVYI	acetylation	[6]
188	AELGARAKEFTNVYI	ubiquitination	[1, 2, 3, 4, 5, 9]
196	EFTNVYIKNFGEDMD	ubiquitination	[1, 2, 3, 5]
208	DMDDERLKDLFGKFG	ubiquitination	[1, 4, 5]
213	RLKDLFGKFGPALSV	acetylation	[7]
213	RLKDLFGKFGPALSV	ubiquitination	[1, 2, 3, 4, 5]
229	VMTDESGKSKGFGFV	ubiquitination	[2]
231	TDESGKSKGFGFVSF	ubiquitination	[1, 2, 3, 4, 5]
246	ERHEDAQKAVDEMNG	ubiquitination	[2, 4]
254	AVDEMNGKELNGKQI	ubiquitination	[4]
259	NGKELNGKQIYVGRA	acetylation	[7]
259	NGKELNGKQIYVGRA	ubiquitination	[1, 2, 3, 4, 5]
279	RQTELKRKFEQMKQD	ubiquitination	[1, 2, 4, 5, 8]
284	KRKFEQMKQDRITRY	ubiquitination	[2, 4, 5, 8]
299	QGVNLYVKNLDDGID	acetylation	[6]
299	QGVNLYVKNLDDGID	methylation	[10]
299	QGVNLYVKNLDDGID	ubiquitination	[1, 2, 3, 4, 5]
312	IDDERLRKEFSPFGT	acetylation	[6]
312	IDDERLRKEFSPFGT	ubiquitination	[1, 2, 3, 4, 5, 8, 9]
324	FGTITSAKVMMEGGR	ubiquitination	[4]
333	MMEGGRSKGFGFVCF	ubiquitination	[1, 2, 3, 4, 5]
348	SSPEEATKAVTEMNG	ubiquitination	[2, 4]
361	NGRIVATKPLYVALA	acetylation	[6]
361	NGRIVATKPLYVALA	ubiquitination	[1, 2, 3, 4, 5]
512	VRTVPQYKYAAGVRN	acetylation	[7]
512	VRTVPQYKYAAGVRN	ubiquitination	[1, 2, 3, 4, 5]
606	SPESLRSKVDEAVAV	acetylation	[6]
620	VLQAHQAKEAAQKAV	ubiquitination	[1, 2, 5]
625	QAKEAAQKAVNSATG	ubiquitination	[2, 4]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities.
 Brook M, McCracken L, Reddington JP, Lu ZL, Morrice NA, Gray NK.
 Biochem J. 2012 Feb 1;441(3):803-12. [PMID: 22004688]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] 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]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681] 

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. 

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.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 116 116 Phosphotyrosine (By similarity).
 MOD_RES 299 299 N6-methyllysine.
 MOD_RES 315 315 Phosphoserine.
 MOD_RES 455 455 Omega-N-methylated arginine; by CARM1;
 MOD_RES 460 460 Omega-N-methylated arginine; by CARM1;
 MOD_RES 493 493 Dimethylated arginine; alternate.
 MOD_RES 493 493 Omega-N-methylarginine; alternate.
 MOD_RES 512 512 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; 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:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008143; F:poly(A) RNA binding; TAS:UniProtKB.
 GO:0008494; F:translation activator activity; TAS:UniProtKB.
 GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
 GO:0006378; P:mRNA polyadenylation; TAS:UniProtKB.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
 GO:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
 GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB.
 GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB.
 GO:0006413; P:translational initiation; TAS:Reactome. 

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