UniProt Accession

 PABP_YEAST; P04147; D3DM73 

Genbank Protein ID

 M12780; M13371; D00023; U18922; AY692854; BK006939 

Genbank Nucleotide ID

 AAA34838.1; AAA34787.1; BAA00017.1; AAB64692.1; AAT92873.1; DAA07827.1 

Protein Name

 Polyadenylate-binding protein, cytoplasmic and nuclear 

Protein Synonyms/Alias

 PABP; Poly(A)-binding protein; ARS consensus-binding protein ACBP-67; Polyadenylate tail-binding protein 

Gene Name

 PAB1 

Gene Synonyms/Alias

 YER165W 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
7	*MADITDKTAEQLEN	acetylation	[1]
7	*MADITDKTAEQLEN	ubiquitination	[2]
76	VCRDAITKTSLGYAY	ubiquitination	[3]
94	NDHEAGRKAIEQLNY	acetylation	[4]
94	NDHEAGRKAIEQLNY	ubiquitination	[3]
105	QLNYTPIKGRLCRIM	acetylation	[4]
105	QLNYTPIKGRLCRIM	ubiquitination	[3]
131	GSGNIFIKNLHPDID	acetylation	[4]
164	IATDENGKSKGFGFV	ubiquitination	[3]
252	IVSASLEKDADGKLK	ubiquitination	[3]
259	KDADGKLKGFGFVNY	acetylation	[4]
268	FGFVNYEKHEDAVKA	acetylation	[4]
274	EKHEDAVKAVEALND	acetylation	[4]
288	DSELNGEKLYVGRAQ	acetylation	[4]
288	DSELNGEKLYVGRAQ	ubiquitination	[3]
306	ERMHVLKKQYEAYRL	ubiquitination	[3]
318	YRLEKMAKYQGVNLF	acetylation	[4]
318	YRLEKMAKYQGVNLF	ubiquitination	[3]
337	DDSVDDEKLEEEFAP	ubiquitination	[2, 3]
382	ATKAITEKNQQIVAG	acetylation	[4]
390	NQQIVAGKPLYVAIA	acetylation	[4]
469	NPMGGMPKNGMPPQF	ubiquitination	[3]
504	NNQFYQQKQRQALGE	acetylation	[4]
504	NNQFYQQKQRQALGE	ubiquitination	[3]
515	ALGEQLYKKVSAKTS	acetylation	[4]
520	LYKKVSAKTSNEEAA	ubiquitination	[3]
568	AAYESFKKEQEQQTE	ubiquitination	[3]

Reference

 [1] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 

Functional Description

 Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA. 

Sequence Annotation

 DOMAIN 38 116 RRM 1.
 DOMAIN 126 203 RRM 2.
 DOMAIN 219 296 RRM 3.
 DOMAIN 322 399 RRM 4.
 DOMAIN 489 568 PABC.
 REGION 9 61 Required and sufficient for nuclear
 REGION 281 317 Required and sufficient for nuclear
 REGION 473 577 Interaction with SUP35.
 MOTIF 12 17 Nuclear export signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 332 332 Phosphoserine.
 MOD_RES 405 405 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; mRNA processing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Translation regulation; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 577 AA 

Protein Sequence

Gene Ontology

 GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005840; C:ribosome; IDA:SGD.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0008143; F:poly(A) RNA binding; IMP:SGD.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0060211; P:regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:SGD.
 GO:0006446; P:regulation of translational initiation; IMP:SGD. 

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