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Polyadenylate-binding protein 1
Known also as: Poly(A)-binding protein 1
Known abbreviations: PABP-1, PAB1, PABP, PABP1, PABPC1, PABPC2, PABPL1
Yeast homolog: PAB1
Protein
Structures Models Domains Secondary structure Disorder |
This protein is highly disordered (48 % of residues are predicted to be disordered)
Top 3 models:
 |  |  |
| Template: 2ghp, chain A Method: hhsearch Fragment: 51-372 | Template: 2ghp, chain C Method: phyre Fragment: 2-269 | Template: 1g9l, chain A Method: mgenthreader Fragment: 491-636 |
This protein has alternative isoforms:
Isoform 1:
| Sequence length: | 636 aa |
| Molecular weight: | 70.671 kDa |
| Isoelectric point: | 9.81 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKV
VCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQ
IYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVR
AVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNP
QQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Isoform 2:
| Sequence length: | 547 aa |
| Molecular weight: | 61.181 kDa |
| Isoelectric point: | 9.35 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKV
VCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQ
IYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVR
AVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDE
AVAVLQAHQAKEAAQKAVNSATGVPTV
Gene location: 8q22.2-q23
Summary
Binds the poly(A) tail of mRNA. The protein shuttles between the nucleus and cytoplasm and binds to the 3' poly(A) tail of eukaryotic messenger RNAs via RNA-recognition motifs. The binding of this protein to poly(A) promotes ribosome recruitment and translation initiation; it is also required for poly(A) shortening which is the first step in mRNA decay. 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.
Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2. Interacts with PAPD4/GLD2. Identified in the spliceosome C complex. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with IGF2BP1 and NFX1. Interacts with PIWIL1.
Many viruses shutoff host mRNA translational machinery by inhibiting cellular PABPC1 activity using different mechanisms. Picornaviruses, caliciviruses or lentiviruses encode proteases that cleave PABPC1 at several defined sites in the proline-rich linker region between RRMs and the C-terminal domain. Rotaviruses, gammherpesviruses and bunyamwera virus relocalize PABPC1 from the cytoplasm to the nucleus thus altering its function. Many of these viruses translate their mRNA in a PABPC1-independent manner and are unaffected by host PABPC1 inhibition.
Phosphorylated by MAPKAPK2. Methylated by CARM1.
See this protein in other databases:
Literature:
- Kozlov G, Trempe JF, Khaleghpour K et al. Structure and function of the C-terminal PABC domain of human poly(A)-binding protein. Proc Natl Acad Sci U S A 2001 98(8):4409-13, doi: 10.1073/pnas.071024998, PMID: 11287632.
- Mangus DA, Evans MC, Jacobson A et al. Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol 2003 4(7):223, doi: 10.1186/gb-2003-4-7-223, PMID: 12844354.
- Kuhn U, Wahle E. Structure and function of poly(A) binding proteins. Biochim Biophys Acta 2004 1678(2-3):67-84, doi: 10.1016/j.bbaexp.2004.03.008, PMID: 15157733.
- Gorgoni B, Gray NK. The roles of cytoplasmic poly(A)-binding proteins in regulating gene expression: a developmental perspective. Brief Funct Genomic Proteomic 2004 3(2):125-41, doi: , PMID: 15355595.
- Kozlov G, Menade M, Rosenauer A et al. Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein. J Mol Biol 2010 397(2):397-407, doi: 10.1016/j.jmb.2010.01.032, PMID: 20096703.
- Smith RW, Gray NK. Poly(A)-binding protein (PABP): a common viral target. Biochem J 2010 426(1):1-12, doi: 10.1042/BJ20091571, PMID: 20102337.
- Lemay JF, Lemieux C, St-Andre O et al. Crossing the borders: poly(A)-binding proteins working on both sides of the fence. RNA Biol 2010 7(3):291-5, doi: , PMID: 20400847.
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