MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP004895

UniProt Annotations

Entry Information
Gene Namepoly(A) binding protein, cytoplasmic 1
Protein EntryPABP1_HUMAN
UniProt IDP11940
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P11940-1; Sequence=Displayed; Name=2; IsoId=P11940-2; Sequence=VSP_009846; Note=No experimental confirmation available.;
CautionWas termed (Ref.5) polyadenylate binding protein II. {ECO:0000305}.
DomainThe RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact with the PABPC1- interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
DomainThe RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1- interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.
FunctionBinds the poly(A) tail of mRNA, including that of its own transcript. 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. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:20573744}.
InteractionQ99700:ATXN2; NbExp=6; IntAct=EBI-81531, EBI-697691; O00571:DDX3X; NbExp=10; IntAct=EBI-81531, EBI-353779; Q04637:EIF4G1; NbExp=2; IntAct=EBI-81531, EBI-73711; P15170-2:GSPT1; NbExp=2; IntAct=EBI-81531, EBI-9094806; Q8IYD1:GSPT2; NbExp=7; IntAct=EBI-81531, EBI-3869637; Q14103-4:HNRNPD; NbExp=2; IntAct=EBI-81531, EBI-432545; P35568:IRS1; NbExp=2; IntAct=EBI-81531, EBI-517592; Q9H074:PAIP1; NbExp=10; IntAct=EBI-81531, EBI-81519; Q9BPZ3:PAIP2; NbExp=5; IntAct=EBI-81531, EBI-2957445; Q58A45:PAN3; NbExp=4; IntAct=EBI-81531, EBI-2513054; Q96Q15:SMG1; NbExp=2; IntAct=EBI-81531, EBI-1049832; Q9UPQ9:TNRC6B; NbExp=3; IntAct=EBI-81531, EBI-947158; Q9HCJ0:TNRC6C; NbExp=17; IntAct=EBI-81531, EBI-6507625; P50616:TOB1; NbExp=4; IntAct=EBI-81531, EBI-723281; Q14106:TOB2; NbExp=4; IntAct=EBI-81531, EBI-2562000;
MiscellaneousMany 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.
PtmMethylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000269|PubMed:11850402, ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
PtmPhosphorylated by MAPKAPK2. {ECO:0000269|PubMed:12565831, ECO:0000269|PubMed:18669648, ECO:0000269|PubMed:20068231}.
SimilarityBelongs to the polyadenylate-binding protein type-1 family. {ECO:0000305}.
SimilarityContains 1 PABC domain. {ECO:0000255|PROSITE- ProRule:PRU00641}.
SimilarityContains 4 RRM (RNA recognition motif) domains. {ECO:0000255|PROSITE-ProRule:PRU00176}.
Subcellular LocationCytoplasm. Nucleus. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus.
SubunitMay form homodimers. Component of a multisubunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Directly 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 IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1. Interacts with PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with LARP1 and LARP4B. {ECO:0000269|PubMed:11051545, ECO:0000269|PubMed:11172725, ECO:0000269|PubMed:11287632, ECO:0000269|PubMed:11438674, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:11997512, ECO:0000269|PubMed:15314026, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:17212783, ECO:0000269|PubMed:17267499, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17932509, ECO:0000269|PubMed:18447585, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:20096703, ECO:0000269|PubMed:20133758, ECO:0000269|PubMed:20430826, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:24532714, ECO:0000269|PubMed:9548260, ECO:0000269|Ref.39}.
Tissue SpecificityUbiquitous.
  logo