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P11940 (PABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyadenylate-binding protein 1

Short name=PABP-1
Short name=Poly(A)-binding protein 1
Gene names
Name:PABPC1
Synonyms:PAB1, PABP1, PABPC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds 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. Ref.11 Ref.20 Ref.25 Ref.33

Subunit structure

May 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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.28 Ref.31 Ref.32 Ref.33 Ref.36 Ref.38

Subcellular location

Cytoplasm. Nucleus. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus. Ref.8 Ref.9 Ref.23 Ref.24 Ref.33

Tissue specificity

Ubiquitous.

Domain

The 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.

The 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.

Post-translational modification

Phosphorylated by MAPKAPK2. Ref.17

Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine. Ref.6 Ref.7 Ref.14

Miscellaneous

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.

Sequence similarities

Belongs to the polyadenylate-binding protein type-1 family.

Contains 1 PABC domain.

Contains 4 RRM (RNA recognition motif) domains.

Caution

Was termed (Ref.5) polyadenylate binding protein II.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Nonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

gene silencing by RNA

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA polyadenylation

Traceable author statement Ref.1. Source: UniProtKB

mRNA splicing, via spliceosome

Inferred by curator Ref.16. Source: UniProtKB

mRNA stabilization

Traceable author statement Ref.15. Source: UniProtKB

negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from direct assay Ref.25. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of nuclear-transcribed mRNA poly(A) tail shortening

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translation

Traceable author statement Ref.15. Source: GOC

translation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay Ref.16. Source: UniProtKB

cytoplasm

Traceable author statement Ref.9. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay PubMed 21883093. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21940797. Source: MGI

ribonucleoprotein complex

Inferred from direct assay Ref.23. Source: UniProtKB

   Molecular_functionmRNA binding

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

poly(A) binding

Traceable author statement Ref.1. Source: UniProtKB

poly(U) RNA binding

Inferred from direct assay PubMed 21984414. Source: MGI

protein C-terminus binding

Inferred from physical interaction PubMed 15663938. Source: UniProtKB

translation activator activity

Traceable author statement Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11940-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11940-2)

The sequence of this isoform differs from the canonical sequence as follows:
     447-535: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Polyadenylate-binding protein 1
PRO_0000081698

Regions

Domain11 – 8979RRM 1
Domain99 – 17577RRM 2
Domain191 – 26878RRM 3
Domain294 – 37077RRM 4
Domain542 – 61978PABC
Region166 – 289124CSDE1-binding
Compositional bias495 – 5017Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine Ref.27
Modified residue2991N6-methyllysine Ref.7
Modified residue3151Phosphoserine Ref.26 Ref.34
Modified residue4551Omega-N-methylated arginine; by CARM1; partial Probable
Modified residue4601Omega-N-methylated arginine; by CARM1; partial Probable
Modified residue4931Dimethylated arginine; alternate Ref.6 Ref.7
Modified residue4931Omega-N-methylarginine; alternate Ref.6 Ref.7
Modified residue5121N6-acetyllysine Ref.29

Natural variations

Alternative sequence447 – 53589Missing in isoform 2.
VSP_009846

Experimental info

Mutagenesis4551R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460. Ref.14
Mutagenesis4601R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. Ref.14
Sequence conflict211 – 2133Missing in CAA68428. Ref.1
Sequence conflict4101M → I in CAA88401. Ref.5
Sequence conflict4281I → V in CAA68428. Ref.1

Secondary structure

.................................................. 636
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 2EB1B02A346132EE

FASTA63670,671
        10         20         30         40         50         60 
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ 

        70         80         90        100        110        120 
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS 

       130        140        150        160        170        180 
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE 

       190        200        210        220        230        240 
AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER 

       250        260        270        280        290        300 
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN 

       310        320        330        340        350        360 
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT 

       370        380        390        400        410        420 
KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA 

       430        440        450        460        470        480 
AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ 

       490        500        510        520        530        540 
RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ 

       550        560        570        580        590        600 
GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP 

       610        620        630 
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV 

« Hide

Isoform 2 [UniParc].

Checksum: 8088B4F7DFABAFB8
Show »

FASTA54761,181

References

« Hide 'large scale' references
[1]"Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif."
Grange T., de Sa C.M., Oddos J., Pictet R.
Nucleic Acids Res. 15:4771-4787(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The human poly(A)-binding protein (PABP) gene: structural and functional analysis."
Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung and Muscle.
[5]"Nucleotide sequence of a partial cDNA encoding a novel human polyadenylate-binding protein."
Murphy E.P., McKenna N.J., Headon D.R.
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-636 (ISOFORM 2).
[6]Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 158-166; 189-196; 214-221; 232-240; 291-309; 312-324; 357-370; 375-385; 482-506; 566-580 AND 605-620, METHYLATION AT ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[7]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166; 187-208; 214-221; 232-240; 291-324; 334-348; 357-370; 375-385; 482-506; 519-559; 566-620 AND 626-636, METHYLATION AT LYS-299 AND ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity."
Goerlach M., Burd C.G., Dreyfuss G.
Exp. Cell Res. 211:400-407(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[9]"The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm."
Afonina E., Stauber R., Pavlakis G.N.
J. Biol. Chem. 273:13015-13021(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAIP1.
[11]"A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
[12]"Translational repression by a novel partner of human poly(A) binding protein, Paip2."
Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N.
Mol. Cell 7:205-216(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAIP2.
[13]"Dual interactions of the translational repressor Paip2 with poly(A) binding protein."
Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N.
Mol. Cell. Biol. 21:5200-5213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAIP2.
[14]"PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays."
Lee J., Bedford M.T.
EMBO Rep. 3:268-273(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-455 AND ARG-460, MUTAGENESIS OF ARG-455 AND ARG-460.
[15]"Paip1 interacts with poly(A) binding protein through two independent binding motifs."
Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N.
Mol. Cell. Biol. 22:3769-3782(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAIP1.
[16]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[17]"Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization."
Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.
Biochem. Biophys. Res. Commun. 301:665-670(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY MAPKAPK2.
[18]"UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSDE1.
[19]"The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex."
Patel G.P., Ma S., Bag J.
Nucleic Acids Res. 33:7074-7089(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
[20]"IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain."
Patel G.P., Bag J.
FEBS J. 273:5678-5690(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH IGF2BP1, RNA-BINDING.
[21]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[22]"NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFX1.
[23]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
[24]"Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[25]"A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay."
Singh G., Rebbapragada I., Lykke-Andersen J.
PLoS Biol. 6:E111-E111(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH GSPT2.
[26]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[27]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[29]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"Poly(A)-binding protein (PABP): a common viral target."
Smith R.W., Gray N.K.
Biochem. J. 426:1-12(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[31]"The RNA binding protein Larp1 regulates cell division, apoptosis and cell migration."
Burrows C., Abd Latip N., Lam S.J., Carpenter L., Sawicka K., Tzolovsky G., Gabra H., Bushell M., Glover D.M., Willis A.E., Blagden S.P.
Nucleic Acids Res. 38:5542-5553(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LARP1.
[32]"Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1."
Aoyagi M., Gaspar M., Shenk T.E.
Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
[33]"A stimulatory role for the La-related protein 4B in translation."
Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND GNB2L1.
[34]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation."
Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P., Roux P.P.
Genes Dev. 28:357-371(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LARP1.
[37]"Recognition of polyadenylate RNA by the poly(A)-binding protein."
Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.
Cell 98:835-845(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
[38]"Structure and function of the C-terminal PABC domain of human poly(A)-binding protein."
Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.
Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 498-636, INTERACTION WITH GSPT1; PAIP1 AND PAIP2.
[39]"Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with chemical exchange using two overlapping motifs."
Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I., Shimada I.
Submitted (MAY-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 541-623 IN COMPLEX WITH GSPT1.
[40]"Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein."
Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.
J. Mol. Biol. 397:397-407(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 544-626 IN COMPLEX WITH PAIP2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00345 mRNA. Translation: CAA68428.1.
U68104 expand/collapse EMBL AC list , U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA. Translation: AAD08718.1.
AP001205 Genomic DNA. No translation available.
BC015958 mRNA. Translation: AAH15958.1.
BC023520 mRNA. Translation: AAH23520.1.
Z48501 mRNA. Translation: CAA88401.1.
PIRDNHUPA. A93668.
S52491.
RefSeqNP_002559.2. NM_002568.3.
XP_005250918.1. XM_005250861.1.
UniGeneHs.387804.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CVJX-ray2.60A/B/C/D/E/F/G/H1-190[»]
1G9LNMR-A498-636[»]
1JGNNMR-A544-636[»]
1JH4NMR-A544-636[»]
2K8GNMR-A90-182[»]
2RQGNMR-B541-623[»]
2RQHNMR-B541-623[»]
2X04X-ray1.49A/B545-619[»]
3KTPX-ray1.50A544-626[»]
3KTRX-ray1.70A544-626[»]
3KUIX-ray2.30A544-626[»]
3KUJX-ray1.40A544-626[»]
3KURX-ray2.50A/B/C/D/E/F/G/H544-617[»]
3KUSX-ray1.40A/B544-626[»]
3KUTX-ray1.50A/B544-626[»]
3PKNX-ray1.80A544-626[»]
3PTHX-ray1.70A543-621[»]
4F02X-ray2.00A/D1-190[»]
4F25X-ray1.90A99-199[»]
4F26X-ray2.00A99-199[»]
ProteinModelPortalP11940.
SMRP11940. Positions 10-376, 494-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117939. 159 interactions.
DIPDIP-31613N.
IntActP11940. 86 interactions.
MINTMINT-96210.
STRING9606.ENSP00000313007.

Chemistry

BindingDBP11940.
ChEMBLCHEMBL1293286.

PTM databases

PhosphoSiteP11940.

Polymorphism databases

DMDM3183544.

Proteomic databases

PaxDbP11940.
PRIDEP11940.

Protocols and materials databases

DNASU26986.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318607; ENSP00000313007; ENSG00000070756. [P11940-1]
GeneID26986.
KEGGhsa:26986.
UCSCuc003yjs.1. human. [P11940-1]

Organism-specific databases

CTD26986.
GeneCardsGC08M101715.
HGNCHGNC:8554. PABPC1.
HPACAB011536.
HPA045423.
MIM604679. gene.
neXtProtNX_P11940.
PharmGKBPA32880.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000217922.
HOVERGENHBG002295.
InParanoidP11940.
KOK13126.
OMAYPTNQLA.
OrthoDBEOG7RV9FP.
PhylomeDBP11940.
TreeFamTF300458.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP11940.
BgeeP11940.
CleanExHS_PABPC1.
GenevestigatorP11940.

Family and domain databases

Gene3D1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMSSF63570. SSF63570. 1 hit.
TIGRFAMsTIGR01628. PABP-1234. 1 hit.
PROSITEPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPABPC1. human.
EvolutionaryTraceP11940.
GeneWikiPABPC1.
GenomeRNAi26986.
NextBio49454.
PMAP-CutDBP11940.
PROP11940.
SOURCESearch...

Entry information

Entry namePABP1_HUMAN
AccessionPrimary (citable) accession number: P11940
Secondary accession number(s): Q15097, Q93004
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM