F1QB54 · PABPA_DANRE

Function

function

Binds the poly(A) tail of mRNA (By similarity).
Prevents mRNA deadenylation and confers poly(A) stability (By similarity).
Binds to N6-methyladenosine (m6A)-containing mRNAs (By similarity).
Stimulates the translation of mRNAs to which it is bound, acting, at least in part, with dazl (By similarity).
Involved in the maternal-to-zygotic transition in early embryo via interaction with ybx1: interaction recruits pabpc1a on C5-methylcytosine (m5C)-containing maternal mRNAs, preventing their degradation (PubMed:31399345).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular FunctionmRNA 3'-UTR binding
Molecular Functionpoly(A) binding
Molecular Functionpoly(U) RNA binding
Biological Processheart development
Biological ProcessmRNA processing
Biological Processregulation of translation
Biological Processtranslation

Keywords

Enzyme and pathway databases

    • R-DRE-156827L13a-mediated translational silencing of Ceruloplasmin expression
    • R-DRE-450408AUF1 (hnRNP D0) binds and destabilizes mRNA
    • R-DRE-975956Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
    • R-DRE-975957Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Names & Taxonomy

Protein names

  • Recommended name
    Polyadenylate-binding protein 1A
  • Short names
    PABP-1A; Poly(A)-binding protein 1A

Gene names

    • Name
      pabpc1a

Organism names

  • Taxonomic identifier
  • Strains
    • Tuebingen
    • AB
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    F1QB54
  • Secondary accessions
    • Q499B6
    • Q6P5M4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004483841-634Polyadenylate-binding protein 1A

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with ybx1; interaction recruits pabpc1a on C5-methylcytosine (m5C)-containing mRNAs, preventing their degradation.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-89RRM 1
Domain99-175RRM 2
Domain191-268RRM 3
Domain294-370RRM 4
Domain541-618PABC

Domain

RRM4, together with the C- and N-terminal regions, is sufficient for RNA-binding. RRM 1 has no RNA-binding activity itself, but improves discrimination between poly(A) and poly(U) in combination with the other repeats.

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    634
  • Mass (Da)
    70,734
  • Last updated
    2011-05-03 v1
  • Checksum
    94F6AA6A33D747EF
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMMTRRSLGYAYVNFQQPADAERALDTMNFDVIKGRPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETHEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAEMGARAKEFTNVYIKNFGEDMDDEKLKEIFCKYGPALSIRVMTDDSGKSKGFGFVSFERHEDAQRAVDEMNGKEMNGKQVYVGRAQKKGERQTELKRKFEQMKQDRMTRYQGVNLYVKNLDDGLDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTSQYMQRMASVRAVPNPVLNPYQPAPPSGYFMAAIPQAQNRAAYYPTSQLAQLRPSPRWATQGVRPQHFQNMPNAAVRPSAPRPQTFNPVRPASQVPRMMTSQRMGSQAMGPRPAAAGAATGPAQVRGVPQYKYAPGVRNPQQHMPTQPQVPMQQPAVHVQGQEPLTASMLAAAPPQEQKQMLGERLFPLIQNMHPSLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKSVPSPAVPAV

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict522in Ref. 2; AAH99992

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU855877
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC062832
EMBL· GenBank· DDBJ
AAH62832.1
EMBL· GenBank· DDBJ
mRNA
BC099992
EMBL· GenBank· DDBJ
AAH99992.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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