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Protein

Polyadenylate-binding protein 1

Gene

Pabpc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-429947. Deadenylation of mRNA.
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-RNO-72649. Translation initiation complex formation.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 1
Short name:
PABP-1
Short name:
Poly(A)-binding protein 1
Gene namesi
Name:Pabpc1
Synonyms:Pabp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi619838. Pabpc1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000817001 – 636Polyadenylate-binding protein 1Add BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei299N6-methyllysineBy similarity1
Modified residuei315PhosphoserineBy similarity1
Modified residuei319PhosphothreonineBy similarity1
Modified residuei385Omega-N-methylarginineBy similarity1
Modified residuei419Omega-N-methylarginineBy similarity1
Modified residuei432Omega-N-methylarginineBy similarity1
Modified residuei436Omega-N-methylarginineBy similarity1
Modified residuei455Omega-N-methylated arginine; by CARM1By similarity1
Modified residuei460Omega-N-methylated arginine; by CARM1By similarity1
Modified residuei475Omega-N-methylarginineBy similarity1
Modified residuei481Omega-N-methylarginineBy similarity1
Modified residuei493Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei493Dimethylated arginine; alternateBy similarity1
Modified residuei493Omega-N-methylarginine; alternateBy similarity1
Modified residuei506Omega-N-methylarginineBy similarity1
Modified residuei512N6-acetyllysineBy similarity1
Modified residuei518Omega-N-methylarginineBy similarity1

Post-translational modificationi

Phosphorylated by MAPKAPK2.By similarity
Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9EPH8.
PRIDEiQ9EPH8.

PTM databases

iPTMnetiQ9EPH8.
PhosphoSitePlusiQ9EPH8.

Expressioni

Gene expression databases

BgeeiENSRNOG00000008639.
ExpressionAtlasiQ9EPH8. baseline and differential.
GenevisibleiQ9EPH8. RN.

Interactioni

Subunit structurei

Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC) with 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 and PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. May interact with SETX (By similarity). Interacts (via the second and third RRM domains and the C-terminus) with PAIP2B (via central acidic portion and C-terminus). Interacts with LARP1. Interacts with RYDEN. Found in a complex with RYDEN and LARP1. Interacts with LARP4 (By similarity). Interacts with ZFC3H1 in a RNase-sensitive manner (By similarity). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Irs1P355702EBI-919825,EBI-520230

GO - Molecular functioni

Protein-protein interaction databases

BioGridi251195. 4 interactors.
CORUMiQ9EPH8.
IntActiQ9EPH8. 4 interactors.
MINTiMINT-4576919.
STRINGi10116.ENSRNOP00000012775.

Structurei

3D structure databases

ProteinModelPortaliQ9EPH8.
SMRiQ9EPH8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 89RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini99 – 175RRM 2PROSITE-ProRule annotationAdd BLAST77
Domaini191 – 268RRM 3PROSITE-ProRule annotationAdd BLAST78
Domaini294 – 370RRM 4PROSITE-ProRule annotationAdd BLAST77
Domaini542 – 619PABCPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni166 – 289UNR-bindingBy similarityAdd BLAST124

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi495 – 501Poly-Ala7

Domaini

The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.By similarity
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.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0123. Eukaryota.
ENOG410XR5X. LUCA.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000217922.
HOVERGENiHBG002295.
InParanoidiQ9EPH8.
KOiK13126.
OMAiRAAYYPA.
OrthoDBiEOG091G03ZE.
PhylomeDBiQ9EPH8.
TreeFamiTF300458.

Family and domain databases

InterProiView protein in InterPro
IPR036053. PABP-dom.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR035979. RBD_domain_sf.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
PfamiView protein in Pfam
PF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
SMARTiView protein in SMART
SM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
SM00361. RRM_1. 3 hits.
SUPFAMiSSF54928. SSF54928. 2 hits.
SSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiView protein in PROSITE
PS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.

Sequencei

Sequence statusi: Complete.

Q9EPH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR
60 70 80 90 100
SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN
110 120 130 140 150
IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA
160 170 180 190 200
AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE
210 220 230 240 250
DMDDERLKEL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE
260 270 280 290 300
MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
310 320 330 340 350
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV
360 370 380 390 400
TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY
410 420 430 440 450
QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM
460 470 480 490 500
PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAATA
510 520 530 540 550
ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML
560 570 580 590 600
ASAPPQEQKQ MLGERLFPLI QAMHPSLAGK ITGMLLEIDN SELLHMLESP
610 620 630
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
Length:636
Mass (Da):70,701
Last modified:March 1, 2001 - v1
Checksum:iE4006DFBA5F86CA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ298278 mRNA. Translation: CAC21554.1.
BC083176 mRNA. Translation: AAH83176.1.
RefSeqiNP_599180.1. NM_134353.3.
UniGeneiRn.127813.

Genome annotation databases

EnsembliENSRNOT00000012775; ENSRNOP00000012775; ENSRNOG00000008639.
GeneIDi171350.
KEGGirno:171350.
UCSCiRGD:619838. rat.

Similar proteinsi

Entry informationi

Entry nameiPABP1_RAT
AccessioniPrimary (citable) accession number: Q9EPH8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2001
Last modified: November 22, 2017
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families