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Protein

Polyadenylate-binding protein 1

Gene

Pabpc1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1349722 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_00000816991 – 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-methylarginineCombined sources1
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-methylarginineCombined sources1
Modified residuei481Omega-N-methylarginineBy similarity1
Modified residuei493Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei493Dimethylated arginine; alternateBy similarity1
Modified residuei493Omega-N-methylarginine; alternateCombined sources1
Modified residuei506Omega-N-methylarginineCombined sources1
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

EPDiP29341
MaxQBiP29341
PaxDbiP29341
PeptideAtlasiP29341
PRIDEiP29341

2D gel databases

REPRODUCTION-2DPAGEP29341

PTM databases

iPTMnetiP29341
PhosphoSitePlusiP29341
SwissPalmiP29341

Expressioni

Gene expression databases

BgeeiENSMUSG00000022283
CleanExiMM_PABPC1
ExpressionAtlasiP29341 baseline and differential
GenevisibleiP29341 MM

Interactioni

Subunit structurei

Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. 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. 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. Identified in the spliceosome C complex. Interacts with NFX1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. May interact with SETX (By similarity). The interaction with CSDE1 is direct and RNA-independent (PubMed:15314026). Found in a mRNP complex with YBX2 (PubMed:10076007). Interacts with PAPD4/GLD2 (PubMed:17927953). Interacts with PIWIL1 (PubMed:19020299). 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 (By similarity). 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 similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202010, 27 interactors
DIPiDIP-32127N
IntActiP29341, 36 interactors
MINTiP29341
STRINGi10090.ENSMUSP00000001809

Structurei

3D structure databases

ProteinModelPortaliP29341
SMRiP29341
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 – 289CSDE1-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
InParanoidiP29341
KOiK13126
OMAiRAAYYPA
OrthoDBiEOG091G03ZE
TreeFamiTF300458

Family and domain databases

Gene3Di3.30.70.330, 4 hits
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
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.

P29341-1 [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 GPRPAAAAAA
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):70,671
Last modified:July 27, 2011 - v2
Checksum:iE5BB6D5BA4F86CB7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti176R → Q in CAA46522 (PubMed:1630930).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65553 mRNA Translation: CAA46522.1
AK044829 mRNA Translation: BAC32110.1
AK133196 mRNA Translation: BAE21553.1
AK159703 mRNA Translation: BAE35302.1
AK159733 mRNA Translation: BAE35327.1
AK160968 mRNA Translation: BAE36120.1
AK161123 mRNA Translation: BAE36203.1
AK161671 mRNA Translation: BAE36522.1
AK168466 mRNA Translation: BAE40360.1
CH466541 Genomic DNA Translation: EDL08818.1
BC003870 mRNA Translation: AAH03870.1
BC011207 mRNA Translation: AAH11207.1
BC023145 mRNA Translation: AAH23145.1
BC046233 mRNA Translation: AAH46233.1
CCDSiCCDS27431.1
PIRiI48718
RefSeqiNP_032800.2, NM_008774.3
XP_011243641.1, XM_011245339.2
UniGeneiMm.371570

Genome annotation databases

EnsembliENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283
GeneIDi18458
KEGGimmu:18458
UCSCiuc007vmx.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPABP1_MOUSE
AccessioniPrimary (citable) accession number: P29341
Secondary accession number(s): Q99L36
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 179 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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