Overview
| Uniprot ID | P29341 |
|---|
| Protein Name | Polyadenylate-binding protein 1 |
|---|
| Gene Name | Pabpc1 |
|---|
| Organism | Mus musculus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 512 |
VRTVPQYKYAAGVRN |
Function
Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. 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. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. 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 binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability
Protein Sequence
10
MNPSAPSYPM
20
ASLYVGDLHP
30
DVTEAMLYEK
40
FSPAGPILSI
50
RVCRDMITRR
60
SLGYAYVNFQ
70
QPADAERALD
80
TMNFDVIKGK
90
PVRIMWSQRD
100
PSLRKSGVGN
110
IFIKNLDKSI
120
DNKALYDTFS
130
AFGNILSCKV
140
VCDENGSKGY
150
GFVHFETQEA
160
AERAIEKMNG
170
MLLNDRKVFV
180
GRFKSRKERE
190
AELGARAKEF
200
TNVYIKNFGE
210
DMDDERLKEL
220
FGKFGPALSV
230
KVMTDESGKS
240
KGFGFVSFER
250
HEDAQKAVDE
260
MNGKELNGKQ
270
IYVGRAQKKV
280
ERQTELKRKF
290
EQMKQDRITR
300
YQGVNLYVKN
310
LDDGIDDERL
320
RKEFSPFGTI
330
TSAKVMMEGG
340
RSKGFGFVCF
350
SSPEEATKAV
360
TEMNGRIVAT
370
KPLYVALAQR
380
KEERQAHLTN
390
QYMQRMASVR
400
AVPNPVINPY
410
QPAPPSGYFM
420
AAIPQTQNRA
430
AYYPPSQIAQ
440
LRPSPRWTAQ
450
GARPHPFQNM
460
PGAIRPAAPR
470
PPFSTMRPAS
480
SQVPRVMSTQ
490
RVANTSTQTM
500
GPRPAAAAAA
510
ATPAVRTVPQ
520
YKYAAGVRNP
530
QQHLNAQPQV
540
TMQQPAVHVQ
550
GQEPLTASML
560
ASAPPQEQKQ
570
MLGERLFPLI
580
QAMHPSLAGK
590
ITGMLLEIDN
600
SELLHMLESP
610
ESLRSKVDEA
620
VAVLQAHQAK
630
EAAQKAVNSA
TGVPTV
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0071013 |
catalytic step 2 spliceosome |
| Cellular Component |
GO:0031252 |
cell leading edge |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0036464 |
cytoplasmic ribonucleoprotein granule |
| Cellular Component |
GO:0010494 |
cytoplasmic stress granule |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0030425 |
dendrite |
| Cellular Component |
GO:0030027 |
lamellipodium |
| Cellular Component |
GO:0106002 |
mCRD-mediated mRNA stability complex |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0032991 |
protein-containing complex |
| Cellular Component |
GO:1990904 |
ribonucleoprotein complex |
| Cellular Component |
GO:0045202 |
synapse |
| Molecular Function |
GO:0003730 |
mRNA 3'-UTR binding |
| Molecular Function |
GO:0003729 |
mRNA binding |
| Molecular Function |
GO:0008143 |
poly(A) binding |
| Molecular Function |
GO:0008266 |
poly(U) RNA binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:2000623 |
negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process |
GO:0000184 |
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| Biological Process |
GO:1900153 |
positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay |
| Biological Process |
GO:0060213 |
positive regulation of nuclear-transcribed mRNA poly(A) tail shortening |
| Biological Process |
GO:0031047 |
regulatory ncRNA-mediated gene silencing |
| Biological Process |
GO:0008380 |
RNA splicing |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.