Search Results

Overview

Uniprot IDP11940
Protein NamePolyadenylate-binding protein 1
Gene NamePABPC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
108 IFIKNLDKSIDNKAL
188 AELGARAKEFTNVYI
284 KRKFEQMKQDRITRY
312 IDDERLRKEFSPFGT
361 NGRIVATKPLYVALA
512 VRTVPQYKYAAGVRN
620 VLQAHQAKEAAQKAV
625 QAKEAAQKAVNSATG
95 QRDPSLRKSGVGNIF

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 (PubMed:11051545, PubMed:17212783, PubMed:25480299). Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2 (PubMed:11051545, PubMed:20573744). 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 (PubMed:32245947). Involved in translationally coupled mRNA turnover (PubMed:11051545). 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 (PubMed:11051545). 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 (PubMed:18447585). By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299)

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 DMDDERLKDL 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 QAMHPTLAGK 590 ITGMLLEIDN 600 SELLHMLESP 610 ESLRSKVDEA 620 VAVLQAHQAK 630 EAAQKAVNSA TGVPTV

Gene Ontology

Classification GO ID Description
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0008494 translation activator activity
Biological Process GO:0070934 CRD-mediated mRNA stabilization
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:1900152 negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
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:2000767 positive regulation of cytoplasmic translation
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:0045070 positive regulation of viral genome replication
Biological Process GO:0031047 regulatory ncRNA-mediated gene silencing
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:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:1990904 ribonucleoprotein complex
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

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.