PABPC1

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Poly(A) binding protein, cytoplasmic 1
Protein PABPC1 PDB 1cvj.png
PDB rendering based on 1cvj.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PABPC1 ; PAB1; PABP; PABP1; PABPC2; PABPL1
External IDs OMIM604679 MGI1349722 HomoloGene37638 ChEMBL: 1293286 GeneCards: PABPC1 Gene
Orthologs
Species Human Mouse
Entrez 26986 18458
Ensembl ENSG00000070756 ENSMUSG00000022283
UniProt P11940 P29341
RefSeq (mRNA) NM_002568 NM_008774
RefSeq (protein) NP_002559 NP_032800
Location (UCSC) Chr 8:
101.7 – 101.74 Mb
Chr 15:
36.6 – 36.61 Mb
PubMed search [1] [2]

Polyadenylate-binding protein 1 is a protein that in humans is encoded by the PABPC1 gene.[1]

Function[edit]

The poly(A)-binding protein (PAB or PABP), which is found complexed to the 3' poly(A) tail of eukaryotic mRNA, is required for poly(A) shortening and translation initiation. In humans, the PABPs comprise a small nuclear isoform and a conserved gene family that displays at least 3 functional proteins: PABP1 (PABPC1), inducible PABP (iPABP, or PABPC4; MIM 603407), and PABP3 (PABPC3; MIM 604680). In addition, there are at least 4 pseudogenes, PABPCP1 to PABPCP4.[supplied by OMIM][2]

Interactions[edit]

PABPC1 has been shown to interact with:

References[edit]

  1. ^ Grange T, de Sa CM, Oddos J, Pictet R (Aug 1987). "Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif". Nucleic Acids Res 15 (12): 4771–87. doi:10.1093/nar/15.12.4771. PMC 305917. PMID 2885805. 
  2. ^ "Entrez Gene: PABPC1 poly(A) binding protein, cytoplasmic 1". 
  3. ^ Koloteva-Levine N, Pinchasi D, Pereman I, Zur A, Brandeis M, Elroy-Stein O (May 2004). "The Apc5 subunit of the anaphase-promoting complex/cyclosome interacts with poly(A) binding protein and represses internal ribosome entry site-mediated translation". Mol. Cell. Biol. 24 (9): 3577–87. doi:10.1128/mcb.24.9.3577-3587.2004. PMC 387753. PMID 15082755. 
  4. ^ Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I et al. (Dec 2007). "Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases". Genes Dev. 21 (23): 3135–48. doi:10.1101/gad.1597707. PMC 2081979. PMID 18056425. 
  5. ^ a b Imataka H, Gradi A, Sonenberg N (Dec 1998). "A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation". EMBO J. 17 (24): 7480–9. doi:10.1093/emboj/17.24.7480. PMC 1171091. PMID 9857202. 
  6. ^ Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T (Jun 1999). "The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein". J. Biol. Chem. 274 (24): 16677–80. doi:10.1074/jbc.274.24.16677. PMID 10358005. 
  7. ^ Roy G, De Crescenzo G, Khaleghpour K, Kahvejian A, O'Connor-McCourt M, Sonenberg N (Jun 2002). "Paip1 interacts with poly(A) binding protein through two independent binding motifs". Mol. Cell. Biol. 22 (11): 3769–82. doi:10.1128/mcb.22.11.3769-3782.2002. PMC 133836. PMID 11997512. 
  8. ^ Craig AW, Haghighat A, Yu AT, Sonenberg N (Apr 1998). "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation". Nature 392 (6675): 520–3. doi:10.1038/33198. PMID 9548260. 
  9. ^ Khaleghpour K, Kahvejian A, De Crescenzo G, Roy G, Svitkin YV, Imataka H et al. (Aug 2001). "Dual interactions of the translational repressor Paip2 with poly(A) binding protein". Mol. Cell. Biol. 21 (15): 5200–13. doi:10.1128/MCB.21.15.5200-5213.2001. PMC 87244. PMID 11438674. 

Further reading[edit]