PABPC1

Poly(A) binding protein, cytoplasmic 1

PDB rendering based on 1cvj.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1CVJ, 1G9L, 1JGN, 1JH4, 2K8G, 2RQG, 2RQH, 2X04, 3KTP, 3KTR, 3KUI, 3KUJ, 3KUR, 3KUS, 3KUT, 3PKN, 3PTH, 4F02, 4F25, 4F26

Identifiers

Symbols

PABPC1 ; PAB1; PABP; PABP1; PABPC2; PABPL1

External IDs

OMIM: 604679 MGI: 1349722 HomoloGene: 37638 ChEMBL: 1293286 GeneCards: PABPC1 Gene

Gene ontology
Molecular function	• nucleotide binding • protein binding • protein C-terminus binding • poly(A) binding • poly(U) RNA binding • translation activator activity • poly(A) RNA binding
Cellular component	• nucleus • cytoplasm • cytosol • cytoplasmic stress granule • membrane • ribonucleoprotein complex • cytoplasmic ribonucleoprotein granule • catalytic step 2 spliceosome
Biological process	• nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay • nuclear-transcribed mRNA poly(A) tail shortening • mRNA splicing, via spliceosome • mRNA polyadenylation • translation • translational initiation • gene expression • RNA metabolic process • mRNA metabolic process • gene silencing by RNA • cellular protein metabolic process • positive regulation of translation • mRNA stabilization • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay • negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
101.7 – 101.74 Mb

Chr 15:
36.6 – 36.61 Mb

PubMed search

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

Function

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

PABPC1 has been shown to interact with:

References

↑ 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.
↑ "Entrez Gene: PABPC1 poly(A) binding protein, cytoplasmic 1".
↑ 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.
↑ 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.
↑ 5.0 5.1 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.

Görlach M, Burd CG, Dreyfuss G (1994). "The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity". Exp. Cell Res. 211 (2): 400–7. doi:10.1006/excr.1994.1104. PMID 7908267. Vancouver style error (help)
Campbell LH, Borg KT, Haines JK, Moon RT, Schoenberg DR, Arrigo SJ (1994). "Human immunodeficiency virus type 1 Rev is required in vivo for binding of poly(A)-binding protein to Rev-dependent RNAs". J. Virol. 68 (9): 5433–8. PMC 236943. PMID 8057425.
Huang Y, Carmichael GG (1996). "Role of polyadenylation in nucleocytoplasmic transport of mRNA". Mol. Cell. Biol. 16 (4): 1534–42. PMC 231138. PMID 8657127.
Craig AW, Haghighat A, Yu AT, Sonenberg N (1998). "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation". Nature 392 (6675): 520–3. doi:10.1038/33198. PMID 9548260.
Afonina E, Stauber R, Pavlakis GN (1998). "The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm". J. Biol. Chem. 273 (21): 13015–21. doi:10.1074/jbc.273.21.13015. PMID 9582337.
Imataka H, Gradi A, Sonenberg N (1999). "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.
Hornstein E, Git A, Braunstein I, Avni D, Meyuhas O (1999). "The expression of poly(A)-binding protein gene is translationally regulated in a growth-dependent fashion through a 5'-terminal oligopyrimidine tract motif". J. Biol. Chem. 274 (3): 1708–14. doi:10.1074/jbc.274.3.1708. PMID 9880551.
Laroia G, Cuesta R, Brewer G, Schneider RJ (1999). "Control of mRNA decay by heat shock-ubiquitin-proteasome pathway". Science 284 (5413): 499–502. doi:10.1126/science.284.5413.499. PMID 10205060.
Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T (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.
Deo RC, Bonanno JB, Sonenberg N, Burley SK (1999). "Recognition of polyadenylate RNA by the poly(A)-binding protein". Cell 98 (6): 835–45. doi:10.1016/S0092-8674(00)81517-2. PMID 10499800.
Féral C, Mattéi MG, Pawlak A, Guellaën G (1999). "Chromosomal localization of three human poly(A)-binding protein genes and four related pseudogenes". Hum. Genet. 105 (4): 347–53. doi:10.1007/s004390051113. PMC 1865476. PMID 10543404. Vancouver style error (help)
Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, Shyu AB (2000). "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex". Cell 103 (1): 29–40. doi:10.1016/S0092-8674(00)00102-1. PMID 11051545.
Khaleghpour K, Svitkin YV, Craig AW, DeMaria CT, Deo RC, Burley SK et al. (2001). "Translational repression by a novel partner of human poly(A) binding protein, Paip2". Mol. Cell 7 (1): 205–16. doi:10.1016/S1097-2765(01)00168-X. PMID 11172725.
Bushell M, Wood W, Carpenter G, Pain VM, Morley SJ, Clemens MJ (2001). "Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages". J. Biol. Chem. 276 (26): 23922–8. doi:10.1074/jbc.M100384200. PMID 11274152.
Féral C, Guellaën G, Pawlak A (2002). "Human testis expresses a specific poly(A)-binding protein". Nucleic Acids Res. 29 (9): 1872–83. doi:10.1093/nar/29.9.1872. PMC 37253. PMID 11328870. Vancouver style error (help)
Khaleghpour K, Kahvejian A, De Crescenzo G, Roy G, Svitkin YV, Imataka H et al. (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.
Woods AJ, Roberts MS, Choudhary J, Barry ST, Mazaki Y, Sabe H et al. (2002). "Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells". J. Biol. Chem. 277 (8): 6428–37. doi:10.1074/jbc.M109446200. PMID 11704675.
Lee J, Bedford MT (2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.
Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.

PDB gallery

1cvj: X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX WITH POLYADENYLATE RNA

1g9l: SOLUTION STRUCTURE OF THE PABC DOMAIN OF HUMAN POLY(A) BINDING PROTEIN

1jgn: Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2

1jh4: Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip1

2d9p: Solution structure of RNA binding domain 4 in Polyadenylation binding protein 3

RNA-binding proteins

Butyrate response factor 1
Fragile X mental retardation protein
Rev
hu paraneoplastic encephalomyelitis antigens
mRNA cleavage and polyadenylation factors (Cleavage and polyadenylation specificity factor
Cleavage stimulation factor)
host factor 1 protein
Aconitase (ACO1
ACO2)
nuclear factor 90 proteins (ILF2)
Poly(A)-binding protein (PABPC1
PABPC3
PABPC4)
polypyrimidine tract-binding protein
ribonucleoprotein
RNA cap-binding protein (Cap binding complex
EIF4E
EIF4G1)
SMN complex proteins (SMN1
SMN2
DDX20)

Index of genetics

Description	Gene expression DNA replication cycle recombination repair binding proteins Transcription factors regulators nucleic acids RNA RNA binding proteins ribonucleoproteins repeated sequence modification Translation ribosome modification nexins Proteins domains Structure primary secondary tertiary quaternary

Disease	Replication and repair Transcription factor Transcription Translation

PABPC1

Function

Interactions

References

Further reading