PABPN1

PABPN1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3B4D, 3B4M, 3UCG
Identifiers
Aliases	PABPN1, OPMD, PAB2, PABII, PABP-2, PABP2, poly(A) binding protein nuclear 1
External IDs	OMIM: 602279 MGI: 1859158 HomoloGene: 3412 GeneCards: PABPN1
Gene location (Human)
Chr.	Chromosome 14 (human)[1]
End	23,326,185 bp[1]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• GO:0001948 protein binding; • nucleic acid binding; • RNA binding; • RNA polymerase binding;
Cellular component	• cytoplasm; • nucleoplasm; • nuclear inclusion body; • cell nucleus; • nuclear speck; • ribonucleoprotein;
Biological process	• mRNA splicing, via spliceosome; • termination of RNA polymerase II transcription; • RNA processing; • muscle contraction; • mRNA processing; • poly(A)+ mRNA export from nucleus; • modification by virus of host mRNA processing; • mRNA 3'-end processing; • MAPK cascade; • cellular response to lipopolysaccharide; • positive regulation of polynucleotide adenylyltransferase activity;
	Sources:Amigo / QuickGO
Orthologs
	8106
	54196
	ENSG00000100836
	ENSMUSG00000022194
	Q86U42
	Q8CCS6
	NM_004643; NM_001360551; NM_001360552
	NM_019402
	NP_004634; NP_001347480; NP_001347481
	NP_062275
	Wikidata
View/Edit Human	View/Edit Mouse

Polyadenylate-binding protein 2 (PABP-2) also known as polyadenylate-binding nuclear protein 1 (PABPN1) is a protein that in humans is encoded by the PABPN1 gene.[4][5] PABN1 is a member of a larger family of poly(A)-binding proteins in the human genome.

Function

This gene encodes an abundant nuclear protein that binds with high affinity to nascent poly(A) tails. The protein is required for progressive and efficient polymerization of poly(A) tails on the 3' ends of eukaryotic genes and controls the size of the poly(A) tail to about 250 nt. At steady-state, this protein is localized in the nucleus whereas a different poly(A) binding protein is localized in the cytoplasm. An expansion of the trinucleotide (GCN) repeat from normal 10 to 11-17 at the 5' end of the coding region of this gene leads to autosomal dominant oculopharyngeal muscular dystrophy (OPMD) disease.[6] Multiple splice variants have been described but their full-length nature is not known. One splice variant includes introns 1 and 6 but no protein is formed.[5]

Interactions

PABPN1 has been shown to interact with SNW1.[7]

References

GRCh38: Ensembl release 89: ENSG00000100836 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Brais B, Xie YG, Sanson M, Morgan K, Weissenbach J, Korczyn AD, Blumen SC, Fardeau M, Tomé FM, Bouchard JP (Aug 1995). "The oculopharyngeal muscular dystrophy locus maps to the region of the cardiac alpha and beta myosin heavy chain genes on chromosome 14q11.2-q13". Hum Mol Genet. 4 (3): 429–34. doi:10.1093/hmg/4.3.429. PMID 7795598.
"Entrez Gene: PABPN1 poly(A) binding protein, nuclear 1".
Brais B (January 2009). "Oculopharyngeal muscular dystrophy: a polyalanine myopathy". Current Neurology and Neuroscience Reports. 9 (1): 76–82. doi:10.1007/s11910-009-0012-y. PMID 19080757.
Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K (May 2001). "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression". Hum. Mol. Genet. England. 10 (11): 1129–39. doi:10.1093/hmg/10.11.1129. ISSN 0964-6906. PMID 11371506.

Brais B, Bouchard JP, Xie YG, Rochefort DL, Chrétien N, Tomé FM, Lafrenière RG, Rommens JM, Uyama E, Nohira O, Blumen S, Korczyn AD, Heutink P, Mathieu J, Duranceau A, Codère F, Fardeau M, Rouleau GA, Korcyn AD (1998). "Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy". Nat. Genet. 18 (2): 164–7. doi:10.1038/ng0298-164. PMID 9462747.
Chen Z, Li Y, Krug RM (1999). "Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery". EMBO J. 18 (8): 2273–83. doi:10.1093/emboj/18.8.2273. PMC 1171310. PMID 10205180.
Smith JJ, Rücknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, Herschman HR, Wahle E (1999). "Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3". J. Biol. Chem. 274 (19): 13229–34. doi:10.1074/jbc.274.19.13229. PMID 10224081.
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.
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.
Calado A, Kutay U, Kühn U, Wahle E, Carmo-Fonseca M (2000). "Deciphering the cellular pathway for transport of poly(A)-binding protein II". RNA. 6 (2): 245–56. doi:10.1017/S1355838200991908. PMC 1369910. PMID 10688363.
Calado A, Tomé FM, Brais B, Rouleau GA, Kühn U, Wahle E, Carmo-Fonseca M (2001). "Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA". Hum. Mol. Genet. 9 (15): 2321–8. doi:10.1093/oxfordjournals.hmg.a018924. PMID 11001936.
Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K (2001). "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression". Hum. Mol. Genet. 10 (11): 1129–39. doi:10.1093/hmg/10.11.1129. PMID 11371506.
Fan X, Dion P, Laganiere J, Brais B, Rouleau GA (2002). "Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death". Hum. Mol. Genet. 10 (21): 2341–51. doi:10.1093/hmg/10.21.2341. PMID 11689481.
van der Sluijs BM, van Engelen BG, Hoefsloot LH (2003). "Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication in the PABPN1 gene". Hum. Mutat. 21 (5): 553. doi:10.1002/humu.9138. PMID 12673802.
Fan X, Messaed C, Dion P, Laganiere J, Brais B, Karpati G, Rouleau GA (2003). "HnRNP A1 and A/B interaction with PABPN1 in oculopharyngeal muscular dystrophy". The Canadian Journal of Neurological Sciences. 30 (3): 244–51. doi:10.1017/s0317167100002675. PMID 12945950.
Sugaya K, Matsubara S, Miyamoto K, Kawata A, Hayashi H (2004). "An aggregate-prone conformational epitope in trinucleotide repeat diseases". NeuroReport. 14 (18): 2331–5. doi:10.1097/00001756-200312190-00009. PMID 14663186.
Villacé P, Marión RM, Ortín J (2004). "The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs". Nucleic Acids Res. 32 (8): 2411–20. doi:10.1093/nar/gkh552. PMC 419443. PMID 15121898.
Dettwiler S, Aringhieri C, Cardinale S, Keller W, Barabino SM (2005). "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization" (PDF). J. Biol. Chem. 279 (34): 35788–97. doi:10.1074/jbc.M403927200. PMID 15169763.
Rodríguez M, Camejo C, Bertoni B, Braida C, Rodríguez MM, Brais B, Medici M, Roche L (2005). "(GCG)11 founder mutation in the PABPN1 gene of OPMD Uruguayan families". Neuromuscul. Disord. 15 (2): 185–90. doi:10.1016/j.nmd.2004.10.012. PMID 15694141.
Goh KJ, Wong KT, Nishino I, Minami N, Nonaka I (2005). "Oculopharyngeal muscular dystrophy with PABPN1 mutation in a Chinese Malaysian woman". Neuromuscul. Disord. 15 (3): 262–4. doi:10.1016/j.nmd.2004.10.016. PMID 15725589.
Dion P, Shanmugam V, Gaspar C, Messaed C, Meijer I, Toulouse A, Laganiere J, Roussel J, Rochefort D, Laganiere S, Allen C, Karpati G, Bouchard JP, Brais B, Rouleau GA (2005). "Transgenic expression of an expanded (GCG)13 repeat PABPN1 leads to weakness and coordination defects in mice". Neurobiol. Dis. 18 (3): 528–36. doi:10.1016/j.nbd.2004.09.021. PMID 15755680.

External links

GeneReviews/NCBI/NIH/UW entry on Oculopharyngeal Muscular Dystrophy
PDBe-KB provides an overview of all the structure information available in the PDB for Human Polyadenylate-binding protein 2

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100836 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7795598-4] Brais B, Xie YG, Sanson M, Morgan K, Weissenbach J, Korczyn AD, Blumen SC, Fardeau M, Tomé FM, Bouchard JP (Aug 1995). "The oculopharyngeal muscular dystrophy locus maps to the region of the cardiac alpha and beta myosin heavy chain genes on chromosome 14q11.2-q13". Hum Mol Genet. 4 (3): 429–34. doi:10.1093/hmg/4.3.429. PMID 7795598.

[entrez-5] "Entrez Gene: PABPN1 poly(A) binding protein, nuclear 1".

[6] Brais B (January 2009). "Oculopharyngeal muscular dystrophy: a polyalanine myopathy". Current Neurology and Neuroscience Reports. 9 (1): 76–82. doi:10.1007/s11910-009-0012-y. PMID 19080757.

[pmid11371506-7] Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K (May 2001). "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression". Hum. Mol. Genet. England. 10 (11): 1129–39. doi:10.1093/hmg/10.11.1129. ISSN 0964-6906. PMID 11371506.

PABPN1

Function

Interactions

References

Further reading

External links