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Identification
HMDB Protein ID HMDBP08498
Secondary Accession Numbers
  • 14210
Name Polyadenylate-binding protein 2
Synonyms
  1. Nuclear poly(A)-binding protein 1
  2. PABII
  3. PABP-2
  4. Poly(A)-binding protein 2
  5. Poly(A)-binding protein II
  6. Polyadenylate-binding nuclear protein 1
Gene Name PABPN1
Protein Type Unknown
Biological Properties
General Function Involved in nucleotide binding
Specific Function Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
nucleotide binding
nucleic acid binding
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 14q11.2-q13
SNPs PABPN1
Gene Sequence
>921 bp
ATGGCGGCGGCGGCGGCGGCGGCAGCAGCAGCGGGGGCTGCGGGCGGTCGGGGCTCCGGG
CCGGGGCGGCGGCGCCATCTTGTGCCCGGGGCCGGTGGGGAGGCCGGGGAGGGGGCCCCG
GGGGGCGCAGGGGACTACGGGAACGGCCTGGAGTCTGAGGAACTGGAGCCTGAGGAGCTG
CTGCTGGAGCCCGAGCCGGAGCCCGAGCCCGAAGAGGAGCCGCCCCGGCCCCGCGCCCCC
CCGGGAGCTCCGGGCCCTGGGCCTGGTTCGGGAGCCCCCGGCAGCCAAGAGGAGGAGGAG
GAGCCGGGACTGGTCGAGGGTGACCCGGGGGACGGCGCCATTGAGGACCCGGAGCTGGAA
GCTATCAAAGCTCGAGTCAGGGAGATGGAGGAAGAAGCTGAGAAGCTAAAGGAGCTACAG
AACGAGGTAGAGAAGCAGATGAATATGAGTCCACCTCCAGGCAATGCTGGCCCGGTGATC
ATGTCCATTGAGGAGAAGATGGAGGCTGATGCCCGTTCCATCTATGTTGGCAATGTGGAC
TATGGTGCAACAGCAGAAGAGCTGGAAGCTCACTTTCATGGCTGTGGTTCAGTCAACCGT
GTTACCATACTGTGTGACAAATTTAGTGGCCATCCCAAAGGGTTTGCGTATATAGAGTTC
TCAGACAAAGAGTCAGTGAGGACTTCCTTGGCCTTAGATGAGTCCCTATTTAGAGGAAGG
CAAATCAAGGTGATCCCAAAACGAACCAACAGACCAGGCATCAGCACAACAGACCGGGGT
TTTCCACGAGCCCGCTACCGCGCCCGGACCACCAACTACAACAGCTCCCGCTCTCGATTC
TACAGTGGTTTTAACAGCAGGCCCCGGGGTCGCGTCTACAGGGGCCGGGCTAGAGCGACA
TCATGGTATTCCCCTTACTAA
Protein Properties
Number of Residues 306
Molecular Weight 32748.8
Theoretical pI 4.73
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Polyadenylate-binding protein 2
MAAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGAPGGAGDYGNGLESEELEPEEL
LLEPEPEPEPEEEPPRPRAPPGAPGPGPGSGAPGSQEEEEEPGLVEGDPGDGAIEDPELE
AIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSIEEKMEADARSIYVGNVD
YGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDESLFRGR
QIKVIPKRTNRPGISTTDRGFPRARYRARTTNYNSSRSRFYSGFNSRPRGRVYRGRARAT
SWYSPY
GenBank ID Protein 2895276
UniProtKB/Swiss-Prot ID Q86U42
UniProtKB/Swiss-Prot Entry Name PABP2_HUMAN
PDB IDs Not Available
GenBank Gene ID AF026029
GeneCard ID PABPN1
GenAtlas ID PABPN1
HGNC ID HGNC:8565
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Dettwiler S, Aringhieri C, Cardinale S, Keller W, Barabino SM: Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization. J Biol Chem. 2004 Aug 20;279(34):35788-97. Epub 2004 May 28. [PubMed:15169763 ]
  6. Jonson L, Vikesaa J, Krogh A, Nielsen LK, Hansen Tv, Borup R, Johnsen AH, Christiansen J, Nielsen FC: Molecular composition of IMP1 ribonucleoprotein granules. Mol Cell Proteomics. 2007 May;6(5):798-811. Epub 2007 Feb 7. [PubMed:17289661 ]
  7. Brais B, Bouchard JP, Xie YG, Rochefort DL, Chretien N, Tome FM, Lafreniere RG, Rommens JM, Uyama E, Nohira O, Blumen S, Korczyn AD, Heutink P, Mathieu J, Duranceau A, Codere F, Fardeau M, Rouleau GA: Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet. 1998 Feb;18(2):164-7. [PubMed:9462747 ]
  8. Chen Z, Li Y, Krug RM: Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery. EMBO J. 1999 Apr 15;18(8):2273-83. [PubMed:10205180 ]
  9. Calado A, Tome FM, Brais B, Rouleau GA, Kuhn U, Wahle E, Carmo-Fonseca M: Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum Mol Genet. 2000 Sep 22;9(15):2321-8. [PubMed:11001936 ]
  10. Calado A, Kutay U, Kuhn U, Wahle E, Carmo-Fonseca M: Deciphering the cellular pathway for transport of poly(A)-binding protein II. RNA. 2000 Feb;6(2):245-56. [PubMed:10688363 ]
  11. Fan X, Dion P, Laganiere J, Brais B, Rouleau GA: Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death. Hum Mol Genet. 2001 Oct 1;10(21):2341-51. [PubMed:11689481 ]
  12. Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K: 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. 2001 May 15;10(11):1129-39. [PubMed:11371506 ]
  13. Sugaya K, Matsubara S, Miyamoto K, Kawata A, Hayashi H: An aggregate-prone conformational epitope in trinucleotide repeat diseases. Neuroreport. 2003 Dec 19;14(18):2331-5. [PubMed:14663186 ]
  14. van der Sluijs BM, van Engelen BG, Hoefsloot LH: Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication in the PABPN1 gene. Hum Mutat. 2003 May;21(5):553. [PubMed:12673802 ]