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Poly(A)-specific ribonuclease PARN

Known also as: Deadenylating nuclease,Deadenylation nuclease, Polyadenylate-specific ribonuclease

Known abbreviations: PARN, DAN


3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization. 
Exonucleolytic cleavage of poly(A) to 5'-AMP. 
Divalent metal cations. Mg2+ is the most probable. 
Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. 
Nucleus. Cytoplasm. Nucleus › nucleolus. Note: Some nuclear fraction is nucleolar. 
Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.

Activities in which Poly(A)-specific ribonuclease PARN is involved: Pathways in which Poly(A)-specific ribonuclease PARN is involved:

NCBI GI number(s): 339715199
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O95453 O95453
KEGG hsa:5073 hsa:5073
PFAM: PF04857
InterPro: IPR012677
CATH: - -
SCOP: - -
Solved crystal structures: 2A1R
[PDB] [details]
[PDB] [details]
[PDB] [details]

Protein sequence:

Poly(A)-specific ribonuclease PARN (Homo sapiens) is product of expression of PARN gene.

Poly(A)-specific ribonuclease PARN (Homo sapiens) belongs to following protein families:

Title Authors Journal Publication date (Issue) PubMed ID
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). 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, K Genome Res 2004-10-01 (14) 15489334
Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K Nat Genet 2004-02-01 (36) 14702039
The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. Korner CG, Wormington M, Muckenthaler M, Schneider S, Dehlin E, Wahle E EMBO J 1998-09-15 (17) 9736620
A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP Nat Biotechnol 2006-10-01 (24) 16964243
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem 2009-06-01 (81) 19413330
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science 2009-08-14 (325) 19608861
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A 2008-08-05 (105) 18669648
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
The sequence and analysis of duplication-rich human chromosome 16. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M Nature 2004-12-23 (432) 15616553
Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Lejeune F, Li X, Maquat LE Mol Cell 2003-09-01 (12) 14527413
The human gene for the poly(A)-specific ribonuclease (PARN) maps to 16p13 and has a truncated copy in the Prader-Willi/Angelman syndrome region on 15q11-->q13. Buiting K, Korner C, Ulrich B, Wahle E, Horsthemke B Cytogenet Cell Genet 1999-01-01 (87) 10640832
A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease. Martinez J, Ren YG, Thuresson AC, Hellman U, Astrom J, Virtanen A J Biol Chem 2000-08-04 (275) 10801819
Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro. Gao M, Fritz DT, Ford LP, Wilusz J Mol Cell 2000-03-01 (5) 10882133
The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. Martinez J, Ren YG, Nilsson P, Ehrenberg M, Virtanen A J Biol Chem 2001-07-27 (276) 11359775
Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage. Ren YG, Martinez J, Virtanen A J Biol Chem 2002-01-22 (277) 11742007
Functional proteomic analysis of human nucleolus. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ Mol Biol Cell 2002-11-01 (13) 12429849
Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Lai WS, Kennington EA, Blackshear PJ Mol Cell Biol 2003-06-01 (23) 12748283
A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Gherzi R, Lee KY, Briata P, Wegmuller D, Moroni C, Karin M, Chen CY Mol Cell 2004-06-04 (14) 15175153
Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease. Ren YG, Kirsebom LA, Virtanen A J Biol Chem 2004-11-19 (279) 15358788
CUG-BP binds to RNA substrates and recruits PARN deadenylase. Moraes KC, Wilusz CJ, Wilusz J RNA 2006-06-01 (12) 16601207
Structural insight into poly(A) binding and catalytic mechanism of human PARN. Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H EMBO J 2005-12-07 (24) 16281054
DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization. Reinhardt HC, Hasskamp P, Schmedding I, Morandell S, van Vugt MA, Wang X, Linding R, Ong SE, Weaver D, Carr SA, Yaffe MB Mol Cell 2010-10-08 (40) 20932473

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Last modification of this entry: Sept. 25, 2012.

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