UniProt Accession

 RRP44_HUMAN; Q9Y2L1; A6NI21; B2RBL2; Q5W0P7; Q5W0P8; Q658Z7; Q7Z481; Q8WWI2; Q9UG36 

Genbank Protein ID

 AF330044; AB023225; AL832266; AK314715; AL080158; AL138695; AL391384; AL138695; AL391384; AL391384; AL138695; AL391384; AL138695; CH471093; BC056143 

Genbank Nucleotide ID

 AAL37479.1; BAA76852.2; CAH56266.1; BAG37259.1; CAB45749.1; CAH72709.1; CAH72709.1; CAH72708.1; CAH72708.1; CAI15670.1; CAI15670.1; CAI15671.1; CAI15671.1; EAW80517.1; AAH56143.1 

Protein Name

 Exosome complex exonuclease RRP44 

Protein Synonyms/Alias

 Protein DIS3 homolog; Ribosomal RNA-processing protein 44 

Gene Name

 DIS3 

Gene Synonyms/Alias

 KIAA1008; RRP44 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
18	TRAGGVMKIVREHYL	acetylation	[1]
18	TRAGGVMKIVREHYL	ubiquitination	[2]
118	DVTNNQEKHFYTFTN	ubiquitination	[3, 4]
199	FTCEEYVKSLTANPE	ubiquitination	[2, 5]
225	GNEIESGKIIFSEHL	ubiquitination	[2]
236	SEHLPLSKLQQGIKS	ubiquitination	[3, 4]
242	SKLQQGIKSGTYLQG	ubiquitination	[2, 3, 4]
331	EETERMLKTAVSEKM	ubiquitination	[2]
462	MPWSITEKDMKNRED	ubiquitination	[2]
535	TTVYLCEKRIDMVPE	ubiquitination	[2]
585	TKSVINSKASLTYAE	ubiquitination	[2]
654	DPIDLQTKELRETNS	ubiquitination	[2]
677	ANISVAKKIHEEFSE	ubiquitination	[2]
690	SEHALLRKHPAPPPS	ubiquitination	[2]
714	RSRNLEIKTDTAKSL	ubiquitination	[2]
809	PELTDKHKLADICKN	ubiquitination	[2]
815	HKLADICKNLNFRHK	ubiquitination	[2, 3, 4]
822	KNLNFRHKMAQYAQR	ubiquitination	[5]
906	TVFHVFDKVKVKIML	ubiquitination	[3, 4]
908	FHVFDKVKVKIMLDS	ubiquitination	[2]
922	SSNLQHQKIRMSLVE	acetylation	[1]
922	SSNLQHQKIRMSLVE	ubiquitination	[2, 3, 4]

Reference

 [1] 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 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 Putative catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. DIS3 has both 3'-5' exonuclease and endonuclease activities. 

Sequence Annotation

 DOMAIN 64 182 PINc.
 MOD_RES 18 18 N6-acetyllysine.  

Keyword

 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Endonuclease; Exonuclease; Exosome; Hydrolase; Magnesium; Manganese; Nuclease; Nucleus; Polymorphism; Reference proteome; RNA-binding; rRNA processing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 958 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000176; C:nuclear exosome (RNase complex); IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0000175; F:3'-5'-exoribonuclease activity; IMP:UniProtKB.
 GO:0004519; F:endonuclease activity; IMP:UniProtKB.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0071034; P:CUT catabolic process; IMP:UniProtKB.
 GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
 GO:0016075; P:rRNA catabolic process; IMP:UniProtKB.
 GO:0006364; P:rRNA processing; TAS:UniProtKB. 

Interpro

 IPR002716; PIN_dom.
 IPR006596; PINc_nuc-bd.
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS. 

Pfam

 PF13638; PIN_4
 PF00773; RNB 

SMART

 SM00670; PINc
 SM00955; RNB 

PROSITE

 PS01175; RIBONUCLEASE_II 

PRINTS