Welcome! Click here to login or here to register.
Home
Pathways
Proteins
Catalytic RNA molecules
Enzymatic complexes
Structures
Publications
Draw a picture
 
Search
 
Links
Help
Contact





Bujnicki Lab Homepage

Exosome complex exonuclease RRP44

 
Known also as: Protein DIS3 homolog, Ribosomal RNA-processing protein 44

Known abbreviations: DIS3, KIAA1008, RRP44

FUNCTION:

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.

COFACTOR:

Magnesium and manganese.

SUBUNIT STRUCTURE:

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms.

CELLULAR LOCALIZATION:

Cytoplasm. Nucleus › nucleolus. Nucleus › nucleoplasm. Nucleus. Note: Predominantly located in the nucleus. According to Ref.12, found in the nucleolus and according to Ref.14, excluded from nucleolus supporting the existence of a nucleolar RNA exosome complex devoid of DIS3.

TISSUE SPECIFICITY:

Widely expressed.




This protein can be a part of a given complexes: Activities in which Exosome complex exonuclease RRP44 is involved: Pathways in which Exosome complex exonuclease RRP44 is involved:

NCBI GI number(s): 190014625
190014623
190014622
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9Y2L1 Q9Y2L1
BRENDA - -
KEGG hsa:22894 hsa:22894
PFAM: - Q9Y2L1 (Link - using uniprot id)
InterPro: - Q9Y2L1 (Link - using uniprot id)
CATH: - -
SCOP: - -


Protein sequence:
MLKSKTFLKKTRAGGVMKIVREHYLRDDIGCGAPGCAACGGAHEGPALEP
QPQDPASSVCPQPHYLLPDTNVLLHQIDVLEDPAIRNVIVLQTVLQEVRN
RSAPVYKRIRDVTNNQEKHFYTFTNEHHRETYVEQEQGENANDRNDRAIR
VAAKWYNEHLKKMSADNQLQVIFITNDRRNKEKAIEEGIPAFTCEEYVKS
LTANPELIDRLACLSEEGNEIESGKIIFSEHLPLSKLQQGIKSGTYLQGT
FRASRENYLEATVWIHGDNEENKEIILQGLKHLNRAVHEDIVAVELLPKS
QWVAPSSVVLHDEGQNEEDVEKEEETERMLKTAVSEKMLKPTGRVVGIIK
RNWRPYCGMLSKSDIKESRRHLFTPADKRIPRIRIETRQASTLEGRRIIV
AIDGWPRNSRYPNGHFVRNLGDVGEKETETEVLLLEHDVPHQPFSQAVLS
FLPKMPWSITEKDMKNREDLRHLCICSVDPPGCTDIDDALHCRELENGNL
EVGVHIADVSHFIRPGNALDQESARRGTTVYLCEKRIDMVPELLSSNLCS
LKCDVDRLAFSCIWEMNHNAEILKTKFTKSVINSKASLTYAEAQLRIDSA
NMNDDITTSLRGLNKLAKILKKRRIEKGALTLSSPEVRFHMDSETHDPID
LQTKELRETNSMVEEFMLLANISVAKKIHEEFSEHALLRKHPAPPPSNYE
ILVKAARSRNLEIKTDTAKSLAESLDQAESPTFPYLNTLLRILATRCMMQ
AVYFCSGMDNDFHHYGLASPIYTHFTSPIRRYADVIVHRLLAVAIGADCT
YPELTDKHKLADICKNLNFRHKMAQYAQRASVAFHTQLFFKSKGIVSEEA
YILFVRKNAIVVLIPKYGLEGTVFFEEKDKPNPQLIYDDEIPSLKIEDTV
FHVFDKVKVKIMLDSSNLQHQKIRMSLVEPQIPGISIPTDTSNMDLNGPK
KKKMKLGK

Exosome complex exonuclease RRP44 (Homo sapiens) is product of expression of DIS3 gene.

Exosome complex exonuclease RRP44 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Human dis3p, which binds to either GTP- or GDP-Ran, complements Saccharomyces cerevisiae dis3. Shiomi T, Fukushima K, Suzuki N, Nakashima N, Noguchi E, Nishimoto T J Biochem 1998-05-01 (123) 9562621
New insights into the mechanism of RNA degradation by ribonuclease II: identification of the residue responsible for setting the RNase II end product. Barbas A, Matos RG, Amblar M, Lopez-Vinas E, Gomez-Puertas P, Arraiano CM J Biol Chem 2008-05-09 (283) 18337246
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 DNA sequence and analysis of human chromosome 13. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S Nature 2004-04-01 (428) 15057823
RNA exosome depletion reveals transcription upstream of active human promoters. Preker P, Nielsen J, Kammler S, Lykke-Andersen S, Christensen MS, Mapendano CK, Schierup MH, Jensen TH Science 2008-12-19 (322) 19056938
The human core exosome interacts with differentially localized processive RNases: hDIS3 and hDIS3L. Tomecki R, Kristiansen MS, Lykke-Andersen S, Chlebowski A, Larsen KM, Szczesny RJ, Drazkowska K, Pastula A, Andersen JS, Stepien PP, Dziembowski A, Jensen TH EMBO J 2010-07-21 (29) 20531386
Initial characterization of the human central proteome. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J BMC Syst Biol 2011-01-01 (5) 21269460
The full-ORF clone resource of the German cDNA Consortium. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I BMC Genomics 2007-01-01 (8) 17974005
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
Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T DNA Res 2002-06-01 (9) 12168954
Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O DNA Res 1999-01-26 (6) 10231032
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
Dis3-like 1: a novel exoribonuclease associated with the human exosome. Staals RH, Bronkhorst AW, Schilders G, Slomovic S, Schuster G, Heck AJ, Raijmakers R, Pruijn GJ EMBO J 2010-07-21 (29) 20531389
A genomic map of a 6-Mb region at 13q21-q22 implicated in cancer development: identification and characterization of candidate genes. Rozenblum E, Vahteristo P, Sandberg T, Bergthorsson JT, Syrjakoski K, Weaver D, Haraldsson K, Johannsdottir HK, Vehmanen P, Nigam S, Golberger N, Robbins C, Pak E, Dutra A, Gillander E, Stephan DA, Bailey-Wilson J, Juo SH, Kainu T, Arason A, Barkardottir RB, Nevanlinna H, Borg A, Kallioniemi OP Hum Genet 2002-01-01 (110) 11935316



Add your own comment!


There are no comments yet.

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

Welcome stranger! Click here to login or here to register.