RRP6/YOR001W Protein Information Help

Standard Name Rrp6p 1
Systematic Name Yor001wp
ORF Classification Verified
Description Nuclear exosome exonuclease component; has 3'-5' exonuclease activity; involved in RNA processing, maturation, surveillance, degradation, tethering, and export; has similarity to E. coli RNase D and to human PM-Sc1 100 (EXOSC10); mutant displays reduced transcription elongation in the G-less-based run-on (GLRO) assay (1, 2, 3, 4, 5, 6, 7)
Name Description Ribosomal RNA Processing 1
Experimental Data
Molecules/cell 2160 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 733
Molecular Weight (Da) 84,038
Isoelectric Point (pI) 7.14

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Rrp6p (InterPro)
Physical Interactions There are 140 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052F38 | Q12149
MIPS: YOR001W
NCBI: 112491261 | 112491264 | 112491267 | 112491277 | 1150996 | 14195186 | 1420088 | 448262643 | 51013151 | 6324574 | NP_014643.1
GenBank/EMBL/DDBJ: DAA10783.1 | AY692850 | U43491 | Z74909
External Classifications EC: 3.1.13.- [Exoribonucleases Producing 5'-Phosphomonoesters]
Amino Acid Sequence (or in FASTA format)
 
       1  MTSENPDVLL SRVINVVRAA SSLASQDVDF YKNLDRGFSK DLKSKADKLA
      51  DMANEIILSI DEHHESFELK EEDISDLWNN FGNIMDNLLE MSDHSLDKLN
     101  CAINSKSRGS DLQYLGEFSG KNFSPTKRVE KPQLKFKSPI DNSESHPFIP
     151  LLKEKPNALK PLSESLRLVD DDENNPSHYP HPYEYEIDHQ EYSPEILQIR
     201  EEIPSKSWDD SVPIWVDTST ELESMLEDLK NTKEIAVDLE HHDYRSYYGI
     251  VCLMQISTRE RDYLVDTLKL RENLHILNEV FTNPSIVKVF HGAFMDIIWL
     301  QRDLGLYVVG LFDTYHASKA IGLPRHSLAY LLENFANFKT SKKYQLADWR
     351  IRPLSKPMTA YARADTHFLL NIYDQLRNKL IESNKLAGVL YESRNVAKRR
     401  FEYSKYRPLT PSSEVYSPIE KESPWKILMY QYNIPPEREV LVRELYQWRD
     451  LIARRDDESP RFVMPNQLLA ALVAYTPTDV IGVVSLTNGV TEHVRQNAKL
     501  LANLIRDALR NIKNTNEEAT PIPSSETKAD GILLETISVP QIRDVMERFS
     551  VLCNSNISKS RAKPVTNSSI LLGKILPREE HDIAYSKDGL PNKVKTEDIR
     601  IRAQNFKSAL ANLEDIIFEI EKPLVVPVKL EEIKTVDPAS APNHSPEIDN
     651  LDDLVVLKKK NIQKKQPAKE KGVTEKDAVD YSKIPNILSN KPGQNNRQQK
     701  KRRFDPSSSD SNGPRAAKKR RPAAKGKNLS FKR*

external links for Rrp6p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Rrp6p
1) Briggs MW, et al.  (1998) Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem 273(21):13255-63
2) Burkard KT and Butler JS  (2000) A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol 20(2):604-16
3) Hilleren P, et al.  (2001) Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 413(6855):538-42
4) Bousquet-Antonelli C, et al.  (2000) Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102(6):765-75
5) Hieronymus H, et al.  (2004) Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev 18(21):2652-62
6) Vodala S, et al.  (2008) The nuclear exosome and adenylation regulate posttranscriptional tethering of yeast GAL genes to the nuclear periphery. Mol Cell 31(1):104-13
7) Tous C, et al.  (2011) A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors. EMBO J 30(10):1953-64
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41