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Ribonuclease P protein subunit p25

 
Known abbreviations: RPP25

FUNCTION:

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA.

CATALYTIC ACTIVITY:

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

SUBUNIT STRUCTURE:

Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. Interacts with the P3 domain of RNase MRP complex. RNase MRP consists of a RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21.

CELLULAR LOCALIZATION:

Nucleus.



This protein can be a part of a given complexes: Activities in which Ribonuclease P protein subunit p25 is involved: Pathways in which Ribonuclease P protein subunit p25 is involved:

NCBI GI number(s): 93277074
93277073
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9BUL9 Q9BUL9
BRENDA - -
KEGG hsa:54913 hsa:54913
PFAM: PF01918
PF01918
InterPro: IPR002775
IPR002775
CATH: - -
SCOP: - -


Protein sequence:
MENFRKVRSEEAPAGCGAEGGGPGSGPFADLAPGAVHMRVKEGSKIRNLM
AFATASMAQPATRAIVFSGCGRATTKTVTCAEILKRRLAGLHQVTRLRYR
SVREVWQSLPPGPTQGQTPGEPAASLSVLKNVPGLAILLSKDALDPRQPG
YQPPNPHPGPSSPPAAPASKRSLGEPAAGEGSAKRSQPEPGVADEDQTA

Ribonuclease P protein subunit p25 (Homo sapiens) is product of expression of Rpp25 gene.

Ribonuclease P protein subunit p25 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Purification and characterization of Rpp25, an RNA-binding protein subunit of human ribonuclease P. Guerrier-Takada C, Eder PS, Gopalan V, Altman S RNA 2002-03-01 (8) 12003489
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
Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex. Welting TJ, van Venrooij WJ, Pruijn GJ Nucleic Acids Res 2004-01-01 (32) 15096576
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
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
Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A Proc Natl Acad Sci U S A 2007-01-13 (104) 17287340



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Entry added on: 2012-04-04 10:03:54, by a user: kaja

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