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Ribonuclease P protein subunit p14

 
Known abbreviations: Rpp14

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 p14 is involved: Pathways in which Ribonuclease P protein subunit p14 is involved:

NCBI GI number(s): 149192851
153791326
388240817
5902066
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O95059 O95059
BRENDA - -
KEGG hsa:11102 hsa:11102
PFAM: PF01900
PF01900
InterPro: - O95059 (Link - using uniprot id)
CATH: - -
SCOP: - -


Protein sequence:
MENFRKVRSEEAPAGCGAEGGGPGSGPFADLAPGAVHMRVKEGSKIRNLM
AFATASMAQPATRAIVFSGCGRATTKTVTCAEILKRRLAGLHQVTRLRYR
SVREVWQSLPPGPTQGQTPGEPAASLSVLKNVPGLAILLSKDALDPRQPG
YQPPNPHPGPSSPPAAPASKRSLGEPAAGEGSAKRSQPEPGVADEDQTA

Ribonuclease P protein subunit p14 (Homo sapiens) is product of expression of Rpp14 gene.

Ribonuclease P protein subunit p14 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
Rpp14 and Rpp29, two protein subunits of human ribonuclease P. Jarrous N, Eder PS, Wesolowski D, Altman S RNA 1999-01-01 (5) 10024167
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
An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing. Autio KJ, Kastaniotis AJ, Pospiech H, Miinalainen IJ, Schonauer MS, Dieckmann CL, Hiltunen JK FASEB J 2008-01-01 (22) 17898086



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Last modification of this entry: 2012-04-04 09:35:29
Edited by a user: kaja
Edited content: Changed publications.

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