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Ribonuclease P protein subunit p30

 
Known also as: RNase P subunit 2

Known abbreviations: RPP30, RNASEP2

FUNCTION:

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.

CATALYTIC ACTIVITY:

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

SUBUNIT STRUCTURE:

RNase P consists of a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.

CELLULAR LOCALIZATION:

Nucleus › nucleolus (Potential).



This protein can be a part of a given complexes: Activities in which Ribonuclease P protein subunit p30 is involved: Pathways in which Ribonuclease P protein subunit p30 is involved:

NCBI GI number(s): 157151755
157151754
157151752
5454024
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P78346 P78346
BRENDA - -
KEGG hsa:10556 hsa:10556
PFAM: PF01876
PF01876
InterPro: - P78346 (Link - using uniprot id)
CATH: - -
SCOP: - -


Protein sequence:
MAVFADLDLRAGSDLKALRGLVETAAHLGYSVVAINHIVDFKEKKQEIEK
PVAVSELFTTLPIVQGKSRPIKILTRLTIIVSDPSHCNVLRATSSRARLY
DVVAVFPKTEKLFHIACTHLDVDLVCITVTEKLPFYFKRPPINVAIDRGL
AFELVYSPAIKDSTMRRYTISSALNLMQICKGKNVIISSAAERPLEIRGP
YDVANLGLLFGLSESDAKAAVSTNCRAALLHGETRKTAFGIISTVKKPRP
SEGDEDCLPASKKAKCEG

Ribonuclease P protein subunit p30 (Homo sapiens) is product of expression of Rpp30 gene.

Ribonuclease P protein subunit p30 (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal Publication date (Issue) PubMed ID
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
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell 2006-11-03 (127) 17081983
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
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal 2009-01-01 (2) 19690332
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd J Proteome Res 2008-03-01 (7) 18220336
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
Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P. Eder PS, Kekuda R, Stolc V, Altman S Proc Natl Acad Sci U S A 1997-01-18 (94) 9037013
The DNA sequence and comparative analysis of human chromosome 10. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C Nature 2004-05-27 (429) 15164054



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Last modification of this entry: 2012-04-04 10:37:41
Edited by a user: kaja
Edited content: Changed interacting_proteins.

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