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Ribonuclease P protein subunit p38

 
Known abbreviations: RPP38

FUNCTION:

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus.

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. RPP38 is probably a dimer.

CELLULAR LOCALIZATION:

Nucleus › nucleolus (Potential).



This protein can be a part of a given complexes: Activities in which Ribonuclease P protein subunit p38 is involved: Pathways in which Ribonuclease P protein subunit p38 is involved:

NCBI GI number(s): 148222745
148222744
148238078
148238077
33859837
147899154
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P78345 P78345
BRENDA - -
KEGG hsa:10557 hsa:10557
PFAM: PF01248
PF01248
InterPro: IPR004038
IPR004038
CATH: - -
SCOP: - -


Protein sequence:
MAAAPQAPGRGSLRKTRPLVVKTSLNNPYIIRWSALESEDMHFILQTLED
RLKAIGLQKIEDKKKKNKTPFLKKESREKCSIAVDISENLKEKKTDAKQQ
VSGWTPAHVRKQLAIGVNEVTRALERRELLLVLVCKSVKPAMITSHLIQL
SLSRSVPACQVPRLSERIAPVIGLKCVLALAFKKNTTDFVDEVRAIIPRV
PSLSVPWLQDRIEDSGENLETEPLESQDRELLDTSFEDLSKPKRKLADGR
QASVTLQPLKIKKLIPNPNKIRKPPKSKKATPK

Ribonuclease P protein subunit p38 (Homo sapiens) is product of expression of Rpp38 gene.

Ribonuclease P protein subunit p38 (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
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
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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Entry added on: 2012-04-04 10:17:24, by a user: kaja

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