RPP30_HUMAN
ID RPP30_HUMAN Reviewed; 268 AA.
AC P78346; B2R799; E9PB02;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ribonuclease P protein subunit p30;
DE Short=RNaseP protein p30;
DE AltName: Full=RNase P subunit 2;
GN Name=RPP30; Synonyms=RNASEP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 21-30; 140-148
RP AND 185-198, FUNCTION, AND SUBUNIT.
RX PubMed=9037013; DOI=10.1073/pnas.94.4.1101;
RA Eder P.S., Kekuda R., Stolc V., Altman S.;
RT "Characterization of two scleroderma autoimmune antigens that copurify with
RT human ribonuclease P.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1101-1106(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Signet-ring cell carcinoma;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-10; 99-108; 139-161; 184-198 AND 237-246, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Lao L., Ryan K.M.;
RL Submitted (JUN-2009) to UniProtKB.
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9630247;
RA Jarrous N., Eder P.S., Guerrier-Takada C., Hoog C., Altman S.;
RT "Autoantigenic properties of some protein subunits of catalytically active
RT complexes of human ribonuclease P.";
RL RNA 4:407-417(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION IN RNASE P AND MRP COMPLEXES, AND SUBUNIT.
RX PubMed=16723659; DOI=10.1261/rna.2293906;
RA Welting T.J., Kikkert B.J., van Venrooij W.J., Pruijn G.J.;
RT "Differential association of protein subunits with the human RNase MRP and
RT RNase P complexes.";
RL RNA 12:1373-1382(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [19]
RP FUNCTION, AND SUBUNIT.
RX PubMed=28115465; DOI=10.1101/gad.286963.116;
RA Goldfarb K.C., Cech T.R.;
RT "Targeted CRISPR disruption reveals a role for RNase MRP RNA in human
RT preribosomal RNA processing.";
RL Genes Dev. 31:59-71(2017).
RN [20] {ECO:0007744|PDB:6AHR, ECO:0007744|PDB:6AHU}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.66 ANGSTROMS) OF RNASE P HOLOENZYME IN
RP COMPLEX WITH TRNA, FUNCTION, AND SUBUNIT.
RX PubMed=30454648; DOI=10.1016/j.cell.2018.10.003;
RA Wu J., Niu S., Tan M., Huang C., Li M., Song Y., Wang Q., Chen J., Shi S.,
RA Lan P., Lei M.;
RT "Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.";
RL Cell 175:1393-1404.e11(2018).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends
CC (PubMed:9037013, PubMed:9630247, PubMed:30454648). Also a component of
CC the MRP ribonuclease complex, which cleaves pre-rRNA sequences
CC (PubMed:28115465). {ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648, ECO:0000269|PubMed:9037013,
CC ECO:0000269|PubMed:9630247}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:9037013, PubMed:9630247, PubMed:16723659, PubMed:30454648).
CC RNase P consists of a catalytic RNA moiety and about 10 protein
CC subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and
CC RPP40 (PubMed:9037013, PubMed:9630247, PubMed:16723659,
CC PubMed:30454648). Within the RNase P complex, POP1, POP7 and RPP25 form
CC the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form
CC the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist'
CC subcomplex. All subunits of the RNase P complex interact with the
CC catalytic RNA (PubMed:30454648). Several subunits of RNase P are also
CC part of the RNase MRP complex. RNase MRP consists of a catalytic RNA
CC moiety and about 8 protein subunits; POP1, POP7, RPP25, RPP30, RPP38,
CC RPP40 and possibly also POP4 and POP5 (PubMed:16723659,
CC PubMed:28115465). {ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648,
CC ECO:0000269|PubMed:9037013, ECO:0000269|PubMed:9630247}.
CC -!- INTERACTION:
CC P78346; Q9NP66: HMG20A; NbExp=11; IntAct=EBI-366553, EBI-740641;
CC P78346; Q969H6: POP5; NbExp=7; IntAct=EBI-366553, EBI-366525;
CC P78346; O95059: RPP14; NbExp=5; IntAct=EBI-366553, EBI-366542;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P78346-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78346-2; Sequence=VSP_045673;
CC -!- MISCELLANEOUS: Autoantibodies against RPP30 are found in sera from
CC scleroderma patients.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 3 family. {ECO:0000305}.
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DR EMBL; U77665; AAC51143.1; -; mRNA.
DR EMBL; AK312900; BAG35746.1; -; mRNA.
DR EMBL; AK225532; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL590622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW50117.1; -; Genomic_DNA.
DR EMBL; BC006991; AAH06991.1; -; mRNA.
DR CCDS; CCDS44458.1; -. [P78346-2]
DR CCDS; CCDS7411.1; -. [P78346-1]
DR RefSeq; NP_001098016.1; NM_001104546.1. [P78346-2]
DR RefSeq; NP_006404.1; NM_006413.4. [P78346-1]
DR RefSeq; XP_011537422.1; XM_011539120.2.
DR RefSeq; XP_011537423.1; XM_011539121.2.
DR RefSeq; XP_016870964.1; XM_017015475.1.
DR RefSeq; XP_016870966.1; XM_017015477.1.
DR PDB; 6AHR; EM; 3.92 A; I/J=1-268.
DR PDB; 6AHU; EM; 3.66 A; I/J=1-268.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; P78346; -.
DR SMR; P78346; -.
DR BioGRID; 115807; 93.
DR CORUM; P78346; -.
DR IntAct; P78346; 35.
DR MINT; P78346; -.
DR STRING; 9606.ENSP00000389182; -.
DR iPTMnet; P78346; -.
DR PhosphoSitePlus; P78346; -.
DR SwissPalm; P78346; -.
DR BioMuta; RPP30; -.
DR EPD; P78346; -.
DR jPOST; P78346; -.
DR MassIVE; P78346; -.
DR MaxQB; P78346; -.
DR PaxDb; P78346; -.
DR PeptideAtlas; P78346; -.
DR PRIDE; P78346; -.
DR ProteomicsDB; 19113; -.
DR ProteomicsDB; 57577; -. [P78346-1]
DR TopDownProteomics; P78346-1; -. [P78346-1]
DR Antibodypedia; 16338; 83 antibodies from 21 providers.
DR DNASU; 10556; -.
DR Ensembl; ENST00000371703.8; ENSP00000360768.3; ENSG00000148688.14. [P78346-1]
DR Ensembl; ENST00000413330.5; ENSP00000389182.1; ENSG00000148688.14. [P78346-2]
DR GeneID; 10556; -.
DR KEGG; hsa:10556; -.
DR MANE-Select; ENST00000371703.8; ENSP00000360768.3; NM_006413.5; NP_006404.1.
DR UCSC; uc009xtx.4; human. [P78346-1]
DR CTD; 10556; -.
DR GeneCards; RPP30; -.
DR HGNC; HGNC:17688; RPP30.
DR HPA; ENSG00000148688; Low tissue specificity.
DR MIM; 606115; gene.
DR neXtProt; NX_P78346; -.
DR OpenTargets; ENSG00000148688; -.
DR PharmGKB; PA134876345; -.
DR VEuPathDB; HostDB:ENSG00000148688; -.
DR eggNOG; KOG2363; Eukaryota.
DR GeneTree; ENSGT00390000000883; -.
DR InParanoid; P78346; -.
DR OMA; PWDVINL; -.
DR OrthoDB; 1197518at2759; -.
DR PhylomeDB; P78346; -.
DR TreeFam; TF106113; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; P78346; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; P78346; -.
DR BioGRID-ORCS; 10556; 627 hits in 1081 CRISPR screens.
DR ChiTaRS; RPP30; human.
DR GeneWiki; RPP30; -.
DR GenomeRNAi; 10556; -.
DR Pharos; P78346; Tbio.
DR PRO; PR:P78346; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P78346; protein.
DR Bgee; ENSG00000148688; Expressed in ventricular zone and 209 other tissues.
DR ExpressionAtlas; P78346; baseline and differential.
DR Genevisible; P78346; HS.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:FlyBase.
DR GO; GO:0004526; F:ribonuclease P activity; TAS:ProtInc.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR002738; RNase_P_p30.
DR PANTHER; PTHR13031; PTHR13031; 1.
DR Pfam; PF01876; RNase_P_p30; 1.
DR SUPFAM; SSF89550; SSF89550; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..268
FT /note="Ribonuclease P protein subunit p30"
FT /id="PRO_0000140031"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 266..268
FT /note="CEG -> WSHSVTQAGVQWHNLGSLQPLPLGLKPSSHLSLPRTRIQQRQLLI
FT SHQRDHTPKNRL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_045673"
FT VARIANT 12
FT /note="G -> D (in dbSNP:rs11544145)"
FT /id="VAR_051870"
FT CONFLICT 65
FT /note="Q -> R (in Ref. 3; AK225532)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT P78346-2:291
FT /note="K -> R (in Ref. 3; AK225532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 29321 MW; 2AB492D98ACDCCBB CRC64;
MAVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT
LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL
DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC
KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG
IISTVKKPRP SEGDEDCLPA SKKAKCEG
