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 24-JAN-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-9626; -. DR EMDB; EMD-9627; -. DR SMR; P78346; -. DR BioGRID; 115807; 115. DR ComplexPortal; CPX-2876; Ribonuclease MRP complex. DR ComplexPortal; CPX-2877; Nucleolar ribonuclease P complex. DR CORUM; P78346; -. DR IntAct; P78346; 36. DR MINT; P78346; -. DR STRING; 9606.ENSP00000389182; -. DR GlyGen; P78346; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000389182; -. DR PeptideAtlas; P78346; -. DR ProteomicsDB; 19113; -. DR ProteomicsDB; 57577; -. [P78346-1] DR Pumba; P78346; -. DR TopDownProteomics; P78346-1; -. [P78346-1] DR Antibodypedia; 16338; 96 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 AGR; HGNC:17688; -. 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; CYGPGIT; -. DR OrthoDB; 10501at2759; -. 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; 659 hits in 1159 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 primordial germ cell in gonad and 211 other cell types or tissues. DR ExpressionAtlas; P78346; baseline and differential. 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: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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR InterPro; IPR002738; RNase_P_p30. DR PANTHER; PTHR13031:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P30; 1. DR PANTHER; PTHR13031; RIBONUCLEASE P SUBUNIT P30; 1. DR Pfam; PF01876; RNase_P_p30; 1. DR SUPFAM; SSF89550; PHP domain-like; 1. DR Genevisible; P78346; HS. 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 //