RPP38_HUMAN
ID RPP38_HUMAN Reviewed; 283 AA.
AC P78345; B3KPY0; D3DRT8; Q53F71; Q8NHS8;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Ribonuclease P protein subunit p38;
DE Short=RNaseP protein p38;
GN Name=RPP38;
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], PROTEIN SEQUENCE OF 24-32; 113-122 AND 212-228,
RP VARIANT VAL-114, 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], AND VARIANT GLY-181.
RC TISSUE=Skeletal muscle;
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].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-181.
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [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 FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10444065; DOI=10.1083/jcb.146.3.559;
RA Jarrous N., Wolenski J.S., Wesolowski D., Lee C., Altman S.;
RT "Localization in the nucleolus and coiled bodies of protein subunits of the
RT ribonucleoprotein ribonuclease P.";
RL J. Cell Biol. 146:559-572(1999).
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-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
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=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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-235, AND
RP IDENTIFICATION BY 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 [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:10444065, PubMed:30454648).
CC Also a component of the MRP ribonuclease complex, which cleaves pre-
CC rRNA sequences (PubMed:28115465). {ECO:0000269|PubMed:10444065,
CC ECO:0000269|PubMed:28115465, ECO:0000269|PubMed:30454648,
CC ECO:0000269|PubMed:9037013, ECO:0000269|PubMed:9630247}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:9037013, PubMed:10444065, PubMed:9630247, PubMed:16723659,
CC PubMed:30454648). RNase P consists of a catalytic RNA moiety and about
CC 10 protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25,
CC RPP30, RPP38 and RPP40 (PubMed:9037013, PubMed:9630247,
CC PubMed:10444065, PubMed:16723659, PubMed:30454648). Within the RNase P
CC complex, POP1, POP7 and RPP25 form the 'finger' subcomplex, POP5,
CC RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex, and
CC RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of the
CC RNase P complex interact with the catalytic RNA (PubMed:30454648).
CC Several subunits of RNase P are also part of the RNase MRP complex.
CC RNase MRP consists of a catalytic RNA moiety and about 8 protein
CC subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly also POP4
CC and POP5 (PubMed:16723659, PubMed:28115465).
CC {ECO:0000269|PubMed:10444065, 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 P78345; P16333: NCK1; NbExp=2; IntAct=EBI-366493, EBI-389883;
CC P78345; O95707: POP4; NbExp=3; IntAct=EBI-366493, EBI-366477;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10444065}.
CC -!- MISCELLANEOUS: Autoantibodies against RPP38 are found in sera from
CC scleroderma patients.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
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DR EMBL; U77664; AAC51142.1; -; mRNA.
DR EMBL; AK057006; BAG51842.1; -; mRNA.
DR EMBL; CR541816; CAG46615.1; -; mRNA.
DR EMBL; AK223418; BAD97138.1; -; mRNA.
DR EMBL; AL590365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86240.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86241.1; -; Genomic_DNA.
DR EMBL; BC029494; AAH29494.1; -; mRNA.
DR CCDS; CCDS7108.1; -.
DR RefSeq; NP_001091059.1; NM_001097590.2.
DR RefSeq; NP_001252530.1; NM_001265601.1.
DR RefSeq; NP_006405.2; NM_006414.4.
DR RefSeq; NP_892117.1; NM_183005.4.
DR RefSeq; XP_006717426.1; XM_006717363.1.
DR RefSeq; XP_006717427.1; XM_006717364.3.
DR RefSeq; XP_011517595.1; XM_011519293.1.
DR RefSeq; XP_016870968.1; XM_017015479.1.
DR RefSeq; XP_016870969.1; XM_017015480.1.
DR RefSeq; XP_016870970.1; XM_017015481.1.
DR PDB; 6AHR; EM; 3.92 A; C=1-283.
DR PDB; 6AHU; EM; 3.66 A; C=1-283.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; P78345; -.
DR SMR; P78345; -.
DR BioGRID; 115808; 129.
DR CORUM; P78345; -.
DR IntAct; P78345; 38.
DR STRING; 9606.ENSP00000478982; -.
DR GlyGen; P78345; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78345; -.
DR PhosphoSitePlus; P78345; -.
DR BioMuta; RPP38; -.
DR DMDM; 83305638; -.
DR EPD; P78345; -.
DR jPOST; P78345; -.
DR MassIVE; P78345; -.
DR MaxQB; P78345; -.
DR PaxDb; P78345; -.
DR PeptideAtlas; P78345; -.
DR PRIDE; P78345; -.
DR ProteomicsDB; 57576; -.
DR Antibodypedia; 25084; 116 antibodies from 21 providers.
DR DNASU; 10557; -.
DR Ensembl; ENST00000378197.5; ENSP00000367439.4; ENSG00000152464.15.
DR Ensembl; ENST00000378202.5; ENSP00000367444.5; ENSG00000152464.15.
DR Ensembl; ENST00000378203.5; ENSP00000367445.1; ENSG00000152464.15.
DR Ensembl; ENST00000616640.1; ENSP00000478982.1; ENSG00000152464.15.
DR GeneID; 10557; -.
DR KEGG; hsa:10557; -.
DR MANE-Select; ENST00000378197.5; ENSP00000367439.4; NM_183005.5; NP_892117.1.
DR UCSC; uc001inx.6; human.
DR CTD; 10557; -.
DR DisGeNET; 10557; -.
DR GeneCards; RPP38; -.
DR HGNC; HGNC:30329; RPP38.
DR HPA; ENSG00000152464; Low tissue specificity.
DR MIM; 606116; gene.
DR neXtProt; NX_P78345; -.
DR OpenTargets; ENSG00000152464; -.
DR PharmGKB; PA134957031; -.
DR VEuPathDB; HostDB:ENSG00000152464; -.
DR eggNOG; KOG3387; Eukaryota.
DR GeneTree; ENSGT00390000007526; -.
DR HOGENOM; CLU_082744_0_0_1; -.
DR InParanoid; P78345; -.
DR OMA; WLQDRTE; -.
DR OrthoDB; 1485783at2759; -.
DR PhylomeDB; P78345; -.
DR TreeFam; TF332558; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; P78345; -.
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; P78345; -.
DR BioGRID-ORCS; 10557; 628 hits in 1080 CRISPR screens.
DR ChiTaRS; RPP38; human.
DR GeneWiki; RPP38; -.
DR GenomeRNAi; 10557; -.
DR Pharos; P78345; Tbio.
DR PRO; PR:P78345; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P78345; protein.
DR Bgee; ENSG00000152464; Expressed in left testis and 200 other tissues.
DR ExpressionAtlas; P78345; baseline and differential.
DR Genevisible; P78345; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005655; C:nucleolar ribonuclease P complex; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000172; C:ribonuclease MRP complex; IEA:InterPro.
DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-EC.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR042848; Rpp38.
DR PANTHER; PTHR46948; PTHR46948; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; rRNA processing;
KW tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..283
FT /note="Ribonuclease P protein subunit p38"
FT /id="PRO_0000136783"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VARIANT 86
FT /note="I -> V (in dbSNP:rs3814171)"
FT /id="VAR_051811"
FT VARIANT 88
FT /note="E -> D (in dbSNP:rs1052157)"
FT /id="VAR_023960"
FT VARIANT 114
FT /note="A -> V (in dbSNP:rs1132078)"
FT /evidence="ECO:0000269|PubMed:9037013"
FT /id="VAR_023961"
FT VARIANT 181
FT /note="A -> G (in dbSNP:rs15772)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT /id="VAR_023962"
FT VARIANT 202
FT /note="S -> R (in dbSNP:rs12249258)"
FT /id="VAR_051812"
FT VARIANT 212
FT /note="I -> T (in dbSNP:rs10242)"
FT /id="VAR_029298"
FT VARIANT 250
FT /note="R -> G (in dbSNP:rs34040166)"
FT /id="VAR_051813"
FT CONFLICT 24
FT /note="S -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 31834 MW; 233F3397DBDE4F18 CRC64;
MAAAPQAPGR GSLRKTRPLV VKTSLNNPYI IRWSALESED MHFILQTLED RLKAIGLQKI
EDKKKKNKTP FLKKESREKC SIAVDISENL KEKKTDAKQQ VSGWTPAHVR KQLAIGVNEV
TRALERRELL LVLVCKSVKP AMITSHLIQL SLSRSVPACQ VPRLSERIAP VIGLKCVLAL
AFKKNTTDFV DEVRAIIPRV PSLSVPWLQD RIEDSGENLE TEPLESQDRE LLDTSFEDLS
KPKRKLADGR QASVTLQPLK IKKLIPNPNK IRKPPKSKKA TPK
