RPP25_HUMAN
ID RPP25_HUMAN Reviewed; 199 AA.
AC Q9BUL9; D3DW70; Q9NX88;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ribonuclease P protein subunit p25;
DE Short=RNase P protein subunit p25;
GN Name=RPP25;
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], FUNCTION, SUBUNIT, RNA-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12003489; DOI=10.1017/s1355838202027954;
RA Guerrier-Takada C., Eder P.S., Gopalan V., Altman S.;
RT "Purification and characterization of Rpp25, an RNA-binding protein subunit
RT of human ribonuclease P.";
RL RNA 8:290-295(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
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 [5]
RP IDENTIFICATION IN THE RNASE P AND RNASE MRP COMPLEXES, AND SUBUNIT.
RX PubMed=15096576; DOI=10.1093/nar/gkh539;
RA Welting T.J., van Venrooij W.J., Pruijn G.J.;
RT "Mutual interactions between subunits of the human RNase MRP
RT ribonucleoprotein complex.";
RL Nucleic Acids Res. 32:2138-2146(2004).
RN [6]
RP IDENTIFICATION IN RNASE P COMPLEX, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, 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 [8]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20215441; DOI=10.1093/nar/gkq141;
RA Hands-Taylor K.L., Martino L., Tata R., Babon J.J., Bui T.T., Drake A.F.,
RA Beavil R.L., Pruijn G.J., Brown P.R., Conte M.R.;
RT "Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a
RT prerequisite for interaction with the P3 arm of RNase MRP RNA.";
RL Nucleic Acids Res. 38:4052-4066(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-182, AND
RP IDENTIFICATION BY 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 [10]
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 [11]
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 [12] {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).
RN [13] {ECO:0007744|PDB:6CWX}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH POP7, SUBUNIT, AND
RP RNA-BINDING.
RX PubMed=29625199; DOI=10.1016/j.jmb.2018.03.029;
RA Chan C.W., Kiesel B.R., Mondragon A.;
RT "Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation
RT of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.";
RL J. Mol. Biol. 430:1403-1416(2018).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends
CC (PubMed:12003489, PubMed:16723659, PubMed:30454648). Also a component
CC of the MRP ribonuclease complex, which cleaves pre-rRNA sequences
CC (PubMed:28115465). {ECO:0000269|PubMed:12003489,
CC ECO:0000269|PubMed:16723659, ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:12003489, PubMed:15096576, PubMed:16723659, PubMed:20215441,
CC PubMed:28115465, PubMed:30454648). RNase P consists of a catalytic RNA
CC moiety and 10 different protein chains; POP1, POP4, POP5, POP7, RPP14,
CC RPP21, RPP25, RPP30, RPP38 and RPP40 (PubMed:12003489, PubMed:16723659,
CC PubMed:20215441, PubMed:30454648). Within the RNase P complex, POP1,
CC POP7 and RPP25 form the 'finger' subcomplex, POP5, RPP14, RPP40 and
CC homodimeric RPP30 form the 'palm' subcomplex, and RPP21, POP4 and RPP38
CC form the 'wrist' subcomplex. All subunits of the RNase P complex
CC interact with the catalytic RNA (PubMed:30454648). Several subunits of
CC RNase P are also part of the RNase MRP complex. RNase MRP consists of a
CC catalytic RNA moiety and about 8 protein subunits; POP1, POP7, RPP25,
CC RPP30, RPP38, RPP40 and possibly also POP4 and POP5 (PubMed:15096576,
CC PubMed:16723659, PubMed:28115465). POP7 forms a heterodimer with RPP25
CC that binds to the P3 stem loop of the catalytic RNA (PubMed:20215441,
CC PubMed:29625199). {ECO:0000269|PubMed:12003489,
CC ECO:0000269|PubMed:15096576, ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:20215441, ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:29625199, ECO:0000269|PubMed:30454648}.
CC -!- INTERACTION:
CC Q9BUL9; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-366570, EBI-11096309;
CC Q9BUL9; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-366570, EBI-1642333;
CC Q9BUL9; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-366570, EBI-11524452;
CC Q9BUL9; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-366570, EBI-748248;
CC Q9BUL9; O75190: DNAJB6; NbExp=3; IntAct=EBI-366570, EBI-1053164;
CC Q9BUL9; Q01658: DR1; NbExp=3; IntAct=EBI-366570, EBI-750300;
CC Q9BUL9; P35637: FUS; NbExp=3; IntAct=EBI-366570, EBI-400434;
CC Q9BUL9; Q00403: GTF2B; NbExp=3; IntAct=EBI-366570, EBI-389564;
CC Q9BUL9; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-366570, EBI-1054873;
CC Q9BUL9; P19012: KRT15; NbExp=3; IntAct=EBI-366570, EBI-739566;
CC Q9BUL9; O95751: LDOC1; NbExp=3; IntAct=EBI-366570, EBI-740738;
CC Q9BUL9; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-366570, EBI-12003882;
CC Q9BUL9; Q5S007: LRRK2; NbExp=3; IntAct=EBI-366570, EBI-5323863;
CC Q9BUL9; Q96CV9: OPTN; NbExp=3; IntAct=EBI-366570, EBI-748974;
CC Q9BUL9; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-366570, EBI-350517;
CC Q9BUL9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-366570, EBI-79165;
CC Q9BUL9; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-366570, EBI-302345;
CC Q9BUL9; Q99575: POP1; NbExp=2; IntAct=EBI-366570, EBI-366741;
CC Q9BUL9; O95707: POP4; NbExp=3; IntAct=EBI-366570, EBI-366477;
CC Q9BUL9; Q969H6: POP5; NbExp=2; IntAct=EBI-366570, EBI-366525;
CC Q9BUL9; O75817: POP7; NbExp=8; IntAct=EBI-366570, EBI-366574;
CC Q9BUL9; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-366570, EBI-740343;
CC Q9BUL9; O95059: RPP14; NbExp=2; IntAct=EBI-366570, EBI-366542;
CC Q9BUL9; P21673: SAT1; NbExp=8; IntAct=EBI-366570, EBI-711613;
CC Q9BUL9; Q15427: SF3B4; NbExp=3; IntAct=EBI-366570, EBI-348469;
CC Q9BUL9; P00441: SOD1; NbExp=3; IntAct=EBI-366570, EBI-990792;
CC Q9BUL9; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-366570, EBI-750109;
CC Q9BUL9; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-366570, EBI-11962468;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12003489,
CC ECO:0000269|PubMed:20215441}.
CC -!- SIMILARITY: Belongs to the histone-like Alba family. {ECO:0000305}.
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DR EMBL; AY034074; AAK54443.1; -; mRNA.
DR EMBL; AK000381; BAA91128.1; -; mRNA.
DR EMBL; CH471136; EAW99285.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99286.1; -; Genomic_DNA.
DR EMBL; BC002497; AAH02497.1; -; mRNA.
DR EMBL; BC007270; AAH07270.1; -; mRNA.
DR CCDS; CCDS10274.1; -.
DR RefSeq; NP_060263.2; NM_017793.2.
DR PDB; 6AHR; EM; 3.92 A; F=1-199.
DR PDB; 6AHU; EM; 3.66 A; F=1-199.
DR PDB; 6CWX; X-ray; 2.25 A; B=1-199.
DR PDB; 6LT7; X-ray; 2.70 A; B/E=2-199.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR PDBsum; 6CWX; -.
DR PDBsum; 6LT7; -.
DR AlphaFoldDB; Q9BUL9; -.
DR SMR; Q9BUL9; -.
DR BioGRID; 120255; 53.
DR CORUM; Q9BUL9; -.
DR IntAct; Q9BUL9; 42.
DR STRING; 9606.ENSP00000317691; -.
DR iPTMnet; Q9BUL9; -.
DR PhosphoSitePlus; Q9BUL9; -.
DR BioMuta; RPP25; -.
DR DMDM; 74733233; -.
DR EPD; Q9BUL9; -.
DR jPOST; Q9BUL9; -.
DR MassIVE; Q9BUL9; -.
DR MaxQB; Q9BUL9; -.
DR PaxDb; Q9BUL9; -.
DR PeptideAtlas; Q9BUL9; -.
DR PRIDE; Q9BUL9; -.
DR ProteomicsDB; 79109; -.
DR Antibodypedia; 50450; 94 antibodies from 23 providers.
DR DNASU; 54913; -.
DR Ensembl; ENST00000322177.6; ENSP00000317691.6; ENSG00000178718.7.
DR GeneID; 54913; -.
DR KEGG; hsa:54913; -.
DR MANE-Select; ENST00000322177.6; ENSP00000317691.6; NM_017793.3; NP_060263.2.
DR UCSC; uc002azj.2; human.
DR CTD; 54913; -.
DR DisGeNET; 54913; -.
DR GeneCards; RPP25; -.
DR HGNC; HGNC:30361; RPP25.
DR HPA; ENSG00000178718; Low tissue specificity.
DR MIM; 619235; gene.
DR neXtProt; NX_Q9BUL9; -.
DR OpenTargets; ENSG00000178718; -.
DR PharmGKB; PA134990737; -.
DR VEuPathDB; HostDB:ENSG00000178718; -.
DR eggNOG; KOG2567; Eukaryota.
DR GeneTree; ENSGT00390000002564; -.
DR HOGENOM; CLU_096311_0_0_1; -.
DR InParanoid; Q9BUL9; -.
DR OMA; CGRAVTK; -.
DR OrthoDB; 1075123at2759; -.
DR PhylomeDB; Q9BUL9; -.
DR TreeFam; TF325688; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; Q9BUL9; -.
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; Q9BUL9; -.
DR BioGRID-ORCS; 54913; 22 hits in 1080 CRISPR screens.
DR GenomeRNAi; 54913; -.
DR Pharos; Q9BUL9; Tbio.
DR PRO; PR:Q9BUL9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BUL9; protein.
DR Bgee; ENSG00000178718; Expressed in vena cava and 177 other tissues.
DR Genevisible; Q9BUL9; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000172; C:ribonuclease MRP complex; IDA:FlyBase.
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: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 DisProt; DP02616; -.
DR Gene3D; 3.30.110.20; -; 1.
DR InterPro; IPR036882; Alba-like_dom_sf.
DR InterPro; IPR002775; DNA/RNA-bd_Alba-like.
DR InterPro; IPR040207; Rpp25.
DR PANTHER; PTHR13516:SF5; PTHR13516:SF5; 1.
DR Pfam; PF01918; Alba; 1.
DR SUPFAM; SSF82704; SSF82704; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW rRNA processing; tRNA processing.
FT CHAIN 1..199
FT /note="Ribonuclease P protein subunit p25"
FT /id="PRO_0000237582"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CONFLICT 73
FT /note="A -> V (in Ref. 2; BAA91128)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6LT7"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6CWX"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 92..105
FT /evidence="ECO:0007829|PDB:6CWX"
FT STRAND 127..142
FT /evidence="ECO:0007829|PDB:6CWX"
SQ SEQUENCE 199 AA; 20632 MW; 9A4494F0297B2A81 CRC64;
MENFRKVRSE EAPAGCGAEG GGPGSGPFAD LAPGAVHMRV KEGSKIRNLM AFATASMAQP
ATRAIVFSGC GRATTKTVTC AEILKRRLAG LHQVTRLRYR SVREVWQSLP PGPTQGQTPG
EPAASLSVLK NVPGLAILLS KDALDPRQPG YQPPNPHPGP SSPPAAPASK RSLGEPAAGE
GSAKRSQPEP GVADEDQTA
