POP5_HUMAN
ID POP5_HUMAN Reviewed; 163 AA.
AC Q969H6; A6NL80; Q53FS5; Q9Y2Q6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ribonuclease P/MRP protein subunit POP5;
DE Short=hPop5;
GN Name=POP5; ORFNames=AD-008, HSPC004, x0003;
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), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11413139; DOI=10.1074/jbc.m103399200;
RA van Eenennaam H., Lugtenberg D., Vogelzangs J.H.P., van Venrooij W.J.,
RA Pruijn G.J.M.;
RT "hPop5, a protein subunit of the human RNase MRP and RNase P
RT endoribonucleases.";
RL J. Biol. Chem. 276:31635-31641(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [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-154, 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 FUNCTION.
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 [18] {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 protein complex that generates
CC mature tRNA molecules by cleaving their 5'-ends (PubMed:11413139,
CC PubMed:30454648). Also a component of the MRP ribonuclease complex,
CC which cleaves pre-rRNA sequences (PubMed:28115465).
CC {ECO:0000269|PubMed:11413139, ECO:0000269|PubMed:28115465,
CC ECO:0000269|PubMed:30454648}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:11413139, PubMed:15096576, PubMed:16723659, PubMed:30454648).
CC RNase P consists of a catalytic RNA moiety and 10 different protein
CC chains; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and
CC RPP40 (PubMed:11413139, PubMed:15096576, 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:11413139,
CC PubMed:15096576, PubMed:16723659). {ECO:0000269|PubMed:11413139,
CC ECO:0000269|PubMed:15096576, ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:30454648}.
CC -!- INTERACTION:
CC Q969H6; Q13554: CAMK2B; NbExp=3; IntAct=EBI-366525, EBI-1058722;
CC Q969H6; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-366525, EBI-10171570;
CC Q969H6; Q9C0F1: CEP44; NbExp=6; IntAct=EBI-366525, EBI-744115;
CC Q969H6; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-366525, EBI-10303987;
CC Q969H6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-366525, EBI-6509505;
CC Q969H6; O76011: KRT34; NbExp=3; IntAct=EBI-366525, EBI-1047093;
CC Q969H6; Q6A162: KRT40; NbExp=3; IntAct=EBI-366525, EBI-10171697;
CC Q969H6; O14561: NDUFAB1; NbExp=3; IntAct=EBI-366525, EBI-1246261;
CC Q969H6; O95707: POP4; NbExp=3; IntAct=EBI-366525, EBI-366477;
CC Q969H6; Q04864: REL; NbExp=3; IntAct=EBI-366525, EBI-307352;
CC Q969H6; Q9BUL9: RPP25; NbExp=2; IntAct=EBI-366525, EBI-366570;
CC Q969H6; P78346: RPP30; NbExp=7; IntAct=EBI-366525, EBI-366553;
CC Q969H6; Q13077: TRAF1; NbExp=6; IntAct=EBI-366525, EBI-359224;
CC Q969H6; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-366525, EBI-739895;
CC Q969H6; P14079: tax; Xeno; NbExp=3; IntAct=EBI-366525, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11413139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969H6-2; Sequence=VSP_042733;
CC -!- MISCELLANEOUS: The last C-terminal 19 amino acids are not required for
CC complex association and RNase activity.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000305}.
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DR EMBL; AJ306296; CAC59822.1; -; mRNA.
DR EMBL; AF117232; AAF17213.1; -; mRNA.
DR EMBL; AF070660; AAD20966.1; -; mRNA.
DR EMBL; AK303144; BAG64248.1; -; mRNA.
DR EMBL; AK223206; BAD96926.1; -; mRNA.
DR EMBL; AC063943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98206.1; -; Genomic_DNA.
DR EMBL; BC012505; AAH12505.1; -; mRNA.
DR CCDS; CCDS9202.1; -. [Q969H6-1]
DR CCDS; CCDS9203.1; -. [Q969H6-2]
DR RefSeq; NP_057002.2; NM_015918.3. [Q969H6-1]
DR RefSeq; NP_937845.1; NM_198202.1. [Q969H6-2]
DR PDB; 6AHR; EM; 3.92 A; E=1-163.
DR PDB; 6AHU; EM; 3.66 A; E=1-163.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; Q969H6; -.
DR SMR; Q969H6; -.
DR BioGRID; 119502; 34.
DR CORUM; Q969H6; -.
DR IntAct; Q969H6; 20.
DR MINT; Q969H6; -.
DR STRING; 9606.ENSP00000350098; -.
DR iPTMnet; Q969H6; -.
DR PhosphoSitePlus; Q969H6; -.
DR BioMuta; POP5; -.
DR DMDM; 74731042; -.
DR EPD; Q969H6; -.
DR jPOST; Q969H6; -.
DR MassIVE; Q969H6; -.
DR MaxQB; Q969H6; -.
DR PaxDb; Q969H6; -.
DR PeptideAtlas; Q969H6; -.
DR PRIDE; Q969H6; -.
DR ProteomicsDB; 75765; -. [Q969H6-1]
DR ProteomicsDB; 75766; -. [Q969H6-2]
DR Antibodypedia; 45552; 51 antibodies from 17 providers.
DR DNASU; 51367; -.
DR Ensembl; ENST00000341039.6; ENSP00000341791.2; ENSG00000167272.11. [Q969H6-2]
DR Ensembl; ENST00000357500.5; ENSP00000350098.4; ENSG00000167272.11. [Q969H6-1]
DR GeneID; 51367; -.
DR KEGG; hsa:51367; -.
DR MANE-Select; ENST00000357500.5; ENSP00000350098.4; NM_015918.4; NP_057002.2.
DR UCSC; uc001tys.3; human. [Q969H6-1]
DR CTD; 51367; -.
DR DisGeNET; 51367; -.
DR GeneCards; POP5; -.
DR HGNC; HGNC:17689; POP5.
DR HPA; ENSG00000167272; Low tissue specificity.
DR MIM; 609992; gene.
DR neXtProt; NX_Q969H6; -.
DR OpenTargets; ENSG00000167272; -.
DR PharmGKB; PA128394660; -.
DR VEuPathDB; HostDB:ENSG00000167272; -.
DR eggNOG; KOG4639; Eukaryota.
DR GeneTree; ENSGT00390000012331; -.
DR HOGENOM; CLU_2132628_0_0_1; -.
DR InParanoid; Q969H6; -.
DR OMA; FLDRAMG; -.
DR OrthoDB; 1492689at2759; -.
DR PhylomeDB; Q969H6; -.
DR TreeFam; TF317496; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; Q969H6; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q969H6; -.
DR BioGRID-ORCS; 51367; 762 hits in 1084 CRISPR screens.
DR ChiTaRS; POP5; human.
DR GeneWiki; POP5; -.
DR GenomeRNAi; 51367; -.
DR Pharos; Q969H6; Tbio.
DR PRO; PR:Q969H6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q969H6; protein.
DR Bgee; ENSG00000167272; Expressed in mucosa of transverse colon and 203 other tissues.
DR Genevisible; Q969H6; 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:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR Gene3D; 3.30.70.3250; -; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR016819; RNase_P/MRP_POP5.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR PIRSF; PIRSF023803; Ribonuclease_P_prd; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; rRNA processing; tRNA processing.
FT CHAIN 1..163
FT /note="Ribonuclease P/MRP protein subunit POP5"
FT /id="PRO_0000239007"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 55..104
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042733"
FT CONFLICT 47..48
FT /note="AA -> P (in Ref. 2; AAF17213 and 3; AAD20966)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="N -> D (in Ref. 5; BAD96926)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="H -> R (in Ref. 5; BAD96926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 18820 MW; DF436E60B3DD50C1 CRC64;
MVRFKHRYLL CELVSDDPRC RLSLDDRVLS SLVRDTIARV HGTFGAAACS IGFAVRYLNA
YTGIVLLRCR KEFYQLVWSA LPFITYLENK GHRYPCFFNT LHVGGTIRTC QKFLIQYNRR
QLLILLQNCT DEGEREAIQK SVTRSCLLEE EEESGEEAAE AME
