RPP29_HUMAN
ID RPP29_HUMAN Reviewed; 220 AA.
AC O95707; Q5XKL7; Q6FHW9; Q9UQQ3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ribonuclease P protein subunit p29;
DE Short=hPOP4 {ECO:0000303|PubMed:10352175};
GN Name=POP4; Synonyms=RPP29;
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 86-95, FUNCTION, AND
RP SUBUNIT.
RX PubMed=10024167; DOI=10.1017/s135583829800185x;
RA Jarrous N., Eder P.S., Wesolowski D., Altman S.;
RT "Rpp14 and Rpp29, two protein subunits of human ribonuclease P.";
RL RNA 5:153-157(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10352175; DOI=10.1093/nar/27.12.2465;
RA van Eenennaam H., Pruijn G.J.M., van Venrooij W.J.;
RT "hPop4: a new protein subunit of the human RNase MRP and RNase P
RT ribonucleoprotein complexes.";
RL Nucleic Acids Res. 27:2465-2472(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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 [6]
RP SUBCELLULAR LOCATION.
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 [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [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).
CC -!- FUNCTION: Component of ribonuclease P, a ribonucleoprotein complex that
CC generates mature tRNA molecules by cleaving their 5'-ends.
CC {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:10352175,
CC ECO:0000269|PubMed:30454648}.
CC -!- SUBUNIT: Component of nuclear RNase P and RNase MRP ribonucleoproteins
CC (PubMed:10024167, PubMed:10352175, PubMed:30454648). RNase P consists
CC of a catalytic RNA moiety and 10 different protein chains; POP1, POP4,
CC POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40
CC (PubMed:16723659, 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 {ECO:0000269|PubMed:10024167, ECO:0000269|PubMed:10352175,
CC ECO:0000269|PubMed:15096576, ECO:0000269|PubMed:16723659,
CC ECO:0000269|PubMed:30454648}.
CC -!- INTERACTION:
CC O95707; Q99575: POP1; NbExp=3; IntAct=EBI-366477, EBI-366741;
CC O95707; Q969H6: POP5; NbExp=3; IntAct=EBI-366477, EBI-366525;
CC O95707; O95059: RPP14; NbExp=2; IntAct=EBI-366477, EBI-366542;
CC O95707; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-366477, EBI-366570;
CC O95707; P78345: RPP38; NbExp=3; IntAct=EBI-366477, EBI-366493;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10352175}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 1 family. {ECO:0000305}.
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DR EMBL; AF001176; AAD00893.2; -; mRNA.
DR EMBL; Y18863; CAB39167.1; -; mRNA.
DR EMBL; CR536569; CAG38806.1; -; mRNA.
DR EMBL; AK314790; BAG37321.1; -; mRNA.
DR EMBL; BC004438; AAH04438.1; -; mRNA.
DR EMBL; BC006098; AAH06098.1; -; mRNA.
DR CCDS; CCDS12416.1; -.
DR RefSeq; NP_006618.1; NM_006627.2.
DR PDB; 6AHR; EM; 3.92 A; D=1-220.
DR PDB; 6AHU; EM; 3.66 A; D=1-220.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; O95707; -.
DR SMR; O95707; -.
DR BioGRID; 115993; 72.
DR CORUM; O95707; -.
DR IntAct; O95707; 41.
DR MINT; O95707; -.
DR STRING; 9606.ENSP00000465213; -.
DR GlyGen; O95707; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95707; -.
DR PhosphoSitePlus; O95707; -.
DR BioMuta; POP4; -.
DR EPD; O95707; -.
DR jPOST; O95707; -.
DR MassIVE; O95707; -.
DR MaxQB; O95707; -.
DR PaxDb; O95707; -.
DR PeptideAtlas; O95707; -.
DR PRIDE; O95707; -.
DR ProteomicsDB; 51006; -.
DR Antibodypedia; 15541; 145 antibodies from 26 providers.
DR DNASU; 10775; -.
DR Ensembl; ENST00000585603.6; ENSP00000465213.1; ENSG00000105171.10.
DR GeneID; 10775; -.
DR KEGG; hsa:10775; -.
DR MANE-Select; ENST00000585603.6; ENSP00000465213.1; NM_006627.3; NP_006618.1.
DR UCSC; uc002nsf.3; human.
DR CTD; 10775; -.
DR DisGeNET; 10775; -.
DR GeneCards; POP4; -.
DR HGNC; HGNC:30081; POP4.
DR HPA; ENSG00000105171; Low tissue specificity.
DR MIM; 606114; gene.
DR neXtProt; NX_O95707; -.
DR OpenTargets; ENSG00000105171; -.
DR PharmGKB; PA134987921; -.
DR VEuPathDB; HostDB:ENSG00000105171; -.
DR eggNOG; KOG4046; Eukaryota.
DR GeneTree; ENSGT00390000010067; -.
DR HOGENOM; CLU_078577_2_1_1; -.
DR InParanoid; O95707; -.
DR OMA; IPKSECV; -.
DR OrthoDB; 1362700at2759; -.
DR PhylomeDB; O95707; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; O95707; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; O95707; -.
DR BioGRID-ORCS; 10775; 508 hits in 1085 CRISPR screens.
DR ChiTaRS; POP4; human.
DR GenomeRNAi; 10775; -.
DR Pharos; O95707; Tbio.
DR PRO; PR:O95707; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O95707; protein.
DR Bgee; ENSG00000105171; Expressed in right adrenal gland and 204 other tissues.
DR ExpressionAtlas; O95707; baseline and differential.
DR Genevisible; O95707; HS.
DR GO; GO:0030681; C:multimeric ribonuclease P complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central.
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 Gene3D; 2.30.30.210; -; 1.
DR InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR InterPro; IPR023534; Rof/RNase_P-like.
DR InterPro; IPR002730; Rpp29/RNP1.
DR PANTHER; PTHR13348; PTHR13348; 1.
DR Pfam; PF01868; RNase_P-MRP_p29; 1.
DR PIRSF; PIRSF027081; RNase_P/MRP_p29_subunit; 1.
DR SMART; SM00538; POP4; 1.
DR SUPFAM; SSF101744; SSF101744; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; tRNA processing.
FT CHAIN 1..220
FT /note="Ribonuclease P protein subunit p29"
FT /id="PRO_0000128418"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 38..39
FT /note="ST -> TS (in Ref. 1; AAD00893)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 25425 MW; 26141947E9F5C61E CRC64;
MKSVIYHALS QKEANDSDVQ PSGAQRAEAF VRAFLKRSTP RMSPQAREDQ LQRKAVVLEY
FTRHKRKEKK KKAKGLSARQ RRELRLFDIK PEQQRYSLFL PLHELWKQYI RDLCSGLKPD
TQPQMIQAKL LKADLHGAII SVTKSKCPSY VGITGILLQE TKHIFKIITK EDRLKVIPKL
NCVFTVETDG FISYIYGSKF QLRSSERSAK KFKAKGTIDL
