RPP14_HUMAN
ID RPP14_HUMAN Reviewed; 124 AA.
AC O95059; Q53X97;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ribonuclease P protein subunit p14;
GN Name=RPP14;
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 2-14, FUNCTION, AND
RP SUBUNIT.
RC TISSUE=Liver, and Spleen;
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 [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 (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, 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 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 [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 IDENTIFICATION OF BICISTRONIC GENE.
RX PubMed=17898086; DOI=10.1096/fj.07-8986;
RA Autio K.J., Kastaniotis A.J., Pospiech H., Miinalainen I.J.,
RA Schonauer M.S., Dieckmann C.L., Hiltunen J.K.;
RT "An ancient genetic link between vertebrate mitochondrial fatty acid
RT synthesis and RNA processing.";
RL FASEB J. 22:569-578(2008).
RN [8]
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 [9]
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 [10] {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:30454648}.
CC -!- SUBUNIT: RNase P consists of a catalytic RNA moiety and about 10
CC protein subunits; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30,
CC RPP38 and RPP40 (PubMed:10024167, PubMed:16723659, PubMed:30454648).
CC Within the RNase P complex, POP1, POP7 and RPP25 form the 'finger'
CC subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm'
CC subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All
CC subunits of the RNase P complex interact with the catalytic RNA
CC (PubMed:30454648). {ECO:0000269|PubMed:10024167,
CC ECO:0000269|PubMed:16723659, ECO:0000269|PubMed:30454648}.
CC -!- INTERACTION:
CC O95059; P35609: ACTN2; NbExp=3; IntAct=EBI-366542, EBI-77797;
CC O95059; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-366542, EBI-371922;
CC O95059; O14893: GEMIN2; NbExp=3; IntAct=EBI-366542, EBI-443648;
CC O95059; O95707: POP4; NbExp=2; IntAct=EBI-366542, EBI-366477;
CC O95059; Q9BUL9: RPP25; NbExp=2; IntAct=EBI-366542, EBI-366570;
CC O95059; P78346: RPP30; NbExp=5; IntAct=EBI-366542, EBI-366553;
CC O95059; G5E9M4: ZNF277; NbExp=3; IntAct=EBI-366542, EBI-11995620;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10444065,
CC ECO:0000305}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the HTD2 protein from an overlapping reading frame.
CC {ECO:0000269|PubMed:17898086}.
CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC component 2 family. {ECO:0000305}.
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DR EMBL; AF001175; AAD00892.1; -; mRNA.
DR EMBL; CR407611; CAG28539.1; -; mRNA.
DR EMBL; AK311969; BAG34908.1; -; mRNA.
DR EMBL; BC002441; AAH02441.1; -; mRNA.
DR EMBL; BC007342; AAH07342.1; -; mRNA.
DR EMBL; BC012017; AAH12017.1; -; mRNA.
DR CCDS; CCDS2888.1; -.
DR RefSeq; NP_001092253.1; NM_001098783.2.
DR RefSeq; NP_008973.1; NM_007042.4.
DR RefSeq; XP_011531615.1; XM_011533313.2.
DR RefSeq; XP_016861130.1; XM_017005641.1.
DR PDB; 6AHR; EM; 3.92 A; H=1-124.
DR PDB; 6AHU; EM; 3.66 A; H=1-124.
DR PDBsum; 6AHR; -.
DR PDBsum; 6AHU; -.
DR AlphaFoldDB; O95059; -.
DR SMR; O95059; -.
DR BioGRID; 116283; 46.
DR CORUM; O95059; -.
DR IntAct; O95059; 25.
DR STRING; 9606.ENSP00000412894; -.
DR GlyGen; O95059; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95059; -.
DR PhosphoSitePlus; O95059; -.
DR BioMuta; RPP14; -.
DR EPD; O95059; -.
DR jPOST; O95059; -.
DR MassIVE; O95059; -.
DR MaxQB; O95059; -.
DR PaxDb; O95059; -.
DR PeptideAtlas; O95059; -.
DR PRIDE; O95059; -.
DR ProteomicsDB; 50635; -.
DR TopDownProteomics; O95059; -.
DR Antibodypedia; 31632; 81 antibodies from 13 providers.
DR DNASU; 11102; -.
DR Ensembl; ENST00000295959.10; ENSP00000295959.5; ENSG00000163684.12.
DR Ensembl; ENST00000445193.7; ENSP00000412894.2; ENSG00000163684.12.
DR Ensembl; ENST00000466547.1; ENSP00000419909.1; ENSG00000163684.12.
DR GeneID; 11102; -.
DR KEGG; hsa:11102; -.
DR MANE-Select; ENST00000295959.10; ENSP00000295959.5; NM_007042.6; NP_008973.1.
DR UCSC; uc003dju.6; human.
DR CTD; 11102; -.
DR DisGeNET; 11102; -.
DR GeneCards; RPP14; -.
DR HGNC; HGNC:30327; RPP14.
DR HPA; ENSG00000163684; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 606112; gene.
DR neXtProt; NX_O95059; -.
DR OpenTargets; ENSG00000163684; -.
DR PharmGKB; PA134896894; -.
DR VEuPathDB; HostDB:ENSG00000163684; -.
DR eggNOG; ENOG502S10S; Eukaryota.
DR GeneTree; ENSGT00510000048121; -.
DR HOGENOM; CLU_157358_0_0_1; -.
DR OMA; PCHFQVI; -.
DR PhylomeDB; O95059; -.
DR TreeFam; TF324711; -.
DR BRENDA; 3.1.26.5; 2681.
DR PathwayCommons; O95059; -.
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; O95059; -.
DR BioGRID-ORCS; 11102; 713 hits in 1073 CRISPR screens.
DR ChiTaRS; RPP14; human.
DR GeneWiki; RPP14; -.
DR GenomeRNAi; 11102; -.
DR Pharos; O95059; Tbio.
DR PRO; PR:O95059; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95059; protein.
DR Bgee; ENSG00000163684; Expressed in hindlimb stylopod muscle and 98 other tissues.
DR Genevisible; O95059; HS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; TAS:Reactome.
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:0001682; P:tRNA 5'-leader removal; IDA:UniProtKB.
DR Gene3D; 3.30.70.3250; -; 1.
DR InterPro; IPR002759; Pop5/Rpp14/Rnp2-like.
DR InterPro; IPR038085; Rnp2-like_sf.
DR Pfam; PF01900; RNase_P_Rpp14; 1.
DR SUPFAM; SSF160350; SSF160350; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome;
KW RNA-binding; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10024167"
FT CHAIN 2..124
FT /note="Ribonuclease P protein subunit p14"
FT /id="PRO_0000140010"
SQ SEQUENCE 124 AA; 13693 MW; 10AF6C947785DD90 CRC64;
MPAPAATYER VVYKNPSEYH YMKVCLEFQD CGVGLNAAQF KQLLISAVKD LFGEVDAALP
LDILTYEEKT LSAILRICSS GLVKLWSSLT LLGSYKGKKC AFRVIQVSPF LLALSGNSRE
LVLD
