RT05_HUMAN
ID RT05_HUMAN Reviewed; 430 AA.
AC P82675; Q4ZFY5; Q96LJ6; Q9BWI4; Q9BYC4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=28S ribosomal protein S5, mitochondrial;
DE Short=MRP-S5;
DE Short=S5mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS5m {ECO:0000303|PubMed:25838379};
GN Name=MRPS5;
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).
RX PubMed=11402041; DOI=10.1074/jbc.m103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Retina;
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 IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small
CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S
CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large
CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial
CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural
CC role, and 52 different proteins. {ECO:0000269|PubMed:25838379}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P82675-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P82675-2; Sequence=VSP_005725, VSP_005726;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000305}.
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DR EMBL; AB049940; BAB40993.1; -; mRNA.
DR EMBL; AK058160; BAB71695.1; -; mRNA.
DR EMBL; AC092835; AAX88980.1; -; Genomic_DNA.
DR EMBL; CH471219; EAX10712.1; -; Genomic_DNA.
DR EMBL; BC000219; AAH00219.2; -; mRNA.
DR EMBL; BC014172; AAH14172.1; -; mRNA.
DR CCDS; CCDS2010.1; -. [P82675-1]
DR RefSeq; NP_114108.1; NM_031902.4. [P82675-1]
DR PDB; 3J9M; EM; 3.50 A; AD=1-430.
DR PDB; 6NU2; EM; 3.90 A; AD=88-430.
DR PDB; 6NU3; EM; 4.40 A; AD=1-430.
DR PDB; 6RW4; EM; 2.97 A; D=1-430.
DR PDB; 6RW5; EM; 3.14 A; D=1-430.
DR PDB; 6VLZ; EM; 2.97 A; AD=1-430.
DR PDB; 6VMI; EM; 2.96 A; AD=1-430.
DR PDB; 6ZM5; EM; 2.89 A; AD=1-430.
DR PDB; 6ZM6; EM; 2.59 A; AD=1-430.
DR PDB; 6ZS9; EM; 4.00 A; AD=1-430.
DR PDB; 6ZSA; EM; 4.00 A; AD=1-430.
DR PDB; 6ZSB; EM; 4.50 A; AD=1-430.
DR PDB; 6ZSC; EM; 3.50 A; AD=1-430.
DR PDB; 6ZSD; EM; 3.70 A; AD=1-430.
DR PDB; 6ZSE; EM; 5.00 A; AD=1-430.
DR PDB; 6ZSG; EM; 4.00 A; AD=1-430.
DR PDB; 7A5F; EM; 4.40 A; D6=1-430.
DR PDB; 7A5G; EM; 4.33 A; D6=1-430.
DR PDB; 7A5I; EM; 3.70 A; D6=1-430.
DR PDB; 7A5K; EM; 3.70 A; D6=1-430.
DR PDB; 7L08; EM; 3.49 A; AD=1-430.
DR PDB; 7OG4; EM; 3.80 A; AD=1-430.
DR PDBsum; 3J9M; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6RW4; -.
DR PDBsum; 6RW5; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7OG4; -.
DR AlphaFoldDB; P82675; -.
DR SMR; P82675; -.
DR BioGRID; 122362; 327.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82675; -.
DR IntAct; P82675; 87.
DR MINT; P82675; -.
DR STRING; 9606.ENSP00000272418; -.
DR GlyGen; P82675; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P82675; -.
DR MetOSite; P82675; -.
DR PhosphoSitePlus; P82675; -.
DR SwissPalm; P82675; -.
DR BioMuta; MRPS5; -.
DR DMDM; 24212347; -.
DR EPD; P82675; -.
DR jPOST; P82675; -.
DR MassIVE; P82675; -.
DR MaxQB; P82675; -.
DR PaxDb; P82675; -.
DR PeptideAtlas; P82675; -.
DR PRIDE; P82675; -.
DR ProteomicsDB; 57714; -. [P82675-1]
DR ProteomicsDB; 57715; -. [P82675-2]
DR Antibodypedia; 32295; 135 antibodies from 24 providers.
DR DNASU; 64969; -.
DR Ensembl; ENST00000272418.7; ENSP00000272418.2; ENSG00000144029.12. [P82675-1]
DR Ensembl; ENST00000345084.9; ENSP00000341660.5; ENSG00000144029.12. [P82675-2]
DR GeneID; 64969; -.
DR KEGG; hsa:64969; -.
DR MANE-Select; ENST00000272418.7; ENSP00000272418.2; NM_031902.5; NP_114108.1.
DR UCSC; uc002sub.4; human. [P82675-1]
DR CTD; 64969; -.
DR DisGeNET; 64969; -.
DR GeneCards; MRPS5; -.
DR HGNC; HGNC:14498; MRPS5.
DR HPA; ENSG00000144029; Low tissue specificity.
DR MIM; 611972; gene.
DR neXtProt; NX_P82675; -.
DR OpenTargets; ENSG00000144029; -.
DR PharmGKB; PA31024; -.
DR VEuPathDB; HostDB:ENSG00000144029; -.
DR eggNOG; KOG2646; Eukaryota.
DR GeneTree; ENSGT00390000001878; -.
DR HOGENOM; CLU_050434_0_0_1; -.
DR InParanoid; P82675; -.
DR OMA; NTVNFFM; -.
DR OrthoDB; 1262134at2759; -.
DR PhylomeDB; P82675; -.
DR TreeFam; TF313823; -.
DR PathwayCommons; P82675; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; P82675; -.
DR SIGNOR; P82675; -.
DR BioGRID-ORCS; 64969; 504 hits in 1095 CRISPR screens.
DR ChiTaRS; MRPS5; human.
DR GeneWiki; MRPS5; -.
DR GenomeRNAi; 64969; -.
DR Pharos; P82675; Tbio.
DR PRO; PR:P82675; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P82675; protein.
DR Bgee; ENSG00000144029; Expressed in left ventricle myocardium and 187 other tissues.
DR Genevisible; P82675; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000851; Ribosomal_S5.
DR InterPro; IPR005324; Ribosomal_S5_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR013810; Ribosomal_S5_N.
DR InterPro; IPR018192; Ribosomal_S5_N_CS.
DR PANTHER; PTHR13718; PTHR13718; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..430
FT /note="28S ribosomal protein S5, mitochondrial"
FT /id="PRO_0000131685"
FT DOMAIN 218..282
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT VAR_SEQ 226..251
FT /note="RNVFTMTAKEGRKKSIRVLVAVGNGK -> FLLGKLLIGWMLSGKQRTEQFT
FT ICII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005725"
FT VAR_SEQ 252..430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005726"
SQ SEQUENCE 430 AA; 48006 MW; 80588064E2AB3E97 CRC64;
MATAVRAVGC LPVLCSGTAG HLLGRQCSLN TLPAASILAW KSVLGNGHLS SLGTRDTHPY
ASLSRALQTQ CCISSPSHLM SQQYRPYSFF TKLTADELWK GALAETGAGA KKGRGKRTKK
KKRKDLNRGQ IIGEGRYGFL WPGLNVPLMK NGAVQTIAQR SKEEQEKVEA DMIQQREEWD
RKKKMKVKRE RGWSGNSWGG ISLGPPDPGP CGETYEDFDT RILEVRNVFT MTAKEGRKKS
IRVLVAVGNG KGAAGFSIGK ATDRMDAFRK AKNRAVHHLH YIERYEDHTI FHDISLRFKR
THIKMKKQPK GYGLRCHRAI ITICRLIGIK DMYAKVSGSI NMLSLTQGLF RGLSRQETHQ
QLADKKGLHV VEIREECGPL PIVVASPRGP LRKDPEPEDE VPDVKLDWED VKTAQGMKRS
VWSNLKRAAT
