ID RT09_HUMAN Reviewed; 396 AA. AC P82933; Q6PG40; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 24-JAN-2024, entry version 179. DE RecName: Full=Small ribosomal subunit protein uS9m {ECO:0000303|PubMed:25838379}; DE AltName: Full=28S ribosomal protein S9, mitochondrial; DE Short=MRP-S9; DE Short=S9mt; DE Flags: Precursor; GN Name=MRPS9; Synonyms=RPMS9; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] 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 [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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 -!- INTERACTION: CC P82933; Q9P287: BCCIP; NbExp=3; IntAct=EBI-721385, EBI-711154; CC P82933; P04618: rev; Xeno; NbExp=2; IntAct=EBI-721385, EBI-6164309; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC010884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107080; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471127; EAX01767.1; -; Genomic_DNA. DR EMBL; BC057240; AAH57240.1; -; mRNA. DR CCDS; CCDS2065.1; -. DR RefSeq; NP_872578.1; NM_182640.2. DR PDB; 3J9M; EM; 3.50 A; AG=1-396. DR PDB; 6NU2; EM; 3.90 A; AG=71-396. DR PDB; 6NU3; EM; 4.40 A; AG=1-396. DR PDB; 6RW4; EM; 2.97 A; G=1-396. DR PDB; 6RW5; EM; 3.14 A; G=1-396. DR PDB; 6VLZ; EM; 2.97 A; AG=1-396. DR PDB; 6VMI; EM; 2.96 A; AG=1-396. DR PDB; 6ZM5; EM; 2.89 A; AG=1-396. DR PDB; 6ZM6; EM; 2.59 A; AG=1-396. DR PDB; 6ZS9; EM; 4.00 A; AG=1-396. DR PDB; 6ZSA; EM; 4.00 A; AG=1-396. DR PDB; 6ZSB; EM; 4.50 A; AG=1-396. DR PDB; 6ZSC; EM; 3.50 A; AG=1-396. DR PDB; 6ZSD; EM; 3.70 A; AG=1-396. DR PDB; 6ZSE; EM; 5.00 A; AG=1-396. DR PDB; 6ZSG; EM; 4.00 A; AG=1-396. DR PDB; 7A5F; EM; 4.40 A; G6=1-396. DR PDB; 7A5G; EM; 4.33 A; G6=1-396. DR PDB; 7A5I; EM; 3.70 A; G6=1-396. DR PDB; 7A5K; EM; 3.70 A; G6=1-396. DR PDB; 7L08; EM; 3.49 A; AG=1-396. DR PDB; 7OG4; EM; 3.80 A; AG=1-396. DR PDB; 7P2E; EM; 2.40 A; G=1-396. DR PDB; 7PNX; EM; 2.76 A; G=1-396. DR PDB; 7PNY; EM; 3.06 A; G=1-396. DR PDB; 7PNZ; EM; 3.09 A; G=1-396. DR PDB; 7PO0; EM; 2.90 A; G=1-396. DR PDB; 7PO1; EM; 2.92 A; G=1-396. DR PDB; 7PO2; EM; 3.09 A; G=1-396. DR PDB; 7PO3; EM; 2.92 A; G=1-396. DR PDB; 7QI4; EM; 2.21 A; AG=1-396. DR PDB; 7QI5; EM; 2.63 A; AG=1-396. DR PDB; 7QI6; EM; 2.98 A; AG=1-396. DR PDB; 8ANY; EM; 2.85 A; AG=1-396. DR PDB; 8CSP; EM; 2.66 A; G=1-396. DR PDB; 8CSQ; EM; 2.54 A; G=1-396. DR PDB; 8CSR; EM; 2.54 A; G=1-396. DR PDB; 8CSS; EM; 2.36 A; G=1-396. DR PDB; 8CST; EM; 2.85 A; G=1-396. DR PDB; 8CSU; EM; 3.03 A; G=1-396. DR PDB; 8OIR; EM; 3.10 A; Ag=1-396. DR PDB; 8OIS; EM; 3.00 A; Ag=1-396. 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 PDBsum; 7P2E; -. DR PDBsum; 7PNX; -. DR PDBsum; 7PNY; -. DR PDBsum; 7PNZ; -. DR PDBsum; 7PO0; -. DR PDBsum; 7PO1; -. DR PDBsum; 7PO2; -. DR PDBsum; 7PO3; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8CSP; -. DR PDBsum; 8CSQ; -. DR PDBsum; 8CSR; -. DR PDBsum; 8CSS; -. DR PDBsum; 8CST; -. DR PDBsum; 8CSU; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIS; -. DR AlphaFoldDB; P82933; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-10021; -. DR EMDB; EMD-10022; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-13170; -. DR EMDB; EMD-13555; -. DR EMDB; EMD-13556; -. DR EMDB; EMD-13557; -. DR EMDB; EMD-13558; -. DR EMDB; EMD-13559; -. DR EMDB; EMD-13560; -. DR EMDB; EMD-13561; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16898; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-26966; -. DR EMDB; EMD-26967; -. DR EMDB; EMD-26968; -. DR EMDB; EMD-26969; -. DR EMDB; EMD-26970; -. DR EMDB; EMD-26971; -. DR SMR; P82933; -. DR BioGRID; 122360; 387. DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit. DR CORUM; P82933; -. DR IntAct; P82933; 120. DR MINT; P82933; -. DR STRING; 9606.ENSP00000258455; -. DR GlyGen; P82933; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P82933; -. DR PhosphoSitePlus; P82933; -. DR SwissPalm; P82933; -. DR BioMuta; MRPS9; -. DR DMDM; 218511769; -. DR EPD; P82933; -. DR jPOST; P82933; -. DR MassIVE; P82933; -. DR MaxQB; P82933; -. DR PaxDb; 9606-ENSP00000258455; -. DR PeptideAtlas; P82933; -. DR ProteomicsDB; 57724; -. DR Pumba; P82933; -. DR TopDownProteomics; P82933; -. DR Antibodypedia; 32981; 210 antibodies from 28 providers. DR DNASU; 64965; -. DR Ensembl; ENST00000258455.8; ENSP00000258455.3; ENSG00000135972.9. DR GeneID; 64965; -. DR KEGG; hsa:64965; -. DR MANE-Select; ENST00000258455.8; ENSP00000258455.3; NM_182640.3; NP_872578.1. DR UCSC; uc002tcn.5; human. DR AGR; HGNC:14501; -. DR CTD; 64965; -. DR GeneCards; MRPS9; -. DR HGNC; HGNC:14501; MRPS9. DR HPA; ENSG00000135972; Low tissue specificity. DR MIM; 611975; gene. DR neXtProt; NX_P82933; -. DR OpenTargets; ENSG00000135972; -. DR PharmGKB; PA31028; -. DR VEuPathDB; HostDB:ENSG00000135972; -. DR eggNOG; KOG1697; Eukaryota. DR GeneTree; ENSGT00390000011204; -. DR HOGENOM; CLU_060546_1_0_1; -. DR InParanoid; P82933; -. DR OMA; PEQIFPR; -. DR OrthoDB; 2907269at2759; -. DR PhylomeDB; P82933; -. DR TreeFam; TF106154; -. DR PathwayCommons; P82933; -. 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; P82933; -. DR SIGNOR; P82933; -. DR BioGRID-ORCS; 64965; 293 hits in 1162 CRISPR screens. DR GenomeRNAi; 64965; -. DR Pharos; P82933; Tdark. DR PRO; PR:P82933; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P82933; Protein. DR Bgee; ENSG00000135972; Expressed in left ventricle myocardium and 184 other cell types or tissues. DR ExpressionAtlas; P82933; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005730; C:nucleolus; 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; NAS:ComplexPortal. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR000754; Ribosomal_uS9. DR InterPro; IPR020574; Ribosomal_uS9_CS. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR PANTHER; PTHR21569:SF1; 28S RIBOSOMAL PROTEIN S9, MITOCHONDRIAL; 1. DR PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 1. DR Genevisible; P82933; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..396 FT /note="Small ribosomal subunit protein uS9m" FT /id="PRO_0000030655" FT REGION 374..396 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 374..389 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 287 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 13 FT /note="S -> L (in dbSNP:rs13399067)" FT /id="VAR_047902" FT HELIX 71..92 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 101..111 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 151..153 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 156..174 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 202..209 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 215..230 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 235..242 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 268..276 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 279..288 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 300..303 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 307..319 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 328..335 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 337..352 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:8CSS" FT HELIX 358..366 FT /evidence="ECO:0007829|PDB:8CSS" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:8CSS" SQ SEQUENCE 396 AA; 45835 MW; 74412E34F0926360 CRC64; MAAPCVSYGG AVSYRLLLWG RGSLARKQGL WKTAAPELQT NVRSQILRLR HTAFVIPKKN VPTSKRETYT EDFIKKQIEE FNIGKRHLAN MMGEDPETFT QEDIDRAIAY LFPSGLFEKR ARPVMKHPEQ IFPRQRAIQW GEDGRPFHYL FYTGKQSYYS LMHDVYGMLL NLEKHQSHLQ AKSLLPEKTV TRDVIGSRWL IKEELEEMLV EKLSDLDYMQ FIRLLEKLLT SQCGAAEEEF VQRFRRSVTL ESKKQLIEPV QYDEQGMAFS KSEGKRKTAK AEAIVYKHGS GRIKVNGIDY QLYFPITQDR EQLMFPFHFV DRLGKHDVTC TVSGGGRSAQ AGAIRLAMAK ALCSFVTEDE VEWMRQAGLL TTDPRVRERK KPGQEGARRK FTWKKR //