RT09_HUMAN
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 03-AUG-2022, entry version 171.
DE RecName: Full=28S ribosomal protein S9, mitochondrial;
DE Short=MRP-S9;
DE Short=S9mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS9m {ECO:0000303|PubMed:25838379};
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}.
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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 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; P82933; -.
DR SMR; P82933; -.
DR BioGRID; 122360; 353.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82933; -.
DR IntAct; P82933; 109.
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; P82933; -.
DR PeptideAtlas; P82933; -.
DR PRIDE; P82933; -.
DR ProteomicsDB; 57724; -.
DR TopDownProteomics; P82933; -.
DR Antibodypedia; 32981; 186 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 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; IFPRQRA; -.
DR OrthoDB; 1430790at2759; -.
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; 285 hits in 1084 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 182 other tissues.
DR ExpressionAtlas; P82933; baseline and differential.
DR Genevisible; P82933; HS.
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:0015935; C:small ribosomal subunit; IBA:GO_Central.
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 Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
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="28S ribosomal protein S9, mitochondrial"
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"
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
