RT02_HUMAN
ID RT02_HUMAN Reviewed; 296 AA.
AC Q9Y399; Q5T899; Q9BSQ4;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=28S ribosomal protein S2, mitochondrial;
DE Short=MRP-S2;
DE Short=S2mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS2m {ECO:0000303|PubMed:25838379};
GN Name=MRPS2; ORFNames=CGI-91;
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] {ECO:0000312|EMBL:BAB62529.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, 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] {ECO:0000305}
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 [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].
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 [8] {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).
RN [9]
RP FUNCTION, INVOLVEMENT IN COXPD36, VARIANTS COXPD36 CYS-110; ASN-114 AND
RP HIS-138, AND CHARACTERIZATION OF VARIANTS COXPD36 CYS-110; ASN-114 AND
RP HIS-138.
RX PubMed=29576219; DOI=10.1016/j.ajhg.2018.02.012;
RA Gardeitchik T., Mohamed M., Ruzzenente B., Karall D., Guerrero-Castillo S.,
RA Dalloyaux D., van den Brand M., van Kraaij S., van Asbeck E., Assouline Z.,
RA Rio M., de Lonlay P., Scholl-Buergi S., Wolthuis D.F.G.J., Hoischen A.,
RA Rodenburg R.J., Sperl W., Urban Z., Brandt U., Mayr J.A., Wong S.,
RA de Brouwer A.P.M., Nijtmans L., Munnich A., Roetig A., Wevers R.A.,
RA Metodiev M.D., Morava E.;
RT "Bi-allelic mutations in the mitochondrial ribosomal protein MRPS2 cause
RT sensorineural hearing loss, hypoglycemia, and multiple OXPHOS complex
RT deficiencies.";
RL Am. J. Hum. Genet. 102:685-695(2018).
CC -!- FUNCTION: Required for mitoribosome formation and stability, and
CC mitochondrial translation. {ECO:0000269|PubMed:29576219}.
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 -!- DISEASE: Combined oxidative phosphorylation deficiency 36 (COXPD36)
CC [MIM:617950]: An autosomal recessive, multisystem disease resulting
CC from deficiencies of mitochondrial respiratory enzyme complexes and
CC mitochondrial dysfunction. Clinical manifestations include
CC sensorineural hearing impairment, mild developmental delay,
CC hypoglycemia, and intellectual disability.
CC {ECO:0000269|PubMed:29576219}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04905.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={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; AB055388; BAB62529.1; -; mRNA.
DR EMBL; AF151849; AAD34086.1; -; mRNA.
DR EMBL; AL161452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004905; AAH04905.2; ALT_SEQ; mRNA.
DR EMBL; BC008017; AAH08017.1; -; mRNA.
DR EMBL; BC013108; AAH13108.1; -; mRNA.
DR CCDS; CCDS6990.1; -.
DR RefSeq; NP_057118.1; NM_016034.4.
DR PDB; 3J9M; EM; 3.50 A; AB=1-296.
DR PDB; 6NU2; EM; 3.90 A; AB=58-274.
DR PDB; 6NU3; EM; 4.40 A; AB=1-296.
DR PDB; 6RW4; EM; 2.97 A; B=1-296.
DR PDB; 6RW5; EM; 3.14 A; B=1-296.
DR PDB; 6VLZ; EM; 2.97 A; AB=1-296.
DR PDB; 6VMI; EM; 2.96 A; AB=1-296.
DR PDB; 6ZM5; EM; 2.89 A; AB=1-296.
DR PDB; 6ZM6; EM; 2.59 A; AB=1-296.
DR PDB; 6ZS9; EM; 4.00 A; AB=1-296.
DR PDB; 6ZSA; EM; 4.00 A; AB=1-296.
DR PDB; 6ZSB; EM; 4.50 A; AB=1-296.
DR PDB; 6ZSC; EM; 3.50 A; AB=1-296.
DR PDB; 6ZSD; EM; 3.70 A; AB=1-296.
DR PDB; 6ZSE; EM; 5.00 A; AB=1-275.
DR PDB; 6ZSG; EM; 4.00 A; AB=1-296.
DR PDB; 7A5F; EM; 4.40 A; B6=1-296.
DR PDB; 7A5G; EM; 4.33 A; B6=1-296.
DR PDB; 7A5I; EM; 3.70 A; B6=1-296.
DR PDB; 7A5K; EM; 3.70 A; B6=1-296.
DR PDB; 7L08; EM; 3.49 A; AB=1-296.
DR PDB; 7OG4; EM; 3.80 A; AB=1-296.
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; Q9Y399; -.
DR SMR; Q9Y399; -.
DR BioGRID; 119304; 259.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q9Y399; -.
DR IntAct; Q9Y399; 67.
DR MINT; Q9Y399; -.
DR STRING; 9606.ENSP00000360850; -.
DR GlyGen; Q9Y399; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y399; -.
DR PhosphoSitePlus; Q9Y399; -.
DR BioMuta; MRPS2; -.
DR DMDM; 24212389; -.
DR EPD; Q9Y399; -.
DR jPOST; Q9Y399; -.
DR MassIVE; Q9Y399; -.
DR MaxQB; Q9Y399; -.
DR PaxDb; Q9Y399; -.
DR PeptideAtlas; Q9Y399; -.
DR PRIDE; Q9Y399; -.
DR ProteomicsDB; 85989; -.
DR Antibodypedia; 32046; 240 antibodies from 25 providers.
DR DNASU; 51116; -.
DR Ensembl; ENST00000241600.10; ENSP00000241600.5; ENSG00000122140.11.
DR Ensembl; ENST00000371785.5; ENSP00000360850.1; ENSG00000122140.11.
DR GeneID; 51116; -.
DR KEGG; hsa:51116; -.
DR MANE-Select; ENST00000241600.10; ENSP00000241600.5; NM_016034.5; NP_057118.1.
DR UCSC; uc004cfv.6; human.
DR CTD; 51116; -.
DR DisGeNET; 51116; -.
DR GeneCards; MRPS2; -.
DR HGNC; HGNC:14495; MRPS2.
DR HPA; ENSG00000122140; Low tissue specificity.
DR MalaCards; MRPS2; -.
DR MIM; 611971; gene.
DR MIM; 617950; phenotype.
DR neXtProt; NX_Q9Y399; -.
DR OpenTargets; ENSG00000122140; -.
DR PharmGKB; PA31007; -.
DR VEuPathDB; HostDB:ENSG00000122140; -.
DR eggNOG; KOG0832; Eukaryota.
DR GeneTree; ENSGT00390000017382; -.
DR InParanoid; Q9Y399; -.
DR OMA; SYIDRAY; -.
DR PhylomeDB; Q9Y399; -.
DR TreeFam; TF313480; -.
DR PathwayCommons; Q9Y399; -.
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; Q9Y399; -.
DR SIGNOR; Q9Y399; -.
DR BioGRID-ORCS; 51116; 299 hits in 1085 CRISPR screens.
DR ChiTaRS; MRPS2; human.
DR GenomeRNAi; 51116; -.
DR Pharos; Q9Y399; Tbio.
DR PRO; PR:Q9Y399; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y399; protein.
DR Bgee; ENSG00000122140; Expressed in apex of heart and 186 other tissues.
DR ExpressionAtlas; Q9Y399; baseline and differential.
DR Genevisible; Q9Y399; 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:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR GO; GO:0061668; P:mitochondrial ribosome assembly; IMP:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_00291_B; Ribosomal_S2_B; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR005706; Ribosomal_S2_bac/mit/plastid.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR12534; PTHR12534; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..296
FT /note="28S ribosomal protein S2, mitochondrial"
FT /id="PRO_0000134343"
FT REGION 274..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 110
FT /note="R -> C (in COXPD36; results in impaired assembly of
FT the small mitoribosomal subunit and impaired mitochondrial
FT translation in patient cells; dbSNP:rs761334309)"
FT /evidence="ECO:0000269|PubMed:29576219"
FT /id="VAR_080787"
FT VARIANT 112
FT /note="D -> G (in dbSNP:rs35140806)"
FT /id="VAR_034479"
FT VARIANT 114
FT /note="D -> N (in COXPD36; results in impaired assembly of
FT the small mitoribosomal subunit and impaired mitochondrial
FT translation in patient cells; dbSNP:rs201229537)"
FT /evidence="ECO:0000269|PubMed:29576219"
FT /id="VAR_080788"
FT VARIANT 138
FT /note="R -> H (in COXPD36; results in impaired assembly of
FT the small mitoribosomal subunit and impaired mitochondrial
FT translation in patient cells; dbSNP:rs758539748)"
FT /evidence="ECO:0000269|PubMed:29576219"
FT /id="VAR_080789"
FT VARIANT 158
FT /note="M -> V (in dbSNP:rs35293407)"
FT /id="VAR_034480"
FT VARIANT 294
FT /note="H -> R (in dbSNP:rs3748199)"
FT /id="VAR_020128"
SQ SEQUENCE 296 AA; 33249 MW; E05A248B09AA1A8B CRC64;
MATSSAALPR ILGAGARAPS RWLGFLGKAT PRPARPSRRT LGSATALMIR ESEDSTDFND
KILNEPLKHS DFFNVKELFS VRSLFDARVH LGHKAGCRHR FMEPYIFGSR LDHDIIDLEQ
TATHLQLALN FTAHMAYRKG IILFISRNRQ FSYLIENMAR DCGEYAHTRY FRGGMLTNAR
LLFGPTVRLP DLIIFLHTLN NIFEPHVAVR DAAKMNIPTV GIVDTNCNPC LITYPVPGND
DSPLAVHLYC RLFQTAITRA KEKRQQVEAL YRLQGQKEPG DQGPAHPPGA DMSHSL
