RT22_HUMAN
ID RT22_HUMAN Reviewed; 360 AA.
AC P82650; Q9H3I1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=28S ribosomal protein S22, mitochondrial;
DE Short=MRP-S22;
DE Short=S22mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS22 {ECO:0000303|PubMed:25838379};
GN Name=MRPS22; Synonyms=C3orf5, RPMS22; ORFNames=GK002;
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=11175783; DOI=10.1038/84781;
RA Crisponi L., Deiana M., Loi A., Chiappe F., Uda M., Amati P., Bisceglia L.,
RA Zelante L., Nagaraja R., Porcu S., Ristaldi M.S., Marzella R., Rocchi M.,
RA Nicolino M., Lienhardt-Roussie A., Nivelon A., Verloes A., Schlessinger D.,
RA Gasparini P., Bonneau D., Cao A., Pilia G.;
RT "The putative forkhead transcription factor FOXL2 is mutated in
RT blepharophimosis/ptosis/epicanthus inversus syndrome.";
RL Nat. Genet. 27:159-166(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver cancer;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver cancer tissue.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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=10938081; DOI=10.1074/jbc.m003596200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Koc H., Spremulli L.L.;
RT "A proteomics approach to the identification of mammalian mitochondrial
RT small subunit ribosomal proteins.";
RL J. Biol. Chem. 275:32585-32591(2000).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
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 [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
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 [12]
RP VARIANT COXPD5 HIS-170.
RX PubMed=17873122; DOI=10.1136/jmg.2007.053116;
RA Saada A., Shaag A., Arnon S., Dolfin T., Miller C., Fuchs-Telem D.,
RA Lombes A., Elpeleg O.;
RT "Antenatal mitochondrial disease caused by mitochondrial ribosomal protein
RT (MRPS22) mutation.";
RL J. Med. Genet. 44:784-786(2007).
RN [13]
RP VARIANTS ODG7 GLN-135 AND HIS-202, AND INVOLVEMENT IN ODG7.
RX PubMed=29566152; DOI=10.1093/hmg/ddy098;
RA Chen A., Tiosano D., Guran T., Baris H.N., Bayram Y., Mory A.,
RA Shapiro-Kulnane L., Hodges C.A., Akdemir Z.C., Turan S., Jhangiani S.N.,
RA van den Akker F., Hoppel C.L., Salz H.K., Lupski J.R., Buchner D.A.;
RT "Mutations in the mitochondrial ribosomal protein MRPS22 lead to primary
RT ovarian insufficiency.";
RL Hum. Mol. Genet. 27:1913-1926(2018).
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=P82650-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P82650-2; Sequence=VSP_056634, VSP_056635, VSP_056636;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 5 (COXPD5)
CC [MIM:611719]: A mitochondrial disease resulting in severe metabolic
CC acidosis, edema, hypertrophic cardiomyopathy, tubulopathy, and
CC hypotonia. {ECO:0000269|PubMed:17873122}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Ovarian dysgenesis 7 (ODG7) [MIM:618117]: A form of ovarian
CC dysgenesis, a disorder characterized by lack of spontaneous pubertal
CC development, primary amenorrhea, uterine hypoplasia, and
CC hypergonadotropic hypogonadism as a result of streak gonads. ODG7 is an
CC autosomal recessive condition. {ECO:0000269|PubMed:29566152}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS22 family. {ECO:0000305}.
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DR EMBL; AF321613; AAK01406.1; -; mRNA.
DR EMBL; AF063603; AAG43162.1; -; mRNA.
DR EMBL; AF226045; AAF86945.1; -; mRNA.
DR EMBL; AC024933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009296; AAH09296.1; -; mRNA.
DR CCDS; CCDS3107.1; -. [P82650-1]
DR RefSeq; NP_064576.1; NM_020191.2. [P82650-1]
DR PDB; 3J9M; EM; 3.50 A; AR=1-360.
DR PDB; 6NU2; EM; 3.90 A; AR=67-308.
DR PDB; 6NU3; EM; 4.40 A; AR=1-360.
DR PDB; 6RW4; EM; 2.97 A; R=1-360.
DR PDB; 6RW5; EM; 3.14 A; R=1-360.
DR PDB; 6VLZ; EM; 2.97 A; AR=1-360.
DR PDB; 6VMI; EM; 2.96 A; AR=1-360.
DR PDB; 6ZM5; EM; 2.89 A; AR=1-360.
DR PDB; 6ZM6; EM; 2.59 A; AR=1-360.
DR PDB; 6ZS9; EM; 4.00 A; AR=1-360.
DR PDB; 6ZSA; EM; 4.00 A; AR=1-360.
DR PDB; 6ZSB; EM; 4.50 A; AR=1-360.
DR PDB; 6ZSC; EM; 3.50 A; AR=1-360.
DR PDB; 6ZSD; EM; 3.70 A; AR=1-360.
DR PDB; 6ZSE; EM; 5.00 A; AR=1-360.
DR PDB; 6ZSG; EM; 4.00 A; AR=1-360.
DR PDB; 7A5F; EM; 4.40 A; R6=1-360.
DR PDB; 7A5G; EM; 4.33 A; R6=1-360.
DR PDB; 7A5I; EM; 3.70 A; R6=1-360.
DR PDB; 7A5K; EM; 3.70 A; R6=1-360.
DR PDB; 7L08; EM; 3.49 A; AR=1-360.
DR PDB; 7OG4; EM; 3.80 A; AR=1-360.
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; P82650; -.
DR SMR; P82650; -.
DR BioGRID; 121269; 267.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82650; -.
DR IntAct; P82650; 89.
DR MINT; P82650; -.
DR STRING; 9606.ENSP00000418008; -.
DR iPTMnet; P82650; -.
DR MetOSite; P82650; -.
DR PhosphoSitePlus; P82650; -.
DR BioMuta; MRPS22; -.
DR DMDM; 13633893; -.
DR EPD; P82650; -.
DR jPOST; P82650; -.
DR MassIVE; P82650; -.
DR MaxQB; P82650; -.
DR PaxDb; P82650; -.
DR PeptideAtlas; P82650; -.
DR PRIDE; P82650; -.
DR ProteomicsDB; 57709; -. [P82650-1]
DR ProteomicsDB; 80721; -.
DR TopDownProteomics; P82650-1; -. [P82650-1]
DR Antibodypedia; 1600; 189 antibodies from 26 providers.
DR DNASU; 56945; -.
DR Ensembl; ENST00000495075.5; ENSP00000418008.1; ENSG00000175110.14. [P82650-1]
DR Ensembl; ENST00000498505.5; ENSP00000420482.1; ENSG00000175110.14. [P82650-2]
DR Ensembl; ENST00000680020.1; ENSP00000505414.1; ENSG00000175110.14. [P82650-1]
DR Ensembl; ENST00000688697.1; ENSP00000510396.1; ENSG00000175110.14. [P82650-1]
DR GeneID; 56945; -.
DR KEGG; hsa:56945; -.
DR MANE-Select; ENST00000680020.1; ENSP00000505414.1; NM_020191.4; NP_064576.1.
DR UCSC; uc003etb.4; human. [P82650-1]
DR CTD; 56945; -.
DR DisGeNET; 56945; -.
DR GeneCards; MRPS22; -.
DR HGNC; HGNC:14508; MRPS22.
DR HPA; ENSG00000175110; Low tissue specificity.
DR MalaCards; MRPS22; -.
DR MIM; 605810; gene.
DR MIM; 611719; phenotype.
DR MIM; 618117; phenotype.
DR neXtProt; NX_P82650; -.
DR OpenTargets; ENSG00000175110; -.
DR Orphanet; 243; 46,XX gonadal dysgenesis.
DR Orphanet; 137908; Hypotonia with lactic acidemia and hyperammonemia.
DR PharmGKB; PA31010; -.
DR VEuPathDB; HostDB:ENSG00000175110; -.
DR eggNOG; KOG3890; Eukaryota.
DR GeneTree; ENSGT00390000006095; -.
DR InParanoid; P82650; -.
DR OMA; TTKRMNQ; -.
DR OrthoDB; 845271at2759; -.
DR PhylomeDB; P82650; -.
DR TreeFam; TF312882; -.
DR PathwayCommons; P82650; -.
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; P82650; -.
DR SIGNOR; P82650; -.
DR BioGRID-ORCS; 56945; 396 hits in 1085 CRISPR screens.
DR ChiTaRS; MRPS22; human.
DR GeneWiki; MRPS22; -.
DR GenomeRNAi; 56945; -.
DR Pharos; P82650; Tbio.
DR PRO; PR:P82650; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P82650; protein.
DR Bgee; ENSG00000175110; Expressed in adrenal tissue and 199 other tissues.
DR ExpressionAtlas; P82650; baseline and differential.
DR Genevisible; P82650; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR019374; Ribosomal_S22_mit.
DR PANTHER; PTHR13071; PTHR13071; 1.
DR Pfam; PF10245; MRP-S22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Mitochondrion; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..360
FT /note="28S ribosomal protein S22, mitochondrial"
FT /id="PRO_0000087703"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_056634"
FT VAR_SEQ 169
FT /note="E -> C (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_056635"
FT VAR_SEQ 170..360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_056636"
FT VARIANT 135
FT /note="R -> Q (in ODG7; unknown pathological significance;
FT dbSNP:rs774237195)"
FT /evidence="ECO:0000269|PubMed:29566152"
FT /id="VAR_081186"
FT VARIANT 170
FT /note="R -> H (in COXPD5; dbSNP:rs119478059)"
FT /evidence="ECO:0000269|PubMed:17873122"
FT /id="VAR_042733"
FT VARIANT 202
FT /note="R -> H (in ODG7; unknown pathological significance;
FT dbSNP:rs753345594)"
FT /evidence="ECO:0000269|PubMed:29566152"
FT /id="VAR_081187"
SQ SEQUENCE 360 AA; 41280 MW; 2DB50257C222D706 CRC64;
MAPLGTTVLL WSLLRSSPGV ERVCFRARIQ PWHGGLLQPL PCSFEMGLPR RRFSSEAAES
GSPETKKPTF MDEEVQSILT KMTGLNLQKT FKPAIQELKP PTYKLMTQAQ LEEATRQAVE
AAKVRLKMPP VLEERVPIND VLAEDKILEG TETTKYVFTD ISYSIPHRER FIVVREPSGT
LRKASWEERD RMIQVYFPKE GRKILTPIIF KEENLRTMYS QDRHVDVLNL CFAQFEPDST
EYIKVHHKTY EDIDKRGKYD LLRSTRYFGG MVWYFVNNKK IDGLLIDQIQ RDLIDDATNL
VQLYHVLHPD GQSAQGAKDQ AAEGINLIKV FAKTEAQKGA YIELTLQTYQ EALSRHSAAS
