ID   RT33_HUMAN              Reviewed;         106 AA.
AC   Q9Y291;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Small ribosomal subunit protein mS33 {ECO:0000303|PubMed:25838379};
DE   AltName: Full=28S ribosomal protein S33, mitochondrial;
DE            Short=MRP-S33;
DE            Short=S33mt;
GN   Name=MRPS33; ORFNames=CGI-139, PTD003;
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 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   [2] {ECO:0000312|EMBL:AAH15462.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary tumor;
RA   Dai M., Peng Y., Song H., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA   Luo M., Chen J., Hu R.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   IDENTIFICATION BY 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   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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), 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:11279123}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mS33 family. {ECO:0000305}.
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DR   EMBL; AF151897; AAD34134.1; -; mRNA.
DR   EMBL; AF078858; AAD44490.1; -; mRNA.
DR   EMBL; AC006006; AAD43190.1; -; Genomic_DNA.
DR   EMBL; BC015462; AAH15462.1; -; mRNA.
DR   CCDS; CCDS5864.1; -.
DR   RefSeq; NP_057155.1; NM_016071.3.
DR   RefSeq; NP_444263.1; NM_053035.2.
DR   PDB; 3J9M; EM; 3.50 A; AZ=1-106.
DR   PDB; 6NU2; EM; 3.90 A; AZ=5-91.
DR   PDB; 6NU3; EM; 4.40 A; AZ=1-106.
DR   PDB; 6RW4; EM; 2.97 A; Z=1-106.
DR   PDB; 6RW5; EM; 3.14 A; Z=1-106.
DR   PDB; 6VLZ; EM; 2.97 A; AZ=1-106.
DR   PDB; 6VMI; EM; 2.96 A; AZ=1-106.
DR   PDB; 6ZM5; EM; 2.89 A; AZ=1-106.
DR   PDB; 6ZM6; EM; 2.59 A; AZ=1-106.
DR   PDB; 6ZS9; EM; 4.00 A; AZ=1-106.
DR   PDB; 6ZSA; EM; 4.00 A; AZ=1-106.
DR   PDB; 6ZSB; EM; 4.50 A; AZ=1-106.
DR   PDB; 6ZSC; EM; 3.50 A; AZ=1-106.
DR   PDB; 6ZSD; EM; 3.70 A; AZ=1-106.
DR   PDB; 6ZSE; EM; 5.00 A; AZ=1-106.
DR   PDB; 6ZSG; EM; 4.00 A; AZ=1-106.
DR   PDB; 7A5F; EM; 4.40 A; Z6=1-106.
DR   PDB; 7A5G; EM; 4.33 A; Z6=1-106.
DR   PDB; 7A5I; EM; 3.70 A; Z6=1-106.
DR   PDB; 7A5K; EM; 3.70 A; Z6=1-106.
DR   PDB; 7L08; EM; 3.49 A; AZ=1-106.
DR   PDB; 7OG4; EM; 3.80 A; AZ=1-106.
DR   PDB; 7P2E; EM; 2.40 A; Z=1-106.
DR   PDB; 7PNX; EM; 2.76 A; Z=1-106.
DR   PDB; 7PNY; EM; 3.06 A; Z=1-106.
DR   PDB; 7PNZ; EM; 3.09 A; Z=1-106.
DR   PDB; 7PO0; EM; 2.90 A; Z=1-106.
DR   PDB; 7PO1; EM; 2.92 A; Z=1-106.
DR   PDB; 7PO2; EM; 3.09 A; Z=1-106.
DR   PDB; 7PO3; EM; 2.92 A; Z=1-106.
DR   PDB; 7QI4; EM; 2.21 A; AZ=1-106.
DR   PDB; 7QI5; EM; 2.63 A; AZ=1-106.
DR   PDB; 7QI6; EM; 2.98 A; AZ=1-106.
DR   PDB; 8ANY; EM; 2.85 A; AZ=1-106.
DR   PDB; 8CSP; EM; 2.66 A; Z=1-106.
DR   PDB; 8CSQ; EM; 2.54 A; Z=1-106.
DR   PDB; 8CSR; EM; 2.54 A; Z=1-106.
DR   PDB; 8CSS; EM; 2.36 A; Z=1-106.
DR   PDB; 8CST; EM; 2.85 A; Z=1-106.
DR   PDB; 8CSU; EM; 3.03 A; Z=1-106.
DR   PDB; 8OIR; EM; 3.10 A; AZ=1-106.
DR   PDB; 8OIS; EM; 3.00 A; AZ=1-106.
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; Q9Y291; -.
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; Q9Y291; -.
DR   BioGRID; 119658; 173.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; Q9Y291; -.
DR   IntAct; Q9Y291; 42.
DR   MINT; Q9Y291; -.
DR   STRING; 9606.ENSP00000320567; -.
DR   iPTMnet; Q9Y291; -.
DR   PhosphoSitePlus; Q9Y291; -.
DR   BioMuta; MRPS33; -.
DR   DMDM; 24212388; -.
DR   EPD; Q9Y291; -.
DR   jPOST; Q9Y291; -.
DR   MassIVE; Q9Y291; -.
DR   MaxQB; Q9Y291; -.
DR   PaxDb; 9606-ENSP00000376732; -.
DR   PeptideAtlas; Q9Y291; -.
DR   ProteomicsDB; 85701; -.
DR   Pumba; Q9Y291; -.
DR   TopDownProteomics; Q9Y291; -.
DR   Antibodypedia; 32470; 140 antibodies from 21 providers.
DR   DNASU; 51650; -.
DR   Ensembl; ENST00000324787.10; ENSP00000320567.5; ENSG00000090263.16.
DR   Ensembl; ENST00000393008.7; ENSP00000376732.3; ENSG00000090263.16.
DR   Ensembl; ENST00000469351.1; ENSP00000417287.1; ENSG00000090263.16.
DR   Ensembl; ENST00000496958.5; ENSP00000418451.1; ENSG00000090263.16.
DR   GeneID; 51650; -.
DR   KEGG; hsa:51650; -.
DR   MANE-Select; ENST00000324787.10; ENSP00000320567.5; NM_053035.3; NP_444263.1.
DR   UCSC; uc003vwd.5; human.
DR   AGR; HGNC:16634; -.
DR   CTD; 51650; -.
DR   DisGeNET; 51650; -.
DR   GeneCards; MRPS33; -.
DR   HGNC; HGNC:16634; MRPS33.
DR   HPA; ENSG00000090263; Low tissue specificity.
DR   MIM; 611993; gene.
DR   neXtProt; NX_Q9Y291; -.
DR   OpenTargets; ENSG00000090263; -.
DR   PharmGKB; PA31020; -.
DR   VEuPathDB; HostDB:ENSG00000090263; -.
DR   eggNOG; KOG4104; Eukaryota.
DR   GeneTree; ENSGT00390000011401; -.
DR   InParanoid; Q9Y291; -.
DR   OMA; VANWYPR; -.
DR   OrthoDB; 4700185at2759; -.
DR   PhylomeDB; Q9Y291; -.
DR   TreeFam; TF313928; -.
DR   PathwayCommons; Q9Y291; -.
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; Q9Y291; -.
DR   SIGNOR; Q9Y291; -.
DR   BioGRID-ORCS; 51650; 146 hits in 1119 CRISPR screens.
DR   ChiTaRS; MRPS33; human.
DR   GeneWiki; MRPS33; -.
DR   GenomeRNAi; 51650; -.
DR   Pharos; Q9Y291; Tdark.
DR   PRO; PR:Q9Y291; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9Y291; Protein.
DR   Bgee; ENSG00000090263; Expressed in mucosa of transverse colon and 202 other cell types or tissues.
DR   ExpressionAtlas; Q9Y291; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; NAS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   InterPro; IPR013219; Ribosomal_mS33.
DR   PANTHER; PTHR13362:SF2; 28S RIBOSOMAL PROTEIN S33, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13362; MITOCHONDRIAL RIBOSOMAL PROTEIN S33; 1.
DR   Pfam; PF08293; MRP-S33; 1.
DR   Genevisible; Q9Y291; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT   CHAIN           2..106
FT                   /note="Small ribosomal subunit protein mS33"
FT                   /id="PRO_0000087727"
FT   REGION          82..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..106
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT   HELIX           6..19
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           32..38
FT                   /evidence="ECO:0007829|PDB:8CSS"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:8CST"
FT   TURN            46..50
FT                   /evidence="ECO:0007829|PDB:8CST"
FT   HELIX           55..67
FT                   /evidence="ECO:0007829|PDB:8CSS"
SQ   SEQUENCE   106 AA;  12629 MW;  E755EDAFB6AF6A46 CRC64;
     MSSLSEYAFR MSRLSARLFG EVTRPTNSKS MKVVKLFSEL PLAKKKETYD WYPNHHTYAE
     LMQTLRFLGL YRDEHQDFMD EQKRLKKLRG KEKPKKGEGK RAAKRK
//