ID   RT11_HUMAN              Reviewed;         194 AA.
AC   P82912; B2RD52; Q969D7; Q96GI3; Q9BYC3;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   12-OCT-2022, entry version 167.
DE   RecName: Full=28S ribosomal protein S11, mitochondrial;
DE            Short=MRP-S11;
DE            Short=S11mt;
DE   AltName: Full=Cervical cancer proto-oncogene 2 protein;
DE            Short=HCC-2;
DE   AltName: Full=Mitochondrial small ribosomal subunit protein uS11m {ECO:0000303|PubMed:25838379};
DE   Flags: Precursor;
GN   Name=MRPS11; Synonyms=RPMS11; ORFNames=HCC2;
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=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 [GENOMIC DNA] (ISOFORM 2).
RA   Kim J.W.;
RT   "Identification of a new proto-oncogene in human cervical cancer.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Cervix, Kidney, and 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=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   [7]
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   [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).
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       P82912; P41227: NAA10; NbExp=3; IntAct=EBI-2371859, EBI-747693;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some isoforms.;
CC       Name=1;
CC         IsoId=P82912-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P82912-2; Sequence=VSP_005719;
CC       Name=3;
CC         IsoId=P82912-3; Sequence=VSP_005720;
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS11 family.
CC       {ECO:0000305}.
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DR   EMBL; AB049944; BAB40997.1; -; mRNA.
DR   EMBL; AF320777; AAK97314.1; -; Genomic_DNA.
DR   EMBL; AK026165; BAB15381.1; -; mRNA.
DR   EMBL; AK315407; BAG37799.1; -; mRNA.
DR   EMBL; CH471101; EAX02000.1; -; Genomic_DNA.
DR   EMBL; BC009451; AAH09451.1; -; mRNA.
DR   EMBL; BC012489; AAH12489.1; -; mRNA.
DR   EMBL; BC032378; AAH32378.1; -; mRNA.
DR   CCDS; CCDS10342.1; -. [P82912-1]
DR   CCDS; CCDS10343.1; -. [P82912-3]
DR   RefSeq; NP_001308899.1; NM_001321970.1. [P82912-2]
DR   RefSeq; NP_001308901.1; NM_001321972.1.
DR   RefSeq; NP_001308902.1; NM_001321973.1.
DR   RefSeq; NP_001308903.1; NM_001321974.1.
DR   RefSeq; NP_001308905.1; NM_001321976.1.
DR   RefSeq; NP_073750.2; NM_022839.4. [P82912-1]
DR   RefSeq; NP_789775.1; NM_176805.3. [P82912-3]
DR   PDB; 3J9M; EM; 3.50 A; AI=1-194.
DR   PDB; 6NU2; EM; 3.90 A; AI=59-194.
DR   PDB; 6NU3; EM; 4.40 A; AI=1-194.
DR   PDB; 6RW4; EM; 2.97 A; I=1-194.
DR   PDB; 6RW5; EM; 3.14 A; I=1-194.
DR   PDB; 6VLZ; EM; 2.97 A; AI=1-194.
DR   PDB; 6VMI; EM; 2.96 A; AI=1-194.
DR   PDB; 6ZM5; EM; 2.89 A; AI=1-194.
DR   PDB; 6ZM6; EM; 2.59 A; AI=1-194.
DR   PDB; 6ZS9; EM; 4.00 A; AI=1-194.
DR   PDB; 6ZSA; EM; 4.00 A; AI=1-194.
DR   PDB; 6ZSB; EM; 4.50 A; AI=1-194.
DR   PDB; 6ZSC; EM; 3.50 A; AI=1-194.
DR   PDB; 6ZSD; EM; 3.70 A; AI=1-194.
DR   PDB; 6ZSE; EM; 5.00 A; AI=1-194.
DR   PDB; 6ZSG; EM; 4.00 A; AI=1-194.
DR   PDB; 7A5F; EM; 4.40 A; I6=1-194.
DR   PDB; 7A5G; EM; 4.33 A; I6=1-194.
DR   PDB; 7A5I; EM; 3.70 A; I6=1-194.
DR   PDB; 7A5K; EM; 3.70 A; I6=1-194.
DR   PDB; 7L08; EM; 3.49 A; AI=1-194.
DR   PDB; 7OG4; EM; 3.80 A; AI=1-194.
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; P82912; -.
DR   SMR; P82912; -.
DR   BioGRID; 122359; 264.
DR   ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR   CORUM; P82912; -.
DR   IntAct; P82912; 100.
DR   MINT; P82912; -.
DR   STRING; 9606.ENSP00000317376; -.
DR   GlyGen; P82912; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P82912; -.
DR   PhosphoSitePlus; P82912; -.
DR   BioMuta; MRPS11; -.
DR   DMDM; 21263985; -.
DR   EPD; P82912; -.
DR   jPOST; P82912; -.
DR   MassIVE; P82912; -.
DR   MaxQB; P82912; -.
DR   PaxDb; P82912; -.
DR   PeptideAtlas; P82912; -.
DR   PRIDE; P82912; -.
DR   ProteomicsDB; 57717; -. [P82912-1]
DR   ProteomicsDB; 57718; -. [P82912-2]
DR   ProteomicsDB; 57719; -. [P82912-3]
DR   Antibodypedia; 28484; 297 antibodies from 24 providers.
DR   DNASU; 64963; -.
DR   Ensembl; ENST00000325844.9; ENSP00000317376.4; ENSG00000181991.16. [P82912-1]
DR   Ensembl; ENST00000353598.6; ENSP00000318054.7; ENSG00000181991.16. [P82912-3]
DR   GeneID; 64963; -.
DR   KEGG; hsa:64963; -.
DR   MANE-Select; ENST00000325844.9; ENSP00000317376.4; NM_022839.5; NP_073750.2.
DR   UCSC; uc002bml.4; human. [P82912-1]
DR   CTD; 64963; -.
DR   DisGeNET; 64963; -.
DR   GeneCards; MRPS11; -.
DR   HGNC; HGNC:14050; MRPS11.
DR   HPA; ENSG00000181991; Low tissue specificity.
DR   MIM; 611977; gene.
DR   neXtProt; NX_P82912; -.
DR   OpenTargets; ENSG00000181991; -.
DR   PharmGKB; PA30994; -.
DR   VEuPathDB; HostDB:ENSG00000181991; -.
DR   eggNOG; KOG0408; Eukaryota.
DR   GeneTree; ENSGT00390000016068; -.
DR   HOGENOM; CLU_072439_1_0_1; -.
DR   InParanoid; P82912; -.
DR   OMA; DNTPHPH; -.
DR   OrthoDB; 1303296at2759; -.
DR   PhylomeDB; P82912; -.
DR   TreeFam; TF354231; -.
DR   PathwayCommons; P82912; -.
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; P82912; -.
DR   SIGNOR; P82912; -.
DR   BioGRID-ORCS; 64963; 461 hits in 1086 CRISPR screens.
DR   ChiTaRS; MRPS11; human.
DR   GeneWiki; MRPS11; -.
DR   GenomeRNAi; 64963; -.
DR   Pharos; P82912; Tdark.
DR   PRO; PR:P82912; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P82912; protein.
DR   Bgee; ENSG00000181991; Expressed in apex of heart and 196 other tissues.
DR   ExpressionAtlas; P82912; baseline and differential.
DR   Genevisible; P82912; HS.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
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:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.420.80; -; 1.
DR   HAMAP; MF_01310; Ribosomal_S11; 1.
DR   InterPro; IPR001971; Ribosomal_S11.
DR   InterPro; IPR018102; Ribosomal_S11_CS.
DR   InterPro; IPR036967; Ribosomal_S11_sf.
DR   PANTHER; PTHR11759; PTHR11759; 1.
DR   Pfam; PF00411; Ribosomal_S11; 1.
DR   PROSITE; PS00054; RIBOSOMAL_S11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Mitochondrion; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..194
FT                   /note="28S ribosomal protein S11, mitochondrial"
FT                   /id="PRO_0000030602"
FT   VAR_SEQ         23
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005719"
FT   VAR_SEQ         62..94
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_005720"
FT   VARIANT         10
FT                   /note="R -> W (in dbSNP:rs16941904)"
FT                   /id="VAR_052054"
FT   VARIANT         51
FT                   /note="Q -> H (in dbSNP:rs16941907)"
FT                   /id="VAR_052055"
FT   CONFLICT        52
FT                   /note="N -> Y (in Ref. 3; BAB15381)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  20616 MW;  6DACB8FDDD0194BE CRC64;
     MQAVRNAGSR FLRSWTWPQT AGRVVARTPA GTICTGARQL QDAAAKQKVE QNAAPSHTKF
     SIYPPIPGEE SSLRWAGKKF EEIPIAHIKA SHNNTQIQVV SASNEPLAFA SCGTEGFRNA
     KKGTGIAAQT AGIAAAARAK QKGVIHIRVV VKGLGPGRLS AMHGLIMGGL EVISITDNTP
     IPHNGCRPRK ARKL
//