RT11_HUMAN
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 03-AUG-2022, entry version 166.
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}.
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; 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; 263.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82912; -.
DR IntAct; P82912; 99.
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; 298 antibodies from 25 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