ID RS12_HUMAN Reviewed; 132 AA.
AC P25398; Q76M58;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 27-MAR-2024, entry version 210.
DE RecName: Full=Small ribosomal subunit protein eS12 {ECO:0000303|PubMed:24524803};
DE AltName: Full=40S ribosomal protein S12;
GN Name=RPS12 {ECO:0000312|HGNC:HGNC:10385};
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].
RX PubMed=1861993; DOI=10.1093/nar/19.14.4001;
RA Herault Y., Michel D., Chatelain G., Brun G.;
RT "cDNA and predicted amino acid sequences of the human ribosomal protein
RT genes rpS12 and rpL17.";
RL Nucleic Acids Res. 19:4001-4001(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative analysis of
RT 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic stem cell, 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 [7]
RP PROTEIN SEQUENCE OF 2-33; 85-93 AND 117-129, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, Hepatoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Boldt K., von Kriegsheim A.F., Matallanas D.,
RA Cooper W.N., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 24-39.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-125.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [16]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [20] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS).
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC of the small eukaryotic ribosomal subunit. During the assembly of the
CC SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC RNA chaperone and ribosomal proteins associate with the nascent pre-
CC rRNA and work in concert to generate RNA folding, modifications,
CC rearrangements and cleavage as well as targeted degradation of pre-
CC ribosomal RNA by the RNA exosome (PubMed:34516797). Subunit of the 40S
CC ribosomal complex (By similarity). {ECO:0000250|UniProtKB:P80455,
CC ECO:0000269|PubMed:34516797}.
CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3
CC (PubMed:23636399, PubMed:34516797). Subunit of the 40S ribosomal
CC complex (By similarity). {ECO:0000250|UniProtKB:P80455,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}.
CC -!- INTERACTION:
CC P25398; P42858: HTT; NbExp=3; IntAct=EBI-354542, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:34516797}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS12 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; X53505; CAA37582.1; -; mRNA.
DR EMBL; AB061840; BAB79478.1; -; Genomic_DNA.
DR EMBL; AK311826; BAG34768.1; -; mRNA.
DR EMBL; AL137783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48011.1; -; Genomic_DNA.
DR EMBL; BC017321; AAH17321.1; -; mRNA.
DR EMBL; BC071930; AAH71930.1; -; mRNA.
DR EMBL; BC095424; AAH95424.1; -; mRNA.
DR EMBL; AB007153; BAA25819.1; -; Genomic_DNA.
DR CCDS; CCDS5164.1; -.
DR PIR; S22989; R3HU12.
DR RefSeq; NP_001007.2; NM_001016.3.
DR PDB; 4V6X; EM; 5.00 A; AM=1-132.
DR PDB; 5A2Q; EM; 3.90 A; M=1-132.
DR PDB; 5AJ0; EM; 3.50 A; BM=1-132.
DR PDB; 5FLX; EM; 3.90 A; M=1-132.
DR PDB; 5LKS; EM; 3.60 A; SM=1-132.
DR PDB; 5OA3; EM; 4.30 A; M=1-132.
DR PDB; 5T2C; EM; 3.60 A; AM=1-132.
DR PDB; 5VYC; X-ray; 6.00 A; M1/M2/M3/M4/M5/M6=1-132.
DR PDB; 6FEC; EM; 6.30 A; r=9-132.
DR PDB; 6G18; EM; 3.60 A; M=1-132.
DR PDB; 6G51; EM; 4.10 A; M=1-132.
DR PDB; 6G53; EM; 4.50 A; M=1-132.
DR PDB; 6G5H; EM; 3.60 A; M=1-132.
DR PDB; 6G5I; EM; 3.50 A; M=1-132.
DR PDB; 6IP5; EM; 3.90 A; 3J=1-132.
DR PDB; 6IP6; EM; 4.50 A; 3J=1-132.
DR PDB; 6IP8; EM; 3.90 A; 3J=1-132.
DR PDB; 6OLE; EM; 3.10 A; SM=15-132.
DR PDB; 6OLF; EM; 3.90 A; SM=15-132.
DR PDB; 6OLG; EM; 3.40 A; BM=11-130.
DR PDB; 6OLI; EM; 3.50 A; SM=15-132.
DR PDB; 6OLZ; EM; 3.90 A; BM=11-130.
DR PDB; 6OM0; EM; 3.10 A; SM=15-132.
DR PDB; 6OM7; EM; 3.70 A; SM=15-132.
DR PDB; 6QZP; EM; 2.90 A; SM=11-132.
DR PDB; 6XA1; EM; 2.80 A; SM=13-132.
DR PDB; 6Y0G; EM; 3.20 A; SM=1-132.
DR PDB; 6Y57; EM; 3.50 A; Sf=1-132.
DR PDB; 6YBS; EM; 3.10 A; m=1-132.
DR PDB; 6Z6L; EM; 3.00 A; SM=1-132.
DR PDB; 6Z6M; EM; 3.10 A; SM=1-132.
DR PDB; 6Z6N; EM; 2.90 A; SM=1-132.
DR PDB; 6ZLW; EM; 2.60 A; O=1-132.
DR PDB; 6ZM7; EM; 2.70 A; SM=1-132.
DR PDB; 6ZME; EM; 3.00 A; SM=1-132.
DR PDB; 6ZMI; EM; 2.60 A; SM=1-132.
DR PDB; 6ZMO; EM; 3.10 A; SM=1-132.
DR PDB; 6ZMT; EM; 3.00 A; O=1-132.
DR PDB; 6ZMW; EM; 3.70 A; m=1-132.
DR PDB; 6ZN5; EM; 3.20 A; O=10-132.
DR PDB; 6ZOJ; EM; 2.80 A; M=1-132.
DR PDB; 6ZOL; EM; 2.80 A; M=1-132.
DR PDB; 6ZON; EM; 3.00 A; v=1-132.
DR PDB; 6ZP4; EM; 2.90 A; v=1-132.
DR PDB; 6ZUO; EM; 3.10 A; M=1-132.
DR PDB; 6ZV6; EM; 2.90 A; M=1-132.
DR PDB; 6ZVH; EM; 2.90 A; M=11-132.
DR PDB; 6ZVJ; EM; 3.80 A; v=14-129.
DR PDB; 6ZXD; EM; 3.20 A; M=1-132.
DR PDB; 6ZXE; EM; 3.00 A; M=1-132.
DR PDB; 6ZXF; EM; 3.70 A; M=1-132.
DR PDB; 6ZXG; EM; 2.60 A; M=1-132.
DR PDB; 6ZXH; EM; 2.70 A; M=1-132.
DR PDB; 7A09; EM; 3.50 A; v=1-132.
DR PDB; 7K5I; EM; 2.90 A; M=1-132.
DR PDB; 7MQ8; EM; 3.60 A; LA=1-132.
DR PDB; 7MQ9; EM; 3.87 A; LA=1-132.
DR PDB; 7MQA; EM; 2.70 A; LA=1-132.
DR PDB; 7QP6; EM; 4.70 A; m=1-132.
DR PDB; 7QP7; EM; 3.70 A; m=1-132.
DR PDB; 7R4X; EM; 2.15 A; M=1-132.
DR PDB; 7TQL; EM; 3.40 A; O=10-129.
DR PDB; 7WTT; EM; 3.10 A; M=1-132.
DR PDB; 7WTU; EM; 3.00 A; M=1-132.
DR PDB; 7WTV; EM; 3.50 A; M=1-132.
DR PDB; 7WTW; EM; 3.20 A; M=1-132.
DR PDB; 7WTX; EM; 3.10 A; M=1-132.
DR PDB; 7WTZ; EM; 3.00 A; M=1-132.
DR PDB; 7WU0; EM; 3.30 A; M=1-132.
DR PDB; 7XNX; EM; 2.70 A; SM=1-132.
DR PDB; 7XNY; EM; 2.50 A; SM=1-132.
DR PDB; 8G5Y; EM; 2.29 A; SM=1-132.
DR PDB; 8G60; EM; 2.54 A; SM=1-132.
DR PDB; 8G61; EM; 2.94 A; SM=1-132.
DR PDB; 8G6J; EM; 2.80 A; SM=1-132.
DR PDB; 8GLP; EM; 1.67 A; SM=1-132.
DR PDB; 8PPK; EM; 2.98 A; M=1-132.
DR PDB; 8PPL; EM; 2.65 A; AM=1-132.
DR PDB; 8T4S; EM; 2.60 A; M=1-132.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR PDBsum; 7QP6; -.
DR PDBsum; 7QP7; -.
DR PDBsum; 7R4X; -.
DR PDBsum; 7TQL; -.
DR PDBsum; 7WTT; -.
DR PDBsum; 7WTU; -.
DR PDBsum; 7WTV; -.
DR PDBsum; 7WTW; -.
DR PDBsum; 7WTX; -.
DR PDBsum; 7WTZ; -.
DR PDBsum; 7WU0; -.
DR PDBsum; 7XNX; -.
DR PDBsum; 7XNY; -.
DR PDBsum; 8G5Y; -.
DR PDBsum; 8G60; -.
DR PDBsum; 8G61; -.
DR PDBsum; 8G6J; -.
DR PDBsum; 8GLP; -.
DR PDBsum; 8PPK; -.
DR PDBsum; 8PPL; -.
DR PDBsum; 8T4S; -.
DR AlphaFoldDB; P25398; -.
DR EMDB; EMD-10668; -.
DR EMDB; EMD-10690; -.
DR EMDB; EMD-10772; -.
DR EMDB; EMD-11098; -.
DR EMDB; EMD-11099; -.
DR EMDB; EMD-11100; -.
DR EMDB; EMD-11276; -.
DR EMDB; EMD-11288; -.
DR EMDB; EMD-11289; -.
DR EMDB; EMD-11292; -.
DR EMDB; EMD-11299; -.
DR EMDB; EMD-11301; -.
DR EMDB; EMD-11302; -.
DR EMDB; EMD-11310; -.
DR EMDB; EMD-11320; -.
DR EMDB; EMD-11322; -.
DR EMDB; EMD-11325; -.
DR EMDB; EMD-11335; -.
DR EMDB; EMD-11440; -.
DR EMDB; EMD-11441; -.
DR EMDB; EMD-11456; -.
DR EMDB; EMD-11458; -.
DR EMDB; EMD-11517; -.
DR EMDB; EMD-11518; -.
DR EMDB; EMD-11519; -.
DR EMDB; EMD-11520; -.
DR EMDB; EMD-11521; -.
DR EMDB; EMD-11602; -.
DR EMDB; EMD-14113; -.
DR EMDB; EMD-14114; -.
DR EMDB; EMD-14317; -.
DR EMDB; EMD-17804; -.
DR EMDB; EMD-17805; -.
DR EMDB; EMD-22681; -.
DR EMDB; EMD-23936; -.
DR EMDB; EMD-23937; -.
DR EMDB; EMD-23938; -.
DR EMDB; EMD-26067; -.
DR EMDB; EMD-29757; -.
DR EMDB; EMD-29758; -.
DR EMDB; EMD-29759; -.
DR EMDB; EMD-29760; -.
DR EMDB; EMD-29771; -.
DR EMDB; EMD-32800; -.
DR EMDB; EMD-32801; -.
DR EMDB; EMD-32802; -.
DR EMDB; EMD-32803; -.
DR EMDB; EMD-32804; -.
DR EMDB; EMD-32806; -.
DR EMDB; EMD-32807; -.
DR EMDB; EMD-33329; -.
DR EMDB; EMD-33330; -.
DR EMDB; EMD-3770; -.
DR EMDB; EMD-3883; -.
DR EMDB; EMD-40205; -.
DR EMDB; EMD-4070; -.
DR EMDB; EMD-41039; -.
DR EMDB; EMD-4242; -.
DR EMDB; EMD-4337; -.
DR EMDB; EMD-4350; -.
DR EMDB; EMD-4351; -.
DR EMDB; EMD-4352; -.
DR EMDB; EMD-4353; -.
DR EMDB; EMD-9701; -.
DR EMDB; EMD-9702; -.
DR EMDB; EMD-9703; -.
DR SMR; P25398; -.
DR BioGRID; 112120; 306.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P25398; -.
DR IntAct; P25398; 56.
DR MINT; P25398; -.
DR STRING; 9606.ENSP00000230050; -.
DR GlyGen; P25398; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P25398; -.
DR MetOSite; P25398; -.
DR PhosphoSitePlus; P25398; -.
DR SwissPalm; P25398; -.
DR BioMuta; RPS12; -.
DR DMDM; 224471878; -.
DR UCD-2DPAGE; P25398; -.
DR EPD; P25398; -.
DR jPOST; P25398; -.
DR MassIVE; P25398; -.
DR MaxQB; P25398; -.
DR PaxDb; 9606-ENSP00000230050; -.
DR PeptideAtlas; P25398; -.
DR ProteomicsDB; 54270; -.
DR Pumba; P25398; -.
DR TopDownProteomics; P25398; -.
DR Antibodypedia; 1252; 301 antibodies from 29 providers.
DR DNASU; 6206; -.
DR Ensembl; ENST00000230050.4; ENSP00000230050.3; ENSG00000112306.8.
DR GeneID; 6206; -.
DR KEGG; hsa:6206; -.
DR MANE-Select; ENST00000230050.4; ENSP00000230050.3; NM_001016.4; NP_001007.2.
DR UCSC; uc003qdx.4; human.
DR AGR; HGNC:10385; -.
DR CTD; 6206; -.
DR DisGeNET; 6206; -.
DR GeneCards; RPS12; -.
DR HGNC; HGNC:10385; RPS12.
DR HPA; ENSG00000112306; Low tissue specificity.
DR MIM; 603660; gene.
DR neXtProt; NX_P25398; -.
DR OpenTargets; ENSG00000112306; -.
DR PharmGKB; PA34784; -.
DR VEuPathDB; HostDB:ENSG00000112306; -.
DR eggNOG; KOG3406; Eukaryota.
DR GeneTree; ENSGT00390000018318; -.
DR HOGENOM; CLU_110343_1_1_1; -.
DR InParanoid; P25398; -.
DR OMA; CDEPMYK; -.
DR OrthoDB; 5045908at2759; -.
DR PhylomeDB; P25398; -.
DR TreeFam; TF300196; -.
DR PathwayCommons; P25398; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P25398; -.
DR SIGNOR; P25398; -.
DR BioGRID-ORCS; 6206; 803 hits in 1151 CRISPR screens.
DR ChiTaRS; RPS12; human.
DR GeneWiki; RPS12; -.
DR GenomeRNAi; 6206; -.
DR Pharos; P25398; Tbio.
DR PRO; PR:P25398; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P25398; Protein.
DR Bgee; ENSG00000112306; Expressed in left ovary and 107 other cell types or tissues.
DR Genevisible; P25398; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:FlyBase.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR InterPro; IPR000530; Ribosomal_eS12.
DR InterPro; IPR047860; Ribosomal_eS12_CS.
DR PANTHER; PTHR11843; 40S RIBOSOMAL PROTEIN S12; 1.
DR PANTHER; PTHR11843:SF0; 40S RIBOSOMAL PROTEIN S12; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00972; RIBSOMALS12E.
DR SUPFAM; SSF55315; L30e-like; 1.
DR PROSITE; PS01189; RIBOSOMAL_S12E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..132
FT /note="Small ribosomal subunit protein eS12"
FT /id="PRO_0000122323"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 129
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63323"
FT CONFLICT 52
FT /note="L -> Q (in Ref. 1; CAA37582)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="C -> L (in Ref. 1; CAA37582)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="K -> N (in Ref. 1; CAA37582)"
FT /evidence="ECO:0000305"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6ZMT"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6ZMT"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:7R4X"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6ZVH"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6ZXE"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7R4X"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:7TQL"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6ZLW"
SQ SEQUENCE 132 AA; 14515 MW; 45AD1274D55FFA25 CRC64;
MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC VLASNCDEPM
YVKLVEALCA EHQINLIKVD DNKKLGEWVG LCKIDREGKP RKVVGCSCVV VKDYGKESQA
KDVIEEYFKC KK
//
