ID   RS15A_HUMAN             Reviewed;         130 AA.
AC   P62244; P39027; P39031; Q3MHD9; Q8C023; Q9BV24;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Small ribosomal subunit protein uS8 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=40S ribosomal protein S15a;
GN   Name=RPS15A {ECO:0000312|HGNC:HGNC:10389}; ORFNames=OK/SW-cl.82;
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].
RA   Schwabe G.;
RL   Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Carcinoma;
RA   Mays G., Burchert-Graeve M.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lian Z., Liu J., Li L., Li X., Tufan S.N.L., Wu M.-C., Wang H.,
RA   Arbuthnot P., Kew M.K., Feitelson M.M.;
RT   "Human S15a expression is up-regulated by HBV X protein.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon adenocarcinoma;
RA   Shichijo S., Itoh K.;
RT   "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT   CTL generated from TIL of colon cancer patients.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Lung, 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   [6]
RP   PROTEIN SEQUENCE OF 2-17 AND 33-60.
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-54.
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   [8]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8185605; DOI=10.1006/bbrc.1994.1620;
RA   Chan Y.-L., Olvera J., Paz V., Wool I.G.;
RT   "The primary structure of rat ribosomal protein S15a.";
RL   Biochem. Biophys. Res. Commun. 200:1498-1504(1994).
RN   [9]
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   [10]
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   [11]
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   [12]
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   [13]
RP   INVOLVEMENT IN DBA20, AND FUNCTION.
RX   PubMed=27909223; DOI=10.3324/haematol.2016.153932;
RA   Ikeda F., Yoshida K., Toki T., Uechi T., Ishida S., Nakajima Y.,
RA   Sasahara Y., Okuno Y., Kanezaki R., Terui K., Kamio T., Kobayashi A.,
RA   Fujita T., Sato-Otsubo A., Shiraishi Y., Tanaka H., Chiba K., Muramatsu H.,
RA   Kanno H., Ohga S., Ohara A., Kojima S., Kenmochi N., Miyano S., Ogawa S.,
RA   Ito E.;
RT   "Exome sequencing identified RPS15A as a novel causative gene for Diamond-
RT   Blackfan anemia.";
RL   Haematologica 102:E93-E96(2017).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF RIBOSOME, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
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   [15] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
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: Component of the small ribosomal subunit (PubMed:23636399).
CC       Part of the small subunit (SSU) processome, first precursor of the
CC       small eukaryotic ribosomal subunit. During the assembly of the SSU
CC       processome in the nucleolus, many ribosome biogenesis factors, an RNA
CC       chaperone and ribosomal proteins associate with the nascent pre-rRNA
CC       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). Required for proper
CC       erythropoiesis (PubMed:27909223). {ECO:0000269|PubMed:23636399,
CC       ECO:0000269|PubMed:27909223, ECO:0000269|PubMed:34516797}.
CC   -!- SUBUNIT: Component of the 40S ribosomal subunit. Part of the small
CC       subunit (SSU) processome, composed of more than 70 proteins and the RNA
CC       chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797).
CC       {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:34516797}.
CC   -!- INTERACTION:
CC       P62244; P22607: FGFR3; NbExp=3; IntAct=EBI-347895, EBI-348399;
CC       P62244; P28799: GRN; NbExp=3; IntAct=EBI-347895, EBI-747754;
CC       P62244; P06396: GSN; NbExp=3; IntAct=EBI-347895, EBI-351506;
CC       P62244; P04792: HSPB1; NbExp=3; IntAct=EBI-347895, EBI-352682;
CC       P62244; P42858: HTT; NbExp=3; IntAct=EBI-347895, EBI-466029;
CC       P62244; O60333-2: KIF1B; NbExp=3; IntAct=EBI-347895, EBI-10975473;
CC       P62244; D3DTS7: PMP22; NbExp=3; IntAct=EBI-347895, EBI-25882629;
CC       P62244; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-347895, EBI-396669;
CC       P62244; O76024: WFS1; NbExp=3; IntAct=EBI-347895, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus,
CC       nucleolus {ECO:0000269|PubMed:34516797}.
CC   -!- DISEASE: Diamond-Blackfan anemia 20 (DBA20) [MIM:618313]: A form of
CC       Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC       anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC       is characterized by a moderate to severe macrocytic anemia,
CC       erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC       Diamond-Blackfan anemia patients present with short stature and
CC       congenital anomalies, the most frequent being craniofacial (Pierre-
CC       Robin syndrome and cleft palate), thumb and urogenital anomalies. DBA20
CC       inheritance is autosomal dominant. {ECO:0000269|PubMed:27909223}.
CC       Note=The disease may be caused by variants affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS8 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44568.1; Type=Frameshift; Evidence={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; X62691; CAA44568.1; ALT_FRAME; mRNA.
DR   EMBL; X84407; CAA59127.1; -; mRNA.
DR   EMBL; AY208299; AAO48936.1; -; mRNA.
DR   EMBL; AB062400; BAB93487.1; -; mRNA.
DR   EMBL; BC001697; AAH01697.1; -; mRNA.
DR   EMBL; BC030569; AAH30569.1; -; mRNA.
DR   EMBL; BC046113; AAH46113.1; -; mRNA.
DR   EMBL; BC105273; AAI05274.1; -; mRNA.
DR   EMBL; BC105292; AAI05293.1; -; mRNA.
DR   EMBL; AB007154; BAA28592.1; -; Genomic_DNA.
DR   CCDS; CCDS10571.1; -.
DR   PIR; S52339; S52339.
DR   RefSeq; NP_001010.2; NM_001019.4.
DR   RefSeq; NP_001025180.1; NM_001030009.1.
DR   PDB; 4UG0; EM; -; SW=1-130.
DR   PDB; 4V6X; EM; 5.00 A; AW=1-130.
DR   PDB; 5A2Q; EM; 3.90 A; W=1-130.
DR   PDB; 5AJ0; EM; 3.50 A; BW=1-130.
DR   PDB; 5FLX; EM; 3.90 A; W=1-130.
DR   PDB; 5LKS; EM; 3.60 A; SW=1-130.
DR   PDB; 5OA3; EM; 4.30 A; W=1-130.
DR   PDB; 5T2C; EM; 3.60 A; AP=1-130.
DR   PDB; 5VYC; X-ray; 6.00 A; W1/W2/W3/W4/W5/W6=1-130.
DR   PDB; 6FEC; EM; 6.30 A; a=2-130.
DR   PDB; 6G18; EM; 3.60 A; W=1-130.
DR   PDB; 6G4S; EM; 4.00 A; W=1-130.
DR   PDB; 6G4W; EM; 4.50 A; W=1-130.
DR   PDB; 6G51; EM; 4.10 A; W=1-130.
DR   PDB; 6G53; EM; 4.50 A; W=1-130.
DR   PDB; 6G5H; EM; 3.60 A; W=1-130.
DR   PDB; 6G5I; EM; 3.50 A; W=1-130.
DR   PDB; 6IP5; EM; 3.90 A; 3M=1-130.
DR   PDB; 6IP6; EM; 4.50 A; 3M=1-130.
DR   PDB; 6IP8; EM; 3.90 A; 3M=1-130.
DR   PDB; 6OLE; EM; 3.10 A; SW=2-130.
DR   PDB; 6OLF; EM; 3.90 A; SW=2-130.
DR   PDB; 6OLG; EM; 3.40 A; BW=2-130.
DR   PDB; 6OLI; EM; 3.50 A; SW=2-130.
DR   PDB; 6OLZ; EM; 3.90 A; BW=2-130.
DR   PDB; 6OM0; EM; 3.10 A; SW=2-130.
DR   PDB; 6OM7; EM; 3.70 A; SW=2-130.
DR   PDB; 6QZP; EM; 2.90 A; SW=2-130.
DR   PDB; 6XA1; EM; 2.80 A; SW=2-130.
DR   PDB; 6Y0G; EM; 3.20 A; SW=1-130.
DR   PDB; 6Y2L; EM; 3.00 A; SW=1-130.
DR   PDB; 6Y57; EM; 3.50 A; SW=1-130.
DR   PDB; 6YBW; EM; 3.10 A; J=1-130.
DR   PDB; 6Z6L; EM; 3.00 A; SW=1-130.
DR   PDB; 6Z6M; EM; 3.10 A; SW=1-130.
DR   PDB; 6Z6N; EM; 2.90 A; SW=1-130.
DR   PDB; 6ZLW; EM; 2.60 A; W=1-130.
DR   PDB; 6ZM7; EM; 2.70 A; SW=1-130.
DR   PDB; 6ZME; EM; 3.00 A; SW=1-130.
DR   PDB; 6ZMI; EM; 2.60 A; SW=1-130.
DR   PDB; 6ZMO; EM; 3.10 A; SW=1-130.
DR   PDB; 6ZMT; EM; 3.00 A; W=1-130.
DR   PDB; 6ZMW; EM; 3.70 A; J=1-130.
DR   PDB; 6ZN5; EM; 3.20 A; W=2-130.
DR   PDB; 6ZOJ; EM; 2.80 A; W=1-130.
DR   PDB; 6ZOK; EM; 2.80 A; W=1-130.
DR   PDB; 6ZON; EM; 3.00 A; f=1-130.
DR   PDB; 6ZP4; EM; 2.90 A; D=1-130.
DR   PDB; 6ZUO; EM; 3.10 A; W=1-130.
DR   PDB; 6ZV6; EM; 2.90 A; W=1-130.
DR   PDB; 6ZVH; EM; 2.90 A; W=2-130.
DR   PDB; 6ZVJ; EM; 3.80 A; f=2-130.
DR   PDB; 6ZXD; EM; 3.20 A; W=1-130.
DR   PDB; 6ZXE; EM; 3.00 A; W=1-130.
DR   PDB; 6ZXF; EM; 3.70 A; W=1-130.
DR   PDB; 6ZXG; EM; 2.60 A; W=1-130.
DR   PDB; 6ZXH; EM; 2.70 A; W=1-130.
DR   PDB; 7A09; EM; 3.50 A; D=1-130.
DR   PDB; 7K5I; EM; 2.90 A; W=1-130.
DR   PDB; 7MQ8; EM; 3.60 A; NO=1-130.
DR   PDB; 7MQ9; EM; 3.87 A; NO=1-130.
DR   PDB; 7MQA; EM; 2.70 A; NO=1-130.
DR   PDB; 7QP6; EM; 4.70 A; J=1-130.
DR   PDB; 7QP7; EM; 3.70 A; J=1-130.
DR   PDB; 7R4X; EM; 2.15 A; W=1-130.
DR   PDB; 7TQL; EM; 3.40 A; W=2-130.
DR   PDB; 7WTS; EM; 3.20 A; W=1-130.
DR   PDB; 7WTT; EM; 3.10 A; W=1-130.
DR   PDB; 7WTU; EM; 3.00 A; W=1-130.
DR   PDB; 7WTV; EM; 3.50 A; W=1-130.
DR   PDB; 7WTW; EM; 3.20 A; W=1-130.
DR   PDB; 7WTX; EM; 3.10 A; W=1-130.
DR   PDB; 7WTZ; EM; 3.00 A; W=1-130.
DR   PDB; 7WU0; EM; 3.30 A; W=1-130.
DR   PDB; 7XNX; EM; 2.70 A; SW=1-130.
DR   PDB; 7XNY; EM; 2.50 A; SW=1-130.
DR   PDB; 8G5Y; EM; 2.29 A; SW=1-130.
DR   PDB; 8G5Z; EM; 2.64 A; SW=2-130.
DR   PDB; 8G60; EM; 2.54 A; SW=1-130.
DR   PDB; 8G61; EM; 2.94 A; SW=1-130.
DR   PDB; 8G6J; EM; 2.80 A; SW=1-130.
DR   PDB; 8GLP; EM; 1.67 A; SW=1-130.
DR   PDB; 8JDJ; EM; 2.50 A; AI=1-130.
DR   PDB; 8JDK; EM; 2.26 A; AI=1-130.
DR   PDB; 8JDL; EM; 2.42 A; AI=1-130.
DR   PDB; 8JDM; EM; 2.67 A; AI=1-130.
DR   PDB; 8PPK; EM; 2.98 A; W=1-130.
DR   PDB; 8PPL; EM; 2.65 A; AW=1-130.
DR   PDB; 8T4S; EM; 2.60 A; W=1-130.
DR   PDBsum; 4UG0; -.
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; 6G4S; -.
DR   PDBsum; 6G4W; -.
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; 6Y2L; -.
DR   PDBsum; 6Y57; -.
DR   PDBsum; 6YBW; -.
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; 6ZOK; -.
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; 7WTS; -.
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; 8G5Z; -.
DR   PDBsum; 8G60; -.
DR   PDBsum; 8G61; -.
DR   PDBsum; 8G6J; -.
DR   PDBsum; 8GLP; -.
DR   PDBsum; 8JDJ; -.
DR   PDBsum; 8JDK; -.
DR   PDBsum; 8JDL; -.
DR   PDBsum; 8JDM; -.
DR   PDBsum; 8PPK; -.
DR   PDBsum; 8PPL; -.
DR   PDBsum; 8T4S; -.
DR   AlphaFoldDB; P62244; -.
DR   EMDB; EMD-10668; -.
DR   EMDB; EMD-10674; -.
DR   EMDB; EMD-10690; -.
DR   EMDB; EMD-10775; -.
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-11321; -.
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-32799; -.
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-4348; -.
DR   EMDB; EMD-4349; -.
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; P62244; -.
DR   BioGRID; 112124; 399.
DR   ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR   CORUM; P62244; -.
DR   IntAct; P62244; 80.
DR   MINT; P62244; -.
DR   STRING; 9606.ENSP00000318646; -.
DR   GlyGen; P62244; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62244; -.
DR   MetOSite; P62244; -.
DR   PhosphoSitePlus; P62244; -.
DR   SwissPalm; P62244; -.
DR   BioMuta; RPS15A; -.
DR   DMDM; 50403624; -.
DR   EPD; P62244; -.
DR   jPOST; P62244; -.
DR   MassIVE; P62244; -.
DR   MaxQB; P62244; -.
DR   PaxDb; 9606-ENSP00000318646; -.
DR   PeptideAtlas; P62244; -.
DR   PRIDE; P62244; -.
DR   ProteomicsDB; 57373; -.
DR   Pumba; P62244; -.
DR   TopDownProteomics; P62244; -.
DR   Antibodypedia; 42904; 112 antibodies from 20 providers.
DR   DNASU; 6210; -.
DR   Ensembl; ENST00000322989.8; ENSP00000318646.4; ENSG00000134419.15.
DR   Ensembl; ENST00000563390.5; ENSP00000457000.1; ENSG00000134419.15.
DR   Ensembl; ENST00000565420.5; ENSP00000458115.1; ENSG00000134419.15.
DR   Ensembl; ENST00000572008.5; ENSP00000458528.1; ENSG00000134419.15.
DR   GeneID; 6210; -.
DR   KEGG; hsa:6210; -.
DR   MANE-Select; ENST00000322989.8; ENSP00000318646.4; NM_001019.5; NP_001010.2.
DR   UCSC; uc002dfh.2; human.
DR   AGR; HGNC:10389; -.
DR   CTD; 6210; -.
DR   DisGeNET; 6210; -.
DR   GeneCards; RPS15A; -.
DR   GeneReviews; RPS15A; -.
DR   HGNC; HGNC:10389; RPS15A.
DR   HPA; ENSG00000134419; Low tissue specificity.
DR   MalaCards; RPS15A; -.
DR   MIM; 603674; gene.
DR   MIM; 618313; phenotype.
DR   neXtProt; NX_P62244; -.
DR   OpenTargets; ENSG00000134419; -.
DR   Orphanet; 124; Diamond-Blackfan anemia.
DR   PharmGKB; PA34788; -.
DR   VEuPathDB; HostDB:ENSG00000134419; -.
DR   eggNOG; KOG1754; Eukaryota.
DR   GeneTree; ENSGT00950000183198; -.
DR   HOGENOM; CLU_098428_1_1_1; -.
DR   InParanoid; P62244; -.
DR   OMA; LPAKNFG; -.
DR   OrthoDB; 5472446at2759; -.
DR   PhylomeDB; P62244; -.
DR   TreeFam; TF300067; -.
DR   PathwayCommons; P62244; -.
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; P62244; -.
DR   SIGNOR; P62244; -.
DR   BioGRID-ORCS; 6210; 842 hits in 1143 CRISPR screens.
DR   ChiTaRS; RPS15A; human.
DR   GeneWiki; RPS15A; -.
DR   GenomeRNAi; 6210; -.
DR   Pharos; P62244; Tbio.
DR   PRO; PR:P62244; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P62244; Protein.
DR   Bgee; ENSG00000134419; Expressed in ganglionic eminence and 162 other cell types or tissues.
DR   ExpressionAtlas; P62244; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0045202; C:synapse; IEA:Ensembl.
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:0045787; P:positive regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   Gene3D; 3.30.1370.30; -; 1.
DR   Gene3D; 3.30.1490.10; -; 1.
DR   HAMAP; MF_01302_A; Ribosomal_uS8_A; 1.
DR   InterPro; IPR000630; Ribosomal_uS8.
DR   InterPro; IPR047863; Ribosomal_uS8_CS.
DR   InterPro; IPR035987; Ribosomal_uS8_sf.
DR   PANTHER; PTHR11758; 40S RIBOSOMAL PROTEIN S15A; 1.
DR   PANTHER; PTHR11758:SF13; 40S RIBOSOMAL PROTEIN S15A; 1.
DR   Pfam; PF00410; Ribosomal_S8; 1.
DR   SUPFAM; SSF56047; Ribosomal protein S8; 1.
DR   PROSITE; PS00053; RIBOSOMAL_S8; 1.
DR   SWISS-2DPAGE; P62244; -.
DR   Genevisible; P62244; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Diamond-Blackfan anemia;
KW   Direct protein sequencing; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8706699"
FT   CHAIN           2..130
FT                   /note="Small ribosomal subunit protein uS8"
FT                   /id="PRO_0000126602"
FT   MOD_RES         88
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62245"
FT   CONFLICT        3
FT                   /note="R -> C (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="V -> L (in Ref. 2; CAA59127)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="F -> S (in Ref. 5; AAH01697)"
FT                   /evidence="ECO:0000305"
FT   HELIX           6..19
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          23..27
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   HELIX           32..43
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          46..54
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          60..65
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   HELIX           83..93
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          109..112
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:7R4X"
SQ   SEQUENCE   130 AA;  14840 MW;  D4AC1E8864E3A184 CRC64;
     MVRMNVLADA LKSINNAEKR GKRQVLIRPC SKVIVRFLTV MMKHGYIGEF EIIDDHRAGK
     IVVNLTGRLN KCGVISPRFD VQLKDLEKWQ NNLLPSRQFG FIVLTTSAGI MDHEEARRKH
     TGGKILGFFF
//