ID RS4Y1_HUMAN Reviewed; 263 AA. AC P22090; A8K9V4; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Small ribosomal subunit protein eS4, Y isoform 1 {ECO:0000303|PubMed:24524803}; DE AltName: Full=40S ribosomal protein S4; GN Name=RPS4Y1; Synonyms=RPS4Y; ORFNames=PRO2646; 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=2124517; DOI=10.1016/0092-8674(90)90416-c; RA Fisher E.M.C., Beer-Romero P., Brown L.G., Ridley A., McNeil J.A., RA Lawrence J.B., Willard H.F., Bieber F.R., Page D.C.; RT "Homologous ribosomal protein genes on the human X and Y chromosomes: RT escape from X inactivation and possible implications for Turner syndrome."; RL Cell 63:1205-1218(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Zuo L., Baybayan P., Kuang W.-J., Brown L., Page D., Chen E.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., RA Liu M., He F.; RT "Functional prediction of the coding sequences of 121 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; 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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 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] 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). CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 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; M58459; AAA63256.1; -; mRNA. DR EMBL; AF041427; AAB96967.1; -; Genomic_DNA. DR EMBL; AF116711; AAF71131.1; -; mRNA. DR EMBL; AK292819; BAF85508.1; -; mRNA. DR EMBL; CH471115; EAX02771.1; -; Genomic_DNA. DR EMBL; BC010286; AAH10286.1; -; mRNA. DR CCDS; CCDS14773.1; -. DR PIR; A36338; R3HU4Y. DR RefSeq; NP_000999.1; NM_001008.3. DR PDB; 5AJ0; EM; 3.50 A; BE=1-263. DR PDB; 5FLX; EM; 3.90 A; E=1-263. DR PDB; 6OLG; EM; 3.40 A; BE=2-258. DR PDB; 6OLZ; EM; 3.90 A; BE=2-258. DR PDBsum; 5AJ0; -. DR PDBsum; 5FLX; -. DR PDBsum; 6OLG; -. DR PDBsum; 6OLZ; -. DR AlphaFoldDB; P22090; -. DR SMR; P22090; -. DR BioGRID; 112106; 116. DR CORUM; P22090; -. DR IntAct; P22090; 1. DR MINT; P22090; -. DR STRING; 9606.ENSP00000250784; -. DR GlyGen; P22090; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P22090; -. DR MetOSite; P22090; -. DR PhosphoSitePlus; P22090; -. DR SwissPalm; P22090; -. DR BioMuta; RPS4Y1; -. DR DMDM; 133948; -. DR EPD; P22090; -. DR jPOST; P22090; -. DR MassIVE; P22090; -. DR MaxQB; P22090; -. DR PeptideAtlas; P22090; -. DR ProteomicsDB; 53960; -. DR Antibodypedia; 594; 232 antibodies from 25 providers. DR DNASU; 6192; -. DR Ensembl; ENST00000250784.13; ENSP00000250784.7; ENSG00000129824.16. DR GeneID; 6192; -. DR KEGG; hsa:6192; -. DR MANE-Select; ENST00000250784.13; ENSP00000250784.7; NM_001008.4; NP_000999.1. DR UCSC; uc004fqi.4; human. DR AGR; HGNC:10425; -. DR CTD; 6192; -. DR DisGeNET; 6192; -. DR GeneCards; RPS4Y1; -. DR HGNC; HGNC:10425; RPS4Y1. DR HPA; ENSG00000129824; Low tissue specificity. DR MIM; 470000; gene. DR neXtProt; NX_P22090; -. DR OpenTargets; ENSG00000129824; -. DR PharmGKB; PA34840; -. DR VEuPathDB; HostDB:ENSG00000129824; -. DR GeneTree; ENSGT00390000005569; -. DR InParanoid; P22090; -. DR OMA; WMLDELT; -. DR OrthoDB; 5471107at2759; -. DR PhylomeDB; P22090; -. DR TreeFam; TF300612; -. DR PathwayCommons; P22090; -. 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; P22090; -. DR SIGNOR; P22090; -. DR BioGRID-ORCS; 6192; 12 hits in 760 CRISPR screens. DR ChiTaRS; RPS4Y1; human. DR GeneWiki; RPS4Y1; -. DR GenomeRNAi; 6192; -. DR Pharos; P22090; Tbio. DR PRO; PR:P22090; -. DR Proteomes; UP000005640; Chromosome Y. DR RNAct; P22090; Protein. DR Bgee; ENSG00000129824; Expressed in upper leg skin and 201 other cell types or tissues. DR ExpressionAtlas; P22090; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IMP:UniProtKB. DR CDD; cd06087; KOW_RPS4; 1. DR CDD; cd00165; S4; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.740; -; 1. DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1. DR HAMAP; MF_00485; Ribosomal_eS4; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR000876; Ribosomal_eS4. DR InterPro; IPR032277; Ribosomal_eS4_C. DR InterPro; IPR013845; Ribosomal_eS4_central_region. DR InterPro; IPR038237; Ribosomal_eS4_central_sf. DR InterPro; IPR041982; Ribosomal_eS4_KOW. DR InterPro; IPR013843; Ribosomal_eS4_N. DR InterPro; IPR018199; Ribosomal_eS4_N_CS. DR InterPro; IPR002942; S4_RNA-bd. DR InterPro; IPR036986; S4_RNA-bd_sf. DR PANTHER; PTHR11581; 30S/40S RIBOSOMAL PROTEIN S4; 1. DR PANTHER; PTHR11581:SF8; 40S RIBOSOMAL PROTEIN S4, Y ISOFORM 1; 1. DR Pfam; PF16121; 40S_S4_C; 1. DR Pfam; PF00467; KOW; 1. DR Pfam; PF00900; Ribosomal_S4e; 1. DR Pfam; PF08071; RS4NT; 1. DR PIRSF; PIRSF002116; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS00528; RIBOSOMAL_S4E; 1. DR PROSITE; PS50889; S4; 1. DR Genevisible; P22090; HS. PE 1: Evidence at protein level; KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein; KW RNA-binding; rRNA-binding. FT CHAIN 1..263 FT /note="Small ribosomal subunit protein eS4, Y isoform 1" FT /id="PRO_0000130812" FT DOMAIN 42..104 FT /note="S4 RNA-binding" SQ SEQUENCE 263 AA; 29456 MW; 3B5D6F1ECFCB120A CRC64; MARGPKKHLK RVAAPKHWML DKLTGVFAPR PSTGPHKLRE CLPLIVFLRN RLKYALTGDE VKKICMQRFI KIDGKVRVDV TYPAGFMDVI SIEKTGEHFR LVYDTKGRFA VHRITVEEAK YKLCKVRKIT VGVKGIPHLV THDARTIRYP DPVIKVNDTV QIDLGTGKII NFIKFDTGNL CMVIGGANLG RVGVITNRER HPGSFDVVHV KDANGNSFAT RLSNIFVIGN GNKPWISLPR GKGIRLTVAE ERDKRLATKQ SSG //