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 04-NOV-2026, entry version 219. 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_001008.4. 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 AlphaFoldDB; P22090; -. DR SMR; P22090; -. DR BioGRID; 112106; 144. DR CORUM; P22090; -. DR FunCoup; P22090; 844. DR IntAct; P22090; 46. DR NDEx; IQUERY-CP-RPS4Y1; 6 NDEx IQuery Curated Pathways. 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 jPOST; P22090; -. DR MassIVE; P22090; -. DR PaxDb; 9606-ENSP00000250784; -. DR PeptideAtlas; P22090; -. DR ProteomicsDB; 53960; -. DR Antibodypedia; 594; 222 antibodies from 27 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 ClinPGx; PA34840; -. 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 OpenTargets; ENSG00000129824; -. DR VEuPathDB; HostDB:ENSG00000129824; -. DR GeneTree; ENSGT00390000005569; -. DR InParanoid; P22090; -. DR OMA; ACNWTPA; -. DR PAN-GO; P22090; 4 GO annotations based on evolutionary models. DR PhylomeDB; P22090; -. 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-9684482; IFIT antiviral response. 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 Reactome; R-HSA-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR Reactome; R-HSA-9954716; ZNF598 and the Ribosome-associated Quality Trigger (RQT) complex dissociate a ribosome stalled on a no-go mRNA. DR SignaLink; P22090; -. DR SIGNOR; P22090; -. DR Agora; ENSG00000129824; -. 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; TAS:ProtInc. 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 FunFam; 2.30.30.30:FF:000005; 40S ribosomal protein S4; 1. DR FunFam; 2.40.50.740:FF:000001; 40S ribosomal protein S4; 1. DR FunFam; 3.10.290.10:FF:000051; 40S ribosomal protein S4, X isoform; 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; SMALL RIBOSOMAL SUBUNIT PROTEIN ES4, 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. PE 1: Evidence at protein level; KW 3D-structure; Proteomics identification; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; 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" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 16..18 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 28..32 FT /evidence="ECO:0007829|PDB:6OLG" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 47..51 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 59..66 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:6OLG" FT TURN 93..96 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 120..131 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:5AJ0" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 159..166 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 168..173 FT /evidence="ECO:0007829|PDB:5AJ0" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:6OLG" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:6OLG" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:6OLG" FT TURN 239..242 FT /evidence="ECO:0007829|PDB:5AJ0" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:6OLG" 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 //