RS30_HUMAN
ID RS30_HUMAN Reviewed; 133 AA.
AC P62861; P35544; Q05472; Q95261; Q9H5V4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=FAU ubiquitin-like and ribosomal protein S30 {ECO:0000312|HGNC:HGNC:3597};
DE Contains:
DE RecName: Full=Ubiquitin-like protein FUBI;
DE Contains:
DE RecName: Full=40S ribosomal protein S30;
DE AltName: Full=Small ribosomal subunit protein eS30 {ECO:0000303|PubMed:24524803};
GN Name=FAU {ECO:0000312|HGNC:HGNC:3597};
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 [GENOMIC DNA].
RX PubMed=1326960; DOI=10.1016/0006-291x(92)91286-y;
RA Kas K., Michiels L., Merregaert J.;
RT "Genomic structure and expression of the human fau gene: encoding the
RT ribosomal protein S30 fused to a ubiquitin-like protein.";
RL Biochem. Biophys. Res. Commun. 187:927-933(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8395683;
RA Michiels L., van der Rauwelaert E., van Hasselt F., Kas K., Merregaert J.;
RT "fau cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as
RT an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus.";
RL Oncogene 8:2537-2546(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-53 AND MET-93.
RG NIEHS SNPs program;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [8]
RP PROTEIN SEQUENCE OF 75-99.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP FUNCTION.
RX PubMed=21550398; DOI=10.1016/j.bbadis.2011.04.009;
RA Pickard M.R., Mourtada-Maarabouni M., Williams G.T.;
RT "Candidate tumour suppressor Fau regulates apoptosis in human cells: an
RT essential role for Bcl-G.";
RL Biochim. Biophys. Acta 1812:1146-1153(2011).
RN [11]
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 [12]
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 [13]
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 [14]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of N-terminal ubiquitin-like domain of FUBI, a
RT ribosomal protein S30 precursor from Homo sapiens. Northeast structural
RT genomics consortium (NESG) target HR6166.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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 [16]
RP PROTEOLYTIC CLEAVAGE, MUTAGENESIS OF GLY-73 AND GLY-74, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=34318747; DOI=10.7554/elife.70560;
RA van den Heuvel J., Ashiono C., Gillet L.C., Doerner K., Wyler E., Zemp I.,
RA Kutay U.;
RT "Processing of the ribosomal ubiquitin-like fusion protein FUBI-eS30/FAU is
RT required for 40S maturation and depends on USP36.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: [Ubiquitin-like protein FUBI]: May have pro-apoptotic
CC activity. {ECO:0000269|PubMed:21550398}.
CC -!- FUNCTION: [40S ribosomal protein S30]: Component of the 40S subunit of
CC the ribosome. Contributes to the assembly and function of 40S ribosomal
CC subunits. {ECO:0000269|PubMed:34318747}.
CC -!- SUBUNIT: [40S ribosomal protein S30]: Component of the 40S subunit of
CC the ribosome. {ECO:0000269|PubMed:34318747}.
CC -!- SUBCELLULAR LOCATION: [40S ribosomal protein S30]: Nucleus
CC {ECO:0000269|PubMed:34318747}.
CC -!- PTM: FUBI is cleaved from ribosomal protein S30 by the deubiquitinase
CC USP36 before the assembly of ribosomal protein S30 into pre-40S
CC ribosomal particles. FUBI removal from ribosomal protein S30 is a
CC crucial event for the final maturation of pre-40S particles.
CC {ECO:0000269|PubMed:34318747}.
CC -!- MISCELLANEOUS: FAU encodes a fusion protein consisting of the
CC ubiquitin-like protein FUBI at the N terminus and ribosomal protein S30
CC at the C terminus. {ECO:0000269|PubMed:1326960,
CC ECO:0000305|PubMed:15489334}.
CC -!- MISCELLANEOUS: [Ubiquitin-like protein FUBI]: Lacks the typical lysine
CC residues that participate in Ub's polyubiquitination. However contains
CC a C-terminal di-glycine signature after its proteolytic separation from
CC ribosomal protein S30 and could theoretically be conjugated onto target
CC proteins. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS30 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/fau/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FAUID40538ch11q13.html";
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DR EMBL; AP003068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X65923; CAA46716.1; -; mRNA.
DR EMBL; X65921; CAA46714.1; -; Genomic_DNA.
DR EMBL; AK026639; BAB15515.1; -; mRNA.
DR EMBL; CR541974; CAG46772.1; -; mRNA.
DR EMBL; AY398663; AAQ87877.1; -; Genomic_DNA.
DR EMBL; BC033877; AAH33877.1; -; mRNA.
DR CCDS; CCDS8095.1; -.
DR PIR; JC1278; JC1278.
DR RefSeq; NP_001988.1; NM_001997.4.
DR PDB; 2L7R; NMR; -; A=1-74.
DR PDB; 4UG0; EM; -; Se=75-133.
DR PDB; 4V6X; EM; 5.00 A; Ae=75-133.
DR PDB; 5A2Q; EM; 3.90 A; e=78-133.
DR PDB; 5AJ0; EM; 3.50 A; Be=75-133.
DR PDB; 5FLX; EM; 3.90 A; e=75-133.
DR PDB; 5OA3; EM; 4.30 A; e=78-133.
DR PDB; 5T2C; EM; 3.60 A; AT=75-133.
DR PDB; 6FEC; EM; 6.30 A; V=75-133.
DR PDB; 6G18; EM; 3.60 A; e=75-133.
DR PDB; 6G4S; EM; 4.00 A; e=75-133.
DR PDB; 6G4W; EM; 4.50 A; e=75-133.
DR PDB; 6G51; EM; 4.10 A; e=75-133.
DR PDB; 6G53; EM; 4.50 A; e=75-133.
DR PDB; 6G5H; EM; 3.60 A; e=75-133.
DR PDB; 6G5I; EM; 3.50 A; e=75-133.
DR PDB; 6IP5; EM; 3.90 A; 3Q=75-133.
DR PDB; 6IP6; EM; 4.50 A; 3Q=75-133.
DR PDB; 6IP8; EM; 3.90 A; 3Q=75-133.
DR PDB; 6OLE; EM; 3.10 A; Se=76-132.
DR PDB; 6OLF; EM; 3.90 A; Se=76-132.
DR PDB; 6OLG; EM; 3.40 A; Be=77-131.
DR PDB; 6OLI; EM; 3.50 A; Se=76-132.
DR PDB; 6OLZ; EM; 3.90 A; Be=77-131.
DR PDB; 6OM0; EM; 3.10 A; Se=76-132.
DR PDB; 6OM7; EM; 3.70 A; Se=76-132.
DR PDB; 6QZP; EM; 2.90 A; Se=76-133.
DR PDB; 6Y0G; EM; 3.20 A; Se=75-133.
DR PDB; 6Y2L; EM; 3.00 A; Se=75-133.
DR PDB; 6Y57; EM; 3.50 A; Se=75-133.
DR PDB; 6YBW; EM; 3.10 A; F=75-133.
DR PDB; 6Z6L; EM; 3.00 A; Se=75-133.
DR PDB; 6Z6M; EM; 3.10 A; Se=75-133.
DR PDB; 6Z6N; EM; 2.90 A; Se=75-133.
DR PDB; 6ZLW; EM; 2.60 A; e=75-133.
DR PDB; 6ZM7; EM; 2.70 A; Se=75-133.
DR PDB; 6ZME; EM; 3.00 A; Se=75-133.
DR PDB; 6ZMI; EM; 2.60 A; Se=75-133.
DR PDB; 6ZMO; EM; 3.10 A; Se=75-133.
DR PDB; 6ZMT; EM; 3.00 A; e=75-133.
DR PDB; 6ZMW; EM; 3.70 A; F=75-133.
DR PDB; 6ZN5; EM; 3.20 A; e=78-133.
DR PDB; 6ZOJ; EM; 2.80 A; e=78-133.
DR PDB; 6ZOK; EM; 2.80 A; e=78-133.
DR PDB; 6ZON; EM; 3.00 A; T=75-133.
DR PDB; 6ZP4; EM; 2.90 A; T=75-133.
DR PDB; 6ZUO; EM; 3.10 A; e=75-133.
DR PDB; 6ZV6; EM; 2.90 A; e=75-133.
DR PDB; 6ZVH; EM; 2.90 A; e=76-117.
DR PDB; 6ZVJ; EM; 3.80 A; T=81-124.
DR PDB; 6ZXD; EM; 3.20 A; e=75-133.
DR PDB; 6ZXE; EM; 3.00 A; e=75-133.
DR PDB; 6ZXF; EM; 3.70 A; e=75-133.
DR PDB; 6ZXG; EM; 2.60 A; e=75-133.
DR PDB; 6ZXH; EM; 2.70 A; e=75-133.
DR PDB; 7A09; EM; 3.50 A; T=75-133.
DR PDB; 7K5I; EM; 2.90 A; e=75-133.
DR PDBsum; 2L7R; -.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
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; 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 AlphaFoldDB; P62861; -.
DR SMR; P62861; -.
DR BioGRID; 108491; 260.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62861; -.
DR IntAct; P62861; 39.
DR MINT; P62861; -.
DR STRING; 9606.ENSP00000435370; -.
DR iPTMnet; P62861; -.
DR PhosphoSitePlus; P62861; -.
DR SwissPalm; P62861; -.
DR BioMuta; FAU; -.
DR DMDM; 549147; -.
DR EPD; P62861; -.
DR jPOST; P62861; -.
DR MassIVE; P62861; -.
DR MaxQB; P62861; -.
DR PeptideAtlas; P62861; -.
DR PRIDE; P62861; -.
DR ProteomicsDB; 55079; -.
DR ProteomicsDB; 57440; -.
DR TopDownProteomics; P62861; -.
DR Antibodypedia; 29676; 393 antibodies from 31 providers.
DR DNASU; 2197; -.
DR Ensembl; ENST00000527548.5; ENSP00000434440.1; ENSG00000149806.11.
DR Ensembl; ENST00000529639.6; ENSP00000435370.1; ENSG00000149806.11.
DR Ensembl; ENST00000531743.5; ENSP00000431822.1; ENSG00000149806.11.
DR KEGG; hsa:2197; -.
DR MANE-Select; ENST00000529639.6; ENSP00000435370.1; NM_001997.5; NP_001988.1.
DR UCSC; uc001ocx.4; human.
DR DisGeNET; 2197; -.
DR GeneCards; FAU; -.
DR HGNC; HGNC:3597; FAU.
DR HPA; ENSG00000149806; Low tissue specificity.
DR MIM; 134690; gene.
DR neXtProt; NX_P62861; -.
DR OpenTargets; ENSG00000149806; -.
DR PharmGKB; PA28010; -.
DR VEuPathDB; HostDB:ENSG00000149806; -.
DR eggNOG; KOG0001; Eukaryota.
DR eggNOG; KOG0009; Eukaryota.
DR GeneTree; ENSGT00390000007479; -.
DR OMA; HCTLEVV; -.
DR OrthoDB; 1484551at2759; -.
DR TreeFam; TF313779; -.
DR PathwayCommons; P62861; -.
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-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; P62861; -.
DR SIGNOR; P62861; -.
DR BioGRID-ORCS; 2197; 715 hits in 1049 CRISPR screens.
DR ChiTaRS; FAU; human.
DR GeneWiki; FAU_(gene); -.
DR GenomeRNAi; 2197; -.
DR Pharos; P62861; Tbio.
DR Proteomes; UP000005640; Chromosome 11.
DR Bgee; ENSG00000149806; Expressed in granulocyte and 97 other tissues.
DR ExpressionAtlas; P62861; baseline and differential.
DR Genevisible; P62861; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
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:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR CDD; cd01793; Ubl_FUBI; 1.
DR InterPro; IPR039415; FUBI.
DR InterPro; IPR006846; Ribosomal_S30.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF04758; Ribosomal_S30; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..133
FT /note="FAU ubiquitin-like and ribosomal protein S30"
FT /id="PRO_0000173999"
FT CHAIN 1..74
FT /note="Ubiquitin-like protein FUBI"
FT /id="PRO_0000455003"
FT CHAIN 75..133
FT /note="40S ribosomal protein S30"
FT /id="PRO_0000455004"
FT REGION 84..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62862"
FT VARIANT 53
FT /note="T -> I (in dbSNP:rs13807)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019644"
FT VARIANT 93
FT /note="V -> M"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_019643"
FT MUTAGEN 73
FT /note="G->A: Abolishes FUBI-ribosomal protein S30
FT processing; when associated with A-74. Impairs 40S ribosome
FT biogenesis."
FT /evidence="ECO:0000269|PubMed:34318747"
FT MUTAGEN 74
FT /note="G->A: Abolishes FUBI-ribosomal protein S30
FT processing; when associated with A-73. Impairs 40S ribosome
FT biogenesis."
FT /evidence="ECO:0000269|PubMed:34318747"
FT MUTAGEN 74
FT /note="G->V: Abolishes FUBI-ribosomal protein S30
FT processing. Impairs 40S ribosome biogenesis."
FT /evidence="ECO:0000269|PubMed:34318747"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:2L7R"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:2L7R"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:2L7R"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2L7R"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2L7R"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2L7R"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6ZN5"
SQ SEQUENCE 133 AA; 14390 MW; 5D2F81F2A355B559 CRC64;
MQLFVRAQEL HTFEVTGQET VAQIKAHVAS LEGIAPEDQV VLLAGAPLED EATLGQCGVE
ALTTLEVAGR MLGGKVHGSL ARAGKVRGQT PKVAKQEKKK KKTGRAKRRM QYNRRFVNVV
PTFGKKKGPN ANS
