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   27-MAR-2024, entry version 159.
DE   RecName: Full=Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein {ECO:0000305};
DE   AltName: Full=FAU ubiquitin like and ribosomal protein S30 fusion {ECO:0000312|HGNC:HGNC:3597};
DE   Contains:
DE     RecName: Full=Ubiquitin-like protein FUBI;
DE   Contains:
DE     RecName: Full=Small ribosomal subunit protein eS30 {ECO:0000303|PubMed:24524803};
DE     AltName: Full=40S ribosomal protein S30;
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) OF 80S 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   [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: [Small ribosomal subunit protein eS30]: Component of the 40S
CC       subunit of the ribosome. Contributes to the assembly and function of
CC       40S ribosomal subunits. {ECO:0000269|PubMed:23636399,
CC       ECO:0000269|PubMed:34318747}.
CC   -!- SUBUNIT: [Small ribosomal subunit protein eS30]: Component of the 40S
CC       subunit of the ribosome. {ECO:0000269|PubMed:23636399,
CC       ECO:0000269|PubMed:34318747}.
CC   -!- INTERACTION:
CC       P62861; Q92876: KLK6; NbExp=3; IntAct=EBI-358093, EBI-2432309;
CC   -!- SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS30]: Cytoplasm
CC       {ECO:0000269|PubMed:23636399}. Nucleus {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="https://atlasgeneticsoncology.org/gene/40538/FAU";
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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   PDB; 7QP6; EM; 4.70 A; F=75-133.
DR   PDB; 7QP7; EM; 3.70 A; F=75-133.
DR   PDB; 7R4X; EM; 2.15 A; e=75-133.
DR   PDB; 7TQL; EM; 3.40 A; e=81-133.
DR   PDB; 7WTS; EM; 3.20 A; e=75-133.
DR   PDB; 7WTT; EM; 3.10 A; e=75-133.
DR   PDB; 7WTU; EM; 3.00 A; e=75-133.
DR   PDB; 7WTV; EM; 3.50 A; e=75-133.
DR   PDB; 7WTW; EM; 3.20 A; e=75-133.
DR   PDB; 7WTX; EM; 3.10 A; e=75-133.
DR   PDB; 7WTZ; EM; 3.00 A; e=75-133.
DR   PDB; 7WU0; EM; 3.30 A; e=75-133.
DR   PDB; 7XNX; EM; 2.70 A; Se=75-133.
DR   PDB; 7XNY; EM; 2.50 A; Se=75-133.
DR   PDB; 8BS3; X-ray; 2.20 A; B=1-73.
DR   PDB; 8G5Y; EM; 2.29 A; Se=1-133.
DR   PDB; 8G5Z; EM; 2.64 A; Se=75-133.
DR   PDB; 8G60; EM; 2.54 A; Se=1-133.
DR   PDB; 8G61; EM; 2.94 A; Se=1-133.
DR   PDB; 8G6J; EM; 2.80 A; Se=1-133.
DR   PDB; 8GLP; EM; 1.67 A; Se=1-133.
DR   PDB; 8JDJ; EM; 2.50 A; AQ=75-133.
DR   PDB; 8JDK; EM; 2.26 A; AQ=75-133.
DR   PDB; 8JDL; EM; 2.42 A; AQ=75-133.
DR   PDB; 8JDM; EM; 2.67 A; AQ=75-133.
DR   PDB; 8PPK; EM; 2.98 A; e=1-133.
DR   PDB; 8PPL; EM; 2.65 A; Ae=1-133.
DR   PDB; 8T4S; EM; 2.60 A; e=1-133.
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   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; 8BS3; -.
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; P62861; -.
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-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-3770; -.
DR   EMDB; EMD-40205; -.
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; P62861; -.
DR   BioGRID; 108491; 314.
DR   ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR   CORUM; P62861; -.
DR   IntAct; P62861; 51.
DR   MINT; P62861; -.
DR   STRING; 9606.ENSP00000431822; -.
DR   GlyGen; P62861; 1 site, 1 O-linked glycan (1 site).
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   PaxDb; 9606-ENSP00000435370; -.
DR   PeptideAtlas; P62861; -.
DR   ProteomicsDB; 55079; -.
DR   ProteomicsDB; 57440; -.
DR   Pumba; P62861; -.
DR   TopDownProteomics; P62861; -.
DR   Antibodypedia; 29676; 417 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   GeneID; 2197; -.
DR   KEGG; hsa:2197; -.
DR   MANE-Select; ENST00000529639.6; ENSP00000435370.1; NM_001997.5; NP_001988.1.
DR   UCSC; uc001ocx.4; human.
DR   AGR; HGNC:3597; -.
DR   CTD; 2197; -.
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   InParanoid; P62861; -.
DR   OMA; HCTLEVV; -.
DR   OrthoDB; 177691at2759; -.
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-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; P62861; -.
DR   SIGNOR; P62861; -.
DR   BioGRID-ORCS; 2197; 752 hits in 1129 CRISPR screens.
DR   ChiTaRS; FAU; human.
DR   GeneWiki; FAU_(gene); -.
DR   GenomeRNAi; 2197; -.
DR   Pharos; P62861; Tbio.
DR   PRO; PR:P62861; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000149806; Expressed in granulocyte and 99 other cell types or tissues.
DR   ExpressionAtlas; P62861; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS: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: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; NAS:ComplexPortal.
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:0006412; P:translation; IC:UniProtKB.
DR   CDD; cd01793; Ubl_FUBI; 1.
DR   InterPro; IPR039415; FUBI.
DR   InterPro; IPR006846; Ribosomal_eS30.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR12650; 40S RIBOSOMAL PROTEIN S30/UBIQUITIN-LIKE PROTEIN FUBI; 1.
DR   PANTHER; PTHR12650:SF15; SIMILAR TO UBIQUITIN-LIKE_S30 RIBOSOMAL FUSION PROTEIN-RELATED; 1.
DR   Pfam; PF04758; Ribosomal_S30; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; P62861; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..133
FT                   /note="Ubiquitin-like FUBI-ribosomal protein eS30 fusion
FT                   protein"
FT                   /id="PRO_0000173999"
FT   CHAIN           1..74
FT                   /note="Ubiquitin-like protein FUBI"
FT                   /id="PRO_0000455003"
FT   CHAIN           75..133
FT                   /note="Small ribosomal subunit protein eS30"
FT                   /id="PRO_0000455004"
FT   DOMAIN          1..74
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
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:8BS3"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:8BS3"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:8BS3"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:8BS3"
FT   HELIX           54..57
FT                   /evidence="ECO:0007829|PDB:8BS3"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:8BS3"
FT   TURN            81..84
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   HELIX           85..89
FT                   /evidence="ECO:0007829|PDB:7R4X"
FT   HELIX           104..116
FT                   /evidence="ECO:0007829|PDB:7R4X"
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
//