RS31_YEAST
ID RS31_YEAST Reviewed; 152 AA.
AC P05759; D6VYH3; P04838; P14800; P61864; Q6LA96;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Ubiquitin-40S ribosomal protein S31;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S31 {ECO:0000303|PubMed:9559554};
DE AltName: Full=CEP76;
DE AltName: Full=S37;
DE AltName: Full=Small ribosomal subunit protein eS31 {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS24;
DE Flags: Precursor;
GN Name=RPS31 {ECO:0000303|PubMed:24524803}; Synonyms=RPS37, UBI3;
GN OrderedLocusNames=YLR167W; ORFNames=L9470.14;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3038523; DOI=10.1002/j.1460-2075.1987.tb02384.x;
RA Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.;
RT "The yeast ubiquitin genes: a family of natural gene fusions.";
RL EMBO J. 6:1429-1439(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PARTIAL PROTEIN SEQUENCE OF 77-95.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
RN [5]
RP IDENTIFICATION OF PROTEIN (S31).
RX PubMed=2538753; DOI=10.1038/338394a0;
RA Finley D., Bartel B., Varshavsky A.;
RT "The tails of ubiquitin precursors are ribosomal proteins whose fusion to
RT ubiquitin facilitates ribosome biogenesis.";
RL Nature 338:394-401(1989).
RN [6]
RP MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63.
RX PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL J. Biol. Chem. 270:17442-17456(1995).
RN [7]
RP MUTAGENESIS OF LYSINE RESIDUES IN UBIQUITIN.
RX PubMed=7862120; DOI=10.1128/mcb.15.3.1265;
RA Spence J., Sadis S., Haas A.L., Finley D.;
RT "A ubiquitin mutant with specific defects in DNA repair and
RT multiubiquitination.";
RL Mol. Cell. Biol. 15:1265-1273(1995).
RN [8]
RP NOMENCLATURE, AND SUBUNIT (S31).
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked is
CC involved in endocytosis, and DNA-damage responses. Linear polymer
CC chains formed via attachment by the initiator Met lead to cell
CC signaling. Ubiquitin is usually conjugated to Lys residues of target
CC proteins, however, in rare cases, conjugation to Cys or Ser residues
CC has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC -!- FUNCTION: [40S ribosomal protein S31]: Component of the ribosome, a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. The small ribosomal subunit (SSU) binds messenger
CC RNAs (mRNAs) and translates the encoded message by selecting cognate
CC aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU)
CC contains the ribosomal catalytic site termed the peptidyl transferase
CC center (PTC), which catalyzes the formation of peptide bonds, thereby
CC polymerizing the amino acids delivered by tRNAs into a polypeptide
CC chain. The nascent polypeptides leave the ribosome through a tunnel in
CC the LSU and interact with protein factors that function in enzymatic
CC processing, targeting, and the membrane insertion of nascent chains at
CC the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [40S ribosomal protein S31]: Cytoplasm
CC {ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by several different genes. UBI1
CC and UBI2 genes code for a single copy of ubiquitin fused to the
CC ribosomal proteins eL40. UBI3 is a polyprotein with one copy of
CC ubiquitin fused to ribosomal protein eS31. UBI4 is a polyprotein
CC containing 5 exact head to tail repeats of ubiquitin. {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 eS31 family. {ECO:0000305}.
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DR EMBL; X05730; CAA29197.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67466.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09489.1; -; Genomic_DNA.
DR PIR; C29456; UQBYR7.
DR RefSeq; NP_013268.1; NM_001182054.1.
DR PDB; 3J6X; EM; 6.10 A; 31=1-152.
DR PDB; 3J6Y; EM; 6.10 A; 31=1-152.
DR PDB; 3J77; EM; 6.20 A; 31=1-152.
DR PDB; 3J78; EM; 6.30 A; 31=1-152.
DR PDB; 4U3M; X-ray; 3.00 A; E1=77-152, e1=78-152.
DR PDB; 4U3N; X-ray; 3.20 A; E1=77-152, e1=78-152.
DR PDB; 4U3U; X-ray; 2.90 A; E1=77-152, e1=78-152.
DR PDB; 4U4N; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 4U4O; X-ray; 3.60 A; E1=78-152, e1=77-152.
DR PDB; 4U4Q; X-ray; 3.00 A; E1/e1=77-152.
DR PDB; 4U4R; X-ray; 2.80 A; E1/e1=77-152.
DR PDB; 4U4U; X-ray; 3.00 A; E1/e1=77-152.
DR PDB; 4U4Y; X-ray; 3.20 A; E1/e1=77-152.
DR PDB; 4U4Z; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 4U50; X-ray; 3.20 A; E1/e1=78-152.
DR PDB; 4U51; X-ray; 3.20 A; E1/e1=77-152.
DR PDB; 4U52; X-ray; 3.00 A; E1/e1=77-152.
DR PDB; 4U53; X-ray; 3.30 A; E1/e1=77-152.
DR PDB; 4U55; X-ray; 3.20 A; E1/e1=77-152.
DR PDB; 4U56; X-ray; 3.45 A; E1/e1=77-152.
DR PDB; 4U6F; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 4V88; X-ray; 3.00 A; Af/Cf=1-152.
DR PDB; 4V8Y; EM; 4.30 A; A5=1-152.
DR PDB; 4V8Z; EM; 6.60 A; A5=1-152.
DR PDB; 4V92; EM; 3.70 A; f=101-152.
DR PDB; 5DAT; X-ray; 3.15 A; E1/e1=77-152.
DR PDB; 5DC3; X-ray; 3.25 A; E1/e1=78-152.
DR PDB; 5DGE; X-ray; 3.45 A; E1/e1=77-152.
DR PDB; 5DGF; X-ray; 3.30 A; E1/e1=77-152.
DR PDB; 5DGV; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 5FCI; X-ray; 3.40 A; E1/e1=77-152.
DR PDB; 5FCJ; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 5I4L; X-ray; 3.10 A; E1/e1=77-152.
DR PDB; 5JUO; EM; 4.00 A; CC=1-152.
DR PDB; 5JUP; EM; 3.50 A; CC=1-152.
DR PDB; 5JUS; EM; 4.20 A; CC=1-152.
DR PDB; 5JUT; EM; 4.00 A; CC=1-152.
DR PDB; 5JUU; EM; 4.00 A; CC=1-152.
DR PDB; 5L6H; X-ray; 2.30 A; B/D/E=1-76.
DR PDB; 5L6I; X-ray; 2.76 A; B/D/E=1-76.
DR PDB; 5L6J; X-ray; 2.68 A; B/D=1-76.
DR PDB; 5LYB; X-ray; 3.25 A; E1/e1=77-152.
DR PDB; 5M1J; EM; 3.30 A; f2=82-152.
DR PDB; 5MC6; EM; 3.80 A; N=1-152.
DR PDB; 5NDG; X-ray; 3.70 A; E1/e1=1-152.
DR PDB; 5NDW; X-ray; 3.70 A; E1/e1=80-152.
DR PDB; 5OBM; X-ray; 3.40 A; E1/e1=81-152.
DR PDB; 5TGA; X-ray; 3.30 A; E1/e1=77-152.
DR PDB; 5TGM; X-ray; 3.50 A; E1/e1=77-152.
DR PDB; 5U4P; X-ray; 2.50 A; C=1-76.
DR PDB; 5WYJ; EM; 8.70 A; Sg=1-152.
DR PDB; 6EML; EM; 3.60 A; N=1-152.
DR PDB; 6GQ1; EM; 4.40 A; AW=116-152.
DR PDB; 6GQB; EM; 3.90 A; AW=116-152.
DR PDB; 6GQV; EM; 4.00 A; AW=116-152.
DR PDB; 6HHQ; X-ray; 3.10 A; e1/g=1-152.
DR PDB; 6I7O; EM; 5.30 A; N/Nb=80-152.
DR PDB; 6Q8Y; EM; 3.10 A; N=102-152.
DR PDB; 6RBE; EM; 3.80 A; f=1-152.
DR PDB; 6S47; EM; 3.28 A; Bg=2-152.
DR PDB; 6SNT; EM; 2.80 A; f=1-152.
DR PDB; 6SV4; EM; 3.30 A; N/Nb/Nc=1-152.
DR PDB; 6T4Q; EM; 2.60 A; Sf=80-152.
DR PDB; 6T7I; EM; 3.20 A; Sf=1-152.
DR PDB; 6T7T; EM; 3.10 A; Sf=1-152.
DR PDB; 6T83; EM; 4.00 A; 6/fb=1-152.
DR PDB; 6TB3; EM; 2.80 A; N=80-152.
DR PDB; 6TNU; EM; 3.10 A; N=80-152.
DR PDB; 6WDR; EM; 3.70 A; f=82-152.
DR PDB; 6WOO; EM; 2.90 A; ff=94-150.
DR PDB; 6Z6J; EM; 3.40 A; Sf=1-152.
DR PDB; 6Z6K; EM; 3.40 A; Sf=1-152.
DR PDB; 6ZCE; EM; 5.30 A; g=1-152.
DR PDB; 6ZQH; X-ray; 2.03 A; B/D=1-76.
DR PDB; 6ZU9; EM; 6.20 A; O=1-152.
DR PDB; 6ZVI; EM; 3.00 A; Q=80-152.
DR PDB; 7A1G; EM; 3.00 A; N=80-152.
DR PDB; 7B7D; EM; 3.30 A; N=80-152.
DR PDB; 7NRC; EM; 3.90 A; SN=80-152.
DR PDB; 7NRD; EM; 4.36 A; SN=80-152.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5L6H; -.
DR PDBsum; 5L6I; -.
DR PDBsum; 5L6J; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5U4P; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQH; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P05759; -.
DR BMRB; P05759; -.
DR SMR; P05759; -.
DR BioGRID; 31440; 106.
DR ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DR DIP; DIP-6389N; -.
DR IntAct; P05759; 22.
DR MINT; P05759; -.
DR STRING; 4932.YLR167W; -.
DR iPTMnet; P05759; -.
DR SWISS-2DPAGE; P61864; -.
DR MaxQB; P05759; -.
DR PaxDb; P05759; -.
DR PRIDE; P05759; -.
DR EnsemblFungi; YLR167W_mRNA; YLR167W; YLR167W.
DR GeneID; 850864; -.
DR KEGG; sce:YLR167W; -.
DR SGD; S000004157; RPS31.
DR VEuPathDB; FungiDB:YLR167W; -.
DR eggNOG; KOG0004; Eukaryota.
DR GeneTree; ENSGT00940000157820; -.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P05759; -.
DR OMA; FMAQHAN; -.
DR BioCyc; YEAST:G3O-32297-MON; -.
DR Reactome; R-SCE-110312; Translesion synthesis by REV1.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SCE-5655862; Translesion synthesis by POLK.
DR Reactome; R-SCE-5656121; Translesion synthesis by POLI.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-5689603; UCH proteinases.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-5689901; Metalloprotease DUBs.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-68949; Orc1 removal from chromatin.
DR Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SCE-69541; Stabilization of p53.
DR Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SCE-8948747; Regulation of PTEN localization.
DR Reactome; R-SCE-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SCE-8951664; Neddylation.
DR Reactome; R-SCE-901032; ER Quality Control Compartment (ERQC).
DR Reactome; R-SCE-9020702; Interleukin-1 signaling.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SCE-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-9664873; Pexophagy.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P05759; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P05759; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031386; F:protein tag; IMP:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0002109; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S); IMP:SGD.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_S27a.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR038582; S27a-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396487"
FT CHAIN 77..152
FT /note="40S ribosomal protein S31"
FT /id="PRO_0000137688"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 121..144
FT /note="C4-type"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT MUTAGEN 29
FT /note="K->R: Deficiency in ubiquitin-protein conjugate
FT formation."
FT /evidence="ECO:0000269|PubMed:7615550"
FT MUTAGEN 48
FT /note="K->R: Deficiency in ubiquitin-protein conjugate
FT formation."
FT /evidence="ECO:0000269|PubMed:7615550"
FT MUTAGEN 63
FT /note="K->R: Deficiency in ubiquitin-protein conjugate
FT formation. Loss of DNA repair function."
FT /evidence="ECO:0000269|PubMed:7615550"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6ZQH"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5L6H"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6ZQH"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 152 AA; 17216 MW; 53BF38E2E2F8B38E CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHKKVKL AVLSYYKVDA EGKVTKLRRE
CSNPTCGAGV FLANHKDRLY CGKCHSVYKV NA
