ID   UBC8_YEAST              Reviewed;         218 AA.
AC   P28263; D3DLN7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   02-SEP-2026, entry version 197.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
DE            EC=2.3.2.23 {ECO:0000269|PubMed:1869573};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 8;
DE   AltName: Full=Glucose-induced degradation protein 3;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC8; Synonyms=GID3; OrderedLocusNames=YEL012W;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=1869573; DOI=10.1016/s0021-9258(18)98652-7;
RA   Qin S., Nakajima B., Nomura M., Arfin S.M.;
RT   "Cloning and characterization of a Saccharomyces cerevisiae gene encoding a
RT   new member of the ubiquitin-conjugating protein family.";
RL   J. Biol. Chem. 266:15549-15554(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169868; DOI=10.1038/387s078;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(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   SEQUENCE REVISION TO N-TERMINUS.
RX   PubMed=8132613; DOI=10.1016/s0021-9258(17)37039-4;
RA   Kaiser P., Seufert W., Hoefferer L., Kofler B., Sachsenmaier C., Herzog H.,
RA   Jentsch S., Schweiger M., Schneider R.;
RT   "A human ubiquitin-conjugating enzyme homologous to yeast UBC8.";
RL   J. Biol. Chem. 269:8797-8802(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9737955; DOI=10.1074/jbc.273.39.25000;
RA   Haemmerle M., Bauer J., Rose M., Szallies A., Thumm M., Duesterhus S.,
RA   Mecke D., Entian K.D., Wolf D.H.;
RT   "Proteins of newly isolated mutants and the amino-terminal proline are
RT   essential for ubiquitin-proteasome-catalyzed catabolite degradation of
RT   fructose-1,6-bisphosphatase of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:25000-25005(1998).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10811607; DOI=10.1093/emboj/19.10.2161;
RA   Schuele T., Rose M., Entian K.-D., Thumm M., Wolf D.H.;
RT   "Ubc8p functions in catabolite degradation of fructose-1, 6-bisphosphatase
RT   in yeast.";
RL   EMBO J. 19:2161-2167(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
RA   Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
RA   Thumm M., Wolf D.H.;
RT   "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
RT   Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
RT   genes and indicates the existence of two degradation pathways.";
RL   Mol. Biol. Cell 14:1652-1663(2003).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=28126757; DOI=10.1126/science.aal3655;
RA   Chen S.J., Wu X., Wadas B., Oh J.H., Varshavsky A.;
RT   "An N-end rule pathway that recognizes proline and destroys gluconeogenic
RT   enzymes.";
RL   Science 355:0-0(2017).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins (By similarity) (PubMed:1869573). Required for the adaptation
CC       to the presence of glucose in the growth medium; mediates the
CC       degradation of enzymes involved in gluconeogenesis when cells are
CC       shifted to glucose-containing medium (PubMed:10811607, PubMed:12686616,
CC       PubMed:9737955). Required for proteasome-dependent catabolite
CC       degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:10811607,
CC       PubMed:12686616, PubMed:28126757, PubMed:9737955).
CC       {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10811607,
CC       ECO:0000269|PubMed:12686616, ECO:0000269|PubMed:1869573,
CC       ECO:0000269|PubMed:28126757, ECO:0000269|PubMed:9737955}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00388,
CC         ECO:0000269|PubMed:1869573};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:1869573}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10811607}.
CC   -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB64489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M65083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U18530; AAB64489.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z29329; CAA82526.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07641.1; -; Genomic_DNA.
DR   PIR; B53516; B53516.
DR   RefSeq; NP_010904.2; NM_001178827.1.
DR   PDB; 8PMQ; EM; 3.53 A; E=1-218.
DR   AlphaFoldDB; P28263; -.
DR   EMDB; EMD-17764; -.
DR   SMR; P28263; -.
DR   BioGRID; 36719; 125.
DR   DIP; DIP-5299N; -.
DR   FunCoup; P28263; 1021.
DR   IntAct; P28263; 6.
DR   MINT; P28263; -.
DR   STRING; 4932.YEL012W; -.
DR   CarbonylDB; P28263; -.
DR   iPTMnet; P28263; -.
DR   PaxDb; 4932-YEL012W; -.
DR   PeptideAtlas; P28263; -.
DR   EnsemblFungi; YEL012W_mRNA; YEL012W; YEL012W.
DR   GeneID; 856704; -.
DR   KEGG; sce:YEL012W; -.
DR   AGR; SGD:S000000738; -.
DR   SGD; S000000738; UBC8.
DR   VEuPathDB; FungiDB:YEL012W; -.
DR   eggNOG; KOG0416; Eukaryota.
DR   HOGENOM; CLU_030988_7_1_1; -.
DR   InParanoid; P28263; -.
DR   OMA; KFYVRFK; -.
DR   OrthoDB; 269518at2759; -.
DR   BioCyc; YEAST:G3O-30138-MONOMER; -.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 856704; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P28263; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P28263; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; EXP:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR   GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IMP:SGD.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   CDD; cd23797; UBCc_UBE2H; 1.
DR   FunFam; 3.10.110.10:FF:000016; Ubiquitin-conjugating enzyme E2 H; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBC.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..218
FT                   /note="Ubiquitin-conjugating enzyme E2-24 kDa"
FT                   /id="PRO_0000082555"
FT   DOMAIN          3..148
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          154..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..183
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..218
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   218 AA;  24633 MW;  24FFAD8B4679CE6F CRC64;
     MSSSKRRIET DVMKLLMSDH QVDLINDSMQ EFHVKFLGPK DTPYENGVWR LHVELPDNYP
     YKSPSIGFVN KIFHPNIDIA SGSICLDVIN STWSPLYDLI NIVEWMIPGL LKEPNGSDPL
     NNEAATLQLR DKKLYEEKIK EYIDKYATKE KYQQMFGGDN DSDDSDSGGD LQEEDSDSDE
     DMDGTGVSSG DDSVDELSED LSDIDVSDDD DYDEVANQ
//