UBC8_YEAST
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 03-AUG-2022, entry version 179.
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;
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 (PubMed:1869573) (By similarity). 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:9737955, PubMed:10811607,
CC PubMed:12686616). Required for proteasome-dependent catabolite
CC degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:9737955,
CC PubMed:10811607, PubMed:12686616, PubMed:28126757).
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 AlphaFoldDB; P28263; -.
DR SMR; P28263; -.
DR BioGRID; 36719; 112.
DR DIP; DIP-5299N; -.
DR IntAct; P28263; 2.
DR MINT; P28263; -.
DR STRING; 4932.YEL012W; -.
DR CarbonylDB; P28263; -.
DR MaxQB; P28263; -.
DR PaxDb; P28263; -.
DR PRIDE; P28263; -.
DR EnsemblFungi; YEL012W_mRNA; YEL012W; YEL012W.
DR GeneID; 856704; -.
DR KEGG; sce:YEL012W; -.
DR SGD; S000000738; UBC8.
DR VEuPathDB; FungiDB:YEL012W; -.
DR eggNOG; KOG0416; Eukaryota.
DR GeneTree; ENSGT00390000004852; -.
DR HOGENOM; CLU_030988_7_1_1; -.
DR InParanoid; P28263; -.
DR OMA; EFCVKFY; -.
DR BioCyc; YEAST:G3O-30138-MON; -.
DR Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P28263; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P28263; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA: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; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Transferase; 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 163..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..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
