ID   UBC5_YEAST              Reviewed;         148 AA.
AC   P15732; D6VS45;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   04-NOV-2026, entry version 208.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-16 kDa;
DE            EC=2.3.2.23 {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 5;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC5; OrderedLocusNames=YDR059C; ORFNames=D4234, YD9609.13C;
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], PROTEIN SEQUENCE OF 40-64 AND 119-125,
RP   FUNCTION, AND INDUCTION.
RX   PubMed=2154373; DOI=10.1002/j.1460-2075.1990.tb08141.x;
RA   Seufert W., Jentsch S.;
RT   "Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation
RT   of short-lived and abnormal proteins.";
RL   EMBO J. 9:543-550(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8789263;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1%3c85::aid-yea890%3e3.0.co;2-u;
RA   Brandt P., Ramlow S., Otto B., Bloecker H.;
RT   "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT   Saccharomyces cerevisiae chromosome IV.";
RL   Yeast 12:85-90(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867; DOI=10.1038/387s075;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, AND IDENTIFICATION IN THE RSP5-UBA1-UBC5 UBIQUITIN LIGASE
RP   COMPLEX.
RX   PubMed=19920177; DOI=10.1073/pnas.0907052106;
RA   Harreman M., Taschner M., Sigurdsson S., Anindya R., Reid J., Somesh B.,
RA   Kong S.E., Banks C.A., Conaway R.C., Conaway J.W., Svejstrup J.Q.;
RT   "Distinct ubiquitin ligases act sequentially for RNA polymerase II
RT   polyubiquitylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:20705-20710(2009).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins (PubMed:19920177, PubMed:2154373). Mediates the selective
CC       degradation of short-lived and abnormal proteins (PubMed:2154373). The
CC       RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming
CC       'Lys-63'-linked polyubiquitin chains (PubMed:19920177).
CC       {ECO:0000269|PubMed:19920177, ECO:0000269|PubMed:2154373}.
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, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Component of the RSP5-UBA1-UBC5 ubiquitin ligase complex
CC       composed of E3 RSP5, E1 UBA1 and E2 UBC5.
CC       {ECO:0000305|PubMed:19920177}.
CC   -!- INDUCTION: By heat shock and cadmium. {ECO:0000269|PubMed:2154373}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Present with 981 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17494; CAA35529.1; -; Genomic_DNA.
DR   EMBL; Z49209; CAA89088.1; -; Genomic_DNA.
DR   EMBL; X84162; CAA58975.1; -; Genomic_DNA.
DR   EMBL; Z74355; CAA98877.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11905.1; -; Genomic_DNA.
DR   PIR; S22858; S22858.
DR   RefSeq; NP_010344.1; NM_001180367.1.
DR   AlphaFoldDB; P15732; -.
DR   SMR; P15732; -.
DR   BioGRID; 32114; 77.
DR   FunCoup; P15732; 1027.
DR   IntAct; P15732; 5.
DR   STRING; 4932.YDR059C; -.
DR   GlyCosmos; P15732; 2 sites, 1 glycan.
DR   GlyGen; P15732; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P15732; -.
DR   PaxDb; 4932-YDR059C; -.
DR   PeptideAtlas; P15732; -.
DR   EnsemblFungi; YDR059C_mRNA; YDR059C; YDR059C.
DR   GeneID; 851631; -.
DR   KEGG; sce:YDR059C; -.
DR   AGR; SGD:S000002466; -.
DR   SGD; S000002466; UBC5.
DR   VEuPathDB; FungiDB:YDR059C; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; P15732; -.
DR   OMA; ANWCSNR; -.
DR   OrthoDB; 7851174at2759; -.
DR   BioCyc; YEAST:G3O-29667-MONOMER; -.
DR   Reactome; R-SCE-9033241; Peroxisomal protein import.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 851631; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P15732; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P15732; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070628; F:proteasome binding; IDA:SGD.
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:0000209; P:protein polyubiquitination; IDA:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd23792; UBCc_UBE2D; 1.
DR   FunFam; 3.10.110.10:FF:000010; Ubiquitin-conjugating enzyme E2-16 kDa; 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   Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW   Reference proteome; Stress response; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..148
FT                   /note="Ubiquitin-conjugating enzyme E2-16 kDa"
FT                   /id="PRO_0000082546"
FT   DOMAIN          2..148
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        86
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15731"
FT   CROSSLNK        91
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P15731"
SQ   SEQUENCE   148 AA;  16281 MW;  DC72805EC1F819AE CRC64;
     MSSSKRIAKE LSDLGRDPPA SCSAGPVGDD LYHWQASIMG PSDSPYAGGV FFLSIHFPTD
     YPFKPPKVNF TTKIYHPNIN SSGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL
     VPEIAQIYKT DKAKYEATAK EWTKKYAV
//