ID   UBC11_YEAST             Reviewed;         156 AA.
AC   P52492; D6W334;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 11;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC11; OrderedLocusNames=YOR339C; ORFNames=O6268;
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].
RC   STRAIN=ATCC 90843 / S288c / FY73;
RX   PubMed=8948102;
RX   DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA   Purnelle B., Goffeau A.;
RT   "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT   chromosome XV reveals 18 open reading frames including a new pyruvate
RT   kinase and three homologues to chromosome I genes.";
RL   Yeast 12:1475-1481(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   CHARACTERIZATION.
RX   PubMed=9675819;
RX   DOI=10.1002/(sici)1097-0061(19980615)14:8<747::aid-yea271>3.0.co;2-t;
RA   Townsley F.M., Ruderman J.V.;
RT   "Functional analysis of the Saccharomyces cerevisiae UBC11 gene.";
RL   Yeast 14:747-757(1998).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X95720; CAA65027.1; -; Genomic_DNA.
DR   EMBL; Z75247; CAA99663.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11100.1; -; Genomic_DNA.
DR   PIR; S67248; S67248.
DR   RefSeq; NP_014984.3; NM_001183759.3.
DR   AlphaFoldDB; P52492; -.
DR   SMR; P52492; -.
DR   BioGRID; 34722; 50.
DR   DIP; DIP-7221N; -.
DR   IntAct; P52492; 5.
DR   STRING; 4932.YOR339C; -.
DR   PaxDb; 4932-YOR339C; -.
DR   PeptideAtlas; P52492; -.
DR   EnsemblFungi; YOR339C_mRNA; YOR339C; YOR339C.
DR   GeneID; 854517; -.
DR   KEGG; sce:YOR339C; -.
DR   AGR; SGD:S000005866; -.
DR   SGD; S000005866; UBC11.
DR   VEuPathDB; FungiDB:YOR339C; -.
DR   eggNOG; KOG0421; Eukaryota.
DR   GeneTree; ENSGT00930000150941; -.
DR   HOGENOM; CLU_030988_9_1_1; -.
DR   InParanoid; P52492; -.
DR   OMA; YNVQTIL; -.
DR   OrthoDB; 46085at2759; -.
DR   BioCyc; YEAST:G3O-33814-MONOMER; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 854517; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P52492; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P52492; Protein.
DR   GO; GO:0005737; C:cytoplasm; IC: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; ISS:SGD.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IBA:GO_Central.
DR   GO; GO:0006513; P:protein monoubiquitination; TAS:SGD.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF338; UBIQUITIN-CONJUGATING ENZYME E2C; 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   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..156
FT                   /note="Ubiquitin-conjugating enzyme E2-18 kDa"
FT                   /id="PRO_0000082559"
FT   DOMAIN          8..155
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        93
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   156 AA;  17753 MW;  950C69F224900197 CRC64;
     MAVEEGGCVT KRLQNELLQL LSSTTESISA FPVDDNDLTY WVGYITGPKD TPYSGLKFKV
     SLKFPQNYPF HPPMIKFLSP MWHPNVDKSG NICLDILKEK WSAVYNVETI LLSLQSLLGE
     PNNRSPLNAV AAELWDADME EYRKKVLACY EEIDDY
//