ID   UBC1_YEAST              Reviewed;         215 AA.
AC   P21734; D6VSF9;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 1;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 1;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=UBC1; OrderedLocusNames=YDR177W; ORFNames=YD9395.10;
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=2265617; DOI=10.1002/j.1460-2075.1990.tb07905.x;
RA   Seufert W., McGrath J.P., Jeutsch S.;
RT   "UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-
RT   conjugating enzymes involved in protein degradation.";
RL   EMBO J. 9:4535-4541(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=10878801; DOI=10.1038/35017001;
RA   Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T.;
RT   "A regulatory link between ER-associated protein degradation and the
RT   unfolded-protein response.";
RL   Nat. Cell Biol. 2:379-384(2000).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH HDR1.
RX   PubMed=11146622; DOI=10.1038/35050524;
RA   Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
RT   "Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
RT   associated degradation.";
RL   Nat. Cell Biol. 3:24-29(2001).
RN   [7]
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   [8]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-93, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND STRUCTURE BY NMR IN COMPLEX WITH
RP   UBIQUITIN.
RX   PubMed=11591345; DOI=10.1016/s0969-2126(01)00657-8;
RA   Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T.,
RA   McKenna S., Ptak C., Glover M., Shaw G.S.;
RT   "Structure of a conjugating enzyme-ubiquitin thiolester intermediate
RT   reveals a novel role for the ubiquitin tail.";
RL   Structure 9:897-904(2001).
RN   [10]
RP   STRUCTURE BY NMR OF 2-215.
RX   PubMed=15328341; DOI=10.1074/jbc.m409576200;
RA   Merkley N., Shaw G.S.;
RT   "Solution structure of the flexible class II ubiquitin-conjugating enzyme
RT   Ubc1 provides insights for polyubiquitin chain assembly.";
RL   J. Biol. Chem. 279:47139-47147(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Functions in degradation of misfolded or regulated proteins
CC       localized in the endoplasmic reticulum (ER) lumen or membrane via the
CC       ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1
CC       ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M
CC       pathways responsible for the rapid degradation of soluble lumenal and
CC       membrane proteins with misfolded lumenal domains (ERAD-L), or ER-
CC       membrane proteins with misfolded transmembrane domains (ERAD-M).
CC       {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10878801,
CC       ECO:0000269|PubMed:11146622}.
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   -!- DEVELOPMENTAL STAGE: Early stages of growth after spore germination.
CC   -!- INDUCTION: By heat shock and cadmium.
CC   -!- MISCELLANEOUS: Present with 8940 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}.
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DR   EMBL; X56402; CAA39812.1; -; Genomic_DNA.
DR   EMBL; Z46727; CAA86682.1; -; Genomic_DNA.
DR   EMBL; AY557675; AAS56001.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12019.1; -; Genomic_DNA.
DR   PIR; S12493; S12493.
DR   RefSeq; NP_010462.3; NM_001180484.3.
DR   PDB; 1FXT; NMR; -; A=2-150.
DR   PDB; 1FZY; X-ray; 1.90 A; A/B=2-150.
DR   PDB; 1TTE; NMR; -; A=1-215.
DR   PDBsum; 1FXT; -.
DR   PDBsum; 1FZY; -.
DR   PDBsum; 1TTE; -.
DR   AlphaFoldDB; P21734; -.
DR   BMRB; P21734; -.
DR   SMR; P21734; -.
DR   BioGRID; 32230; 173.
DR   DIP; DIP-6594N; -.
DR   IntAct; P21734; 6.
DR   MINT; P21734; -.
DR   STRING; 4932.YDR177W; -.
DR   iPTMnet; P21734; -.
DR   MaxQB; P21734; -.
DR   PaxDb; 4932-YDR177W; -.
DR   PeptideAtlas; P21734; -.
DR   EnsemblFungi; YDR177W_mRNA; YDR177W; YDR177W.
DR   GeneID; 851757; -.
DR   KEGG; sce:YDR177W; -.
DR   AGR; SGD:S000002584; -.
DR   SGD; S000002584; UBC1.
DR   VEuPathDB; FungiDB:YDR177W; -.
DR   eggNOG; KOG0418; Eukaryota.
DR   GeneTree; ENSGT00940000170562; -.
DR   HOGENOM; CLU_030988_13_1_1; -.
DR   InParanoid; P21734; -.
DR   OMA; TGYFKGP; -.
DR   OrthoDB; 102270at2759; -.
DR   BioCyc; YEAST:G3O-29766-MONOMER; -.
DR   BRENDA; 2.3.2.24; 984.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 851757; 4 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P21734; -.
DR   PRO; PR:P21734; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P21734; Protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0016050; P:vesicle organization; IMP:SGD.
DR   CDD; cd14311; UBA_II_E2_UBC1; 1.
DR   CDD; cd00195; UBCc; 1.
DR   DisProt; DP02193; -.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR015368; UBA_C_fun.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF347; E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF09288; UBA_3; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF46934; UBA-like; 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; ATP-binding; Isopeptide bond; Nucleotide-binding;
KW   Reference proteome; Stress response; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..215
FT                   /note="Ubiquitin-conjugating enzyme E2 1"
FT                   /id="PRO_0000082525"
FT   DOMAIN          2..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   HELIX           3..15
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:1TTE"
FT   STRAND          32..40
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          43..45
FT                   /evidence="ECO:0007829|PDB:1FXT"
FT   TURN            46..49
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   TURN            60..63
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1TTE"
FT   TURN            82..84
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   HELIX           102..114
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:1FXT"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   HELIX           134..148
FT                   /evidence="ECO:0007829|PDB:1FZY"
FT   HELIX           170..179
FT                   /evidence="ECO:0007829|PDB:1TTE"
FT   HELIX           183..192
FT                   /evidence="ECO:0007829|PDB:1TTE"
FT   HELIX           204..213
FT                   /evidence="ECO:0007829|PDB:1TTE"
SQ   SEQUENCE   215 AA;  24178 MW;  899CC397A1285145 CRC64;
     MSRAKRIMKE IQAVKDDPAA HITLEFVSES DIHHLKGTFL GPPGTPYEGG KFVVDIEVPM
     EYPFKPPKMQ FDTKVYHPNI SSVTGAICLD ILKNAWSPVI TLKSALISLQ ALLQSPEPND
     PQDAEVAQHY LRDRESFNKT AALWTRLYAS ETSNGQKGNV EESDLYGIDH DLIDEFESQG
     FEKDKIVEVL RRLGVKSLDP NDNNTANRII EELLK
//