UBC1_YEAST
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 03-AUG-2022, entry version 202.
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; 165.
DR DIP; DIP-6594N; -.
DR IntAct; P21734; 6.
DR MINT; P21734; -.
DR STRING; 4932.YDR177W; -.
DR iPTMnet; P21734; -.
DR MaxQB; P21734; -.
DR PaxDb; P21734; -.
DR PRIDE; P21734; -.
DR EnsemblFungi; YDR177W_mRNA; YDR177W; YDR177W.
DR GeneID; 851757; -.
DR KEGG; sce:YDR177W; -.
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; HHLKGSF; -.
DR BioCyc; YEAST:G3O-29766-MON; -.
DR BRENDA; 2.3.2.24; 984.
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 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; cd00195; UBCc; 1.
DR DisProt; DP02193; -.
DR Gene3D; 3.10.110.10; -; 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 Pfam; PF09288; UBA_3; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF46934; SSF46934; 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 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
