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Ubiquitin-conjugating enzyme E2 1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 1) (Ubiquitin carrier protein) (Ubiquitin-conjugating enzyme E2-24 kDa) (Ubiquitin-protein ligase)

 UBC1_YEAST              Reviewed;         215 AA.
P21734; D6VSF9;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
20-JUN-2018, entry version 179.
RecName: Full=Ubiquitin-conjugating enzyme E2 1;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme 1;
AltName: Full=Ubiquitin carrier protein;
AltName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
AltName: Full=Ubiquitin-protein ligase;
Name=UBC1; OrderedLocusNames=YDR177W; ORFNames=YD9395.10;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2265617;
Seufert W., McGrath J.P., Jeutsch S.;
"UBC1 encodes a novel member of an essential subfamily of yeast
ubiquitin-conjugating enzymes involved in protein degradation.";
EMBO J. 9:4535-4541(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=10878801; DOI=10.1038/35017001;
Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T.;
"A regulatory link between ER-associated protein degradation and the
unfolded-protein response.";
Nat. Cell Biol. 2:379-384(2000).
[6]
FUNCTION, AND INTERACTION WITH HDR1.
PubMed=11146622; DOI=10.1038/35050524;
Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.;
"Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-
associated degradation.";
Nat. Cell Biol. 3:24-29(2001).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-93, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND STRUCTURE BY NMR IN COMPLEX
WITH UBIQUITIN.
PubMed=11591345; DOI=10.1016/S0969-2126(01)00657-8;
Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T.,
McKenna S., Ptak C., Glover M., Shaw G.S.;
"Structure of a conjugating enzyme-ubiquitin thiolester intermediate
reveals a novel role for the ubiquitin tail.";
Structure 9:897-904(2001).
[10]
STRUCTURE BY NMR OF 2-215.
PubMed=15328341; DOI=10.1074/jbc.M409576200;
Merkley N., Shaw G.S.;
"Solution structure of the flexible class II ubiquitin-conjugating
enzyme Ubc1 provides insights for polyubiquitin chain assembly.";
J. Biol. Chem. 279:47139-47147(2004).
-!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins. Functions in degradation of misfolded or regulated
proteins localized in the endoplasmic reticulum (ER) lumen or
membrane via the ubiquitin-proteasome system. Cognate E2
conjugating enzyme for the HRD1 ubiquitin ligase complex, which is
part of the ERAD-L and ERAD-M pathways responsible for the rapid
degradation of soluble lumenal and membrane proteins with
misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
misfolded transmembrane domains (ERAD-M). {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000269|PubMed:10878801,
ECO:0000269|PubMed:11146622}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- INTERACTION:
P61864:UBI4 (xeno); NbExp=2; IntAct=EBI-19717, EBI-19797;
-!- DEVELOPMENTAL STAGE: Early stages of growth after spore
germination.
-!- INDUCTION: By heat shock and cadmium.
-!- MISCELLANEOUS: Present with 8940 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X56402; CAA39812.1; -; Genomic_DNA.
EMBL; Z46727; CAA86682.1; -; Genomic_DNA.
EMBL; AY557675; AAS56001.1; -; Genomic_DNA.
EMBL; BK006938; DAA12019.1; -; Genomic_DNA.
PIR; S12493; S12493.
RefSeq; NP_010462.3; NM_001180484.3.
PDB; 1FXT; NMR; -; A=2-150.
PDB; 1FZY; X-ray; 1.90 A; A/B=2-150.
PDB; 1TTE; NMR; -; A=1-215.
PDBsum; 1FXT; -.
PDBsum; 1FZY; -.
PDBsum; 1TTE; -.
ProteinModelPortal; P21734; -.
SMR; P21734; -.
BioGrid; 32230; 158.
DIP; DIP-6594N; -.
IntAct; P21734; 6.
MINT; P21734; -.
STRING; 4932.YDR177W; -.
iPTMnet; P21734; -.
MaxQB; P21734; -.
PaxDb; P21734; -.
PRIDE; P21734; -.
EnsemblFungi; YDR177W; YDR177W; YDR177W.
GeneID; 851757; -.
KEGG; sce:YDR177W; -.
EuPathDB; FungiDB:YDR177W; -.
SGD; S000002584; UBC1.
GeneTree; ENSGT00670000098059; -.
HOGENOM; HOG000233455; -.
InParanoid; P21734; -.
KO; K04649; -.
OMA; NKEIADC; -.
OrthoDB; EOG092C50OL; -.
BioCyc; YEAST:G3O-29766-MONOMER; -.
Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
EvolutionaryTrace; P21734; -.
PRO; PR:P21734; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000502; C:proteasome complex; IPI:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0016050; P:vesicle organization; IMP:SGD.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR015368; UBA_C_fun.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF09288; UBA_3; 1.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Isopeptide bond;
Nucleotide-binding; Reference proteome; Stress response; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 215 Ubiquitin-conjugating enzyme E2 1.
/FTId=PRO_0000082525.
ACT_SITE 88 88 Glycyl thioester intermediate.
CROSSLNK 93 93 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
HELIX 3 15 {ECO:0000244|PDB:1FZY}.
HELIX 18 20 {ECO:0000244|PDB:1FZY}.
STRAND 22 27 {ECO:0000244|PDB:1FZY}.
STRAND 28 31 {ECO:0000244|PDB:1TTE}.
STRAND 32 40 {ECO:0000244|PDB:1FZY}.
STRAND 43 45 {ECO:0000244|PDB:1FXT}.
TURN 46 49 {ECO:0000244|PDB:1FZY}.
STRAND 51 57 {ECO:0000244|PDB:1FZY}.
TURN 60 63 {ECO:0000244|PDB:1FZY}.
STRAND 68 73 {ECO:0000244|PDB:1FZY}.
STRAND 78 80 {ECO:0000244|PDB:1TTE}.
TURN 82 84 {ECO:0000244|PDB:1FZY}.
HELIX 90 92 {ECO:0000244|PDB:1FZY}.
TURN 93 95 {ECO:0000244|PDB:1FZY}.
HELIX 102 114 {ECO:0000244|PDB:1FZY}.
STRAND 118 120 {ECO:0000244|PDB:1FXT}.
HELIX 124 132 {ECO:0000244|PDB:1FZY}.
HELIX 134 148 {ECO:0000244|PDB:1FZY}.
HELIX 170 179 {ECO:0000244|PDB:1TTE}.
HELIX 183 192 {ECO:0000244|PDB:1TTE}.
HELIX 204 213 {ECO:0000244|PDB:1TTE}.
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


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