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P21734 (UBC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 1

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-conjugating enzyme E2-24 kDa
Ubiquitin-protein ligase
Gene names
Name:UBC1
Ordered Locus Names:YDR177W
ORF Names:YD9395.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.5 Ref.6

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

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.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Ubiquitin-conjugating enzyme E2 1
PRO_0000082525

Sites

Active site881Glycyl thioester intermediate

Secondary structure

....................................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21734 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 899CC397A1285145

FASTA21524,178
        10         20         30         40         50         60 
MSRAKRIMKE IQAVKDDPAA HITLEFVSES DIHHLKGTFL GPPGTPYEGG KFVVDIEVPM 

        70         80         90        100        110        120 
EYPFKPPKMQ FDTKVYHPNI SSVTGAICLD ILKNAWSPVI TLKSALISLQ ALLQSPEPND 

       130        140        150        160        170        180 
PQDAEVAQHY LRDRESFNKT AALWTRLYAS ETSNGQKGNV EESDLYGIDH DLIDEFESQG 

       190        200        210 
FEKDKIVEVL RRLGVKSLDP NDNNTANRII EELLK 

« Hide

References

« Hide 'large scale' references
[1]"UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation."
Seufert W., McGrath J.P., Jeutsch S.
EMBO J. 9:4535-4541(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"A regulatory link between ER-associated protein degradation and the unfolded-protein response."
Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T.
Nat. Cell Biol. 2:379-384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation."
Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y.
Nat. Cell Biol. 3:24-29(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HDR1.
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail."
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 9:897-904(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.
[10]"Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly."
Merkley N., Shaw G.S.
J. Biol. Chem. 279:47139-47147(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-215.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56402 Genomic DNA. Translation: CAA39812.1.
Z46727 Genomic DNA. Translation: CAA86682.1.
AY557675 Genomic DNA. Translation: AAS56001.1.
BK006938 Genomic DNA. Translation: DAA12019.1.
PIRS12493.
RefSeqNP_010462.3. NM_001180484.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXTNMR-A2-150[»]
1FZYX-ray1.90A/B2-150[»]
1TTENMR-A1-215[»]
ProteinModelPortalP21734.
SMRP21734. Positions 2-215.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32230. 29 interactions.
DIPDIP-6594N.
IntActP21734. 5 interactions.
MINTMINT-591274.
STRING4932.YDR177W.

Proteomic databases

MaxQBP21734.
PaxDbP21734.
PeptideAtlasP21734.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR177W; YDR177W; YDR177W.
GeneID851757.
KEGGsce:YDR177W.

Organism-specific databases

CYGDYDR177w.
SGDS000002584. UBC1.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00670000098059.
HOGENOMHOG000233455.
KOK04649.
OMANKEIADC.
OrthoDBEOG7SBP18.

Enzyme and pathway databases

BioCycYEAST:G3O-29766-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP21734.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR009060. UBA-like.
IPR015368. UBA_C_fun.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF09288. UBA_3. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21734.
NextBio969525.
PROP21734.

Entry information

Entry nameUBC1_YEAST
AccessionPrimary (citable) accession number: P21734
Secondary accession number(s): D6VSF9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways