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P21734

- UBC1_YEAST

UniProt

P21734 - UBC1_YEAST

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Protein

Ubiquitin-conjugating enzyme E2 1

Gene

UBC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).2 PublicationsPROSITE-ProRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediate

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: SGD
  2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  3. response to stress Source: UniProtKB-KW
  4. vesicle organization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Stress response, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29766-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBC1
Ordered Locus Names:YDR177W
ORF Names:YD9395.10
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR177w.
SGDiS000002584. UBC1.

Subcellular locationi

GO - Cellular componenti

  1. proteasome complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Ubiquitin-conjugating enzyme E2 1PRO_0000082525Add
BLAST

Proteomic databases

MaxQBiP21734.
PaxDbiP21734.
PeptideAtlasiP21734.

Expressioni

Developmental stagei

Early stages of growth after spore germination.

Inductioni

By heat shock and cadmium.

Gene expression databases

GenevestigatoriP21734.

Interactioni

Protein-protein interaction databases

BioGridi32230. 35 interactions.
DIPiDIP-6594N.
IntActiP21734. 5 interactions.
MINTiMINT-591274.
STRINGi4932.YDR177W.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1513
Helixi18 – 203
Beta strandi22 – 276
Beta strandi28 – 314
Beta strandi32 – 409
Beta strandi43 – 453
Turni46 – 494
Beta strandi51 – 577
Turni60 – 634
Beta strandi68 – 736
Beta strandi78 – 803
Turni82 – 843
Helixi90 – 923
Turni93 – 953
Helixi102 – 11413
Beta strandi118 – 1203
Helixi124 – 1329
Helixi134 – 14815
Helixi170 – 17910
Helixi183 – 19210
Helixi204 – 21310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXTNMR-A2-150[»]
1FZYX-ray1.90A/B2-150[»]
1TTENMR-A1-215[»]
ProteinModelPortaliP21734.
SMRiP21734. Positions 2-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21734.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00670000098059.
HOGENOMiHOG000233455.
InParanoidiP21734.
KOiK04649.
OMAiNKEIADC.
OrthoDBiEOG7SBP18.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR009060. UBA-like.
IPR015368. UBA_C_fun.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF09288. UBA_3. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21734-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRAKRIMKE IQAVKDDPAA HITLEFVSES DIHHLKGTFL GPPGTPYEGG
60 70 80 90 100
KFVVDIEVPM EYPFKPPKMQ FDTKVYHPNI SSVTGAICLD ILKNAWSPVI
110 120 130 140 150
TLKSALISLQ ALLQSPEPND PQDAEVAQHY LRDRESFNKT AALWTRLYAS
160 170 180 190 200
ETSNGQKGNV EESDLYGIDH DLIDEFESQG FEKDKIVEVL RRLGVKSLDP
210
NDNNTANRII EELLK
Length:215
Mass (Da):24,178
Last modified:May 1, 1991 - v1
Checksum:i899CC397A1285145
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56402 Genomic DNA. Translation: CAA39812.1.
Z46727 Genomic DNA. Translation: CAA86682.1.
AY557675 Genomic DNA. Translation: AAS56001.1.
BK006938 Genomic DNA. Translation: DAA12019.1.
PIRiS12493.
RefSeqiNP_010462.3. NM_001180484.3.

Genome annotation databases

EnsemblFungiiYDR177W; YDR177W; YDR177W.
GeneIDi851757.
KEGGisce:YDR177W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56402 Genomic DNA. Translation: CAA39812.1 .
Z46727 Genomic DNA. Translation: CAA86682.1 .
AY557675 Genomic DNA. Translation: AAS56001.1 .
BK006938 Genomic DNA. Translation: DAA12019.1 .
PIRi S12493.
RefSeqi NP_010462.3. NM_001180484.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FXT NMR - A 2-150 [» ]
1FZY X-ray 1.90 A/B 2-150 [» ]
1TTE NMR - A 1-215 [» ]
ProteinModelPortali P21734.
SMRi P21734. Positions 2-215.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32230. 35 interactions.
DIPi DIP-6594N.
IntActi P21734. 5 interactions.
MINTi MINT-591274.
STRINGi 4932.YDR177W.

Proteomic databases

MaxQBi P21734.
PaxDbi P21734.
PeptideAtlasi P21734.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR177W ; YDR177W ; YDR177W .
GeneIDi 851757.
KEGGi sce:YDR177W.

Organism-specific databases

CYGDi YDR177w.
SGDi S000002584. UBC1.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00670000098059.
HOGENOMi HOG000233455.
InParanoidi P21734.
KOi K04649.
OMAi NKEIADC.
OrthoDBi EOG7SBP18.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-29766-MONOMER.

Miscellaneous databases

EvolutionaryTracei P21734.
NextBioi 969525.
PROi P21734.

Gene expression databases

Genevestigatori P21734.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR009060. UBA-like.
IPR015368. UBA_C_fun.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF09288. UBA_3. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF46934. SSF46934. 1 hit.
SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. 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.

Entry informationi

Entry nameiUBC1_YEAST
AccessioniPrimary (citable) accession number: P21734
Secondary accession number(s): D6VSF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 29, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3