P21734 (UBC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UBC1
Ordered Locus Names:	YDR177W
ORF Names:	YD9395.10

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Stress response Ubl conjugation pathway
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER-associated protein catabolic process Inferred from mutant phenotype Ref.5. Source: SGD endocytosis Traceable author statement PubMed 8982460. Source: SGD protein monoubiquitination Traceable author statement PubMed 8982460. Source: SGD protein polyubiquitination Traceable author statement PubMed 8982460. Source: SGD protein ubiquitination involved in ubiquitin-dependent protein catabolic process Inferred from mutant phenotype PubMed 11134048Ref.1. Source: SGD response to stress Inferred from electronic annotation. Source: UniProtKB-KW spore germination Traceable author statement PubMed 8982460. Source: SGD vesicle organization Inferred from mutant phenotype PubMed 11134048. Source: SGD
Cellular_component	proteasome complex Inferred from physical interaction PubMed 10848595. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Ubiquitin-conjugating enzyme E2 1

PRO_0000082525

Sites

Active site

88

1

Glycyl thioester intermediate

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

215

Helix Strand Turn

Details...

Helix

3 – 15

13

Helix

18 – 20

3

Beta strand

22 – 27

6

Beta strand

28 – 31

4

Beta strand

32 – 40

9

Beta strand

43 – 45

3

Turn

46 – 49

4

Beta strand

51 – 57

7

Turn

60 – 63

4

Beta strand

68 – 73

6

Beta strand

78 – 80

3

Turn

82 – 84

3

Helix

90 – 92

3

Turn

93 – 95

3

Helix

102 – 114

13

Beta strand

118 – 120

3

Helix

124 – 132

9

Helix

134 – 148

15

Helix

170 – 179

10

Helix

183 – 192

10

Helix

204 – 213

10

Sequences

	Sequence		Length	Mass (Da)
	P21734 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 899CC397A1285145	FASTA	215	24,178
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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]	"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.
[9]	"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.

PIR

S12493.

RefSeq

NP_010462.3. NM_001180484.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FXT	NMR	-	A	2-150	[»]
1FZY	X-ray	1.90	A/B	2-150	[»]
1TTE	NMR	-	A	2-215	[»]

ProteinModelPortal

P21734.

SMR

P21734. Positions 2-215.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6594N.

IntAct

P21734. 5 interactions.

MINT

MINT-591274.

STRING

4932.YDR177W.

Proteomic databases

PaxDb

P21734.

PeptideAtlas

P21734.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR177W; YDR177W; YDR177W.

GeneID

851757.

KEGG

sce:YDR177W.
sce:YDR180W.

Organism-specific databases

CYGD

YDR177w.

SGD

S000002584. UBC1.

Phylogenomic databases

eggNOG

COG5078.

GeneTree

ENSGT00670000098059.

HOGENOM

HOG000233455.

KO

K04649.
K06672.

OMA

SESDIHH.

OrthoDB

EOG46HKM6.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

Genevestigator

P21734.

GermOnline

YDR177W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR009060. UBA-like.
IPR015368. UBA_C_fun.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF09288. UBA_3. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF46934. UBA_like. 1 hit.
SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P21734.

NextBio

969525.

Entry information

Entry name

UBC1_YEAST

Accession

Primary (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:	April 3, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program