Reviewed, UniProtKB/Swiss-Prot P21734 (UBC1_YEAST)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2-24 kDa
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase
    Ubiquitin carrier protein

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
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. Ref.4
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
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Inferred from genetic interaction. Source: SGD endocytosis Traceable author statement. Source: SGD protein monoubiquitination Traceable author statement. Source: SGD protein polyubiquitination Traceable author statement. Source: SGD protein ubiquitination during ubiquitin-dependent protein catabolic process Ref.1 Inferred from mutant phenotype. Source: SGD regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro response to stress Inferred from electronic annotation. Source: UniProtKB-KW spore germination Traceable author statement. Source: SGD vesicle organization Inferred from mutant phenotype. Source: SGD
Cellular component	proteasome complex Inferred from physical interaction. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct ubiquitin-protein ligase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-19717,EBI-19717
ADK1	P07170	1	EBI-19717,EBI-9447

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 215

215

Ubiquitin-conjugating enzyme E2-24 kDa

PRO_0000082525

Sites

Active site

88

1

Glycyl thioester intermediate By similarity

Secondary structure

1

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215

Helix Strand Turn

Details...

Helix

3 – 15

13

Helix

18 – 20

3

Beta strand

22 – 27

6

Beta strand

32 – 40

9

Turn

46 – 49

4

Beta strand

51 – 57

7

Turn

60 – 63

4

Beta strand

68 – 73

6

Turn

82 – 84

3

Helix

90 – 92

3

Turn

93 – 95

3

Helix

102 – 114

13

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)
	P21734-1 [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: 2265617] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"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: 11591345] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X56402 Genomic DNA. Translation: CAA39812.1.
Z46727 Genomic DNA. Translation: CAA86682.1.
AY557675 Genomic DNA. Translation: AAS56001.1.

PIR

S12493.

RefSeq

NP_010462.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6594N.

IntAct

P21734. 4 interactions.

Proteomic databases

PeptideAtlas

P21734.

PRIDE

P21734.

Genome annotation databases

Ensembl

YDR177W. Saccharomyces cerevisiae. [Contig view]

GeneID

851757.

GenomeReviews

Gene locus YDR177W in contig Z71256_GR.

KEGG

sce:YDR177W.

NMPDR

fig|4932.3.peg.1212.

Organism-specific databases

CYGD

YDR177w.

SGD

S000002584. UBC1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P21734.

OMA

P21734. LQSPEPN.

Enzyme and pathway databases

BRENDA

6.3.2.19. 250.

Gene expression databases

GermOnline

YDR177W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR015368. UBA_C_fun.
IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

Pfam

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

ProDom

PD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00212. UBCc. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

969525.

Entry information

Entry name

UBC1_YEAST

Accession

Primary (citable) accession number: P21734

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	June 16, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)