Reviewed, UniProtKB/Swiss-Prot P15731 (UBC4_YEAST)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2 4
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase 4
    Ubiquitin carrier protein 4

Gene names

Name:	UBC4
Ordered Locus Names:	YBR082C
ORF Names:	YBR0745

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	148 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.
Subunit structure	Interacts with TUL1. Ref.4
Induction	By heat shock and cadmium.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	Present with 13500 molecules/cell in log phase SD medium. Ref.5
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
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ascospore formation Traceable author statement. Source: SGD protein monoubiquitination Inferred from direct assay. Source: SGD protein polyubiquitination Ref.1 Inferred from direct assay. Source: SGD regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro response to stress Ref.1 Inferred from direct assay. Source: SGD ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Ref.4 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 ubiquitin-protein ligase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 148

148

Ubiquitin-conjugating enzyme E2 4

PRO_0000082545

Sites

Active site

86

1

Glycyl thioester intermediate

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.6

Secondary structure

1

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148

Helix Strand Turn

Details...

Helix

2 – 14

13

Beta strand

20 – 27

8

Beta strand

30 – 40

11

Beta strand

50 – 56

7

Turn

59 – 62

4

Beta strand

67 – 70

4

Helix

88 – 90

3

Turn

91 – 93

3

Helix

100 – 112

13

Helix

122 – 130

9

Helix

132 – 146

15

Sequences

	Sequence		Length	Mass (Da)
	P15731-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 8E96137D3EB20F80	FASTA	148	16,456
	10 20 30 40 50 60 MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD 70 80 90 100 110 120 YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL 130 140 VPEIAHIYKT DRPKYEATAR EWTKKYAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins." Seufert W., Jentsch S. EMBO J. 9:543-550(1990) [PubMed: 2154373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-64 AND 119-125.
[2]	"Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II." van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y. Yeast 10:959-964(1994) [PubMed: 7985423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies." Reggiori F., Pelham H.R.B. Nat. Cell Biol. 4:117-123(2002) [PubMed: 11788821] [Abstract] Cited for: INTERACTION WITH TUL1.
[5]	"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].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.
[7]	"Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4." Cook W.J., Jeffrey L.C., Xu Y., Chau V. Biochemistry 32:13809-13817(1993) [PubMed: 8268156] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X17493 Genomic DNA. Translation: CAA35528.1.
X76294 Genomic DNA. Translation: CAA53942.1.
Z35951 Genomic DNA. Translation: CAA85027.1.

PIR

S22857.

RefSeq

NP_009638.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QCQ	X-ray	2.70	A	1-148	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6596N.

IntAct

P15731. 15 interactions.

Proteomic databases

PeptideAtlas

P15731.

Genome annotation databases

Ensembl

YBR082C. Saccharomyces cerevisiae. [Contig view]

GeneID

852376.

GenomeReviews

Gene locus YBR082C in contig Y13134_GR.

KEGG

sce:YBR082C.

NMPDR

fig|4932.3.peg.336.

Organism-specific databases

CYGD

YBR082c.

SGD

S000000286. UBC4.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P15731.

OMA

P15731. NFTTRIY.

Enzyme and pathway databases

BRENDA

6.3.2.19. 250.

Gene expression databases

ArrayExpress

P15731.

GermOnline

YBR082C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

Pfam

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

971168.

Entry information

Entry name

UBC4_YEAST

Accession

Primary (citable) accession number: P15731

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)