UBC4/YBR082C Summary Help

UBC4 BASIC INFORMATION

Standard Name UBC4
Systematic Name YBR082C
Feature Type ORF, Verified
Description Ubiquitin-conjugating enzyme (E2), mediates degradation of abnormal or excess proteins, including calmodulin and histone H3; interacts with many SCF ubiquitin protein ligases; component of the cellular stress response (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description UBiquitin-Conjugating
GO Annotations All UBC4 GO evidence and references
    View Computational GO annotations for UBC4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All UBC4 Phenotype details and references
Classical genetics
null
overexpression
Large-scale survey
null
Interactions UBC4 All interactions details and references
160 total interaction(s) for 130 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 7
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 10
  • Biochemical Activity: 5
  • Co-purification: 2
  • Protein-RNA: 1
  • Two-hybrid: 5

Genetic Interactions
  • Dosage Rescue: 1
  • Phenotypic Enhancement: 66
  • Phenotypic Suppression: 27
  • Synthetic Growth Defect: 17
  • Synthetic Lethality: 12
  • Synthetic Rescue: 5

Sequence Information
ChrII:407163 to 406622 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2004-07-16 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..47 407163..407117 2004-07-16 1997-01-28
Intron 48..142 407116..407022 2004-07-16 1997-01-28
CDS 143..542 407021..406622 2004-07-16 1997-01-28
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000286

UBC4 RESOURCES

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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

SUMMARY PARAGRAPH for UBC4

UBC4 encodes a ubiquitin conjugating enzyme that links ubiquitin (Ubi4p) to lysine residues of target proteins (2, 6). This function may be performed in conjunction with an E3, ubiquitin-protein ligase. Ubc4p interacts with the ubiquitin ligase E3-CaM in ubiquitinating calmodulin (Cmd1p) (1) and also interacts with several SCF ubiquitin ligase complexes in vitro (4). Ubc4p plays a role in both protein polyubiquitination (2) and protein monoubiquitination (1), and is also a central component of the cellular stress response (3). Indeed, expression of Ubc4p is heat-inducible and its interaction with the proteasome complex is strongly induced by heat stress (7). UBC4 is also involved in sporulation (6). A related ubiquitin conjugating enzyme, (UBC5), shows strong sequence similarity to UBC4 and both are complementary in function (2). Together, Ubc4p and Ubc5p mediate the selective degradation of short-lived and abnormal proteins. Loss of UBC4 and UBC5 results in cell growth defects, temperature sensitivity, inviability in the presence of an amino acid analog, and the induction of the stress response (2).

Last updated: 2005-05-24

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for UBC4]

1) Parag HA, et al.  (1993) Selective ubiquitination of calmodulin by UBC4 and a putative ubiquitin protein ligase (E3) from Saccharomyces cerevisiae. FEBS Lett 325(3):242-6
2) Seufert W and Jentsch S  (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J 9(2):543-50
3) Seufert W and Jentsch S  (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol Hung 42(1-3):27-37
4) Kus BM, et al.  (2004) Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro. Proteins 54(3):455-67
5) Singh RK, et al.  (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
6) Hochstrasser M  (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30:405-39
7) Tongaonkar P, et al.  (2000) Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome. Mol Cell Biol 20(13):4691-8