UBC4/YBR082C Summary Help

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; UBC4 has a paralog, UBC5, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6 and see Summary Paragraph)
Name Description UBiquitin-Conjugating
Chromosomal Location
ChrII:407169 to 406628 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology 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 phenotypes All UBC4 Phenotype evidence and references
Classical genetics
null
overexpression
Large-scale survey
null
Resources
interactions All UBC4 Interaction evidence and references
386 total interaction(s) for 253 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 10
  • Affinity Capture-RNA: 4
  • Affinity Capture-Western: 16
  • Biochemical Activity: 5
  • Co-crystal Structure: 1
  • Co-purification: 2
  • Protein-RNA: 1
  • Reconstituted Complex: 32
  • Two-hybrid: 7
Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 180
  • Phenotypic Enhancement: 18
  • Phenotypic Suppression: 4
  • Positive Genetic: 55
  • Synthetic Growth Defect: 27
  • Synthetic Lethality: 15
  • Synthetic Rescue: 7
Resources
Expression Summary
histogram
Resources
Protein Information All UBC4 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:407169 to 406628 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..47 407169..407123 2011-02-03 1997-01-28
Intron 48..142 407122..407028 2011-02-03 1997-01-28
CDS 143..542 407027..406628 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000286
SUMMARY PARAGRAPH for UBC4

UBC4 encodes a ubiquitin conjugating enzyme that links ubiquitin (Ubi4p) to lysine residues of target proteins (2, 7). 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 (8). UBC4 is also involved in sporulation (7). 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) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6) Singh RK, et al.  (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
7) Hochstrasser M  (1996) Ubiquitin-dependent protein degradation. Annu Rev Genet 30:405-39
8) Tongaonkar P, et al.  (2000) Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome. Mol Cell Biol 20(13):4691-8