UBC5/YDR059C Summary Help

Standard Name UBC5 1
Systematic Name YDR059C
Feature Type ORF, Verified
Description Ubiquitin-conjugating enzyme; mediates selective degradation of short-lived, abnormal, or excess proteins, including histone H3; central component of the cellular stress response; expression is heat inducible; protein abundance increases in response to DNA replication stress; UBC5 has a paralog, UBC4, that arose from the whole genome duplication (1, 2, 3, 4, 5 and see Summary Paragraph)
Name Description UBiquitin-Conjugating 1
Chromosomal Location
ChrIV:569770 to 569234 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All UBC5 GO evidence and references
  View Computational GO annotations for UBC5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Classical genetics
Large-scale survey
61 total interaction(s) for 35 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 4
  • Affinity Capture-RNA: 2
  • Affinity Capture-Western: 3
  • Biochemical Activity: 2
  • Co-purification: 1
  • Reconstituted Complex: 5
  • Two-hybrid: 8

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 6
  • Phenotypic Enhancement: 12
  • Phenotypic Suppression: 1
  • Positive Genetic: 4
  • Synthetic Growth Defect: 6
  • Synthetic Lethality: 4
  • Synthetic Rescue: 2

Expression Summary
Length (a.a.) 148
Molecular Weight (Da) 16,280
Isoelectric Point (pI) 6.76
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:569770 to 569234 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..47 569770..569724 2011-02-03 1996-07-31
Intron 48..137 569723..569634 2011-02-03 1996-07-31
CDS 138..537 569633..569234 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002466

UBC5 encodes a ubiquitin conjugating enzyme that links ubiquitin (Ubi4p) to lysine residues of target proteins (1, 6). Ubc5p plays a role in protein polyubiquitination (1), acts as a central component of the cellular stress response (2) and is also involved in sporulation (6). Ubc5p is associated with the proteasome complex (7). A related ubiquitin conjugating enzyme, (UBC4), shows strong sequence similarity to UBC5 and both are complementary in function (1). Together, Ubc5p and Ubc4p 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 (1).

Last updated: 2005-05-24 Contact SGD

References cited on this page View Complete Literature Guide for UBC5
1) 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
2) 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
3) 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
4) Singh RK, et al.  (2009) Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis. Nat Cell Biol 11(8):925-33
5) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
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