GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:7708685

From GONUTS
Jump to: navigation, search
Citation

Huibregtse, JM, Scheffner, M, Beaudenon, S and Howley, PM (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. U.S.A. 92:2563-7

Abstract

E6-AP is a 100-kDa cellular protein that interacts with the E6 protein of the cancer-associated human papillomavirus types 16 and 18. The E6/E6-AP complex binds to and targets the p53 tumor-suppressor protein for ubiquitin-mediated proteolysis. E6-AP is an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. The amino acid sequence of E6-AP shows similarity to a number of protein sequences over an approximately 350-aa region corresponding to the carboxyl termini of both E6-AP and the E6-AP-related proteins. Of particular note is a conserved cysteine residue within the last 32-34 aa, which in E6-AP is likely to be the site of ubiquitin thioester formation. Two of the E6-AP-related proteins, a rat 100-kDa protein and a yeast 95-kDa protein (RSP5), both of previously unknown function, are shown here to form thioesters with ubiquitin. Mutation of the conserved cysteine residue of these proteins destroys their ability to accept ubiquitin. These data strongly suggest that the rat 100-kDa protein and RSP5, as well as the other E6-AP-related proteins, belong to a class of functionally related E3 ubiquitin-protein ligases, defined by a domain homologous to the E6-AP carboxyl terminus (hect domain).

Links

PubMed PMC42258

Keywords

Amino Acid Sequence; Animals; Conserved Sequence; Cysteine; Endosomal Sorting Complexes Required for Transport; Humans; Ligases/chemistry; Ligases/metabolism; Mice; Molecular Sequence Data; Mutagenesis; Papillomaviridae/metabolism; Rabbits; Rats; Reticulocytes/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins; Sequence Homology, Amino Acid; Ubiquitin-Protein Ligase Complexes; Ubiquitin-Protein Ligases; Viral Proteins/chemistry; Viral Proteins/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:UBE3A

enables

GO:0061630: ubiquitin protein ligase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:UBE3A

GO:0061630: ubiquitin protein ligase activity

ECO:0000315:

F

Fig4; panel A shows E3 ubiquitin-protein ligase activity.

complete
CACAO 10253

YEAST:RSP5

enables

GO:0061630: ubiquitin protein ligase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

YEAST:RSP5

GO:0061630: ubiquitin protein ligase activity

ECO:0000247:

UniProtKB:Q05086


F

Fig 1B shows sequence alignment, including highly conserved cysteine residue necessary for Ubiquitin thioester formation.

complete
CACAO 10316

YEAST:RSP5

GO:0061630: ubiquitin protein ligase activity

ECO:0000315:

F

Fig3 shows evidence for E3 Ubiquitin-protein ligase activty

complete
CACAO 10317

RAT:UBR5

enables

GO:0061630: ubiquitin protein ligase activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

RAT:UBR5

GO:0061630: ubiquitin protein ligase activity

ECO:0000315:

F

See Figure 2 for evidence of E3 ubiquitin-protein ligase activity. Note that Genbank PIR S22659 has been replaced with PIR Q62671.3 since the publication of this paper.

complete
CACAO 10254

RAT:UBR5

GO:0061630: ubiquitin protein ligase activity

ECO:0000247:

UniProtKB:Q05086


F

Fig 1B shows sequence alignment, including highly conserved cysteine residue necessary for Ubiquitin thioester formation.

complete
CACAO 10302

DROME:HYD

GO:0061630: ubiquitin protein ligase activity

ECO:0000247:

UniProtKB:Q05086


F

Fig 1B shows sequence alignment, including highly conserved cysteine residue necessary for Ubiquitin thioester formation.

complete
CACAO 10328

Notes

See also

References

See Help:References for how to manage references in GONUTS.