To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00163 [for PROSITE entry PS00183]

Ubiquitin-conjugating enzymes signature and profile





Description

Ubiquitin-conjugating enzymes (EC 6.3.2.19) (UBC or E2 enzymes) [1,2,3] catalyze the covalent attachment of ubiquitin to target proteins. An activated ubiquitin moiety is transferred from an ubiquitin-activating enzyme (E1) to E2 which later ligates ubiquitin directly to substrate proteins with or without the assistance of 'N-end' recognizing proteins (E3).

In most species there are many forms of UBC (at least 9 in yeast) which are implicated in diverse cellular functions.

A cysteine residue is required for ubiquitin-thiolester formation. There is a single conserved cysteine in UBC's and the region around that residue is conserved in the sequence of known UBC isozymes. We have used that region as a signature pattern. We also developed a profile that spans the complete catalytical domain.

Expert(s) to contact by email:

Jentsch S.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

UBIQUITIN_CONJUGAT_1, PS00183; Ubiquitin-conjugating enzymes active site  (PATTERN)

UBIQUITIN_CONJUGAT_2, PS50127; Ubiquitin-conjugating enzymes family profile  (MATRIX)


References

1AuthorsJentsch S., Seufert W., Sommer T., Reins H.-A.
TitleUbiquitin-conjugating enzymes: novel regulators of eukaryotic cells.
SourceTrends Biochem. Sci. 15:195-198(1990).
PubMed ID2193438

2AuthorsJentsch S., Seufert W., Hauser H.-P.
TitleGenetic analysis of the ubiquitin system.
SourceBiochim. Biophys. Acta 1089:127-139(1991).
PubMed ID1647207

3AuthorsHershko A.
TitleThe ubiquitin pathway for protein degradation.
SourceTrends Biochem. Sci. 16:265-268(1991).
PubMed ID1656558



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)