Home | Contact

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.

Jentsch S.

April 2006 / Pattern revised.

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

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

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Domain architecture view of Swiss-Prot proteins matching PS50127 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50127 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50127 • Scan Swiss-Prot/TrEMBL entries against PS50127 • view ligand binding statistics

Matching PDB structures: 1A3S 1AYZ 1C4Z 1FBV ... [ALL]

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

Consensus pattern: [FYWLSP]-H-[PC]-[NHL]-[LIV]-x(3,4)-G-x-[LIVP]-C-[LIV]-x(1,2)-[LIVR] C is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for yeast UBC6 (DOA2) Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00183 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00183 • Scan Swiss-Prot/TrEMBL entries against PS00183 • view ligand binding statistics

Matching PDB structures: 1A3S 1AYZ 1C4Z 1FBV ... [ALL]

1	Authors	Jentsch S., Seufert W., Sommer T., Reins H.-A.
	Title	Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells.
	Source	Trends Biochem. Sci. 15:195-198(1990).
	PubMed ID	2193438

2	Authors	Jentsch S., Seufert W., Hauser H.-P.
	Title	Genetic analysis of the ubiquitin system.
	Source	Biochim. Biophys. Acta 1089:127-139(1991).
	PubMed ID	1647207

3	Authors	Hershko A.
	Title	The ubiquitin pathway for protein degradation.
	Source	Trends Biochem. Sci. 16:265-268(1991).
	PubMed ID	1656558

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.


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

SIB Swiss Institute of Bioinformatics | Disclaimer