The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation.

Trends in biochemical sciences ·Vol. 26 ·No. 5 ·2001-05-00 ·Pages 273-5

Aravind L

Abstract

Sequence profile analysis was used to detect a conserved globular domain in several proteins including deltex, Trip12 and poly-ADP-ribose polymerase homologs. It was named the WWE domain after its most conserved residues and is predicted to mediate specific protein-protein interactions in ubiquitin and ADP-ribose conjugation systems.

MeSH Terms

ADP-Ribosylation Factors/chemistry Amino Acid Sequence Animals Conserved Sequence Drosophila Proteins Humans Insect Proteins/chemistry Ligases/chemistry Membrane Proteins Molecular Sequence Data Poly(ADP-ribose) Polymerases/chemistry Protein Structure, Secondary Protein Structure, Tertiary Software Ubiquitin-Protein Ligases Ubiquitins/metabolism

Chemicals

DX protein, Drosophila Drosophila Proteins Insect Proteins Membrane Proteins Ubiquitins Ubiquitin-Protein Ligases Poly(ADP-ribose) Polymerases ADP-Ribosylation Factors Ligases

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Aravind L

National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. [email protected]

Article Info

Journal

Trends in biochemical sciences

Abbr.

Trends Biochem Sci

ISSN

0968-0004

DOI

10.1016/s0968-0004(01)01787-x

[email protected]

Published

2001-05-00

Pages

273-5

Language

English

Region

England

NLM ID

7610674

Subset

External Links

PubMed source DOI: 10.1016/s0968-0004(01)01787-x View journal details

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The WWE domain: a common interaction module in protein ubiquitination and ADP ribosylation.

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