Publikation: Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The hect domain protein family was originally identified by sequence similarity of its members to the Cterminal region of E6-AP, an E3 ubiquitin-protein ligase. Since the C terminus of E6-AP mediates thioester complex formation with ubiquitin, a necessary intermediate step in E6-AP-dependent ubiquitination, it was proposed that members of the hect domain family in general have E3 activity. The hect domain is approximately 350 amino acids in length, and we show here that the hect domain of E6-AP is necessary and sufficient for ubiquitin thioester adduct formation. Furthermore, the human genome encodes at least 20 different hect domain proteins, and in further support of the hypothesis that hect domain proteins represent a family of E3s, several of these are shown to form thioester complexes with ubiquitin. In addition, some hect domain proteins interact preferentially with UbcH5, whereas others interact with UbcH7, indicating that human hect domain proteins can be grouped into at least two classes based on their E2 specificity. Since E3s are thought to play a major role in substrate recognition, the presence of a large family of E3s should contribute to ensure the specificity and selectivity of ubiquitin-dependent proteolytic pathways.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
SCHWARZ, Sylvia E., José L. ROSA, Martin SCHEFFNER, 1998. Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7. In: The Journal of Biological Chemistry : JBC. 1998, 273(20), pp. 12148-12154. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.273.20.12148BibTex
@article{Schwarz1998-05-15Chara-42646, year={1998}, doi={10.1074/jbc.273.20.12148}, title={Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7}, number={20}, volume={273}, issn={0021-9258}, journal={The Journal of Biological Chemistry : JBC}, pages={12148--12154}, author={Schwarz, Sylvia E. and Rosa, José L. and Scheffner, Martin} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/42646"> <dc:creator>Rosa, José L.</dc:creator> <dc:creator>Schwarz, Sylvia E.</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/42646"/> <dc:contributor>Schwarz, Sylvia E.</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-06-22T08:11:50Z</dcterms:available> <dc:creator>Scheffner, Martin</dc:creator> <dc:contributor>Rosa, José L.</dc:contributor> <dc:language>eng</dc:language> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:title>Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7</dcterms:title> <dc:contributor>Scheffner, Martin</dc:contributor> <dcterms:issued>1998-05-15</dcterms:issued> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-06-22T08:11:50Z</dc:date> <dcterms:abstract xml:lang="eng">The hect domain protein family was originally identified by sequence similarity of its members to the Cterminal region of E6-AP, an E3 ubiquitin-protein ligase. Since the C terminus of E6-AP mediates thioester complex formation with ubiquitin, a necessary intermediate step in E6-AP-dependent ubiquitination, it was proposed that members of the hect domain family in general have E3 activity. The hect domain is approximately 350 amino acids in length, and we show here that the hect domain of E6-AP is necessary and sufficient for ubiquitin thioester adduct formation. Furthermore, the human genome encodes at least 20 different hect domain proteins, and in further support of the hypothesis that hect domain proteins represent a family of E3s, several of these are shown to form thioester complexes with ubiquitin. In addition, some hect domain proteins interact preferentially with UbcH5, whereas others interact with UbcH7, indicating that human hect domain proteins can be grouped into at least two classes based on their E2 specificity. Since E3s are thought to play a major role in substrate recognition, the presence of a large family of E3s should contribute to ensure the specificity and selectivity of ubiquitin-dependent proteolytic pathways.</dcterms:abstract> </rdf:Description> </rdf:RDF>