Human Interaction Network Ontology

Last uploaded: June 27, 2014
Preferred Name

THEM4 (CTMP) and/or TRIB3 inhibit AKT phosphorylation
Synonyms
Definitions

Reviewed: Yuzugullu, Haluk, 2012-08-13 Edited: Matthews, L, 2012-08-03 Authored: Nasi, S, Annibali, D, 2006-10-10 09:07:07 Reviewed: Greene, LA, 2007-11-08 15:39:37 The phosphorylation of membrane-recruited AKT at threonine and serine can be inhibited by direct binding of two different proteins, C-terminal modulator protein (THEM4 i.e. CTMP), which binds to the carboxy-terminal tail of AKT (Maira et al. 2001), or Tribbles homolog 3 (TRIB3), which binds to the catalytic domain of AKT (Du et al. 2003). Reviewed: Zhao, Jean J, 2012-08-13 Reviewed: Thorpe, Lauren, 2012-08-13

ID

http://purl.obolibrary.org/obo/HINO_0009493

comment

Reviewed: Yuzugullu, Haluk, 2012-08-13

Edited: Matthews, L, 2012-08-03

Authored: Nasi, S, Annibali, D, 2006-10-10 09:07:07

Reviewed: Greene, LA, 2007-11-08 15:39:37

The phosphorylation of membrane-recruited AKT at threonine and serine can be inhibited by direct binding of two different proteins, C-terminal modulator protein (THEM4 i.e. CTMP), which binds to the carboxy-terminal tail of AKT (Maira et al. 2001), or Tribbles homolog 3 (TRIB3), which binds to the catalytic domain of AKT (Du et al. 2003).

Reviewed: Zhao, Jean J, 2012-08-13

Reviewed: Thorpe, Lauren, 2012-08-13

definition source

Reactome, http://www.reactome.org

Pubmed11598301

Pubmed12791994

has input

http://purl.obolibrary.org/obo/HINO_0012344

http://purl.obolibrary.org/obo/HINO_0024906

has output

http://purl.obolibrary.org/obo/HINO_0012352

label

THEM4 (CTMP) and/or TRIB3 inhibit AKT phosphorylation

prefixIRI

HINO:0009493

prefLabel

THEM4 (CTMP) and/or TRIB3 inhibit AKT phosphorylation

seeAlso

ReactomeREACT_12567

Reactome Database ID Release 43199443

subClassOf

http://purl.obolibrary.org/obo/INO_0000040

Delete Subject Author Type Created
No notes to display
Create mapping

Delete Mapping To Ontology Source
There are currently no mappings for this class.