STAMBP binds STAM

Stable Identifier
R-HSA-5693061
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

STAMBP (AMSH) was identified as an interacting partner of the SH3 domain of STAM (Tanaka et al. 1999) and later characterized as a Zn2+-dependent ubiquitin isopeptidase with a substrate preference for Lys-63-linked polyubiquitin chains (McCullough et al. 2004, 2006). At the N terminus STAMBP contains a nuclear localization signal and a microtubule-interacting and transport (MIT) domain that can interact with several chromatin-modifying proteins that are components of the Endosomal sorting complex required for transport (ESCRT) III complex (Sierra et al. 2010). STAMBP binds clathrin heavy chains, which anchors it to endosomes (McCullough et al. 2006, Nakamura et al. 2006) and contains a STAM-interacting motif that binds the SH3 domain of STAM, stimulating the deubiquitinating activity of STAMBP (McCullough et al. 2006, Kim et al. 2006, Sierra et al. 2010).

Literature References
PubMed ID Title Journal Year
10383417 Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines

Tanaka, N, Kaneko, K, Asao, H, Kasai, H, Endo, Y, Fujita, T, Takeshita, T, Sugamura, K

J. Biol. Chem. 1999
Participants
Participant Of
Orthologous Events
Authored
Reviewed
Created