MSB3 protein (Saccharomyces cerevisiae) - STRING interaction network
"MSB3" - GTPase-activating protein for Sec4p and several other Rab GTPases, regulates exocytosis via its action on Sec4p, also required for proper actin organization in Saccharomyces cerevisiae
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
MSB3GTPase-activating protein for Sec4p and several other Rab GTPases, regulates exocytosis via its action on Sec4p, also required for proper actin organization; similar to Msb4p; both Msb3p and Msb4p localize to sites of polarized growth; Regulates exocytosis by functioning as a GAP for SEC4. Stimulates specifically the GTPase activity of YPT6. Also required for efficient polarization of the actin patches (633 aa)    
Predicted Functional Partners:
GTPase-activating protein of the Ras superfamily that acts primarily on Sec4p, localizes to the bud site and bud tip, has similarity to Msb3p; msb3 msb4 double mutation causes defects in secretion and actin organization; Regulates exocytosis by functioning as a GAP for SEC4. Also required for efficient polarization of the actin patches (492 aa)
Formin, nucleates the formation of linear actin filaments, involved in cell processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables, functionally redundant with BNR1; Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-acti [...] (1953 aa)
Actin- and formin-interacting protein; stimulates actin cable nucleation by recruiting actin monomers to Bni1p; involved in polarized cell growth; isolated as bipolar budding mutant; potential Cdc28p substrate; Not essential for mitotic growth but is necessary for normal morphogenesis. Involved in the organization and/or function of the actin cytoskeleton (788 aa)
Component of the polarisome, which functions in actin cytoskeletal organization during polarized growth; acts as a scaffold for Mkk1p and Mpk1p cell wall integrity signaling components; potential Cdc28p substrate; Involved in pheromone-induced morphogenesis and efficient mating, perhaps as a cytoskeletal protein (1466 aa)
Coiled-coil polarisome protein required for polarized morphogenesis, cell fusion, and low affinity Ca2+ influx; forms polarisome complex with Bni1p, Bud6p, and Spa2p; localizes to sites of polarized growth; Localized to sites of polarized growth and is required for efficient mating and bipolar budding (420 aa)
Rab family GTPase, involved in the ER-to-Golgi step of the secretory pathway; complex formation with the Rab escort protein Mrs6p is required for prenylation of Ypt1p by protein geranylgeranyltransferase type II (Bet2p-Bet4p); The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tetherin [...] (206 aa)
Rab family GTPase; GTP-binding protein of the rab family; required for homotypic fusion event in vacuole inheritance, for endosome-endosome fusion, similar to mammalian Rab7; Needed for homotypic vacuole fusion, the last step in the vacuole inheritance process (208 aa)
Rab family GTPase required for endocytic transport and for sorting of vacuolar hydrolases; localized in endocytic intermediates; detected in mitochondria; geranylgeranylation required for membrane association; mammalian Rab5 homolog; Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation (210 aa)
Rab family GTPase essential for vesicle-mediated exocytic secretion and autophagy; associates with the exocyst component Sec15p and may regulate polarized delivery of transport vesicles to the exocyst at the plasma membrane; Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP- bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as [...] (215 aa)
Rab family GTPase, very similar to Ypt32p; involved in the exocytic pathway; mediates intra-Golgi traffic or the budding of post-Golgi vesicles from the trans-Golgi; Required for protein transport in the secretory pathway. Probably involved in regulation of secretory vesicle formation at the trans-Golgi compartment. Plays a role in autophagy (223 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (4%) [HD]