LSB3 protein (Saccharomyces cerevisiae) - STRING interaction network
"LSB3" - Protein containing a C-terminal SH3 domain 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
LSB3Protein containing a C-terminal SH3 domain; binds Las17p, which is a homolog of human Wiskott-Aldrich Syndrome protein involved in actin patch assembly and actin polymerization; protein abundance increases in response to DNA replication stress; LSB3 has a paralog, YSC84, that arose from the whole genome duplication (459 aa)    
Predicted Functional Partners:
Proline-rich protein LAS17; Actin assembly factor; C-terminal WCA domain activates Arp2/3 complex-mediated nucleation of branched actin filaments, polyproline domain nucleates actin filaments independent of Arp2/3; mutants are defective in endocytosis, bud site selection, cytokinesis; human homolog WAS (Wiskott-Aldrich Syndrome) implicated in severe immunodeficiency; human WAS complements yeast null mutant, but only in presence of WIPF1, which mediates localization of WAS to cortical patches (633 aa)
Actin cytoskeleton-regulatory complex protein SLA1; Cytoskeletal protein binding protein; required for assembly of the cortical actin cytoskeleton; interacts with proteins regulating actin dynamics and proteins required for endocytosis; found in the nucleus and cell cortex; has 3 SH3 domains; Belongs to the SLA1 family (1244 aa)
SH3 domain protein implicated in regulating actin polymerization; able to recruit actin polymerization machinery through its SH3 domains; colocalizes with cortical actin patches and Las17p; interacts with type I myosins (633 aa)
Ubiquitin-binding protein; functions as ubiquitin-Atg8p adaptor in ubiquitin-dependent autophagy; serves as proteaphagy receptor for inactivated 26S proteasomes; contains CUE domain that binds ubiquitin, which may facilitate intramolecular monoubiquitination; CUE5 has a paralog, DON1, that arose from the whole genome duplication; human TOLLIP is a functional CUE-domain homolog, can complement yeast null mutant, rescuing hypersensitivity of cue5 null mutant cells to Htt-96Q (411 aa)
Myosin tail region-interacting protein MTI1; Protein possibly involved in assembly of actin patches; interacts with an actin assembly factor Las17p and with the SH3 domains of Type I myosins Myo3p and Myo5p; localized predominantly to cortical actin patches (1157 aa)
Myosin-5; One of two type I myosin motors; contains proline-rich tail homology 2 (TH2) and SH3 domains; MYO5 deletion has little effect on growth, but myo3 myo5 double deletion causes severe defects in growth and actin cytoskeleton organization; MYO5 has a paralog, MYO3, that arose from the whole genome duplication; Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family (1219 aa)
Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homolog of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa) (592 aa)
Protein BSP1; Adapter that links synaptojanins to the cortical actin cytoskeleton; the synaptojanins are Inp52p and Inp53p (576 aa)
Mevalonate kinase; acts in the biosynthesis of isoprenoids and sterols, including ergosterol, from mevalonate; human MVK functionally complements the lethality of the erg12 null mutation; Belongs to the GHMP kinase family. Mevalonate kinase subfamily (443 aa)
Protein implicated in polar growth, functionally redundant with Boi1p; interacts with bud-emergence protein Bem1p; contains an SH3 (src homology 3) domain and a PH (pleckstrin homology) domain; BOI2 has a paralog, BOI1, that arose from the whole genome duplication (1040 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (12%) [HD]