STRINGSTRING
BUD14 BUD14 CDC28 CDC28 ACT1 ACT1 BNR1 BNR1 SMY1 SMY1 CDC3 CDC3 HOF1 HOF1 BNI1 BNI1 ABP140 ABP140
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
BUD14Protein involved in bud-site selection; Bud14p-Glc7p complex is a cortical regulator of dynein; forms a complex with Kel1p and Kel2p that regulates Bnr1p (formin) to affect actin cable assembly, cytokinesis, and polarized growth; diploid mutants display a random budding pattern instead of the wild-type bipolar pattern; relative distribution to the nucleus increases upon DNA replication stress. (709 aa)
CDC28Cyclin-dependent kinase (CDK) catalytic subunit; master regulator of mitotic and meiotic cell cycles; alternately associates with G1, S, G2/M phase cyclins, which provide substrate specificity; regulates metabolism, basal transcription, chromosome dynamics, growth and morphogenesis; transcript induction in osmostress involves antisense RNA; human homologs CDK1, CDK2, CDK3 can complement yeast conditional cdc28 mutants; human CDK1, CDK2 can complement yeast cdc28 null mutant. (298 aa)
ACT1Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions. (375 aa)
BNR1BNI1-related protein 1; Formin; nucleates the formation of linear actin filaments; involved in processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables; activity is regulated by Hof1p and by the Bud14p-Kel1p-Kel2p complex; dephosphorylated and delocalized from the division site in a Glc7p/Ref2p-dependent manner; functionally redundant with BNI1. (1375 aa)
SMY1Kinesin-related protein SMY1; Kinesin-like myosin passenger-protein; interacts with Myo2p and enhances its interaction with Sec4p during transport of secretory vesicles; controls actin cable structure and dynamics. (656 aa)
CDC3Cell division control protein 3; Component of the septin ring that is required for cytokinesis; septins are GTP-binding proteins that assemble with other septins into rod-like complexes that can associate with other rods to form filament polymers; septin rings at the mother-bud neck act as scaffolds for recruiting factors needed for cell division and as barriers to prevent diffusion of specific proteins between mother and daughter cells; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family. (520 aa)
HOF1Cytokinesis protein 2; Protein that regulates actin cytoskeleton organization; required for cytokinesis, actin cable organization, and secretory vesicle trafficking; localized to bud neck; phosphorylated by Dbf2p; regulates actomyosin ring dynamics and septin localization; contains an SH3 domain; N terminus controls cell size and levels of actin cables, while C terminus controls actin cable organization via direct regulation of the formin Bnr1p. (669 aa)
BNI1Protein BNI1; Formin; polarisome component; 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; recruited to the division site in a Glc7p/Ref2p dependent manner following release of Bnr1p; functionally redundant with BNR1. (1953 aa)
ABP140tRNA(Thr) (cytosine(32)-N(3))-methyltransferase; AdoMet-dependent tRNA methyltransferase and actin binding protein; C-terminal domain is responsible for 3-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA-Thr and tRNA-Ser and contains an S-adenosylmethionine (AdoMet) binding motif; N-terminal actin binding sequence interacts with actin filaments and localizes to actin patches and cables; N- and C-terminal domains are encoded in separate ORFs that are translated into one protein via a +1 frameshift. (628 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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