Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
BUD16 BUD16 BUD17 BUD17 SNZ2 SNZ2 SNO2 SNO2 SNZ3 SNZ3 PDX3 PDX3 SNO1 SNO1 SNO3 SNO3 SNZ1 SNZ1 TPN1 TPN1 PRO1 PRO1
"SNO1" - Protein of unconfirmed function, involved in pyridoxine metabolism in Saccharomyces cerevisiae
Nodes:
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
Edges:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SNO1Protein of unconfirmed function, involved in pyridoxine metabolism; expression is induced during stationary phase; forms a putative glutamine amidotransferase complex with Snz1p, with Sno1p serving as the glutaminase; May be required for the production of pyridoxine (vitamin B6) (224 aa)    
Predicted Functional Partners:
SNZ1
Protein involved in vitamin B6 biosynthesis; member of a stationary phase-induced gene family; coregulated with SNO1; interacts with Sno1p and with Yhr198p, perhaps as a multiprotein complex containing other Snz and Sno proteins; Required for the production of pyridoxine (vitamin B6). May be involved in growth arrest and cellular response to nutrient limitation. Required for growth in the presence of low level of intracellular pyridoxine (297 aa)
score_image   score_image score_image score_image score_image score_image   0.999
SNZ3
Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO3; May be required for the production of pyridoxine (vitamin B6) (298 aa)
score_image   score_image   score_image   score_image   0.999
SNZ2
Member of a stationary phase-induced gene family; transcription of SNZ2 is induced prior to diauxic shift, and also in the absence of thiamin in a Thi2p-dependent manner; forms a coregulated gene pair with SNO2; interacts with Thi11p; May be required for the production of pyridoxine (vitamin B6) (298 aa)
score_image   score_image   score_image   score_image   0.999
BUD16
Putative pyridoxal kinase, a key enzyme involved in pyridoxal 5’-phosphate synthesis, the active form of vitamin B6; required for genome integrity; involved in bud-site selection; similarity to yeast BUD17 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (312 aa)
score_image         score_image score_image   0.966
BUD17
Putative pyridoxal kinase, a key enzyme in vitamin B6 metabolism; involved in bud-site selection; diploid mutants display a random rather than a bipolar budding pattern; similarity to yeast BUD16 and human pyridoxal kinase (PDXK); Required for synthesis of pyridoxal-5-phosphate from vitamin B6 (By similarity). Important for bud site selection (317 aa)
score_image         score_image score_image   0.955
PDX3
Pyridoxine (pyridoxamine) phosphate oxidase, has homologs in E. coli and Myxococcus xanthus; transcription is under the general control of nitrogen metabolism; Catalyzes the oxidation of either pyridoxine 5’- phosphate (PNP) or pyridoxamine 5’-phosphate (PMP) into pyridoxal 5’-phosphate (PLP) (228 aa)
          score_image score_image   0.934
PRO1
Gamma-glutamyl kinase, catalyzes the first step in proline biosynthesis; Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5- oxoproline (428 aa)
          score_image     0.900
TPN1
Plasma membrane pyridoxine (vitamin B6) transporter; member of the purine-cytosine permease subfamily within the major facilitator superfamily; proton symporter with similarity to Fcy21p, Fcy2p, and Fcy22p; Thiamine-regulated, high affinity import carrier of pyridoxine, pyridoxal and pyridoxamine (579 aa)
        score_image   score_image   0.777
SNO2
Protein of unknown function, nearly identical to Sno3p; expression is induced before the diauxic shift and also in the absence of thiamin; May be required for the production of pyridoxine (vitamin B6) (222 aa)
    score_image   score_image   score_image score_image 0.775
SNO3
Protein of unknown function, nearly identical to Sno2p; expression is induced before the diauxic shift and also in the absence of thiamin; May be required for the production of pyridoxine (vitamin B6) (222 aa)
    score_image   score_image   score_image score_image 0.774
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