STRINGSTRING
RME1 RME1 URA9 URA9 SES1 SES1 PMS1 PMS1 NAM2 NAM2 CDC60 CDC60 YKU80 YKU80 SIR2 SIR2 CSE4 CSE4 CaO19.1201 CaO19.1201 MLH1 MLH1 HHT21 HHT21 HHT3 HHT3
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 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:
a 3D structure is known or predicted
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
RME1Rme1p. (507 aa)
URA9Dihydroorotate dehydrogenase (quinone), mitochondrial; In the de novo pyrimidine biosynthesis pathway, catalyzes the stereospecific oxidation of (S)-dihydroorotate to orotate with reduction of flavin and the transfer of electrons to ubiquinone, which is part of the repiratory chain. Does not use fumarate and NAD as electron acceptors. (444 aa)
SES1Serine--tRNA ligase, cytoplasmic; Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). (462 aa)
PMS1ATP-binding mismatch repair protein. (910 aa)
NAM2Leucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (861 aa)
CDC60Leucine--tRNA ligase. (1097 aa)
YKU80ATP-dependent DNA helicase. (609 aa)
SIR2NAD-dependent histone deacetylase SIR2; NAD-dependent deacetylase. Heterochromatin component that silences transcription at silent mating loci, telomeres and the ribosomal DNA, and that also suppresses recombination in the rDNA and extends replicative life span. It acts as a NAD-dependent histone deacetylase, which deacetylates 'Lys-9' and 'Lys-14' of Histone H3 and 'Lys-16' of Histone H4. Functions in the distribution of oxidatively damaged proteins during cell division. Mediates phenotypic switching. (519 aa)
CSE4Histone H3-like centromeric protein CSE4; Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). (211 aa)
CaO19.1201Putative serine--tRNA ligase. (496 aa)
MLH1Mismatch repair ATPase. (717 aa)
HHT21Histone H3.1/H3.2; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). (136 aa)
HHT3Histone H3.3; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). (136 aa)
Your Current Organism:
Candida albicans
NCBI taxonomy Id: 237561
Other names: C. albicans SC5314, Candida albicans SC5314
Server load: low (10%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.