STRINGSTRING
ESC1 protein (Saccharomyces cerevisiae) - STRING interaction network
"ESC1" - Protein localized to the nuclear periphery, involved in telomeric silencing 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 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:
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
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ESC1Protein localized to the nuclear periphery, involved in telomeric silencing; interacts with PAD4-domain of Sir4p; Involved in the clustering of telomeres at the nuclear periphery, forming discrete subcompartments that accumulate a complex of histone-binding silencing factors like SIR4. Required for SIR4-mediated anchoring and partitioning of plasmids (1658 aa)    
Predicted Functional Partners:
SIR4
Silent information regulator that, together with SIR2 and SIR3, is involved in assembly of silent chromatin domains at telomeres and the silent mating-type loci; potentially phosphorylated by Cdc28p; some alleles of SIR4 prolong lifespan; The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form (1358 aa)
       
 
  0.945
YRA1
RNA binding protein required for export of poly(A)+ mRNA from the nucleus; proposed to couple mRNA export with 3’ end processing via its interactions with Mex67p and Pcf11p; functionally redundant with Yra2p, another REF family member; RNA-binding RNA annealing protein. May have a role in pre-mRNA metabolism. Component the TREX complex, which operates in coupling transcription elongation to mRNA export (226 aa)
       
 
  0.901
CAP1
Alpha subunit of the capping protein (CP) heterodimer (Cap1p and Cap2p) which binds to the barbed ends of actin filaments preventing further polymerization; localized predominantly to cortical actin patches; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (268 aa)
       
      0.868
YKU70
Subunit of the telomeric Ku complex (Yku70p-Yku80p), involved in telomere length maintenance, structure and telomere position effect; relocates to sites of double-strand cleavage to promote nonhomologous end joining during DSB repair; Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appe [...] (602 aa)
       
 
  0.827
RAP1
DNA-binding protein involved in either activation or repression of transcription, depending on binding site context; also binds telomere sequences and plays a role in telomeric position effect (silencing) and telomere structure; Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements- promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are not intrinsic to its bindi [...] (827 aa)
       
 
  0.814
ULP1
Protease that specifically cleaves Smt3p protein conjugates; required for cell cycle progression; associates with nucleoporins and may interact with septin rings during telophase; sequestered to the nucleolus under stress conditions; Protease that catalyzes two essential functions in the SUMO pathway- processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle (621 aa)
       
 
  0.756
NFI1
SUMO E3 ligase, catalyzes the covalent attachment of SUMO (Smt3p) to proteins; primary E3 ligase for Sir4p; sumoylates Yku70p/Yku80p and Sir4p in vivo to promote chromatin anchoring; promotes telomere anchoring to the nuclear envelope; involved in m /.../ance of proper telomere length; May act as an E3 ligase mediating SUMO/Smt3 attachment to septins. May be involved in chromosome maintenance (726 aa)
       
 
  0.742
SRP1
Karyopherin alpha homolog, forms a dimer with karyopherin beta Kap95p to mediate import of nuclear proteins, binds the nuclear localization signal of the substrate during import; may also play a role in regulation of protein degradation; Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity) (542 aa)
       
 
  0.743
YKU80
Subunit of the telomeric Ku complex (Yku70p-Yku80p), involved in telomere length maintenance, structure and telomere position effect; relocates to sites of double-strand cleavage to promote nonhomologous end joining during DSB repair; Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appe [...] (629 aa)
           
  0.738
ULP2
Peptidase that deconjugates Smt3/SUMO-1 peptides from proteins, plays a role in chromosome cohesion at centromeric regions and recovery from checkpoint arrest induced by DNA damage or DNA replication defects; potential Cdc28p substrate; Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2 (1034 aa)
       
 
  0.732
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 (3%) [HD]