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CDC13 protein (Saccharomyces cerevisiae) - STRING interaction network
"CDC13" - Single stranded DNA-binding protein found at TG1-3 telomere G-tails in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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textmining
co-expression
protein homology
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CDC13Single stranded DNA-binding protein found at TG1-3 telomere G-tails; regulates telomere replication through recruitment of specific sub-complexes, but the essential function is telomere capping; Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomera [...] (924 aa)    
Predicted Functional Partners:
POL1
Catalytic subunit of the DNA polymerase I alpha-primase complex, required for the initiation of DNA replication during mitotic DNA synthesis and premeiotic DNA synthesis; Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha-primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13 (1468 aa)
       
 
  0.987
EST1
TLC1 RNA-associated factor involved in telomere length regulation as recruitment subunit of telomerase; has G-quadruplex promoting activity that is required for telomere elongation; possible role in activating telomere-bound Est2p-TLC1-RNA; Directly involved in telomere replication. Associates with telomerase and during its interaction with CDC13, telomerase activity is promoted (699 aa)
       
 
  0.984
STN1
Telomere end-binding and capping protein, plays a key role with Pol12p in linking telomerase action with completion of lagging strand synthesis, and in a regulatory step required for telomere capping; Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13 (494 aa)
       
 
  0.983
MEC1
Genome integrity checkpoint protein and PI kinase superfamily member; signal transducer required for cell cycle arrest and transcriptional responses prompted by damaged or unreplicated DNA; monitors and participates in meiotic recombination; Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein comp [...] (2368 aa)
       
 
  0.976
TEN1
Protein that regulates telomeric length; protects telomeric ends in a complex with Cdc13p and Stn1p; Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13 (160 aa)
       
 
  0.976
RIF2
Protein that binds to the Rap1p C-terminus and acts synergistically with Rif1p to help control telomere length and establish telomeric silencing; deletion results in telomere elongation; Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres (395 aa)
       
 
  0.961
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)
       
 
  0.956
RAD50
Subunit of MRX complex, with Mre11p and Xrs2p, involved in processing double-strand DNA breaks in vegetative cells, initiation of meiotic DSBs, telomere maintenance, and nonhomologous end joining; Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site (1312 aa)
       
 
  0.953
CDC28
Catalytic subunit of the main cell cycle cyclin-dependent kinase (CDK); alternately associates with G1 cyclins (CLNs) and G2/M cyclins (CLBs) which direct the CDK to specific substrates; This protein is essential for the completion of the start, the controlling event, in the cell cycle. More than 200 substrates have been identified (298 aa)
       
 
  0.940
TEL1
Protein kinase primarily involved in telomere length regulation; contributes to cell cycle checkpoint control in response to DNA damage; functionally redundant with Mec1p; homolog of human ataxia telangiectasia (ATM) gene; Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited by the MRX-complex to sites of DNA lesions immediately after damage to initiate non- homo [...] (2787 aa)
       
 
  0.938
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
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