STRINGSTRING
MSH2 MSH2 HSC82 HSC82 MLH1 MLH1 PMS1 PMS1 HSP82 HSP82 EXO1 EXO1 POL30 POL30 MSH3 MSH3 MSH6 MSH6
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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MSH2Protein that binds to DNA mismatches; forms heterodimers with Msh3p and Msh6p that bind to DNA mismatches to initiate the mismatch repair process; contains a Walker ATP-binding motif required for repair activity and involved in interstrand cross-link repair; Msh2p-Msh6p binds to and hydrolyzes ATP. (964 aa)
HSC82ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. (705 aa)
MLH1Protein required for mismatch repair in mitosis and meiosis; also required for crossing over during meiosis; forms a complex with Pms1p and Msh2p-Msh3p during mismatch repair; human homolog is associated with hereditary non-polyposis colon cancer; Belongs to the DNA mismatch repair MutL/HexB family. (769 aa)
PMS1ATP-binding protein required for mismatch repair; required for both mitosis and meiosis; functions as a heterodimer with Mlh1p; binds double- and single-stranded DNA via its N-terminal domain, similar to E. coli MutL. (873 aa)
HSP82ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication. (709 aa)
EXO1Exodeoxyribonuclease 1; 5'-3' exonuclease and flap-endonuclease; involved in recombination, double-strand break repair, MMS2 error-free branch of the post replication (PRR) pathway and DNA mismatch repair; role in telomere maintenance; member of the Rad2p nuclease family, with conserved N and I nuclease domains; relative distribution to the nucleus increases upon DNA replication stress; EXO1 has a paralog, DIN7, that arose from the whole genome duplication. (702 aa)
POL30Proliferating cell nuclear antigen (PCNA); functions as the sliding replication clamp for DNA polymerase delta; may function as a docking site for other proteins required for mitotic and meiotic chromosomal DNA replication and for DNA repair; PCNA ubiquitination at K164 plays a crucial role during Okazaki fragment processing. (258 aa)
MSH3Mismatch repair protein; forms dimers with Msh2p that mediate repair of insertion or deletion mutations and removal of nonhomologous DNA ends, contains a PCNA (Pol30p) binding motif required for genome stability; Belongs to the DNA mismatch repair MutS family. MSH3 subfamily. (1018 aa)
MSH6Protein required for mismatch repair in mitosis and meiosis; forms a complex with Msh2p to repair both single-base & insertion-deletion mispairs; also involved in interstrand cross-link repair; potentially phosphorylated by Cdc28p. (1242 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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