STRINGSTRING
A0A1L9U1P2 A0A1L9U1P2 A0A1L9U2T4 A0A1L9U2T4 A0A1L9U3Z6 A0A1L9U3Z6 A0A1L9U609 A0A1L9U609 A0A1L9UBX3 A0A1L9UBX3 A0A1L9UC00 A0A1L9UC00 A0A1L9UCI3 A0A1L9UCI3 A0A1L9UI62 A0A1L9UI62 A0A1L9UK56 A0A1L9UK56 A0A1L9UKR8 A0A1L9UKR8 A0A1L9UP58 A0A1L9UP58 A0A1L9UP68 A0A1L9UP68 A0A1L9USK0 A0A1L9USK0 A0A1L9UT08 A0A1L9UT08 A0A1L9UUV4 A0A1L9UUV4 A0A1L9UVP5 A0A1L9UVP5 A0A1L9UXB3 A0A1L9UXB3 A0A1L9UXT0 A0A1L9UXT0 A0A1L9UYL3 A0A1L9UYL3 A0A1L9UZW3 A0A1L9UZW3 A0A1L9V0A9 A0A1L9V0A9 FEN1 FEN1
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:
A0A1L9U1P2AAA domain-containing protein. (315 aa)
A0A1L9U2T4Uncharacterized protein. (755 aa)
A0A1L9U3Z6EthD domain-containing protein. (171 aa)
A0A1L9U609Pectinesterase; Involved in maceration and soft-rotting of plant tissue. (327 aa)
A0A1L9UBX3Checkpoint protein; Belongs to the HUS1 family. (393 aa)
A0A1L9UC00AAA domain-containing protein. (352 aa)
A0A1L9UCI3BRCT domain-containing protein. (1349 aa)
A0A1L9UI62Uncharacterized protein. (598 aa)
A0A1L9UK56Uncharacterized protein. (759 aa)
A0A1L9UKR8AAA domain-containing protein. (400 aa)
A0A1L9UP58RPA_C domain-containing protein. (291 aa)
A0A1L9UP68Double-strand break repair protein; Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing. (797 aa)
A0A1L9USK0Uncharacterized protein. (473 aa)
A0A1L9UT08Uncharacterized protein. (575 aa)
A0A1L9UUV4Replication protein A subunit; As part of the replication protein A (RPA/RP-A), a single- stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism. (606 aa)
A0A1L9UVP5AAA domain-containing protein. (758 aa)
A0A1L9UXB3AAA domain-containing protein. (582 aa)
A0A1L9UXT0DNA repair protein rad9; Acts in DNA repair and mutagenesis. Involved in promoting resistance to ionizing radiation and UV light, as well as regulating cell cycle progression after irradiation. (456 aa)
A0A1L9UYL3Uncharacterized protein; Belongs to the PI3/PI4-kinase family. (2462 aa)
A0A1L9UZW3Uncharacterized protein. (784 aa)
A0A1L9V0A9Serine/threonine-protein kinase Tel1; 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. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the regulation of DNA damage response mechanism. Required for the control of telomere length and genome stability; Belongs to the PI3/PI4-kinase family. ATM subfamily. (2901 aa)
FEN1Flap endonuclease 1; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site- terminated flap. Acts as [...] (359 aa)
Your Current Organism:
Aspergillus brasiliensis
NCBI taxonomy Id: 767769
Other names: A. brasiliensis CBS 101740, Aspergillus brasiliensis CBS 101740
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