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EME1 EME1 EME2 EME2 POLN POLN DCLRE1B DCLRE1B MUS81 MUS81 C19orf40 C19orf40 UBA52 UBA52 BLM BLM TOP3A TOP3A RPS27A RPS27A UBB UBB DCLRE1A DCLRE1A FANCB FANCB FANCI FANCI RPA1 RPA1 FAN1 FAN1 UBC UBC RPA3 RPA3 FANCL FANCL RAD1 RAD1 FANCE FANCE RFC5 RFC5 HUS1 HUS1 TOPBP1 TOPBP1 RAD9A RAD9A BARD1 BARD1
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.
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small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
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gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
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RPA3replication protein A3, 14kDa; Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions (121 aa)
FANCEFanconi anemia, complementation group E; As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2 (536 aa)
RPA1replication protein A1, 70kDa; Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing (616 aa)
HUS1HUS1 checkpoint homolog (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavag [...] (280 aa)
TOPBP1topoisomerase (DNA) II binding protein 1; Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double- stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1- responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR (1522 aa)
BARD1BRCA1 associated RING domain 1; Probable E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of ’Lys-6’-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP I [...] (777 aa)
RPS27Aribosomal protein S27a (156 aa)
EME2essential meiotic endonuclease 1 homolog 2 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3’-flap structures (444 aa)
UBBubiquitin B (229 aa)
MUS81MUS81 endonuclease homolog (S. cerevisiae); Interacts with EME1 and EME2 to form a DNA structure- specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’-flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks (551 aa)
FANCIFanconi anemia, complementation group I; Plays an essential role in the repair of DNA double- strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA- binds both single- stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage (1328 aa)
RAD9ARAD9 homolog A (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activit [...] (391 aa)
TOP3Atopoisomerase (DNA) III alpha; Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5’-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3’-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA superco [...] (1001 aa)
FANCBFanconi anemia, complementation group B; DNA repair protein required for FANCD2 ubiquitination (859 aa)
RAD1RAD1 homolog (S. pombe); Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair. The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3’-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity [...] (282 aa)
UBCubiquitin C (685 aa)
BLMBloom syndrome, RecQ helicase-like; Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3’-5’ direction. Involved in 5’-end resection of DNA during double-strand break (DSB) repair- unwinds DNA and recruits DNA2 which mediates the cleavage of 5’-ssDNA (1417 aa)
FAN1FANCD2/FANCI-associated nuclease 1; Nuclease required for maintenance of chromosomal stability. Plays a key role in DNA repair of DNA interstrand cross-links (ICL) by being recruited to sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL- induced DNA breaks by being required for efficient homologous recombination, possibly in the resolution of homologous recombination intermediates. Not involved in DNA double-strand breaks resection. Has both endonuclease activity toward 5’-flaps and 5’-exonuclease activity- may act in concert with the 3’-flap- speci [...] (1017 aa)
DCLRE1ADNA cross-link repair 1A; May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons (1040 aa)
DCLRE1BDNA cross-link repair 1B; 5’-3’ exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)- mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity- generates 3’ single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomer [...] (532 aa)
POLNpolymerase (DNA directed) nu (900 aa)
EME1essential meiotic endonuclease 1 homolog 1 (S. pombe); Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5’-end at the branch nick. Typical substrates include 3’- flap structures, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication forks (583 aa)
FANCLFanconi anemia, complementation group L; Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth (380 aa)
UBA52ubiquitin A-52 residue ribosomal protein fusion product 1 (128 aa)
RFC5replication factor C (activator 1) 5, 36.5kDa; The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1 (340 aa)
C19orf40chromosome 19 open reading frame 40; Plays a role in DNA repair through recruitment of the FA core complex to damaged DNA. Regulates FANCD2 monoubiquitination upon DNA damage. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. Targets FANCM/FAAP24 complex to the DNA, preferentially to single strand DNA (215 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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