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MUS81 MUS81 ERCC4 ERCC4 FANCM FANCM RFC5 RFC5 RAD17 RAD17 CHTF18 CHTF18 DNLZ DNLZ HSPA4 HSPA4 HSPA9 HSPA9 HSPA12A HSPA12A HSPH1 HSPH1 HSPA8 HSPA8 HSPA12B HSPA12B HSPA6 HSPA6 HSPA1A HSPA1A HSPA4L HSPA4L HSPA5 HSPA5 ANKRD45 ANKRD45 HSPA2 HSPA2 HSPA1L HSPA1L HYOU1 HYOU1 HSPA1B HSPA1B HSPA13 HSPA13 ACTG2 ACTG2 ACTC1 ACTC1 HSPA14 HSPA14
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
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
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
HSPA8heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (646 aa)
HSPA2heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (639 aa)
HSPA12Bheat shock 70kD protein 12B (686 aa)
CHTF18CTF18, chromosome transmission fidelity factor 18 homolog (S. cerevisiae); Chromosome cohesion factor involved in sister chromatid cohesion and fidelity of chromosome transmission. Component of one of the cell nuclear antigen loader complexes, CTF18-replication factor C (CTF18-RFC), which consists of CTF18, CTF8, DCC1, RFC2, RFC3, RFC4 and RFC5. The CTF18-RFC complex binds to single- stranded and primed DNAs and has weak ATPase activity that is stimulated by the presence of primed DNA, replication protein A (RPA) and by proliferating cell nuclear antigen (PCNA). The CTF18- RFC complex [...] (975 aa)
FANCMFanconi anemia, complementation group M; ATPase required for FANCD2 ubiquitination, a key reaction in DNA repair. Binds to ssDNA but not to dsDNA. Recruited to forks stalled by DNA interstrand cross-links, and required for cellular resistance to such lesions (2048 aa)
HSPA13heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity (471 aa)
ACTC1actin, alpha, cardiac muscle 1; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (377 aa)
ACTG2actin, gamma 2, smooth muscle, enteric; Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells (376 aa)
HSPA4Lheat shock 70kDa protein 4-like; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase (By similarity) (839 aa)
HSPA9heat shock 70kDa protein 9 (mortalin) (679 aa)
HSPA4heat shock 70kDa protein 4 (840 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)
HSPA6heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) (643 aa)
ERCC4excision repair cross-complementing rodent repair deficiency, complementation group 4; Structure-specific DNA repair endonuclease responsible for the 5-prime incision during DNA repair. Involved in homologous recombination that assists in removing interstrand cross-link (916 aa)
HSPH1heat shock 105kDa/110kDa protein 1; Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity) (858 aa)
HSPA5heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa)
ANKRD45ankyrin repeat domain 45 (266 aa)
HSPA12Aheat shock 70kDa protein 12A (675 aa)
DNLZDNL-type zinc finger; May function as a co-chaperone towards HSPA9/mortalin which, by itself, is prone to self-aggregation (178 aa)
HSPA1Bheat shock 70kDa protein 1B (641 aa)
HSPA1Aheat shock 70kDa protein 1A (641 aa)
HSPA1Lheat shock 70kDa protein 1-like (641 aa)
HSPA14heat shock 70kDa protein 14; Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (509 aa)
RAD17RAD17 homolog (S. pombe) (681 aa)
HYOU1hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (999 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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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