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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | FKBP4 | FK506 binding protein 4, 59kDa; Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembl [...] (459 aa) | ||
 | FKBP3 | FK506 binding protein 3, 25kDa; FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins (224 aa) | ||
 | FKBP8 | FK506 binding protein 8, 38kDa; Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The active form of FKBP8 may therefore play a role in the regulation of apoptosis (413 aa) | ||
 | FKBP14 | FK506 binding protein 14, 22 kDa; PPIases accelerate the folding of proteins during protein synthesis (211 aa) | ||
 | DDX55 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 55; Probable ATP-binding RNA helicase (600 aa) | ||
 | FKBP9 | FK506 binding protein 9, 63 kDa; PPIases accelerate the folding of proteins during protein synthesis (570 aa) | ||
 | FKBP6 | FK506 binding protein 6, 36kDa (327 aa) | ||
 | MKI67IP | MKI67 (FHA domain) interacting nucleolar phosphoprotein (293 aa) | ||
 | DDB1 | damage-specific DNA binding protein 1, 127kDa; Required for DNA repair. Binds to DDB2 to form the UV- damaged DNA-binding protein complex (the UV-DDB complex). The UV- DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which [...] (1140 aa) | ||
 | FKBP2 | FK506 binding protein 2, 13kDa; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (142 aa) | ||
 | FKBP10 | FK506 binding protein 10, 65 kDa; PPIases accelerate the folding of proteins during protein synthesis (582 aa) | ||
 | FKBP5 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP (457 aa) | ||
 | PPP4R2 | protein phosphatase 4, regulatory subunit 2; Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on ’Ser-140’ (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruitin [...] (417 aa) | ||
 | WDR55 | WD repeat domain 55; Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity) (383 aa) | ||
 | GTPBP4 | GTP binding protein 4; Involved in the biogenesis of the 60S ribosomal subunit (By similarity) (634 aa) | ||
 | FKBP1C | FK506 binding protein 1C (108 aa) | ||
 | DDX31 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 31 (851 aa) | ||
 | DLG5 | discs, large homolog 5 (Drosophila) (1919 aa) | ||
 | SRPK1 | SRSF protein kinase 1; Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activiti [...] (655 aa) | ||
 | FKBP1B | FK506 binding protein 1B, 12.6 kDa; Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (108 aa) | ||
 | FKBP1A | FK506 binding protein 1A, 12kDa; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (108 aa) | ||
 | KIAA0020 | KIAA0020 (648 aa) | ||
 | RPF2 | ribosome production factor 2 homolog (S. cerevisiae) (306 aa) | ||
 | FKBP7 | FK506 binding protein 7; PPIases accelerate the folding of proteins during protein synthesis (222 aa) | ||
 | FKBP11 | FK506 binding protein 11, 19 kDa; PPIases accelerate the folding of proteins during protein synthesis (201 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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