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PPIL3 PPIL3 CDC37L1 CDC37L1 HSP90B1 HSP90B1 CSNK2A1 CSNK2A1 ENSG00000108825 ENSG00000108825 TRAP1 TRAP1 SKP1 SKP1 CDC37 CDC37 S100A4 S100A4 CHORDC1 CHORDC1 HSP90AB1 HSP90AB1 SUGT1 SUGT1 S100P S100P HSPA8 HSPA8 HSP90AA1 HSP90AA1 PHLPP1 PHLPP1 UBC UBC USP12 USP12 APP APP MIS12 MIS12 USP46 USP46 NOD1 NOD1 PANX1 PANX1 P2RX7 P2RX7
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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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small nodes:
protein of unknown 3D structure
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large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
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white nodes:
second shell of interactors
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experimentally determined
Predicted Interactions
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fusion edge
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textmining
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CSNK2A1casein kinase 2, alpha 1 polypeptide; Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly che [...] (391 aa)
CDC37cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (378 aa)
NOD1nucleotide-binding oligomerization domain containing 1; Enhances caspase-9-mediated apoptosis. Induces NF-kappa- B activity via RIPK2 and IKK-gamma. Confers responsiveness to intracellular bacterial lipopolysaccharides (LPS). Forms an intracellular sensing system along with ARHGEF2 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIPK2 dependent NF-kappa-B signaling pathway activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides but also in the activation of NF-kappa-B by Shigella e [...] (953 aa)
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)
PANX1pannexin 1; Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (426 aa)
SKP1S-phase kinase-associated protein 1; Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC [...] (163 aa)
TRAP1TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa)
PHLPP1PH domain and leucine rich repeat protein phosphatase 1; Protein phosphatase that mediates dephosphorylation of ’Ser-473’ of AKT1, ’Ser-660’ of PRKCB isoform beta-II and ’Ser- 657’ of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of ’Ser-473’ of AKT1 triggers apoptosis and suppression of tumor growth. Controls the phosphorylation of AKT2 and AKT3 more efficiently than that of AKT1. Dephosphorylation of PRKCA and PRKCB leads [...] (1717 aa)
USP12ubiquitin specific peptidase 12; Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 (370 aa)
APPamyloid beta (A4) precursor protein (770 aa)
PPIL3peptidylprolyl isomerase (cyclophilin)-like 3; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be involved in pre-mRNA splicing (165 aa)
S100PS100 calcium binding protein P; May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE) (95 aa)
HSP90B1heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa)
CHORDC1cysteine and histidine-rich domain (CHORD) containing 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (332 aa)
HSP90AB1heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (724 aa)
HSP90AA1heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (854 aa)
UBCubiquitin C (685 aa)
S100A4S100 calcium binding protein A4 (101 aa)
SUGT1SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins (365 aa)
MIS12MIS12, MIND kinetochore complex component, homolog (S. pombe); Part of the MIS12 complex which is required for normal chromosome alignment and segregation and for kinetochore formation during mitosis (205 aa)
CDC37L1cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity) (337 aa)
ENSG00000108825PTGES3L-AARSD1 readthrough; Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) (By similarity) (586 aa)
USP46ubiquitin specific peptidase 46; Deubiquitinating enzyme that plays a role in behavior, possibly by regulating GABA action. May act by mediating the deubiquitination of GAD1/GAD67. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2 (366 aa)
P2RX7purinergic receptor P2X, ligand-gated ion channel, 7; Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells (595 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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