Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
BUD31 BUD31 MS4A13 MS4A13 CAD CAD HRAS HRAS PPIAL4A PPIAL4A NUDCD2 NUDCD2 HSP90AA1 HSP90AA1 PIN1 PIN1 HSP90AB1 HSP90AB1 FKBP10 FKBP10 TRAP1 TRAP1
"PPIAL4A" - peptidylprolyl isomerase A (cyclophilin A)-like 4A in Homo sapiens
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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
PPIAL4Apeptidylprolyl isomerase A (cyclophilin A)-like 4A (164 aa)    
Predicted Functional Partners:
HSP90AB1
heat 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)
      score_image score_image   score_image   0.656
NUDCD2
NudC domain containing 2; May regulate the LIS1/dynein pathway by stabilizing LIS1 with Hsp90 chaperone (157 aa)
        score_image   score_image   0.652
CAD
carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 aa)
      score_image score_image   score_image   0.638
HSP90AA1
heat 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)
      score_image score_image   score_image   0.622
TRAP1
TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity (704 aa)
      score_image score_image   score_image   0.541
FKBP10
FK506 binding protein 10, 65 kDa; PPIases accelerate the folding of proteins during protein synthesis (582 aa)
        score_image   score_image   0.540
HRAS
v-Ha-ras Harvey rat sarcoma viral oncogene homolog; Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (189 aa)
            score_image   0.529
PIN1
peptidylprolyl cis/trans isomerase, NIMA-interacting 1; Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML [...] (163 aa)
        score_image   score_image   0.491
BUD31
BUD31 homolog (S. cerevisiae) (144 aa)
        score_image   score_image   0.466
MS4A13
membrane-spanning 4-domains, subfamily A, member 13; May be involved in signal transduction as a component of a multimeric receptor complex (By similarity) (152 aa)
      score_image score_image   score_image   0.411
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (29%)