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CWC27 CWC27 PPIL1 PPIL1 SRGAP3 SRGAP3 VANGL2 VANGL2 RANBP2 RANBP2 PPIL3 PPIL3 PSG9 PSG9 PPIL2 PPIL2 PPIAL4B PPIAL4B PPIF PPIF PPIL6 PPIL6 PPIE PPIE CELSR3 CELSR3 SRGAP2 SRGAP2 PPIAL4C PPIAL4C SRGAP1 SRGAP1 PPIAL4D PPIAL4D PPIL4 PPIL4 VANGL1 VANGL1 PPIH PPIH PPID PPID DLL1 DLL1 PPIAL4A PPIAL4A CPA4 CPA4 PPIA PPIA PPIAL4G PPIAL4G
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:
CELSR3cadherin, EGF LAG seven-pass G-type receptor 3 (flamingo homolog, Drosophila); Receptor that may have an important role in cell/cell signaling during nervous system formation (3312 aa)
CPA4carboxypeptidase A4; Metalloprotease that could be involved in the histone hyperacetylation pathway (421 aa)
PPIFpeptidylprolyl isomerase F; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probablity of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial TP53 is involved in activating oxidative stress- i [...] (207 aa)
PPIL4peptidylprolyl isomerase (cyclophilin)-like 4; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (492 aa)
PSG9pregnancy specific beta-1-glycoprotein 9 (426 aa)
RANBP2RAN binding protein 2; E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2 conjugation by UBE2I. Involved in transport factor (Ran-GTP, karyopherin)-mediated protein import via the F-G repeat-containing domain which acts as a docking site for substrates. Could also have isomerase or chaperone activity and may bind RNA or DNA. Component of the nuclear export pathway. Specific docking site for the nuclear export factor exportin-1. Sumoylates PML at ’Lys-490’ which is essential for the proper assembly of PML-NB (3224 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)
SRGAP2SLIT-ROBO Rho GTPase activating protein 2; RAC1 GTPase activating protein (GAP) that binds and deforms membranes, and regulates actin dynamics to regulate cell migration and differentiation. Plays an important role in different aspects of neuronal morphogenesis and migration mainly during development of the cerebral cortex. This includes the biogenesis of neurites, where it is required for both axons and dendrites outgrowth, and the maturation of the dendritic spines. Also stimulates the branching of the leading process and negatively regulates neuron radial migration in the cerebral c [...] (985 aa)
PPIDpeptidylprolyl isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] (370 aa)
PPIHpeptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone (177 aa)
VANGL1vang-like 1 (van gogh, Drosophila) (524 aa)
SRGAP1SLIT-ROBO Rho GTPase activating protein 1; GTPase-activating protein for RhoA and Cdc42 small GTPases. Together with CDC42 seems to be involved in the pathway mediating the repulsive signaling of Robo and Slit proteins in neuronal migration. SLIT2, probably through interaction with ROBO1, increases the interaction of SRGAP1 with ROBO1 and inactivates CDC42 (1085 aa)
DLL1delta-like 1 (Drosophila); Acts as a ligand for Notch receptors. Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (723 aa)
VANGL2vang-like 2 (van gogh, Drosophila); Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process (By similarity) (521 aa)
PPIAL4Cpeptidylprolyl isomerase A (cyclophilin A)-like 4C; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (164 aa)
PPIEpeptidylprolyl isomerase E (cyclophilin E); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (314 aa)
PPIL1peptidylprolyl isomerase (cyclophilin)-like 1; 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 (166 aa)
CWC27CWC27 spliceosome-associated protein homolog (S. cerevisiae); PPIases accelerate the folding of proteins (By similarity) (472 aa)
SRGAP3SLIT-ROBO Rho GTPase activating protein 3; GTPase-activating protein for RAC1 and perhaps Cdc42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons (1099 aa)
PPIL2peptidylprolyl isomerase (cyclophilin)-like 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (527 aa)
PPIL6peptidylprolyl isomerase (cyclophilin)-like 6; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (337 aa)
PPIAL4Gpeptidylprolyl isomerase A (cyclophilin A)-like 4G; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (164 aa)
PPIApeptidylprolyl isomerase A (cyclophilin A); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity) (165 aa)
PPIAL4Apeptidylprolyl isomerase A (cyclophilin A)-like 4A (164 aa)
PPIAL4Dpeptidylprolyl isomerase A (cyclophilin A)-like 4D (164 aa)
PPIAL4Bpeptidylprolyl isomerase A (cyclophilin A)-like 4B (164 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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