Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
UPB1 UPB1 PPIG PPIG GGT2 GGT2 NADSYN1 NADSYN1 NUBPL NUBPL NIT2 NIT2 PPIA PPIA LIMS2 LIMS2 VNN1 VNN1 LIMS1 LIMS1 NIT1 NIT1 KIFC1 KIFC1 RAD21 RAD21 VNN3 VNN3 PPIF PPIF VNN2 VNN2 KIFC3 KIFC3 KIF11 KIF11 BTD BTD KIF25 KIF25 KIFC2 KIFC2
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:
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)
KIF11kinesin family member 11; Motor protein required for establishing a bipolar spindle. Blocking of KIF11 prevents centrosome migration and arrest cells in mitosis with monoastral microtubule arrays (1056 aa)
PPIGpeptidylprolyl isomerase G (cyclophilin G); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing (754 aa)
NUBPLnucleotide binding protein-like; Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). May deliver of one or more Fe-S clusters to complex I subunits (319 aa)
RAD21RAD21 homolog (S. pombe); Cleavable component of the cohesin complex, involved in chromosome cohesion during cell cycle, in DNA repair, and in apoptosis. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by separase/ESPL1 and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Als [...] (631 aa)
KIFC2kinesin family member C2; May play a role in microtubule-dependent retrograde axonal transport. May function as the motor for the transport of multivesicular body (MVB)-like organelles in dendrites (By similarity) (838 aa)
BTDbiotinidase; Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation (543 aa)
VNN2vanin 2 (520 aa)
UPB1ureidopropionase, beta; Converts N-carbamyl-beta-aminoisobutyric acid and N- carbamyl-beta-alanine to, respectively, beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide (384 aa)
NADSYN1NAD synthetase 1 (706 aa)
LIMS2LIM and senescent cell antigen-like domains 2 (365 aa)
KIF25kinesin family member 25; Negative regulator of amino acid starvation-induced autophagy (384 aa)
VNN1vanin 1; Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine (513 aa)
NIT1nitrilase 1; Plays a role in cell growth and apoptosis- loss of expression promotes cell growth and resistance to DNA damage stress. Has tumor suppressor properties that enhances the apoptotic responsiveness in cancer cells; this effect is additive to the tumor suppressor activity of FHIT. It is also a negative regulator of primary T-cells. Has apparently no omega-amidase activity such as NIT2 (By similarity) (327 aa)
KIFC3kinesin family member C3; Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance (833 aa)
NIT2nitrilase family, member 2; Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha- ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. Overexpression decreases the colony-forming capacity of cultured cells by arresting cells in the G2 phase of the cell cycle (276 aa)
GGT2gamma-glutamyltransferase 2; Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors (By similarity) (569 aa)
KIFC1kinesin family member C1 (673 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)
VNN3vanin 3 (500 aa)
LIMS1LIM and senescent cell antigen-like domains 1; Adapter protein in a cytoplasmic complex linking beta- integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation (387 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Server load: low (34%)