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  • 11.0 [archived version]
STRINGSTRING
GDPGP1 GDPGP1 TNXB TNXB HSPD1 HSPD1 CCT6B CCT6B FGL2 FGL2 CCT6A CCT6A TNN TNN TCP1 TCP1 CCT4 CCT4 MKKS MKKS CCT2 CCT2 PDPK1 PDPK1 CCT3 CCT3 ATIC ATIC BBS10 BBS10 CCT5 CCT5 CCT7 CCT7 HDHD2 HDHD2 ARL13B ARL13B VKORC1L1 VKORC1L1 LHPP LHPP ANGPTL1 ANGPTL1 FCN3 FCN3 TNC TNC ANGPTL6 ANGPTL6 ARFRP1 ARFRP1
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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
Your Input:
ANGPTL1Angiopoietin-related protein 1; Fibrinogen C domain containing; Angiopoietin like (491 aa)
ATICBifunctional purine biosynthesis protein PURH; Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis; Belongs to the PurH family (592 aa)
TNNTenascin-N; Extracellular matrix protein that seems to be a ligand for ITGA8-ITGB1, ITGAV-ITGB1 and ITGA4-ITGB1 (By similarity). Involved in neurite outgrowth and cell migration in hippocampal explants (By similarity). During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling (By similarity). In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells; Belon [...] (1299 aa)
MKKSMcKusick-Kaufman/Bardet-Biedl syndromes putative chaperonin; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis; Belongs to the TCP-1 chaperonin family (570 aa)
FGL2Fibroleukin; May play a role in physiologic lymphocyte functions at mucosal sites; Fibrinogen C domain containing (439 aa)
ANGPTL6Angiopoietin-related protein 6; May play a role in the wound healing process. May promote epidermal proliferation, remodeling and regeneration. May promote the chemotactic activity of endothelial cells and induce neovascularization. May counteract high-fat diet-induced obesity and related insulin resistance through increased energy expenditure; Angiopoietin like (470 aa)
CCT7T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity); Chaperonins (543 aa)
TNCTenascin; Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells; Belongs to the tenascin family (2201 aa)
FCN3Ficolin-3; May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc- binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota; Fibrinogen C domain containing (299 aa)
CCT6AT-complex protein 1 subunit zeta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family (531 aa)
CCT5T-complex protein 1 subunit epsilon; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (541 aa)
CCT3T-complex protein 1 subunit gamma; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (545 aa)
CCT2T-complex protein 1 subunit beta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (535 aa)
HDHD2Haloacid dehalogenase like hydrolase domain containing 2 (259 aa)
TCP1T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Belongs to the TCP-1 chaperonin family (556 aa)
CCT6BT-complex protein 1 subunit zeta-2; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity); Chaperonins (530 aa)
PDPK13-phosphoinositide-dependent protein kinase 1; Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include- protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central rol [...] (556 aa)
LHPPPhospholysine phosphohistidine inorganic pyrophosphate phosphatase; Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity); Belongs to the HAD-like hydrolase superfamily (270 aa)
HSPD160 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] (573 aa)
BBS10Bardet-Biedl syndrome 10 protein; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation; Belongs to the TCP-1 chaperonin family (723 aa)
ARL13BADP-ribosylation factor-like protein 13B; Cilium-specific protein required to control the microtubule-based, ciliary axoneme structure. May act by maintaining the association between IFT subcomplexes A and B. Binds GTP but is not able to hydrolyze it; the GTPase activity remains unclear. Required to pattern the neural tube. Involved in cerebral cortex development- required for the initial formation of a polarized radial glial scaffold, the first step in the construction of the cerebral cortex, by regulating ciliary signaling. Regulates the migration and placement of postmitotic interne [...] (428 aa)
CCT4T-complex protein 1 subunit delta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin; Chaperonins (539 aa)
VKORC1L1Vitamin K epoxide reductase complex subunit 1 like 1 (177 aa)
TNXBTenascin-X; Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors; Fibrinogen C domain containing (673 aa)
GDPGP1GDP-D-glucose phosphorylase 1; Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells (385 aa)
ARFRP1ADP-ribosylation factor-related protein 1; Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver; ARF GTPase family (201 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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