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STRINGSTRING
SURF4 SURF4 ATP8A2 ATP8A2 ATP9B ATP9B ATP8A1 ATP8A1 ATP8B3 ATP8B3 SCAMP3 SCAMP3 JAGN1 JAGN1 SEC61A1 SEC61A1 SCAMP5 SCAMP5 ATP2B2 ATP2B2 TECR TECR CEPT1 CEPT1 ATP8B1 ATP8B1 DDOST DDOST OSTC OSTC EPT1 EPT1 CHPT1 CHPT1 ATP2B3 ATP2B3 VDAC2 VDAC2 SLC35F5 SLC35F5 ATP2B1 ATP2B1 SCAMP2 SCAMP2 SCAMP4 SCAMP4 VDAC3 VDAC3 ATP2B4 ATP2B4 ATP9A ATP9A
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:
TECRtrans-2,3-enoyl-CoA reductase; Reduces trans-2,3-stearoyl-CoA to stearoyl-CoA of long and very long chain fatty acids (308 aa)
CHPT1choline phosphotransferase 1 (406 aa)
SEC61A1Sec61 alpha 1 subunit (S. cerevisiae) (476 aa)
SLC35F5solute carrier family 35, member F5; Putative solute transporter (Potential) (523 aa)
EPT1ethanolaminephosphotransferase 1 (CDP-ethanolamine-specific); Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via ’Kennedy’ pathway (397 aa)
ATP2B1ATPase, Ca++ transporting, plasma membrane 1; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (1220 aa)
ATP2B3ATPase, Ca++ transporting, plasma membrane 3 (1220 aa)
SCAMP2secretory carrier membrane protein 2; Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface (329 aa)
ATP8B1ATPase, aminophospholipid transporter, class I, type 8B, member 1; May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both (1251 aa)
JAGN1jagunal homolog 1 (Drosophila); May be required for endoplasmic reticulum organization (By similarity) (183 aa)
SCAMP3secretory carrier membrane protein 3; Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface (347 aa)
ATP8B3ATPase, aminophospholipid transporter, class I, type 8B, member 3 (1300 aa)
SCAMP4secretory carrier membrane protein 4; Probably involved in membrane protein trafficking (By similarity) (229 aa)
ATP2B2ATPase, Ca++ transporting, plasma membrane 2; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (1243 aa)
ATP9AATPase, class II, type 9A (1047 aa)
CEPT1choline/ethanolamine phosphotransferase 1; Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity (416 aa)
ATP2B4ATPase, Ca++ transporting, plasma membrane 4; This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (1205 aa)
OSTColigosaccharyltransferase complex subunit (149 aa)
SCAMP5secretory carrier membrane protein 5; Required for the calcium-dependent exocytosis of signal sequence-containing cytokines such as CCL5. Probably acts in cooperation with the SNARE machinery. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) in case of endoplasmic reticulum stress by inhibiting the endocytosis pathway (235 aa)
SURF4surfeit 4; May play a role in the maintenance of the architecture of the endoplasmic reticulum-Golgi intermediate compartment and of the Golgi (269 aa)
VDAC2voltage-dependent anion channel 2; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules. The channel adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation- selective (309 aa)
DDOSTdolichyl-diphosphooligosaccharide--protein glycosyltransferase; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (456 aa)
ATP8A2ATPase, aminophospholipid transporter, class I, type 8A, member 2 (1188 aa)
ATP8A1ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1; May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles (1164 aa)
ATP9BATPase, class II, type 9B (1147 aa)
VDAC3voltage-dependent anion channel 3; Forms a channel through the mitochondrial outer membrane that allows diffusion of small hydrophilic molecules (By similarity) (284 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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