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NUP210 NUP210 UGGT2 UGGT2 PLOD2 PLOD2 GLT25D1 GLT25D1 FOXRED2 FOXRED2 RPN1 RPN1 SERPINH1 SERPINH1 HSP90B1 HSP90B1 PPIB PPIB EGLN2 EGLN2 OS9 OS9 HSPA5 HSPA5 EGLN1 EGLN1 SEL1L SEL1L BSG BSG HIF1A HIF1A VCP VCP UBE2J1 UBE2J1 USP33 USP33 DERL2 DERL2 SERPINA1 SERPINA1 SYVN1 SYVN1 SPATA5 SPATA5 SEL1L2 SEL1L2
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
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DERL2derlin 2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation (239 aa)
FOXRED2FAD-dependent oxidoreductase domain containing 2; Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation (684 aa)
GLT25D1glycosyltransferase 25 domain containing 1; Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues of collagen (622 aa)
NUP210nucleoporin 210kDa; Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity (1887 aa)
SPATA5spermatogenesis associated 5; May be involved in morphological and functional mitochondrial transformations during spermatogenesis (By similarity) (893 aa)
PLOD2procollagen-lysine, 2-oxoglutarate 5-dioxygenase 2; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (758 aa)
SEL1L2sel-1 suppressor of lin-12-like 2 (C. elegans) (688 aa)
RPN1ribophorin I; 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 (607 aa)
HSP90B1heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (803 aa)
PPIBpeptidylprolyl isomerase B (cyclophilin B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (216 aa)
EGLN2egl nine homolog 2 (C. elegans); Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF2A. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation [...] (407 aa)
OS9osteosarcoma amplified 9, endoplasmic reticulum lectin (667 aa)
HSPA5heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER (654 aa)
BSGbasigin (Ok blood group); Plays pivotal roles in spermatogenesis, embryo implantation, neural network formation and tumor progression. Stimulates adjacent fibroblasts to produce matrix metalloproteinases (MMPS). May target monocarboxylate transporters SLC16A1, SLC16A3 and SLC16A8 to plasma membranes of retinal pigment epithelium and neural retina. Seems to be a receptor for oligomannosidic glycans. In vitro, promotes outgrowth of astrocytic processes (By similarity) (385 aa)
SEL1Lsel-1 suppressor of lin-12-like (C. elegans); May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (794 aa)
HIF1Ahypoxia inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor); Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to [...] (826 aa)
SERPINA1serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 (418 aa)
USP33ubiquitin specific peptidase 33; Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube [...] (942 aa)
SERPINH1serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1); Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen (418 aa)
VCPvalosin containing protein; Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the e [...] (806 aa)
EGLN1egl nine homolog 1 (C. elegans); Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation [...] (426 aa)
UGGT2UDP-glucose glycoprotein glucosyltransferase 2; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity) (1516 aa)
SYVN1synovial apoptosis inhibitor 1, synoviolin; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons f [...] (617 aa)
UBE2J1ubiquitin-conjugating enzyme E2, J1 (318 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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