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LEPREL2 LEPREL2 C4A C4A IL32 IL32 C2 C2 C4B C4B ATP12A ATP12A C1R C1R C1S C1S SERPING1 SERPING1 C1QB C1QB HRG HRG C1QC C1QC C1QA C1QA METAP2 METAP2 PTX3 PTX3 CRP CRP MYOC MYOC FN1 FN1 CALR CALR C6orf120 C6orf120 USP30 USP30 VHL VHL COL4A2 COL4A2 LEPREL4 LEPREL4 DEFA1 DEFA1
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:
MYOCmyocilin, trabecular meshwork inducible glucocorticoid response; May participate in the obstruction of fluid outflow in the trabecular meshwork (504 aa)
ATP12AATPase, H+/K+ transporting, nongastric, alpha polypeptide; Catalyzes the hydrolysis of ATP coupled with the exchange of H(+) and K(+) ions across the plasma membrane. Responsible for potassium absorption in various tissues (1045 aa)
HRGhistidine-rich glycoprotein; Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell [...] (525 aa)
CRPC-reactive protein, pentraxin-related; Displays several functions associated with host defense- it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells (224 aa)
VHLvon Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase; Involved in the ubiquitination and subsequent proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Seems to act as target recruitment subunit in the E3 ubiquitin ligase complex and recruits hydroxylated hypoxia- inducible factor (HIF) under normoxic conditions. Involved in transcriptional repression through interaction with HIF1A, HIF1AN and histone deacetylases. Ubiquitinates, in an oxygen-responsive manner, ADRB2 (213 aa)
USP30ubiquitin specific peptidase 30; May participate in the maintenance of mitochondrial morphology (517 aa)
SERPING1serpin peptidase inhibitor, clade G (C1 inhibitor), member 1 (500 aa)
C1Rcomplement component 1, r subcomponent (668 aa)
PTX3pentraxin 3, long; Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self- components and female fertility (By similarity) (381 aa)
C2complement component 2 (752 aa)
C1QBcomplement component 1, q subcomponent, B chain; C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes (253 aa)
CALRcalreticulin; Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity) (417 aa)
IL32interleukin 32 (188 aa)
METAP2methionyl aminopeptidase 2; Removes the N-terminal methionine from nascent proteins. The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo (478 aa)
C1Scomplement component 1, s subcomponent (688 aa)
FN1fibronectin 1 (2477 aa)
C6orf120chromosome 6 open reading frame 120; May be involved in induction of apoptosis in CD4(+) T- cells, but not CD8(+) T-cells or hepatocytes (191 aa)
LEPREL4leprecan-like 4 (437 aa)
COL4A2collagen, type IV, alpha 2; Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a ’chicken-wire’ meshwork together with laminins, proteoglycans and entactin/nidogen (1712 aa)
C1QCcomplement component 1, q subcomponent, C chain; C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes (245 aa)
C1QAcomplement component 1, q subcomponent, A chain; C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes (245 aa)
DEFA1defensin, alpha 1 (94 aa)
LEPREL2leprecan-like 2; Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V (By similarity) (735 aa)
C4Acomplement component 4A (Rodgers blood group) (1744 aa)
C4Bcomplement component 4B (Chido blood group) (1744 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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