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STRINGSTRING
HP protein (human) - STRING interaction network
"HP" - Haptoglobin in Homo sapiens
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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
HPHaptoglobin; As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation [...] (406 aa)    
Predicted Functional Partners:
HBB
Hemoglobin subunit beta; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family (147 aa)
     
  0.993
CD163
Scavenger receptor cysteine-rich type 1 protein M130; Acute phase-regulated receptor involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Exhibits a higher affinity for complexes of hemoglobin and multimeric haptoglobin of HP*1F phenotype than for complexes of [...] (1156 aa)
     
  0.988
APOA1
Apolipoprotein A-I; Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility; Apolipoproteins (267 aa)
     
  0.979
HBA1
Hemoglobin subunit alpha; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family (142 aa)
     
  0.977
HBA2
Hemoglobin subunit alpha 2; Involved in oxygen transport from the lung to the various peripheral tissues; Hemoglobin subunits (142 aa)
     
  0.976
ORM1
Alpha-1-acid glycoprotein 1; Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction; Belongs to the calycin superfamily. Lipocalin family (201 aa)
     
 
  0.976
ORM2
Alpha-1-acid glycoprotein 2; Functions as transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta- barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction; Lipocalins (201 aa)
     
 
  0.968
LRG1
Leucine rich alpha-2-glycoprotein 1 (347 aa)
     
  0.959
LTF
Lactotransferrin; Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors; Transferrins (710 aa)
     
  0.953
APOE
Apolipoprotein E; Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues; Apolipoproteins (317 aa)
     
  0.953
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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