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STRINGSTRING
HBM HBM HBG2 HBG2 HBB HBB HBZ HBZ HBD HBD CYB5R3 CYB5R3 HBA2 HBA2 HBE1 HBE1 HBA1 HBA1 HBG1 HBG1 HBQ1 HBQ1 AHSP AHSP TMEM165 TMEM165 FKBP1A FKBP1A ZC3H12A ZC3H12A UBE3A UBE3A
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:
HBQ1hemoglobin, theta 1 (142 aa)
HBA2hemoglobin, alpha 2 (142 aa)
HBZhemoglobin, zeta; The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac (142 aa)
HBE1hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin (147 aa)
AHSPalpha hemoglobin stabilizing protein; Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia (102 aa)
HBA1hemoglobin, alpha 1; Involved in oxygen transport from the lung to the various peripheral tissues (By similarity) (142 aa)
HBG1hemoglobin, gamma A; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains (147 aa)
HBBhemoglobin, beta (147 aa)
HBG2hemoglobin, gamma G; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains (147 aa)
HBMhemoglobin, mu (141 aa)
CYB5R3cytochrome b5 reductase 3 (334 aa)
ZC3H12Azinc finger CCCH-type containing 12A; Has RNase activity and selectively degrades specific target mRNA species. Modulates the immune response and inflammation by regulating the decay of specific mRNA molecules. Recognizes the 3’-untranslated region (UTR) of the mRNA for IL6, CALCR and IL12B. Required for normal decay of IL6 mRNA (By similarity). Triggers apoptosis and promotes angiogenesis in response to the binding of CCL2 to CCR2. Regulates expression of CDH12 and CHD19 (599 aa)
HBDhemoglobin, delta; Involved in oxygen transport from the lung to the various peripheral tissues (147 aa)
TMEM165transmembrane protein 165 (324 aa)
FKBP1AFK506 binding protein 1A, 12kDa; Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (108 aa)
UBE3Aubiquitin protein ligase E3A (875 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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