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MAFF MAFF MAFG MAFG NFE2 NFE2 HBB HBB HBE1 HBE1 HBG2 HBG2 HBD HBD HBZ HBZ AHSP AHSP HBA2 HBA2 HBA1 HBA1
"HBE1" - hemoglobin, epsilon 1 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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
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colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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Known Interactions
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from curated databases
experiment edge
experimentally determined
Predicted Interactions
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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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[Homology]
Score
HBE1hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin (147 aa)    
Predicted Functional Partners:
HBA1
hemoglobin, alpha 1; Involved in oxygen transport from the lung to the various peripheral tissues (By similarity) (142 aa)
      score_image score_image score_image score_image score_image 0.928
HBA2
hemoglobin, alpha 2 (142 aa)
      score_image score_image score_image score_image score_image 0.927
NFE2
nuclear factor (erythroid-derived 2), 45kDa; Component of the NF-E2 complex essential for regulating erythroid and megakaryocytic maturation and differentiation. Binds to the hypersensitive site 2 (HS2) of the beta-globin control region (LCR). This subunit (NFE2) recognizes the TCAT/C sequence of the AP-1-like core palindrome present in a number of erythroid and megakaryocytic gene promoters. Requires MAFK or other small MAF proteins for binding to the NF-E2 motif. May play a role in all aspects of hemoglobin production from globin and heme synthesis to procurement of iron (373 aa)
          score_image score_image   0.921
HBZ
hemoglobin, zeta; The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac (142 aa)
      score_image score_image score_image score_image score_image 0.919
AHSP
alpha 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)
          score_image score_image   0.907
HBG2
hemoglobin, gamma G; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains (147 aa)
      score_image   score_image score_image score_image 0.904
MAFG
v-maf musculoaponeurotic fibrosarcoma oncogene homolog G (avian); Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NF- E2. Activates glob [...] (162 aa)
          score_image score_image   0.902
HBD
hemoglobin, delta; Involved in oxygen transport from the lung to the various peripheral tissues (147 aa)
          score_image score_image score_image 0.901
HBB
hemoglobin, beta (147 aa)
          score_image score_image score_image 0.901
MAFF
v-maf musculoaponeurotic fibrosarcoma oncogene homolog F (avian); Interacts with the upstream promoter region of the oxytocin receptor gene. May be a transcriptional enhancer in the up-regulation of the oxytocin receptor gene at parturition. Since it lacks a putative transactivation domain, it may behave as a transcriptional repressor when it dimerize among himself. May also serve as a transcriptional activator by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. May be involved in the cellular stress response (164 aa)
          score_image score_image   0.901
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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