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 nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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 | HBQ1 | hemoglobin, theta 1 (142 aa) | ||
 | DMC1 | DMC1 dosage suppressor of mck1 homolog, meiosis-specific homologous recombination (yeast); May participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks (By similarity) (340 aa) | ||
 | AANAT | aralkylamine N-acetyltransferase; Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N- acetylserotonin, the penultimate step in the synthesis of melatonin (252 aa) | ||
 | HBA2 | hemoglobin, alpha 2 (142 aa) | ||
 | HBZ | hemoglobin, zeta; The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac (142 aa) | ||
 | DMWD | dystrophia myotonica, WD repeat containing; Could have a regulatory function in meiosis (674 aa) | ||
 | HBE1 | hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin (147 aa) | ||
 | CYGB | cytoglobin; May have a protective function during conditions of oxidative stress. May be involved in intracellular oxygen storage or transfer (190 aa) | ||
 | 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) | ||
 | 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) | ||
 | HBA1 | hemoglobin, alpha 1; Involved in oxygen transport from the lung to the various peripheral tissues (By similarity) (142 aa) | ||
 | HBG1 | hemoglobin, gamma A; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains (147 aa) | ||
 | HBB | hemoglobin, beta (147 aa) | ||
 | HBG2 | hemoglobin, gamma G; Gamma chains make up the fetal hemoglobin F, in combination with alpha chains (147 aa) | ||
 | PUM2 | pumilio homolog 2 (Drosophila); Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3’-UTR of mRNA targets. Its interactions and tissue specificity suggest that it may be required to support proliferation and self-renewal of stem cells by regulating the translation of key transcripts (1064 aa) | ||
 | MAFK | v-maf musculoaponeurotic fibrosarcoma oncogene homolog K (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 (156 aa) | ||
 | 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) | ||
 | HP | haptoglobin; 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) | ||
 | HBM | hemoglobin, mu (141 aa) | ||
 | 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) | ||
 | CYB5R3 | cytochrome b5 reductase 3 (334 aa) | ||
 | SMC3 | structural maintenance of chromosomes 3; Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex plays also an important role in spindle pole assembly during mitosis and in chromosomes movement (1217 aa) | ||
 | HBD | hemoglobin, delta; Involved in oxygen transport from the lung to the various peripheral tissues (147 aa) | ||
 | RAD51 | RAD51 homolog (S. cerevisiae); Participates in a common DNA damage response pathway associated with the activation of homologous recombination and double-strand break repair. Binds to single and double stranded DNA and exhibits DNA-dependent ATPase activity. Underwinds duplex DNA and forms helical nucleoprotein filaments. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (340 aa) | ||
 | PUM1 | pumilio homolog 1 (Drosophila); Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3’-UTR of mRNA targets. May be required to support proliferation and self-renewal of stem cells (By similarity) (1188 aa) | ||
 | HPR | haptoglobin-related protein (348 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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