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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Your Input:
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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) | ||
 | JUND | jun D proto-oncogene; Transcription factor binding AP-1 sites (347 aa) | ||
 | HBZ | hemoglobin, zeta; The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin, synthesized primarily in the yolk sac (142 aa) | ||
 | HBE1 | hemoglobin, epsilon 1; The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin (147 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) | ||
 | HNRNPD | heterogeneous nuclear ribonucleoprotein D (AU-rich element RNA binding protein 1, 37kDa) (355 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) | ||
 | SP1 | Sp1 transcription factor; Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR- alpha G-box promoter. May have a role in modulating the cellular response to DNA d [...] (785 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) | ||
 | UPF2 | UPF2 regulator of nonsense transcripts homolog (yeast) (1272 aa) | ||
 | HBM | hemoglobin, mu (141 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) | ||
 | IKBKG | inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma; Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either ’Lys-63’- linked or linear polyubiquitin) and its functional importance is reported conflictingly. Als [...] (487 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) | ||
 | RAD51B | RAD51 homolog B (S. cerevisiae) (384 aa) | ||
 | RAD51D | RAD51 homolog D (S. cerevisiae) (348 aa) | ||
 | ENSG00000267618 | Uncharacterized protein (272 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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