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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 | RELB | v-rel reticuloendotheliosis viral oncogene homolog B; NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF- kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they [...] (579 aa) | ||
 | NFKB1 | nuclear factor of kappa light polypeptide gene enhancer in B-cells 1; NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to b [...] (969 aa) | ||
 | XPO7 | exportin 7; Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. XPO7 then return to the nuclear compartment and mediate ano [...] (1087 aa) | ||
 | COMMD9 | COMM domain containing 9 (198 aa) | ||
 | COMMD4 | COMM domain containing 4; Down-regulates activation of NF-kappa-B (199 aa) | ||
 | COMMD10 | COMM domain containing 10 (202 aa) | ||
 | COMMD7 | COMM domain containing 7; Associates with the NF-kappa-B complex and suppresses its transcriptional activity (200 aa) | ||
 | COMMD5 | COMM domain containing 5; Down-regulates activation of NF-kappa-B (224 aa) | ||
 | COMMD6 | COMM domain containing 6; Down-regulates activation of NF-kappa-B. Inhibits TNF- induced NFKB1 activation (98 aa) | ||
 | AKR7A3 | aldo-keto reductase family 7, member A3 (aflatoxin aldehyde reductase); Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity) (331 aa) | ||
 | CCDC22 | coiled-coil domain containing 22 (627 aa) | ||
 | CCDC93 | coiled-coil domain containing 93 (631 aa) | ||
 | COMMD3 | COMM domain containing 3; May down-regulate activation of NF-kappa-B (195 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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