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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Neighborhood |
Gene Fusion |
Cooccurence |
Coexpression |
Experiments |
Databases |
Textmining |
[Homology] |
Score |
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 | TMEM9B | TMEM9 domain family, member B (198 aa) | ||||||||||||
Predicted Functional Partners:
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 | UBC | ubiquitin C (685 aa) |
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0.795 | ||||||||||
 | CLPTM1 | cleft lip and palate associated transmembrane protein 1; May play a role in T-cell development (By similarity) (669 aa) |
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0.637 | ||||||||||
 | EHD1 | EH-domain containing 1; Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (534 aa) |
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0.517 | ||||||||||
 | EHD3 | EH-domain containing 3; Plays a role in endocytic transport (535 aa) |
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0.473 | ||||||||||
 | EHD2 | EH-domain containing 2; Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for normal fusion of myoblasts to skeletal muscle myotubes. Binds ATP; does not bind GTP (By similarity) (543 aa) |
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0.454 | ||||||||||
 | CLPTM1L | CLPTM1-like; Enhances cisplatin-mediated apoptosis, when overexpressed (538 aa) |
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0.442 | ||||||||||
 | RIPK3 | receptor-interacting serine-threonine kinase 3; Essential for programmed necrosis in response to death- inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 to form a necrosis- inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes- GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity) (518 aa) |
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0.434 | ||||||||||
 | NUTF2 | nuclear transport factor 2; Facilitates protein transport into the nucleus. Interacts with the nucleoporin p62 and with Ran. Acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (127 aa) |
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0.427 | ||||||||||
 | NFU1 | NFU1 iron-sulfur cluster scaffold homolog (S. cerevisiae); Iron-sulfur cluster scaffold protein which can assemble [4Fe-2S] clusters and deliver them to target proteins (254 aa) |
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0.426 | ||||||||||
 | PEX19 | peroxisomal biogenesis factor 19; Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53 (299 aa) |
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0.411 | ||||||||||
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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