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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 | AHCY | adenosylhomocysteinase; Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine (432 aa) | ||
 | BET1 | blocked early in transport 1 homolog (S. cerevisiae); Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane (By similarity) (118 aa) | ||
 | GOSR2 | golgi SNAP receptor complex member 2; Involved in transport of proteins from the cis/medial- Golgi to the trans-Golgi network (213 aa) | ||
 | SYS1 | SYS1 Golgi-localized integral membrane protein homolog (S. cerevisiae); Involved in protein trafficking. May serve as a receptor for ARFRP1 (156 aa) | ||
 | LRRK2 | leucine-rich repeat kinase 2; May play a role in the phosphorylation of proteins central to Parkinson disease. Phosphorylates PRDX3. May also have GTPase activity. Positively regulates autophagy through a calcium- dependent activation of the CaMKK/AMPK signaling pathway. The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (2527 aa) | ||
 | YWHAB | tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide; Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in bloc [...] (246 aa) | ||
 | AHCYL2 | adenosylhomocysteinase-like 2 (611 aa) | ||
 | COPG1 | coatomer protein complex, subunit gamma 1; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; t [...] (874 aa) | ||
 | COPB2 | coatomer protein complex, subunit beta 2 (beta prime); The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding [...] (906 aa) | ||
 | RIPK4 | receptor-interacting serine-threonine kinase 4; Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation (784 aa) | ||
 | UBC | ubiquitin C (685 aa) | ||
 | DDX46 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 46; Plays an essential role in splicing, either prior to, or during splicing A complex formation (1031 aa) | ||
 | SYNJ2 | synaptojanin 2; Inositol 5-phosphatase which may be involved in distinct membrane trafficking and signal transduction pathways. May mediate the inhibitory effect of Rac1 on endocytosis (1496 aa) | ||
 | SH3YL1 | SH3 domain containing, Ysc84-like 1 (S. cerevisiae) (342 aa) | ||
 | COPA | coatomer protein complex, subunit alpha; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the [...] (1233 aa) | ||
 | AHCYL1 | adenosylhomocysteinase-like 1 (530 aa) | ||
 | BET1L | blocked early in transport 1 homolog (S. cerevisiae)-like; Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex (By similarity) (111 aa) | ||
 | DDX42 | DEAD (Asp-Glu-Ala-Asp) box polypeptide 42; ATP-dependent RNA helicase. Binds to partially double- stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity- ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and [...] (938 aa) | ||
 | AGAP3 | ArfGAP with GTPase domain, ankyrin repeat and PH domain 3; GTPase-activating protein for the ADP ribosylation factor family (Potential). GTPase which may be involved in the degradation of expanded polyglutamine proteins through the ubiquitin-proteasome pathway (911 aa) | ||
 | COPG2 | coatomer protein complex, subunit gamma 2 (246 aa) | ||
 | ZDHHC13 | zinc finger, DHHC-type containing 13; Palmitoyltransferase for HD and GAD2 (By similarity). Mediates Mg(2+) transport (By similarity) (622 aa) | ||
 | ZDHHC17 | zinc finger, DHHC-type containing 17; Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD. Palmitoylates MPP1 in erythrocytes. May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. Has transforming activity. Mediates Mg(2+) transport (632 aa) | ||
 | SYNJ1 | synaptojanin 1; Inositol 5-phosphatase which has a role in clathrin- mediated endocytosis (1612 aa) | ||
 | KIAA1432 | KIAA1432 (1423 aa) | ||
 | USO1 | USO1 vesicle docking protein homolog (yeast); General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity (By similarity) (971 aa) | ||
 | ENSG00000262633 | Golgi SNAP receptor complex member 2; Uncharacterized protein (232 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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