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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 | PSMA4 | proteasome (prosome, macropain) subunit, alpha type, 4; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity) (261 aa) | ||
 | P4HA2 | prolyl 4-hydroxylase, alpha polypeptide II; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (535 aa) | ||
 | PYCRL | pyrroline-5-carboxylate reductase-like (286 aa) | ||
 | PSMB3 | proteasome (prosome, macropain) subunit, beta type, 3; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (205 aa) | ||
 | LAP3 | leucine aminopeptidase 3; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides (519 aa) | ||
 | L3HYPDH | L-3-hydroxyproline dehydratase (trans-); Catalyzes the dehydration of trans-3-hydroxy-L-proline to delta-1-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it (354 aa) | ||
 | PSMA6 | proteasome (prosome, macropain) subunit, alpha type, 6; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity) (246 aa) | ||
 | PSMB1 | proteasome (prosome, macropain) subunit, beta type, 1; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity) (241 aa) | ||
 | DGCR8 | DiGeorge syndrome critical region gene 8 (773 aa) | ||
 | P4HA1 | prolyl 4-hydroxylase, alpha polypeptide I; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (534 aa) | ||
 | CDKN2B | cyclin-dependent kinase inhibitor 2B (p15, inhibits CDK4); Interacts strongly with CDK4 and CDK6. Potent inhibitor. Potential effector of TGF-beta induced cell cycle arrest (138 aa) | ||
 | GPD1L | glycerol-3-phosphate dehydrogenase 1-like; Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3-phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L (351 aa) | ||
 | ALDH4A1 | aldehyde dehydrogenase 4 family, member A1 (563 aa) | ||
 | PYCR1 | pyrroline-5-carboxylate reductase 1; Housekeeping enzyme that catalyzes the last step in proline biosynthesis. Can utilize both NAD and NADP, but has higher affinity for NAD. Involved in the cellular response to oxidative stress (319 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) | ||
 | P4HA3 | prolyl 4-hydroxylase, alpha polypeptide III; Catalyzes the post-translational formation of 4- hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins (544 aa) | ||
 | PYCR2 | pyrroline-5-carboxylate reductase family, member 2; Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP(+). Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH (320 aa) | ||
 | SNX11 | sorting nexin 11; May be involved in several stages of intracellular trafficking (By similarity) (270 aa) | ||
 | BABAM1 | BRISC and BRCA1 A complex member 1; Component of the BRCA1-A complex, a complex that specifically recognizes ’Lys-63’-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes ’Lys-63’-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Probably also plays a role as a component of the BRISC complex, a multiprote [...] (329 aa) | ||
 | ULK2 | unc-51-like kinase 2 (C. elegans); Serine/threonine-protein kinase involved in autophagy in response to starvation. Acts upstream of phosphatidylinositol 3- kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes. Part of regulatory feedback loops in autophagy- acts both as a downstream effector and a negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR. Activated via phosphorylation by AMPK, also acts as a negative regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1, PRKAB2 and PRKAG1. [...] (1036 aa) | ||
 | PSMB5 | proteasome (prosome, macropain) subunit, beta type, 5 (263 aa) | ||
 | PCMT1 | protein-L-isoaspartate (D-aspartate) O-methyltransferase (285 aa) | ||
 | PSMA7 | proteasome (prosome, macropain) subunit, alpha type, 7; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Plays an important role in the regulation of cell proliferation or cell cycle control, transcriptional regulation, immune and stress response, cell differentiation, and apoptosis. Interacts with some important proteins involved in transcription factor regulation, cell cy [...] (248 aa) | ||
 | PSMB2 | proteasome (prosome, macropain) subunit, beta type, 2; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit has a trypsin-like activity (201 aa) | ||
 | UIMC1 | ubiquitin interaction motif containing 1 (719 aa) | ||
 | P5CR2 | Uncharacterized protein (359 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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