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STRINGSTRING
NU NU HC3 HC3 PSMB4 PSMB4 PSMA7 PSMA7 PSMB3 PSMB3 PSMA8 PSMA8 PSMB2 PSMB2 PSMA2 PSMA2 PSMA5 PSMA5 PSMA1 PSMA1 TERF1 TERF1 UBC UBC PRPS2 PRPS2 RPIA RPIA TKT TKT PRPSAP1 PRPSAP1 UMPS UMPS PRPS1L1 PRPS1L1 PRPSAP2 PRPSAP2 TKTL2 TKTL2 PGM2 PGM2 PGM1 PGM1 PPAT PPAT NUDT5 NUDT5 ADPRM ADPRM NUDT9 NUDT9
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 protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
PSMA2proteasome (prosome, macropain) subunit, alpha 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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation (234 aa)
PSMB3proteasome (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)
UMPSuridine monophosphate synthetase (480 aa)
PPATphosphoribosyl pyrophosphate amidotransferase (517 aa)
PRPSAP2phosphoribosyl pyrophosphate synthetase-associated protein 2; Seems to play a negative regulatory role in 5- phosphoribose 1-diphosphate synthesis (369 aa)
PSMA5proteasome (prosome, macropain) subunit, alpha type, 5; 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)
TERF1telomeric repeat binding factor (NIMA-interacting) 1; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double- stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair [...] (439 aa)
TKTL2transketolase-like 2; Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis (626 aa)
RPIAribose 5-phosphate isomerase A (311 aa)
PSMB4proteasome (prosome, macropain) subunit, beta 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. Mediates the lipopolysaccharide-induced signal macrophage proteasome (By similarity). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (264 aa)
NUDT9nudix (nucleoside diphosphate linked moiety X)-type motif 9; Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5’- phosphate (350 aa)
PSMA8proteasome (prosome, macropain) subunit, alpha type, 8; 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). This may be a testis-specific subunit (256 aa)
UBCubiquitin C (685 aa)
PSMA7proteasome (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)
PGM1phosphoglucomutase 1 (580 aa)
PSMB2proteasome (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)
ADPRMADP-ribose/CDP-alcohol diphosphatase, manganese-dependent; Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP- choline and CDP-ethanolamine, but not other non-reducing ADP- sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity) (342 aa)
PGM2phosphoglucomutase 2; Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity (612 aa)
PRPS2phosphoribosyl pyrophosphate synthetase 2; Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis (321 aa)
TKTtransketolase; Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (623 aa)
PSMA1proteasome (prosome, macropain) subunit, alpha 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. Mediates the lipopolysaccharide-induced signal transduction in the macrophage proteasome (By similarity). Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity) (269 aa)
PRPSAP1phosphoribosyl pyrophosphate synthetase-associated protein 1; Seems to play a negative regulatory role in 5- phosphoribose 1-diphosphate synthesis (385 aa)
NUDT5nudix (nucleoside diphosphate linked moiety X)-type motif 5; Hydrolyzes with similar activities ADP-ribose ADP- mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (219 aa)
PRPS1L1phosphoribosyl pyrophosphate synthetase 1-like 1; Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis (318 aa)
HC3Proteasome subunit alpha 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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation (234 aa)
NUproteasome subunit alpha type-1 isoform 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 (By similarity) (164 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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