STRINGSTRING
psmD8-1 psmD8-1 ubqD ubqD ubqF ubqF ubqG ubqG ubqI ubqI ubqH ubqH ubqJ ubqJ ubqB ubqB ubqC ubqC psmA4 psmA4 psmA7 psmA7 psmC4 psmC4 psmC5 psmC5 psmD3 psmD3 psmA1 psmA1 psmA3 psmA3 psmD2 psmD2 psmB5 psmB5 ubqO ubqO PsmE4 PsmE4 psmA2 psmA2 DDB0219336 DDB0219336 psmD1 psmD1 psmD13 psmD13 psmC6 psmC6 psmC3 psmC3 psmB7 psmB7 PsmF1 PsmF1 DDB0204791 DDB0204791 psmD11 psmD11 psmD12 psmD12 psmD7 psmD7 psmA6 psmA6 psmD9 psmD9 psmD4 psmD4 smg1 smg1 psmB4-1 psmB4-1 DDB0217054 DDB0217054 psmC1 psmC1 psmD6 psmD6 psmB3 psmB3 psmB2 psmB2 psmA5 psmA5 psmB6 psmB6 psmD14 psmD14 psmC2 psmC2 psmE3 psmE3
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 Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
psmD8-1Probable 26S proteasome non-ATPase regulatory subunit 8; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (263 aa)
ubqDPolyubiquitin-D; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (229 aa)
ubqFPolyubiquitin-F; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (533 aa)
ubqGPolyubiquitin-G; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (381 aa)
ubqIPolyubiquitin-I; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (305 aa)
ubqHPolyubiquitin-H; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (381 aa)
ubqJPolyubiquitin-J; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradat [...] (305 aa)
ubqBUbiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...] (128 aa)
ubqCUbiquitin-40S ribosomal protein S27a; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involve [...] (154 aa)
psmA4Proteasome 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; Belongs to the peptidase T1A family. (250 aa)
psmA7Proteasome 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; Belongs to the peptidase T1A family. (250 aa)
psmC426S proteasome regulatory subunit 6B homolog; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). (403 aa)
psmC526S proteasome regulatory subunit 8; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). (403 aa)
psmD326S proteasome non-ATPase regulatory subunit 3; Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (504 aa)
psmA1Proteasome 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; Belongs to the peptidase T1A family. (248 aa)
psmA3Proteasome subunit alpha 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; Belongs to the peptidase T1A family. (248 aa)
psmD226S proteasome non-ATPase regulatory subunit 2; Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (893 aa)
psmB5Proteasome subunit beta 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); Belongs to the peptidase T1B family. (272 aa)
ubqOUbiquitin-like domain-containing protein. (77 aa)
PsmE4Uncharacterized protein. (1905 aa)
psmA2Proteasome 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 (By similarity); Belongs to the peptidase T1A family. (232 aa)
DDB0219336Uncharacterized protein. (970 aa)
psmD126S proteasome non-ATPase regulatory subunit 1; Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (975 aa)
psmD1326S proteasome non-ATPase regulatory subunit 13; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (385 aa)
psmC626S proteasome regulatory subunit 10B; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). (393 aa)
psmC326S proteasome regulatory subunit 6A homolog; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). (421 aa)
psmB7Proteasome subunit beta 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 (By similarity); Belongs to the peptidase T1B family. (266 aa)
PsmF1Uncharacterized protein. (326 aa)
DDB0204791ANK_REP_REGION domain-containing protein. (311 aa)
psmD1126S proteasome non-ATPase regulatory subunit 11; Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, psmD11 is required for proteasome assembly (By similarity); Belongs to the proteasome subunit S9 family. (413 aa)
psmD1226S proteasome non-ATPase regulatory subunit 12; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (447 aa)
psmD726S proteasome non-ATPase regulatory subunit 7; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (325 aa)
psmA6Proteasome 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); Belongs to the peptidase T1A family. (250 aa)
psmD9Probable 26S proteasome non-ATPase regulatory subunit 9; Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC). (262 aa)
psmD426S proteasome non-ATPase regulatory subunit 4; Binds and presumably selects ubiquitin-conjugates for destruction; Belongs to the proteasome subunit S5A family. (349 aa)
smg1Probable serine/threonine-protein kinase smg1; Serine/threonine protein kinase involved in mRNA surveillance. Recognizes the substrate consensus sequence [ST]-Q. Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating upf1 (By similarity). (2344 aa)
psmB4-1Proteasome 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 (By similarity); Belongs to the peptidase T1B family. (259 aa)
DDB0217054Uncharacterized protein. (559 aa)
psmC126S proteasome regulatory subunit 4 homolog; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). Plays an important role in regulating both growth and multicellular development. (439 aa)
psmD626S proteasome non-ATPase regulatory subunit 6; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. (382 aa)
psmB3Proteasome 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 (By similarity); Belongs to the peptidase T1B family. (205 aa)
psmB2Proteasome 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 chymotrypsin-like activity (By similarity). Belongs to the peptidase T1B family. (198 aa)
psmA5Proteasome 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); Belongs to the peptidase T1A family. (241 aa)
psmB6Proteasome subunit beta 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. (214 aa)
psmD1426S proteasome non-ATPase regulatory subunit 14; Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear (By similarity). Belongs to the peptidase M67A family. PSMD14 subfamily. (306 aa)
psmC226S proteasome regulatory subunit 7; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). (428 aa)
psmE3Proteasome activator 28; Subunit of the 11S REG (also called PA28) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates preferentially the trypsin-like catalytic subunit of the proteasome. May also be involved in cell cycle regulation. (225 aa)
Your Current Organism:
Dictyostelium discoideum
NCBI taxonomy Id: 44689
Other names: D. discoideum
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.