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PSME3 PSME3 PSMD1 PSMD1 PSMC3 PSMC3 PSMA8 PSMA8 PSMC5 PSMC5 PSMD2 PSMD2 PSMD6 PSMD6 PSMB4 PSMB4 PSMB6 PSMB6 PSMC2 PSMC2 PSMA5 PSMA5 SEC61G SEC61G RPS11 RPS11 RPN1 RPN1 RPN2 RPN2 SEC62 SEC62 SEC11A SEC11A SSR2 SSR2 RPS15A RPS15A DDOST DDOST SRP14 SRP14 RPS23 RPS23 RPLP2 RPLP2 RPS14 RPS14 SRP9 SRP9 SRP68 SRP68
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:
RPN2ribophorin II; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (631 aa)
SRP14signal recognition particle 14kDa (homologous Alu RNA binding protein); Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (136 aa)
SEC11ASEC11 homolog A (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity) (179 aa)
PSMB6proteasome (prosome, macropain) 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. This unit is responsible of the peptidyl glutamyl-like activity. May catalyze basal processing of intracellular antigens (239 aa)
RPS11ribosomal protein S11 (158 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)
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)
PSMC2proteasome (prosome, macropain) 26S subunit, ATPase, 2; The 26S protease 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. In case of HIV-1 infection, positive modulator of Tat-mediated transactivation (433 aa)
PSME3proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki); Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also b [...] (267 aa)
SSR2signal sequence receptor, beta (translocon-associated protein beta); TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins (183 aa)
PSMD6proteasome (prosome, macropain) 26S subunit, non-ATPase, 6; Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (389 aa)
RPN1ribophorin I; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (607 aa)
RPS23ribosomal protein S23 (143 aa)
PSMC3proteasome (prosome, macropain) 26S subunit, ATPase, 3; The 26S protease 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). In case of HIV-1 infection, suppresses Tat-mediated transactivation (439 aa)
SRP9signal recognition particle 9kDa; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP. The complex of SRP9 and SRP14 is required for SRP RNA binding (86 aa)
PSMD1proteasome (prosome, macropain) 26S subunit, non-ATPase, 1 (953 aa)
PSMD2proteasome (prosome, macropain) 26S subunit, non-ATPase, 2; Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins (908 aa)
PSMC5proteasome (prosome, macropain) 26S subunit, ATPase, 5; The 26S protease 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 (406 aa)
RPS14ribosomal protein S14 (151 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)
SRP68signal recognition particle 68kDa; Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function (627 aa)
RPS15Aribosomal protein S15a (130 aa)
RPLP2ribosomal protein, large, P2; Plays an important role in the elongation step of protein synthesis (115 aa)
SEC62SEC62 homolog (S. cerevisiae); Required for preprotein translocation (By similarity) (399 aa)
SEC61GSec61 gamma subunit; Necessary for protein translocation in the endoplasmic reticulum (By similarity) (68 aa)
DDOSTdolichyl-diphosphooligosaccharide--protein glycosyltransferase; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (456 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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