Full Link:
  • Version:
  • 10.0 (archived version)
STRINGSTRING
ERV25 ERV25 SBH2 SBH2 SBH1 SBH1 SPC2 SPC2 SPC1 SPC1 SEC6 SEC6 SEC11 SEC11 KAR2 KAR2 SEC9 SEC9 UBI4 UBI4 SPC3 SPC3
"SEC11" - 18kDa catalytic subunit of the Signal Peptidase Complex (SPC in Saccharomyces cerevisiae
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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
SEC1118kDa catalytic subunit of the Signal Peptidase Complex (SPC; Spc1p, Spc2p, Spc3p, and Sec11p) which cleaves the signal sequence of proteins targeted to the endoplasmic reticulum; Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) (167 aa)    
Predicted Functional Partners:
SPC1
Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity (94 aa)
      score_image score_image score_image score_image   0.999
SPC3
Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC22/23; Component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post- translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is required for signal peptidase activity and is essential for [...] (184 aa)
      score_image score_image score_image score_image   0.999
SPC2
Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC25; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC2 enhances the enzymatic activity of SPC and facilitate [...] (178 aa)
        score_image score_image score_image   0.999
SBH1
Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] (82 aa)
      score_image     score_image   0.999
SBH2
Ssh1p-Sss1p-Sbh2p complex component, involved in protein translocation into the endoplasmic reticulum; homologous to Sbh1p; Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import (88 aa)
      score_image     score_image   0.999
ERV25
Protein that forms a heterotrimeric complex with Erp1, Erp2p, and Emp24, member of the p24 family involved in endoplasmic reticulum to Golgi transport; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. Possesses a C-terminal dilysine motif that interacts with COPI coat subunits. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (211 aa)
      score_image score_image   score_image   0.999
UBI4
Ubiquitin, becomes conjugated to proteins, marking them for selective degradation via the ubiquitin-26S proteasome system; essential for the cellular stress response; encoded as a polyubiquitin precursor comprised of 5 head-to-tail repeats; 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 ubiqui [...] (381 aa)
        score_image       0.964
KAR2
ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
score_image       score_image   score_image   0.912
SEC6
Essential 88kDa subunit of the exocyst complex, which mediates polarized targeting of secretory vesicles to active sites of exocytosis; dimeric form of Sec6p interacts with Sec9p in vitro and inhibits t-SNARE assembly; Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane (805 aa)
            score_image   0.895
SEC9
t-SNARE protein important for fusion of secretory vesicles with the plasma membrane; similar to but not functionally redundant with Spo20p; SNAP-25 homolog; Component of a SNARE complex that may be the effector of SEC4 function in exocytosis (651 aa)
            score_image   0.891
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast