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HEH2 protein (Saccharomyces cerevisiae) - STRING interaction network
"HEH2" - Inner nuclear membrane in Saccharomyces cerevisiae
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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HEH2Inner nuclear membrane (INM) protein; contains helix-extension-helix (HEH) motif, nuclear localization signal sequence; targeting to the INM requires the Srp1p-Kap95p karyopherins and the Ran cycle (663 aa)    
Predicted Functional Partners:
SRP1
Karyopherin alpha homolog, forms a dimer with karyopherin beta Kap95p to mediate import of nuclear proteins, binds the nuclear localization signal of the substrate during import; may also play a role in regulation of protein degradation; Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity) (542 aa)
       
 
  0.962
NUP170
Subunit of the nuclear pore complex (NPC), required for NPC localization of specific nucleoporins; involved in nuclear envelope permeability and chromosome segregation; has similar to Nup157p; essential role, with Nup157p, in NPC assembly; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP170 probably plays an important role in NPC assembly and organization. In addit [...] (1502 aa)
       
 
  0.846
ERG24
C-14 sterol reductase, acts in ergosterol biosynthesis; mutants accumulate the abnormal sterol ignosterol (ergosta-8,14 dienol), and are viable under anaerobic growth conditions but inviable on rich medium under aerobic conditions; Reduces the C14=C15 double bond of 4,4-dimethyl- cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24- dienol (438 aa)
       
      0.800
VPS4
AAA-ATPase involved in multivesicular body (MVB) protein sorting, ATP-bound Vps4p localizes to endosomes and catalyzes ESCRT-III disassembly and membrane release; ATPase activity is activated by Vta1p; regulates cellular sterol metabolism; Involved in the transport of biosynthetic membrane proteins from the prevacuolar/endosomal compartment to the vacuole. Required for multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent dissociation of class E VPS proteins from endosomal membranes, such as the disassembly of the ESCRT-III complex (437 aa)
       
      0.654
SNF7
One of four subunits of the endosomal sorting complex required for transport III (ESCRT-III); involved in the sorting of transmembrane proteins into the multivesicular body (MVB) pathway; recruited from the cytoplasm to endosomal membranes; Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed-11559748, PubMed-12194857). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane inva [...] (240 aa)
       
      0.654
NUP188
Subunit of the inner ring of the nuclear pore complex (NPC); contributes to NPC organization and nucleocytoplasmic transport; homologous to human NUP188; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization (1655 aa)
       
 
  0.625
NUP84
Subunit of the nuclear pore complex (NPC); forms a subcomplex with Nup85p, Nup120p, Nup145p-C, Sec13p, and Seh1p that plays a role in nuclear mRNA export, and NPC biogenesis; required also for transcription elongation as demonstrated by the G-less-b /.../un-on (GLRO) assay; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA expor [...] (726 aa)
       
 
  0.617
ASM4
Nuclear pore complex subunit, part of a subcomplex also containing Nup53p, Nup170p, and Pse1p; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPa [...] (528 aa)
       
 
  0.576
LAP2
Leucyl aminopeptidase yscIV (leukotriene A4 hydrolase) with epoxide hydrolase activity, metalloenzyme containing one zinc atom; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; Aminopeptidase that preferentially cleaves tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze an epoxide moiety of LTA(4) to form LTB(4) (in vitro) (671 aa)
           
  0.568
POM152
Nuclear pore membrane glycoprotein; may be involved in duplication of nuclear pores and nuclear pore complexes during S-phase;; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs (1337 aa)
       
 
  0.525
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
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