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UBQ9 UBQ9 AT1G23940 AT1G23940 UBQ8 UBQ8 UBQ4 UBQ4 UBQ3 UBQ3 UBQ10 UBQ10 AT1G06210 AT1G06210 UBQ13 UBQ13 UBQ7 UBQ7 GAMMA-ADR GAMMA-ADR AT1G60070 AT1G60070
"AT1G06210" - ENTH/VHS/GAT family protein in Arabidopsis thaliana
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
AT1G06210ENTH/VHS/GAT family protein (383 aa)    
Predicted Functional Partners:
AT1G60070
AP-1 complex subunit gamma-2; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity) (898 aa)
     
  0.943
AT1G23940
ARM repeat superfamily protein (495 aa)
     
  0.943
GAMMA-ADR
Gamma-adaptin 1; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting at the trans-Golgi network and early endosomes (TGN/EE). The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity) (876 aa)
     
  0.943
UBQ4
Ubiquitin 4; 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-11-linked is involved in ERAD (endoplasmic re [...] (382 aa)
     
  0.941
UBQ9
Ubiquitin 9; 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-11-linked is involved in ERAD (endoplasmic re [...] (322 aa)
       
  0.939
UBQ3
Polyubiquitin 3; 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-11-linked is involved in ERAD (endoplasmi [...] (306 aa)
       
  0.939
UBQ10
Polyubiquitin 10; 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-11-linked is involved in ERAD (endoplasm [...] (457 aa)
       
  0.939
UBQ8
Ubiquitin 8; 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-11-linked is involved in ERAD (endoplasmic re [...] (631 aa)
       
  0.939
UBQ7
Ubiquitin 7; 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-11-linked is involved in ERAD (endoplasmic re [...] (154 aa)
       
  0.939
UBQ13
Ubiquitin 13 (319 aa)
       
  0.939
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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