Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Publication

GORAB scaffolds COPI at the trans-Golgi for efficient enzyme recycling and correct protein glycosylation.

Witkos TM, Chan WL, Joensuu M, Rhiel M, Pallister E, Thomas-Oates J, Mould AP, Mironov AA, Biot C, Guerardel Y, Morelle W, Ungar D, Wieland FT, Jokitalo E, Tassabehji M, Kornak U, Lowe M

COPI is a key mediator of protein trafficking within the secretory pathway. COPI is recruited to the membrane primarily through binding to Arf GTPases, upon which it undergoes assembly to form coated transport intermediates responsible for trafficking numerous proteins, including Golgi-resident enzymes. Here, we identify GORAB, the protein mutated in the skin and bone disorder gerodermia osteodysplastica, as a component ... [more]

Nat Commun Dec. 10, 2018; 10(1);127 [Pubmed: 30631079]

Throughput

Low Throughput

Additional Notes

Source of COPB2 not clear

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
COPB2 SCYL1	Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.	Cho NH (2022)	High	-	BioGRID	3352039
COPB2 SCYL1	Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.	Havugimana PC (2022)	High	-	BioGRID	3442837

Curated By

BioGRID

Interaction Summary

COPB2

Gene Ontology Biological Process

Gene Ontology Cellular Component

SCYL1