Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97.

Haenzelmann P, Schindelin H

p97 belongs to the superfamily of AAA+ ATPases and is characterized by a tandem AAA module, an N-terminal domain involved in substrate and cofactor interactions, and a functionally important unstructured C-terminal tail. The ATPase activity is controlled by an intradomain communication within the same protomer and an interdomain communication between neighboring protomers. Here, we present for the first time crystal ... [more]

Structure Jan. 05, 2016; 24(1);127-139 [Pubmed: 26712278]

Throughput

Low Throughput

Additional Notes

hexamer

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
VCP VCP	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.	Huelsmann J (2018)	High	-	BioGRID	2534242
VCP VCP	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.	Pu Z (2022)	Low	-	BioGRID	-
VCP VCP	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.	Yu CC (2013)	High	-	BioGRID	817427
VCP VCP	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Arumughan A (2016)	Low	-	BioGRID	-
VCP VCP	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Matsuoka S (2007)	Low	-	BioGRID	-
VCP VCP	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Song C (2007)	Low	-	BioGRID	935310
VCP VCP	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Vij N (2006)	Low	-	BioGRID	-
VCP VCP	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Arumughan A (2016)	Low	-	BioGRID	2521313
VCP VCP	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Niwa H (2012)	Low	-	BioGRID	722330
VCP VCP	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Stach L (2020)	Low	-	BioGRID	-
VCP VCP	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Tang WK (2010)	Low	-	BioGRID	-
VCP VCP	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.	Mayr PS (1999)	Low	-	BioGRID	-
VCP VCP	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.	Petrovic S (2023)	Low	-	BioGRID	-
VCP VCP	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.	Wang Q (2003)	Low	-	BioGRID	-
VCP VCP	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Niwa H (2012)	Low	-	BioGRID	722331
VCP VCP	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Stach L (2020)	Low	-	BioGRID	-
VCP VCP	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Wang Q (2003)	Low	-	BioGRID	3308557
VCP VCP	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Rolland T (2014)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

VCP

Gene Ontology Biological Process

Gene Ontology Molecular Function

ATPase activity [TAS]deubiquitinase activator activity [IDA]poly(A) RNA binding [IDA]polyubiquitin binding [IDA]protein binding [IPI]protein domain specific binding [IPI]protein phosphatase binding [IPI]ubiquitin-specific protease binding [IPI]

Gene Ontology Cellular Component

VCP