HUMAN:TERA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	VCP
Protein Name(s)	Transitional endoplasmic reticulum ATPase TER ATPase 15S Mg(2+)-ATPase p97 subunit Valosin-containing protein VCP
External Links
UniProt	P55072
EMBL	AC004472 AF100752 AK312310 AL353795 CH471071 BC110913 BC121794 Z70768
CCDS	CCDS6573.1
PIR	T02243
RefSeq	NP_009057.1
UniGene	Hs.529782
PDB	3EBB 3HU1 3HU2 3HU3 3QC8 3QQ7 3QQ8 3QWZ 3TIW 4KDI 4KDL 4KLN 4KO8 4KOD 4P0A
PDBsum	3EBB 3HU1 3HU2 3HU3 3QC8 3QQ7 3QQ8 3QWZ 3TIW 4KDI 4KDL 4KLN 4KO8 4KOD 4P0A
ProteinModelPortal	P55072
SMR	P55072
BioGrid	113258
DIP	DIP-33543N
IntAct	P55072
MINT	MINT-272884
STRING	9606.ENSP00000351777
BindingDB	P55072
ChEMBL	CHEMBL1075145
TCDB	3.A.16.1.1
PhosphoSite	P55072
DMDM	6094447
DOSAC-COBS-2DPAGE	P55072
OGP	P55072
REPRODUCTION-2DPAGE	IPI00022774 P55072
MaxQB	P55072
PaxDb	P55072
PRIDE	P55072
Ensembl	ENST00000358901
GeneID	7415
KEGG	hsa:7415
UCSC	uc003zvy.2
CTD	7415
GeneCards	GC09M035056
GeneReviews	VCP
HGNC	HGNC:12666
HPA	CAB005593 HPA012728 HPA012814
MIM	167320 601023 613954
neXtProt	NX_P55072
Orphanet	329478 803 275864 52430 100070 100069 329475
PharmGKB	PA37289
eggNOG	COG0464
HOGENOM	HOG000223224
HOVERGEN	HBG001226
InParanoid	P55072
KO	K13525
OMA	EIFDKPC
OrthoDB	EOG7H4DSW
PhylomeDB	P55072
TreeFam	TF300542
Reactome	REACT_200744 REACT_228111 REACT_228209
SignaLink	P55072
ChiTaRS	VCP
EvolutionaryTrace	P55072
GeneWiki	Valosin-containing_protein
GenomeRNAi	7415
NextBio	29034
PRO	PR:P55072
Proteomes	UP000005640
Bgee	P55072
CleanEx	HS_VCP
ExpressionAtlas	P55072
Genevestigator	P55072
GO	GO:0005737 GO:0005829 GO:0005783 GO:0005789 GO:0070062 GO:0000836 GO:0043231 GO:0005811 GO:0005634 GO:0048471 GO:0000502 GO:0035861 GO:0043531 GO:0005524 GO:0016887 GO:0035800 GO:0008289 GO:0044822 GO:0031593 GO:0019904 GO:0019903 GO:1990381 GO:0006919 GO:0070842 GO:0006974 GO:0006281 GO:0006302 GO:0030968 GO:0006888 GO:0030433 GO:0045184 GO:1903007 GO:0032436 GO:0045732 GO:0031334 GO:1903006 GO:0043161 GO:0034214 GO:0051260 GO:0018279 GO:0016567 GO:0042981 GO:0030970 GO:0019985
Gene3D	3.10.330.10 3.40.50.300
InterPro	IPR003593 IPR005938 IPR009010 IPR003959 IPR003960 IPR004201 IPR029067 IPR003338 IPR027417 IPR015415
Pfam	PF00004 PF02933 PF02359 PF09336
SMART	SM00382 SM01072 SM01073
SUPFAM	SSF50692 SSF52540 SSF54585
TIGRFAMs	TIGR01243
PROSITE	PS00674

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0019079	viral genome replication	PMID:22379090^[1]	ECO:0000315			P		As seen in figure 6, VCP acts as a PV-specific host factor of viral replication via a cellular secretion pathway.Thus, VCP could provide a novel link between the cellular protein secretion pathway and PV replication.	complete CACAO 6890
involved_in	GO:0034605	cellular response to heat	PMID:29804830^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903843	cellular response to arsenite ion	PMID:29804830^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035617	stress granule disassembly	PMID:29804830^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	PMID:29804830^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:27753622^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016236	macroautophagy	PMID:27753622^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	PMID:25125609^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:25125609^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:25878907^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	PMID:20104022^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:20104022^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0036503	ERAD pathway	PMID:20104022^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097352	autophagosome maturation	PMID:20104022^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010498	proteasomal protein catabolic process	PMID:26565908^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061857	endoplasmic reticulum stress-induced pre-emptive quality control	PMID:26565908^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:21822278^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:23349634^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:23349634^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032510	endosome to lysosome transport via multivesicular body sorting pathway	PMID:21822278^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034098	VCP-NPL4-UFD1 AAA ATPase complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P46462	C		Seeded From UniProt	complete
part_of	GO:1990730	VCP-NSFL1C complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P46462	C		Seeded From UniProt	complete
enables	GO:1904288	BAT3 complex binding	PMID:21636303^[10]	ECO:0000353	physical interaction evidence used in manual assertion	ComplexPortal:CPX-132	F		Seeded From UniProt	complete
involved_in	GO:0036503	ERAD pathway	PMID:25088257^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	has_input:(UniProtKB:O60337)	Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:22590560^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q86TM6	F		Seeded From UniProt	complete
enables	GO:1990381	ubiquitin-specific protease binding	PMID:22590560^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9UHP3	F		Seeded From UniProt	complete
enables	GO:0044389	ubiquitin-like protein ligase binding	PMID:16186510^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q86TM6	F		Seeded From UniProt	complete
involved_in	GO:2001171	positive regulation of ATP biosynthetic process	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903862	positive regulation of oxidative phosphorylation	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903715	regulation of aerobic respiration	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072389	flavin adenine dinucleotide catabolic process	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(CHEBI:24040)	Seeded From UniProt	complete
involved_in	GO:0006734	NADH metabolic process	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(CHEBI:16908)	Seeded From UniProt	complete
involved_in	GO:0010918	positive regulation of mitochondrial membrane potential	PMID:23498975^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071712	ER-associated misfolded protein catabolic process	PMID:24089527^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P35354)	Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:24089527^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0036513	Derlin-1 retrotranslocation complex	PMID:15215856^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030970	retrograde protein transport, ER to cytosol	PMID:25660456^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019079	viral genome replication	PMID:22379090^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[18]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:1990381	ubiquitin-specific protease binding	PMID:22970133^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P54252	F		Seeded From UniProt	complete
involved_in	GO:1903007	positive regulation of Lys63-specific deubiquitinase activity	PMID:22970133^[19]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P54252)	Seeded From UniProt	complete
involved_in	GO:1903006	positive regulation of protein K63-linked deubiquitination	PMID:22970133^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:16275660^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0035800	deubiquitinase activator activity	PMID:22970133^[19]	ECO:0000314	direct assay evidence used in manual assertion		F	has_regulation_target:(UniProtKB:P54252)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[22]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:17872946^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:17872946^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21630459^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0036513	Derlin-1 retrotranslocation complex	PMID:17872946^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:26842564^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:11483959^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045732	positive regulation of protein catabolic process	PMID:18775313^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:9452483^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031593	polyubiquitin modification-dependent protein binding	PMID:11483959^[26]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0031334	positive regulation of protein complex assembly	PMID:18775313^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019903	protein phosphatase binding	PMID:10364224^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P26045	F		Seeded From UniProt	complete
part_of	GO:0000502	proteasome complex	PMID:9452483^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[30]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q01853	C		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	PMID:15743842^[31]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035861	site of double-strand break	PMID:22120668^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030970	retrograde protein transport, ER to cytosol	PMID:15215856^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:22607976^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019985	translesion synthesis	PMID:23042605^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	PMID:15362974^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q04323	F		Seeded From UniProt	complete
involved_in	GO:0018279	protein N-linked glycosylation via asparagine	PMID:22607976^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:22120668^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	PMID:15215856^[16]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:23042605^[34]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:22120668^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:16140914^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q01853	P		Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	PMID:22120668^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006302	double-strand break repair	PMID:10855792^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	PMID:16140914^[36]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:10855792^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15215856^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:15215856^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10855792^[37]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0097352	autophagosome maturation	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0261014 PANTHER:PTN000554506 UniProtKB:P55072	P		Seeded From UniProt	complete
involved_in	GO:0071712	ER-associated misfolded protein catabolic process	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 SGD:S000002284 UniProtKB:P55072 WB:WBGene00007352 WB:WBGene00008053	P		Seeded From UniProt	complete
involved_in	GO:0051228	mitotic spindle disassembly	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 PomBase:SPAC1565.08 SGD:S000002284	P		Seeded From UniProt	complete
part_of	GO:0034098	VCP-NPL4-UFD1 AAA ATPase complex	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99919 PANTHER:PTN000554506 RGD:621595 SGD:S000002284 WB:WBGene00007352 WB:WBGene00008053	C		Seeded From UniProt	complete
enables	GO:0031593	polyubiquitin modification-dependent protein binding	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99919 PANTHER:PTN000554506 UniProtKB:P55072	F		Seeded From UniProt	complete
involved_in	GO:0030970	retrograde protein transport, ER to cytosol	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99919 PANTHER:PTN000554506 SGD:S000002284 UniProtKB:P55072	P		Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 SGD:S000002284 UniProtKB:P46468 UniProtKB:P55072	P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99919 PANTHER:PTN000554398 RGD:621595 SGD:S000001680 SGD:S000002284 SGD:S000004389 SGD:S000005273 UniProtKB:P46468 UniProtKB:P55072 UniProtKB:P9WQN5 UniProtKB:Q13608 WB:WBGene00007352 WB:WBGene00008053 WB:WBGene00010562	F		Seeded From UniProt	complete
involved_in	GO:0016236	macroautophagy	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 SGD:S000002284 UniProtKB:P55072	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 RGD:621595 SGD:S000002284 TAIR:locus:2085064 TAIR:locus:2101933 TAIR:locus:2831844 UniProtKB:P55072	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0261014 PANTHER:PTN000554506 PomBase:SPAC1565.08 TAIR:locus:2085064 UniProtKB:P55072 WB:WBGene00007352 dictyBase:DDB_G0288065	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[38]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000554506 PomBase:SPAC1565.08 SGD:S000002284 TAIR:locus:2085064 UniProtKB:P55072 WB:WBGene00007352 WB:WBGene00008053	C		Seeded From UniProt	complete
part_of	GO:0005811	lipid droplet	PMID:23297223^[39]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26849035^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55072	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26822609^[41]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55072	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:26712278^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55072	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24055316^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55072	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20512113^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55072	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	PMID:28689657^[45]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000158	positive regulation of ubiquitin-specific protease activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0035800	P		Seeded From UniProt	complete
part_of	GO:1990730	VCP-NSFL1C complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	P		Seeded From UniProt	complete
involved_in	GO:0050807	regulation of synapse organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
enables	GO:0043531	ADP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
involved_in	GO:0034214	protein hexamerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	P		Seeded From UniProt	complete
part_of	GO:0034098	VCP-NPL4-UFD1 AAA ATPase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
involved_in	GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
involved_in	GO:0006888	endoplasmic reticulum to Golgi vesicle-mediated transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P46462 ensembl:ENSRNOP00000040121	F		Seeded From UniProt	complete
part_of	GO:1990730	VCP-NSFL1C complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
enables	GO:1990381	ubiquitin-specific protease binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
part_of	GO:1904949	ATPase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
involved_in	GO:0070842	aggresome assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
involved_in	GO:0046034	ATP metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
enables	GO:0043531	ADP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
involved_in	GO:0043161	proteasome-mediated ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
enables	GO:0042288	MHC class I protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
part_of	GO:0036513	Derlin-1 retrotranslocation complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
enables	GO:0036435	K48-linked polyubiquitin modification-dependent protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
involved_in	GO:0034214	protein hexamerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
part_of	GO:0034098	VCP-NPL4-UFD1 AAA ATPase complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
enables	GO:0031593	polyubiquitin modification-dependent protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
involved_in	GO:0030970	retrograde protein transport, ER to cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
involved_in	GO:0010918	positive regulation of mitochondrial membrane potential	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	P		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q01853 ensembl:ENSMUSP00000030164	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003959 InterPro:IPR003960	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005938	F		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16186510^[13] Reactome:R-HSA-8932276 Reactome:R-HSA-8866857 Reactome:R-HSA-8866856 Reactome:R-HSA-8866854 Reactome:R-HSA-8866551 Reactome:R-HSA-8866546 Reactome:R-HSA-8866542 Reactome:R-HSA-8850594 Reactome:R-HSA-6781953 Reactome:R-HSA-5483238 Reactome:R-HSA-5387389 Reactome:R-HSA-5387386 Reactome:R-HSA-5362459 Reactome:R-HSA-5362441 Reactome:R-HSA-5362412 Reactome:R-HSA-5324632	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0034098	VCP-NPL4-UFD1 AAA ATPase complex	PMID:16186510^[13]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0045184	establishment of protein localization	PMID:15215856^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	PMID:16130169^[46]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030968	endoplasmic reticulum unfolded protein response	PMID:15215856^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030433	ubiquitin-dependent ERAD pathway	PMID:15215856^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0016887	ATPase activity	PMID:15215856^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16130169^[46]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1904813	ficolin-1-rich granule lumen	Reactome:R-HSA-6800434	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070987	error-free translesion synthesis	Reactome:R-HSA-110320	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055085	transmembrane transport	Reactome:R-HSA-382556	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035578	azurophil granule lumen	Reactome:R-HSA-6798751	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	Reactome:R-HSA-8866654	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	Reactome:R-HSA-532668	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	Reactome:R-HSA-8943083 Reactome:R-HSA-8943080	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5688834 Reactome:R-HSA-5654989 Reactome:R-HSA-5654985	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-6800434 Reactome:R-HSA-6798751 Reactome:R-HSA-6798748	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0256 UniProtKB-SubCell:SL-0095	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F		Seeded From UniProt	complete
involved_in	GO:0006914	autophagy	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0072	P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0010494	cytoplasmic stress granule	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0496	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Arita, M et al. (2012) Valosin-containing protein (VCP/p97) is required for poliovirus replication and is involved in cellular protein secretion pathway in poliovirus infection. J. Virol. 86 5541-53 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Turakhiya, A et al. (2018) ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules. Mol. Cell 70 906-919.e7 PubMed GONUTS page
↑ ^3.0 ^3.1 Papadopoulos, C et al. (2017) VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy. EMBO J. 36 135-150 PubMed GONUTS page
↑ ^4.0 ^4.1 Gonzalez, MA et al. (2014) A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease. Brain 137 2897-902 PubMed GONUTS page
↑ Jerath, NU et al. (2015) Rare Manifestation of a c.290 C>T, p.Gly97Glu VCP Mutation. Case Rep Genet 2015 239167 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Tresse, E et al. (2010) VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6 217-27 PubMed GONUTS page
↑ ^7.0 ^7.1 Kadowaki, H et al. (2015) Pre-emptive Quality Control Protects the ER from Protein Overload via the Proximity of ERAD Components and SRP. Cell Rep 13 944-56 PubMed GONUTS page
↑ ^8.0 ^8.1 Ritz, D et al. (2011) Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. Nat. Cell Biol. 13 1116-23 PubMed GONUTS page
↑ ^9.0 ^9.1 Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page
↑ Wang, Q et al. (2011) A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol. Cell 42 758-70 PubMed GONUTS page
↑ Nakamura, N et al. (2014) Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6. Exp. Cell Res. 328 207-16 PubMed GONUTS page
↑ ^12.0 ^12.1 Blount, JR et al. (2012) Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. PLoS ONE 7 e36542 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 Ye, Y et al. (2005) Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. U.S.A. 102 14132-8 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Bartolome, F et al. (2013) Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels. Neuron 78 57-64 PubMed GONUTS page
↑ ^15.0 ^15.1 Chen, SF et al. (2013) Caveolin-1 interacts with Derlin-1 and promotes ubiquitination and degradation of cyclooxygenase-2 via collaboration with p97 complex. J. Biol. Chem. 288 33462-9 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 ^16.8 Ye, Y et al. (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429 841-7 PubMed GONUTS page
↑ Zhong, Y et al. (2015) Identification of ERAD components essential for dislocation of the null Hong Kong variant of α-1-antitrypsin (NHK). Biochem. Biophys. Res. Commun. 458 424-8 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 Laço, MN et al. (2012) Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3. PLoS ONE 7 e43563 PubMed GONUTS page
↑ Grelle, G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol. Cell Proteomics 5 234-44 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Ballar, P et al. (2007) Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation. J. Biol. Chem. 282 33908-14 PubMed GONUTS page
↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Franz, A et al. (2016) Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard DNA replication fork progression. Nat Commun 7 10612 PubMed GONUTS page
↑ ^26.0 ^26.1 Dai, RM & Li, CC (2001) Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3 740-4 PubMed GONUTS page
↑ ^27.0 ^27.1 Alexandru, G et al. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134 804-16 PubMed GONUTS page
↑ ^28.0 ^28.1 Dai, RM et al. (1998) Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J. Biol. Chem. 273 3562-73 PubMed GONUTS page
↑ Zhang, SH et al. (1999) Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 274 17806-12 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ Song, EJ et al. (2005) Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway. Mol. Cell. Biol. 25 2511-24 PubMed GONUTS page
↑ ^32.0 ^32.1 ^32.2 ^32.3 Acs, K et al. (2011) The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18 1345-50 PubMed GONUTS page
↑ ^33.0 ^33.1 Sato, T et al. (2012) STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. Mol. Cell 47 99-110 PubMed GONUTS page
↑ ^34.0 ^34.1 Mosbech, A et al. (2012) DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks. Nat. Struct. Mol. Biol. 19 1084-92 PubMed GONUTS page
↑ McNeill, H et al. (2004) A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs. Biochem. J. 384 391-400 PubMed GONUTS page
↑ ^36.0 ^36.1 Livingstone, M et al. (2005) Valosin-containing protein phosphorylation at Ser784 in response to DNA damage. Cancer Res. 65 7533-40 PubMed GONUTS page
↑ ^37.0 ^37.1 ^37.2 Zhang, H et al. (2000) VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol. 19 253-63 PubMed GONUTS page
↑ ^38.00 ^38.01 ^38.02 ^38.03 ^38.04 ^38.05 ^38.06 ^38.07 ^38.08 ^38.09 ^38.10 ^38.11 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Olzmann, JA et al. (2013) Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. U.S.A. 110 1345-50 PubMed GONUTS page
↑ Schuller, JM et al. (2016) Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. FEBS Lett. 590 595-604 PubMed GONUTS page
↑ Banerjee, S et al. (2016) 2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science 351 871-5 PubMed GONUTS page
↑ Hänzelmann, P & Schindelin, H (2016) Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97. Structure 24 127-139 PubMed GONUTS page
↑ Noi, K et al. (2013) High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97. Structure 21 1992-2002 PubMed GONUTS page
↑ Tang, WK et al. (2010) A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J. 29 2217-29 PubMed GONUTS page
↑ Flack, JE et al. (2017) Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5. Mol. Cell 67 181-193.e5 PubMed GONUTS page
↑ ^46.0 ^46.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:22379090-1] 1.0 ^1.1 Arita, M et al. (2012) Valosin-containing protein (VCP/p97) is required for poliovirus replication and is involved in cellular protein secretion pathway in poliovirus infection. J. Virol. 86 5541-53 PubMed GONUTS page

[PMID:29804830-2] 2.0 ^2.1 ^2.2 ^2.3 Turakhiya, A et al. (2018) ZFAND1 Recruits p97 and the 26S Proteasome to Promote the Clearance of Arsenite-Induced Stress Granules. Mol. Cell 70 906-919.e7 PubMed GONUTS page

[PMID:27753622-3] 3.0 ^3.1 Papadopoulos, C et al. (2017) VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy. EMBO J. 36 135-150 PubMed GONUTS page

[PMID:25125609-4] 4.0 ^4.1 Gonzalez, MA et al. (2014) A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease. Brain 137 2897-902 PubMed GONUTS page

[PMID:25878907-5] Jerath, NU et al. (2015) Rare Manifestation of a c.290 C>T, p.Gly97Glu VCP Mutation. Case Rep Genet 2015 239167 PubMed GONUTS page

[PMID:20104022-6] 6.0 ^6.1 ^6.2 ^6.3 Tresse, E et al. (2010) VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6 217-27 PubMed GONUTS page

[PMID:26565908-7] 7.0 ^7.1 Kadowaki, H et al. (2015) Pre-emptive Quality Control Protects the ER from Protein Overload via the Proximity of ERAD Components and SRP. Cell Rep 13 944-56 PubMed GONUTS page

[PMID:21822278-8] 8.0 ^8.1 Ritz, D et al. (2011) Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations. Nat. Cell Biol. 13 1116-23 PubMed GONUTS page

[PMID:23349634-9] 9.0 ^9.1 Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page

[PMID:21636303-10] Wang, Q et al. (2011) A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol. Cell 42 758-70 PubMed GONUTS page

[PMID:25088257-11] Nakamura, N et al. (2014) Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6. Exp. Cell Res. 328 207-16 PubMed GONUTS page

[PMID:22590560-12] 12.0 ^12.1 Blount, JR et al. (2012) Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation. PLoS ONE 7 e36542 PubMed GONUTS page

[PMID:16186510-13] 13.0 ^13.1 ^13.2 Ye, Y et al. (2005) Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc. Natl. Acad. Sci. U.S.A. 102 14132-8 PubMed GONUTS page

[PMID:23498975-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 ^14.5 Bartolome, F et al. (2013) Pathogenic VCP mutations induce mitochondrial uncoupling and reduced ATP levels. Neuron 78 57-64 PubMed GONUTS page

[PMID:24089527-15] 15.0 ^15.1 Chen, SF et al. (2013) Caveolin-1 interacts with Derlin-1 and promotes ubiquitination and degradation of cyclooxygenase-2 via collaboration with p97 complex. J. Biol. Chem. 288 33462-9 PubMed GONUTS page

[PMID:15215856-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 ^16.6 ^16.7 ^16.8 Ye, Y et al. (2004) A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429 841-7 PubMed GONUTS page

[PMID:25660456-17] Zhong, Y et al. (2015) Identification of ERAD components essential for dislocation of the null Hong Kong variant of α-1-antitrypsin (NHK). Biochem. Biophys. Res. Commun. 458 424-8 PubMed GONUTS page

[PMID:23533145-18] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:22970133-19] 19.0 ^19.1 ^19.2 ^19.3 Laço, MN et al. (2012) Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3. PLoS ONE 7 e43563 PubMed GONUTS page

[PMID:16275660-20] Grelle, G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol. Cell Proteomics 5 234-44 PubMed GONUTS page

[PMID:19056867-21] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:20458337-22] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:17872946-23] 23.0 ^23.1 ^23.2 Ballar, P et al. (2007) Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation. J. Biol. Chem. 282 33908-14 PubMed GONUTS page

[PMID:21630459-24] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:26842564-25] Franz, A et al. (2016) Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard DNA replication fork progression. Nat Commun 7 10612 PubMed GONUTS page

[PMID:11483959-26] 26.0 ^26.1 Dai, RM & Li, CC (2001) Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3 740-4 PubMed GONUTS page

[PMID:18775313-27] 27.0 ^27.1 Alexandru, G et al. (2008) UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134 804-16 PubMed GONUTS page

[PMID:9452483-28] 28.0 ^28.1 Dai, RM et al. (1998) Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J. Biol. Chem. 273 3562-73 PubMed GONUTS page

[PMID:10364224-29] Zhang, SH et al. (1999) Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 274 17806-12 PubMed GONUTS page

[PMID:22681889-30] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:15743842-31] Song, EJ et al. (2005) Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway. Mol. Cell. Biol. 25 2511-24 PubMed GONUTS page

[PMID:22120668-32] 32.0 ^32.1 ^32.2 ^32.3 Acs, K et al. (2011) The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18 1345-50 PubMed GONUTS page

[PMID:22607976-33] 33.0 ^33.1 Sato, T et al. (2012) STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein. Mol. Cell 47 99-110 PubMed GONUTS page

[PMID:23042605-34] 34.0 ^34.1 Mosbech, A et al. (2012) DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocks. Nat. Struct. Mol. Biol. 19 1084-92 PubMed GONUTS page

[PMID:15362974-35] McNeill, H et al. (2004) A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs. Biochem. J. 384 391-400 PubMed GONUTS page

[PMID:16140914-36] 36.0 ^36.1 Livingstone, M et al. (2005) Valosin-containing protein phosphorylation at Ser784 in response to DNA damage. Cancer Res. 65 7533-40 PubMed GONUTS page

[PMID:10855792-37] 37.0 ^37.1 ^37.2 Zhang, H et al. (2000) VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol. 19 253-63 PubMed GONUTS page

[PMID:21873635-38] 38.00 ^38.01 ^38.02 ^38.03 ^38.04 ^38.05 ^38.06 ^38.07 ^38.08 ^38.09 ^38.10 ^38.11 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23297223-39] Olzmann, JA et al. (2013) Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. U.S.A. 110 1345-50 PubMed GONUTS page

[PMID:26849035-40] Schuller, JM et al. (2016) Nucleotide-dependent conformational changes of the AAA+ ATPase p97 revisited. FEBS Lett. 590 595-604 PubMed GONUTS page

[PMID:26822609-41] Banerjee, S et al. (2016) 2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science 351 871-5 PubMed GONUTS page

[PMID:26712278-42] Hänzelmann, P & Schindelin, H (2016) Structural Basis of ATP Hydrolysis and Intersubunit Signaling in the AAA+ ATPase p97. Structure 24 127-139 PubMed GONUTS page

[PMID:24055316-43] Noi, K et al. (2013) High-speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97. Structure 21 1992-2002 PubMed GONUTS page

[PMID:20512113-44] Tang, WK et al. (2010) A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants. EMBO J. 29 2217-29 PubMed GONUTS page

[PMID:28689657-45] Flack, JE et al. (2017) Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5. Mol. Cell 67 181-193.e5 PubMed GONUTS page

[PMID:16130169-46] 46.0 ^46.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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