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VCP (valosin containing protein)

Written2013-02Yalcin Erzurumlu, Recep Ilhan, Oguz Gozen, Petek Ballar
Ege University, Faculty of Pharmacy, Biochemistry Department, Bornova, 35100, Izmir, Turkey (YE, RI, PB); Ege University, Faculty of Medicine, Department of Physiology, Bornova, 35100, Izmir, Turkey (OG)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesvalosin-containing protein
Alias_symbol (synonym)IBMPFD
p97
Other aliasALS14
TERA
HGNC (Hugo) VCP
LocusID (NCBI) 7415
Atlas_Id 42786
Location 9p13.3  [Link to chromosome band 9p13]
Location_base_pair Starts at 35056068 and ends at 35072742 bp from pter ( according to hg19-Feb_2009)  [Mapping VCP.png]
 
  Genomic location of VCP/p97 gene at chromosome 9p13.3 (minus strand).
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ACTN4 (19q13.2) / VCP (9p13.3)BORA (13q22.1) / VCP (9p13.3)GART (21q22.11) / VCP (9p13.3)
PABPC1 (8q22.3) / VCP (9p13.3)SLC3A2 (11q12.3) / VCP (9p13.3)SNRPD2 (19q13.32) / VCP (9p13.3)
VCP (9p13.3) / C9orf131 (9p13.3)VCP (9p13.3) / HNRNPA2B1 (7p15.2)VCP (9p13.3) / KIAA0753 (17p13.2)
VCP (9p13.3) / LGALS3BP (17q25.3)VCP (9p13.3) / PIGR (1q32.1)VCP (9p13.3) / VCP (9p13.3)

DNA/RNA

 
  A. The alignment of VCP/p97 mRNA to its genomic sequence. B. VCP/p97 mRNA and its amino acid coding.
Description The p97/VCP gene spans a genomic region of 16674 bases on minus strand. The DNA of p97/VCP consists of 17 exons and the coding sequence starts in the first exon.
Transcription The p97/VCP gene has one protein coding transcript which is 3859 bp long (Accession Number: NM_007126.3). The DNA has been cloned and sequenced by Koller and Brownstein in 1987 (Koller and Brownstein, 1987).
Pseudogene According to Hoyle et al., p97/VCP has a mouse pseudogene namely Vcp-rs (valosin containing protein, related sequence) (Hoyle et al., 1997). For further information: Ensembl, Vega

Protein

 
  A schematic representation of the domain structure.
Description VCP (Ter94 in D. melanogaster and CDC48 in S. cerevisiae) is a member of the AAA (ATPase associated with various cellular activities) ATPase family. It is one of the most abundant cytosolic proteins conserved throughout evolution from archaea to mammals. The complete protein contains 806 amino acids. The calculated molecular weight of p97/VCP is 89322 Da and the basal isoelectric point is 5.14.
p97/VCP functions as a homohexamer composed of six subunits. Each protomer composed of four domains vital for its proper functioning, namely the N domain (1-187), D1 weak ATPase (209-460), D2 the major ATPase (481-761), and C (762-806) domains (DeLaBarre et al., 2006; Pye et al., 2007). p97/VCP gene consists of 17 coding exons. Its N domain is encoded by exons 1, 2, 3, 4 and 5, while the D1 and D2 domains are encoded by exons 6, 7, 8, 9, 10 and 12, 13, 14, respectively. There are two linker domains in the protein: N-D1 linker and flexible D1-D2 linker.
The N domain of p97/VCP is responsible for the cofactor and ubiquitin binding function (Wang et al., 2003; Ye et al., 2003). While the D1 domain mediates oligomerization independent nucleotide binding, the D2 domain confers most of the ATPase activity (Wang et al., 2003). The two AAA domains contain the conserved Walker A, Walker B and a second region of homology (SRH). Walker A is required for nucleotide binding, whereas Walker B and SRH motifs mediate efficient ATP hydrolysis. ATP binding and hydrolysis lead to changes in the conformation of the hexameric ring, which is consistent with its role as a chaperone in disassembling protein complexes and mediating extraction of ubiquitinated proteins from the ER (Bays and Hampton, 2002; Rouiller et al., 2002).
Expression Northern blot analyses showed that p97/VCP was ubiquitously expressed in all tissues and throughout the brain (Hirabayashi et al., 2001).
Localisation Cytosol, nucleus. p97/VCP is recruited to the cytoplasmic surface of the ER via interaction with Endoplasmic reticulum-ubiquitin ligases.
Function p97/VCP functions as segregase or unfoldase by utilizing the energy derived from ATP hydrolysis for conformational changes of target proteins. It is an essential protein having many roles in diverse biological processes, such as endoplasmic reticulum-associated degradation (ERAD), homotypic membrane fusion, transcriptional control, cell cycle regulation, autophagy, endosomal sorting and regulating protein degradation at the outer mitochondrial membrane (Woodman, 2003; Wang et al., 2004; Meyer et al., 2012).
The diversity in cellular functions of p97/VCP is dictated by the variety of its interacting partner proteins. For example, p97/VCP has function in membrane fusion function via two different cofactors p47 and p37 (Uchiyama et al., 2006). The UBX-containing protein p47 functions together with p97/VCP in the fragmentation process of Golgi stacks during mitosis and for their reassembly after mitosis (Uchiyama et al., 2002; Uchiyama et al., 2003). The p97/VCP-p37 complex also brings about Golgi membrane fusion, however it might be required for organelle maintenance during interphase as well as their reassembly during mitosis (Uchiyama et al., 2006). p97/VCP has critical roles not only in Golgi membrane fusion but also in ER membrane fusion and nuclear assembly (Latterich et al., 1995; Hetzer et al., 2001).
p97/VCP forms another complex with Ufd1-Npl4 dimer (Ye et al., 2001; Braun et al., 2002; Jarosch et al., 2002; Rabinovich et al., 2002). This complex is involved in regulating spindle disassembly at the end of mitosis, assembly of the nuclear envelope and retro-translocation during ERAD by binding ubiquitinated proteins and exporting them from the ER to the cytoplasm (Hetzer et al., 2001; Cao et al., 2003).
Another molecular machinery where p97/VCP interacts with ubiquitin ligases, gp78 and Hrd1 functions in ERAD (Zhong et al., 2004; Lilley and Ploegh, 2005). Through this interaction p97/VCP is recruited from cytosol to the ER. The role of p97/VCP in ERAD is to interact with polyubiquitinated proteins and retrotranslocate them from ER to the cytosol. It has been recently suggested that Hrd1-mediated ERAD requires well-established retrotranslocation machinery, the p97/VCP-Ufd1-Npl4 complex, whereas the gp78 pathway needs only p97/VCP and Npl4 (Ballar et al., 2011). Another role of p97/VCP in ERAD is to bridge the ER to the proteasome by forming a complex with mHR23B (homolog of yeast Rad23)-PNGase (Li et al., 2005).
p97/VCP is also indicated in autophagy where it is required for the autophagosome and lysosome fusion and this function is impaired with mutations in IBMPFD disease (Ju and Weihl, 2010; Tresse et al., 2010).
Additionally, p97/VCP has role in endolysosomal sorting, where it binds to monoubiquitinated cargo, cavealin, on endosomes and functions in Cav1 transport to the endolysosomes (Ritz et al., 2011).
There are several reports linking p97/VCP to the DNA repair mechanism (Ramadan, 2012). Ubiquitin binding domain containing DVC1 protein recruits p97/VCP to DNA damage sites, where p97/VCP facilitates the extraction of the translesion synthesis (TLS) polymerase (Pol) η during DNA repair (Davis et al., 2012). p97/VCP also promotes recruitment of human tumor suppressor 53BP1 by removing Polycomb protein L3MBTL1 from chromatin (Acs et al., 2011).
p97/VCP has an essential role in DNA replication and cell cycle progression (Deichsel et al., 2009; Mouysset et al., 2008). Moreover, p97/VCP has a central regulatory role in the coordination of licensing and elongation events during eukaryotic DNA replication (Franz et al., 2011).
A recently identified role of p97/VCP is related to mitophagy (Tanaka et al., 2010). The Vms-Npl4-Cdc48 complex organized upon mitochondrial stress plays a role in maintaining the mitochondrial function via protein quality control (Heo et al., 2010). p97/VCP also functions in degradation of mitochondrial proteins and retrotranslocates these proteins from mitochondria to the cytosol for proteasomal degradation (Xu et al., 2011).
Homology Human p97/VCP gene is homolog to murine and rattus p97/VCP with 99.9pc.

Mutations

Somatic There are several p97/VCP mutations identified related with Inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia (IBMPFD) and amyotrophic lateral sclerosis (ALS).

Implicated in

Note
  
Entity Inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia (IBMPFD)
Note This rare proteinopathy, affecting mainly muscle, brain and bone, is associated with mutations in the p97/VCP gene (Watts et al., 2004). Muscle biopsies in IBMPFD patients have revealed the presence of rimmed vacuoles, cytoplasmic inclusion bodies and p97/VCP aggregates in scattered muscle fibers (Watts et al., 2004). IBMPFD neuropathologic changes are characterized by ubiquitin-positive neuronal intranuclear inclusions and dystrophic neurites mainly abundant in the neocortex (Forman et al., 2006). There are 26 mutations in p97/VCP identified so far in IBMPFD patients and these mutations are primarily in the N-terminal domain involved in ubiquitin binding and protein-protein interactions (Nalbandian et al., 2012).
  
  
Entity Amyotrophic lateral sclerosis (ALS)
Note Mutations in p97/VCP gene have been recently found also in familial cases of amyotrophic lateral sclerosis (ALS). A study using whole exome sequencing identified a pathogenic p97/VCP variant in an autosomal dominant Italian family with an ALS phenotype, and subsequently found that p97/VCP mutations were present in ~1-2% of our large cohort of familial ALS cases from unrelated families (Johnson et al., 2010). Whereas, no mutations were identified indicating that p97/VCP mutations do not have main contribution of classic ALS among Australian cases and Italian population (Tiloca et al., 2012; Williams et al., 2012). The p97/VCP expression was found to be increased in the skin of ALS patients (Ishikawa et al., 2012).
  
  
Entity Hepatocellular carcinoma
Note miRNA-129-5p downregulates p97/VCP expression and this regulation plays an important role in the progression of hepatacellular carcinoma (Liu et al., 2012). p97/VCP expression was found to be prognostic significant for disease-free and overall survival of patients with hepatocellular carcinoma (Yamamoto et al., 2003).
  
  
Entity Colorectal carcinoma
Note There is one study with 129 patients showing an association between high level-expression of p97/VCP with colorectal cancer prognosis (Yamamoto et al., 2004d).
  
  
Entity Esophageal carcinoma
Note The prognostic significance of p97/VCP expression in 156 esophageal squamous cell carcinoma (ESCC) patients has been revealed by Yamamoto et al. in 2004 (Yamamoto et al., 2004b).
  
  
Entity Prostate cancer
Note Elevated expression of p97/VCP has been associated with poor prognosis of prostate cancer with the study performed by analyzing p97/VCP expression in 136 patients (Tsujimoto et al., 2004).
  
  
Entity Breast cancer
Note The p97/VCP gene is underexpressed in patients who died of breast cancer within 5 years of surgery compared to patients who survived disease-free for more than 5 years (Asaka et al., 2006). Increased serum p97/VCP levels were observed in clinically significant proportions of breast cancer patients (Laguë et al., 2012).
  
  
Entity Pancreatic cancer
Note A global genomic analysis of pancreatic cancer has confirmed p97/VCP overexpression and association with tumor metastasis by Serial Analysis of Gene Expression (SAGE). Other studies have indicated the generalized role of UPS in regulating the metastatic potential of pancreatic cancer (Jones et al., 2008). Increased expression of p97/VCP is associated with lymph node metastasis and prognosis of pancreatic ductal adenocarcinoma (Yamamoto et al., 2004a). Moreover, elevated serum p97/VCP levels were detected in clinically significant proportions of patients with pancreatic cancer (8 of 12) (Laguë et al., 2012). p97/VCP was also found to be a useful marker in detecting malignant behavior of pancreatic endocrine neoplasms (Yamamoto et al., 2004f).
  
  
Entity Gingival squamous cell carcinoma
Note It has been shown that the expression level of p97/VCP may be used as prognostic marker for gingival squamous cell carcinoma (GSCC) (Yamamoto et al., 2004e). Moreover, the expression patterns of PBX2, a strong prognostic factor in GSCC, and p97/VCP proteins were evaluated in 66 subjects with GSCC who underwent curative surgery, and high PBX2 expression was associated with high p97/VCP expression (Qiu et al., 2012).
  
  
Entity Thyroid carcinoma
Note A study examining the p97/VCP expression in 332 patients who underwent operation for differentiated thyroid carcinoma showed that increased expression of valosin-containing protein (p97) is correlated with disease recurrence in follicular thyroid cancer (Yamamoto et al., 2005).
  
  
Entity Non-small cell lung carcinoma
Note Elevated p97/VCP expression is correlated with the progression and clinical prognosis of non-small cell lung carcinoma (NSCLC) (Yamamoto et al., 2004c). Moreover, p97/VCP inhibition suppressed proliferation, induced G0/G1-phase cell cycle arrest of NSCLCs and migration in H1299 cells and reduced NSCLC tumor growth in both in vitro and xenograft murine (athymic-nude) models after EerI treatment (Valle CW et al., 2011).
  
  
Entity Gastric cancer
Note Expression level of p97/VCP was found to be associated with prognosis and progression of gastric cancer (Yamamoto et al., 2003).
  
  
Entity Leukemia
Note Monocytic differentiation and G0/G1 growth arrest in human U937 leukemia cells is accompanied by an increase in VCP/p97 expression and a distinct subcellular distribution to be reverted during retrodifferentiation (Bertram et al., 2008). Furthermore, high p97/VCP expression has been shown to be associated with poor prednisone response in childhood acute lymphoblastic leukaemia patients (Lauten et al., 2006).
  
  
Entity Osteosarcoma
Note A study on osteosarcoma indicates the function of p97/VCP as a regulator of NFkB mediated tumor metastasis (Asai et al., 2002).
  
  
Entity Neurodegeneration
Note Excessive accumulation of misfolded proteins may inactivate p97/VCP in several neurodegenerative disorders, eventually leading to the neurodegenerations (Hirabayashi et al., 2001; Hsueh, 2012).
  
  
Entity Werner syndrome
Note It has been proposed that a novel role for p97/VCP in the DNA damage response pathway via modulating the availabilty of Werner protein, mutations of which causes Werner syndrome, a genetic disorder characterized by premature onset of aging symptoms (Partridge et al., 2003; Indig et al., 2004).
  
  
Entity Machado-joseph disease
Note Expansion of a polyglutamine tract in ataxin-3 (AT3), a deubiquitylating enzyme, results in spinocerebellar ataxia type 3/Machado-Joseph disease. AT3 interacts with p97/VCP and regulates flow through the ERAD pathway by modulating VCP-dependent extraction of proteins from the ER (Zhong and Pittman, 2006). Furthermore, p97/VCP was shown to be an activator specifically of wild-type ataxin-3, exhibiting no effect on expanded ataxin-3 (Laco et al., 2012).
  
  
Entity Hepatitis
Note Hepatitis B virus X protein (HBx protein) transactivates NF-kB, which is important in the pathogenesis of HBV-related diseases. It has been shown that Hbx interacts with VCP, and enhances the VCP-mediated activation of NF-kB (Jiao et al., 2011).
  
  
Entity Chronic obstructive pulmonary disease and emphysema
Note There is a study correlating the higher expression of valosin-containing protein (VCP) retrograde translocation complex (VCP-Rma1-gp78) with severity of emphysema in chronic obstructive pulmonary disease (COPD) lung tissues and over-expression of inflammatory, ER stress and apoptotic mediators like NFκB, GADD-153/CHOP, and p-eIF2α (Min et al., 2011).
  
  
Entity Cholesterol
Note Insig-1, a negative regulator of cholesterol synthesis is rapidly degraded by proteasomes when cells lack of cholesterol, and its degradation is inhibited when sterols accumulate. p97/VCP was shown to recruit proteasomes to Insig-1 before extraction from membrane (Ikeda et al., 2009). It is also known that ubiqitinated 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) is recognized by the ATPase VCP/p97, which mediates extraction and delivery of reductase from ER membranes to cytosolic 26 S proteasomes for degradation (Hartman et al., 2010).
  
  
Entity Antiviral immunity
Note p97/VCP is implicated as a host factor in antiviral immunity, where depletion or catalytic inhibition of p97/VCP prevents capsid degradation and reduces neutralization (Hauler et al., 2012).
  

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PLoS One. 2012;7(9):e46308. doi: 10.1371/journal.pone.0046308. Epub 2012 Sep 28.
PMID 23029473
 
DNA damage modulates nucleolar interaction of the Werner protein with the AAA ATPase p97/VCP.
Partridge JJ, Lopreiato JO Jr, Latterich M, Indig FE.
Mol Biol Cell. 2003 Oct;14(10):4221-9. Epub 2003 Aug 22.
PMID 12937274
 
Structural insights into the p97-Ufd1-Npl4 complex.
Pye VE, Beuron F, Keetch CA, McKeown C, Robinson CV, Meyer HH, Zhang X, Freemont PS.
Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):467-72. Epub 2007 Jan 3.
PMID 17202270
 
Expression level of pre-B-cell leukemia transcription factor 2 (PBX2) as a prognostic marker for gingival squamous cell carcinoma.
Qiu Y, Wang ZL, Jin SQ, Pu YF, Toyosawa S, Aozasa K, Morii E.
J Zhejiang Univ Sci B. 2012 Mar;13(3):168-75. doi: 10.1631/jzus.B1100077.
PMID 22374608
 
AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation.
Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S.
Mol Cell Biol. 2002 Jan;22(2):626-34.
PMID 11756557
 
p97/VCP- and Lys48-linked polyubiquitination form a new signaling pathway in DNA damage response.
Ramadan K.
Cell Cycle. 2012 Mar 15;11(6):1062-9. doi: 10.4161/cc.11.6.19446. Epub 2012 Mar 15.
PMID 22391235
 
Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.
Ritz D, Vuk M, Kirchner P, Bug M, Schutz S, Hayer A, Bremer S, Lusk C, Baloh RH, Lee H, Glatter T, Gstaiger M, Aebersold R, Weihl CC, Meyer H.
Nat Cell Biol. 2011 Aug 7;13(9):1116-23. doi: 10.1038/ncb2301.
PMID 21822278
 
Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle.
Rouiller I, DeLaBarre B, May AP, Weis WI, Brunger AT, Milligan RA, Wilson-Kubalek EM.
Nat Struct Biol. 2002 Dec;9(12):950-7.
PMID 12434150
 
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin.
Tanaka A, Cleland MM, Xu S, Narendra DP, Suen DF, Karbowski M, Youle RJ.
J Cell Biol. 2010 Dec 27;191(7):1367-80. doi: 10.1083/jcb.201007013. Epub 2010 Dec 20.
PMID 21173115
 
Mutational analysis of VCP gene in familial amyotrophic lateral sclerosis.
Tiloca C, Ratti A, Pensato V, Castucci A, Soraru G, Del Bo R, Corrado L, Cereda C, D'Ascenzo C, Comi GP, Mazzini L, Castellotti B, Ticozzi N, Gellera C, Silani V; SLAGEN Consortium.
Neurobiol Aging. 2012 Mar;33(3):630.e1-2. doi: 10.1016/j.neurobiolaging.2011.10.025. Epub 2011 Dec 3.
PMID 22137929
 
VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes and this function is impaired by mutations that cause IBMPFD.
Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, Dantuma NP, Taylor JP.
Autophagy. 2010 Feb;6(2):217-27. Epub 2010 Feb 22.
PMID 20104022
 
Elevated expression of valosin-containing protein (p97) is associated with poor prognosis of prostate cancer.
Tsujimoto Y, Tomita Y, Hoshida Y, Kono T, Oka T, Yamamoto S, Nonomura N, Okuyama A, Aozasa K.
Clin Cancer Res. 2004 May 1;10(9):3007-12.
PMID 15131036
 
p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis.
Uchiyama K, Totsukawa G, Puhka M, Kaneko Y, Jokitalo E, Dreveny I, Beuron F, Zhang X, Freemont P, Kondo H.
Dev Cell. 2006 Dec;11(6):803-16.
PMID 17141156
 
Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma.
Valle CW, Min T, Bodas M, Mazur S, Begum S, Tang D, Vij N.
PLoS One. 2011;6(12):e29073. doi: 10.1371/journal.pone.0029073. Epub 2011 Dec 22.
PMID 22216170
 
Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions.
Wang Q, Song C, Li CC.
J Struct Biol. 2004 Apr-May;146(1-2):44-57. (REVIEW)
PMID 15037236
 
Mutation analysis of VCP in familial and sporadic amyotrophic lateral sclerosis.
Williams KL, Solski JA, Nicholson GA, Blair IP.
Neurobiol Aging. 2012 Jul;33(7):1488.e15-6. doi: 10.1016/j.neurobiolaging.2011.11.022. Epub 2011 Dec 22.
PMID 22196955
 
p97, a protein coping with multiple identities.
Woodman PG.
J Cell Sci. 2003 Nov 1;116(Pt 21):4283-90.
PMID 14514884
 
The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover.
Xu S, Peng G, Wang Y, Fang S, Karbowski M.
Mol Biol Cell. 2011 Feb 1;22(3):291-300. doi: 10.1091/mbc.E10-09-0748. Epub 2010 Nov 30.
PMID 21118995
 
Increased expression of valosin-containing protein (p97) is correlated with disease recurrence in follicular thyroid cancer.
Yamamoto S, Tomita Y, Uruno T, Hoshida Y, Qiu Y, Iizuka N, Nakamichi I, Miyauchi A, Aozasa K.
Ann Surg Oncol. 2005 Nov;12(11):925-34. Epub 2005 Sep 29.
PMID 16189643
 
Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains.
Ye Y, Meyer HH, Rapoport TA.
J Cell Biol. 2003 Jul 7;162(1):71-84.
PMID 12847084
 
Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates.
Zhong X, Pittman RN.
Hum Mol Genet. 2006 Aug 15;15(16):2409-20. Epub 2006 Jul 5.
PMID 16822850
 
AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation.
Zhong X, Shen Y, Ballar P, Apostolou A, Agami R, Fang S.
J Biol Chem. 2004 Oct 29;279(44):45676-84. Epub 2004 Aug 24.
PMID 15331598
 

Citation

This paper should be referenced as such :
Erzurumlu, Y ; Ilhan, R ; Gozen, O ; Ballar, P
VCP (valosin containing protein)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(8):550-556.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/VCPID42786ch9p13.html


External links

Nomenclature
HGNC (Hugo)VCP   12666
LRG (Locus Reference Genomic)LRG_657
Cards
AtlasVCPID42786ch9p13
Entrez_Gene (NCBI)VCP  7415  valosin containing protein
AliasesALS14; CDC48; CMT2Y; HEL-220; 
HEL-S-70; IBMPFD; IBMPFD1; TERA; p97
GeneCards (Weizmann)VCP
Ensembl hg19 (Hinxton)ENSG00000165280 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000165280 [Gene_View]  chr9:35056068-35072742 [Contig_View]  VCP [Vega]
ICGC DataPortalENSG00000165280
TCGA cBioPortalVCP
AceView (NCBI)VCP
Genatlas (Paris)VCP
WikiGenes7415
SOURCE (Princeton)VCP
Genetics Home Reference (NIH)VCP
Genomic and cartography
GoldenPath hg38 (UCSC)VCP  -     chr9:35056068-35072742 -  9p13.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)VCP  -     9p13.3   [Description]    (hg19-Feb_2009)
EnsemblVCP - 9p13.3 [CytoView hg19]  VCP - 9p13.3 [CytoView hg38]
Mapping of homologs : NCBIVCP [Mapview hg19]  VCP [Mapview hg38]
OMIM167320   601023   613954   616687   
Gene and transcription
Genbank (Entrez)AF100752 AH009961 AH009961 AI343015 AK307735
RefSeq transcript (Entrez)NM_007126
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)VCP
Cluster EST : UnigeneHs.529782 [ NCBI ]
CGAP (NCI)Hs.529782
Alternative Splicing GalleryENSG00000165280
Gene ExpressionVCP [ NCBI-GEO ]   VCP [ EBI - ARRAY_EXPRESS ]   VCP [ SEEK ]   VCP [ MEM ]
Gene Expression Viewer (FireBrowse)VCP [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)7415
GTEX Portal (Tissue expression)VCP
Human Protein AtlasENSG00000165280-VCP [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP55072   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP55072  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP55072
Splice isoforms : SwissVarP55072
PhosPhoSitePlusP55072
Domaine pattern : Prosite (Expaxy)AAA (PS00674)   
Domains : Interpro (EBI)AAA+_ATPase    AAA_ATPase_CDC48    Asp_de-COase-like_dom    ATPase_AAA_core    ATPase_AAA_CS    Cdc48_dom2    CDC48_domain_2-like    CDC4_N-term_subdom    P-loop_NTPase    Vps4_C   
Domain families : Pfam (Sanger)AAA (PF00004)    CDC48_2 (PF02933)    CDC48_N (PF02359)    Vps4_C (PF09336)   
Domain families : Pfam (NCBI)pfam00004    pfam02933    pfam02359    pfam09336   
Domain families : Smart (EMBL)AAA (SM00382)  CDC48_2 (SM01072)  CDC48_N (SM01073)  
Conserved Domain (NCBI)VCP
DMDM Disease mutations7415
Blocks (Seattle)VCP
PDB (SRS)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
PDB (PDBSum)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
PDB (IMB)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
PDB (RSDB)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
Structural Biology KnowledgeBase3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
SCOP (Structural Classification of Proteins)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
CATH (Classification of proteins structures)3EBB    3HU1    3HU2    3HU3    3QC8    3QQ7    3QQ8    3QWZ    3TIW    4KDI    4KDL    4KLN    4KO8    4KOD    4P0A    5B6C    5C18    5C19    5C1A    5C1B    5DYG    5DYI    5EPP    5FTJ    5FTK    5FTL    5FTM    5FTN    5GLF    5IFS    5IFW   
SuperfamilyP55072
Human Protein Atlas [tissue]ENSG00000165280-VCP [tissue]
Peptide AtlasP55072
HPRD03013
IPIIPI00022774   IPI00916175   IPI00915799   
Protein Interaction databases
DIP (DOE-UCLA)P55072
IntAct (EBI)P55072
FunCoupENSG00000165280
BioGRIDVCP
STRING (EMBL)VCP
ZODIACVCP
Ontologies - Pathways
QuickGOP55072
Ontology : AmiGOproteasome complex  RNA binding  protein binding  ATP binding  extracellular region  nucleus  nucleus  nucleoplasm  nucleoplasm  endoplasmic reticulum  endoplasmic reticulum membrane  lipid particle  cytosol  cytosol  DNA repair  double-strand break repair  protein folding  protein methylation  NADH metabolic process  ER to Golgi vesicle-mediated transport  autophagy  activation of cysteine-type endopeptidase activity involved in apoptotic process  cellular response to DNA damage stimulus  lipid binding  proteasomal protein catabolic process  positive regulation of mitochondrial membrane potential  protein ubiquitination  protein ubiquitination  protein deubiquitination  ATPase activity  ATPase activity  protein N-linked glycosylation via asparagine  viral genome replication  protein phosphatase binding  protein domain specific binding  translesion synthesis  ubiquitin-dependent ERAD pathway  ubiquitin-dependent ERAD pathway  ubiquitin-dependent ERAD pathway  endoplasmic reticulum unfolded protein response  retrograde protein transport, ER to cytosol  retrograde protein transport, ER to cytosol  positive regulation of protein complex assembly  polyubiquitin binding  ubiquitin protein ligase binding  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  VCP-NPL4-UFD1 AAA ATPase complex  VCP-NPL4-UFD1 AAA ATPase complex  protein hexamerization  secretory granule lumen  azurophil granule lumen  deubiquitinase activator activity  site of double-strand break  K48-linked polyubiquitin binding  ERAD pathway  ERAD pathway  Derlin-1 retrotranslocation complex  MHC class I protein binding  identical protein binding  regulation of apoptotic process  proteasome-mediated ubiquitin-dependent protein catabolic process  proteasome-mediated ubiquitin-dependent protein catabolic process  myelin sheath  intracellular membrane-bounded organelle  neutrophil degranulation  ADP binding  ubiquitin-like protein ligase binding  establishment of protein localization  positive regulation of protein catabolic process  ATP metabolic process  perinuclear region of cytoplasm  protein homooligomerization  transmembrane transport  endoplasmic reticulum stress-induced pre-emptive quality control  extracellular exosome  aggresome assembly  error-free translesion synthesis  ER-associated misfolded protein catabolic process  flavin adenine dinucleotide catabolic process  autophagosome maturation  positive regulation of protein K63-linked deubiquitination  positive regulation of Lys63-specific deubiquitinase activity  regulation of aerobic respiration  positive regulation of oxidative phosphorylation  BAT3 complex binding  ficolin-1-rich granule lumen  ATPase complex  ubiquitin-specific protease binding  VCP-NSFL1C complex  positive regulation of ubiquitin-specific protease activity  positive regulation of ATP biosynthetic process  
Ontology : EGO-EBIproteasome complex  RNA binding  protein binding  ATP binding  extracellular region  nucleus  nucleus  nucleoplasm  nucleoplasm  endoplasmic reticulum  endoplasmic reticulum membrane  lipid particle  cytosol  cytosol  DNA repair  double-strand break repair  protein folding  protein methylation  NADH metabolic process  ER to Golgi vesicle-mediated transport  autophagy  activation of cysteine-type endopeptidase activity involved in apoptotic process  cellular response to DNA damage stimulus  lipid binding  proteasomal protein catabolic process  positive regulation of mitochondrial membrane potential  protein ubiquitination  protein ubiquitination  protein deubiquitination  ATPase activity  ATPase activity  protein N-linked glycosylation via asparagine  viral genome replication  protein phosphatase binding  protein domain specific binding  translesion synthesis  ubiquitin-dependent ERAD pathway  ubiquitin-dependent ERAD pathway  ubiquitin-dependent ERAD pathway  endoplasmic reticulum unfolded protein response  retrograde protein transport, ER to cytosol  retrograde protein transport, ER to cytosol  positive regulation of protein complex assembly  polyubiquitin binding  ubiquitin protein ligase binding  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  VCP-NPL4-UFD1 AAA ATPase complex  VCP-NPL4-UFD1 AAA ATPase complex  protein hexamerization  secretory granule lumen  azurophil granule lumen  deubiquitinase activator activity  site of double-strand break  K48-linked polyubiquitin binding  ERAD pathway  ERAD pathway  Derlin-1 retrotranslocation complex  MHC class I protein binding  identical protein binding  regulation of apoptotic process  proteasome-mediated ubiquitin-dependent protein catabolic process  proteasome-mediated ubiquitin-dependent protein catabolic process  myelin sheath  intracellular membrane-bounded organelle  neutrophil degranulation  ADP binding  ubiquitin-like protein ligase binding  establishment of protein localization  positive regulation of protein catabolic process  ATP metabolic process  perinuclear region of cytoplasm  protein homooligomerization  transmembrane transport  endoplasmic reticulum stress-induced pre-emptive quality control  extracellular exosome  aggresome assembly  error-free translesion synthesis  ER-associated misfolded protein catabolic process  flavin adenine dinucleotide catabolic process  autophagosome maturation  positive regulation of protein K63-linked deubiquitination  positive regulation of Lys63-specific deubiquitinase activity  regulation of aerobic respiration  positive regulation of oxidative phosphorylation  BAT3 complex binding  ficolin-1-rich granule lumen  ATPase complex  ubiquitin-specific protease binding  VCP-NSFL1C complex  positive regulation of ubiquitin-specific protease activity  positive regulation of ATP biosynthetic process  
Pathways : KEGGProtein processing in endoplasmic reticulum    Legionellosis   
REACTOMEP55072 [protein]
REACTOME PathwaysR-HSA-8876725 [pathway]   
NDEx NetworkVCP
Atlas of Cancer Signalling NetworkVCP
Wikipedia pathwaysVCP
Orthology - Evolution
OrthoDB7415
GeneTree (enSembl)ENSG00000165280
Phylogenetic Trees/Animal Genes : TreeFamVCP
HOVERGENP55072
HOGENOMP55072
Homologs : HomoloGeneVCP
Homology/Alignments : Family Browser (UCSC)VCP
Gene fusions - Rearrangements
Fusion : MitelmanVCP/C9orf131 [9p13.3/9p13.3]  
Fusion: TCGA_MDACCVCP 9p13.3 C9orf131 9p13.3 LGG
Tumor Fusion PortalVCP
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerVCP [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)VCP
dbVarVCP
ClinVarVCP
1000_GenomesVCP 
Exome Variant ServerVCP
ExAC (Exome Aggregation Consortium)ENSG00000165280
GNOMAD BrowserENSG00000165280
Genetic variants : HAPMAP7415
Genomic Variants (DGV)VCP [DGVbeta]
DECIPHERVCP [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisVCP 
Mutations
ICGC Data PortalVCP 
TCGA Data PortalVCP 
Broad Tumor PortalVCP
OASIS PortalVCP [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICVCP  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDVCP
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)Leiden Muscular Dystrophy pages
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch VCP
DgiDB (Drug Gene Interaction Database)VCP
DoCM (Curated mutations)VCP (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)VCP (select a term)
intoGenVCP
NCG5 (London)VCP
Cancer3DVCP(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM167320    601023    613954    616687   
Orphanet106    20341    20340    21937    21938    23294    10698    14642    14643   
DisGeNETVCP
MedgenVCP
Genetic Testing Registry VCP
NextProtP55072 [Medical]
TSGene7415
GENETestsVCP
Target ValidationVCP
Huge Navigator VCP [HugePedia]
snp3D : Map Gene to Disease7415
BioCentury BCIQVCP
ClinGenVCP
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD7415
Chemical/Pharm GKB GenePA37289
Clinical trialVCP
Miscellaneous
canSAR (ICR)VCP (select the gene name)
Probes
Litterature
PubMed419 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineVCP
EVEXVCP
GoPubMedVCP
iHOPVCP
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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