UniProt Accession

 TERA_MOUSE; Q01853; Q3TFH9; Q3TIM2; Q3TXN9; Q6PI18; Q8BSR6; Q8CEG4 

Genbank Protein ID

 Z14044; AK028264; AK030751; AK149931; AK151109; AK151418; AK153249; AK159177; AK159509; AK167794; AK169140; AL672276; BC043053; BC049114 

Genbank Nucleotide ID

 CAA78412.1; BAC25849.1; BAC27119.1; BAE29175.1; BAE30119.1; BAE30383.1; BAE31840.1; BAE34876.1; BAE35141.1; BAE39824.1; BAE40919.1; CAM14316.1; AAH43053.1; AAH49114.1 

Protein Name

 Transitional endoplasmic reticulum ATPase 

Protein Synonyms/Alias

 TER ATPase; 15S Mg(2+)-ATPase p97 subunit; Valosin-containing protein; VCP 

Gene Name

 Vcp 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
18	DLSTAILKQKNRPNR	ubiquitination	[1]
45	VVSLSQPKMDELQLF	ubiquitination	[1]
60	RGDTVLLKGKKRREA	acetylation	[2, 3]
60	RGDTVLLKGKKRREA	succinylation	[3]
60	RGDTVLLKGKKRREA	ubiquitination	[1]
109	IQPCPDVKYGKRIHV	acetylation	[4]
109	IQPCPDVKYGKRIHV	ubiquitination	[1, 5]
148	EAYRPIRKGDIFLVR	acetylation	[3]
148	EAYRPIRKGDIFLVR	succinylation	[3]
148	EAYRPIRKGDIFLVR	ubiquitination	[1]
211	DDIGGCRKQLAQIKE	ubiquitination	[1]
217	RKQLAQIKEMVELPL	acetylation	[2]
217	RKQLAQIKEMVELPL	ubiquitination	[1]
231	LRHPALFKAIGVKPP	acetylation	[2]
231	LRHPALFKAIGVKPP	ubiquitination	[1]
236	LFKAIGVKPPRGILL	ubiquitination	[1]
251	YGPPGTGKTLIARAV	acetylation	[2]
251	YGPPGTGKTLIARAV	ubiquitination	[1]
288	ESESNLRKAFEEAEK	ubiquitination	[1, 5]
295	KAFEEAEKNAPAIIF	ubiquitination	[1, 5]
312	ELDAIAPKREKTHGE	ubiquitination	[1]
336	LTLMDGLKQRAHVIV	acetylation	[2]
336	LTLMDGLKQRAHVIV	ubiquitination	[1]
386	EILQIHTKNMKLADD	ubiquitination	[1]
486	IGGLEDVKRELQELV	ubiquitination	[1]
502	YPVEHPDKFLKFGMT	acetylation	[2, 3]
502	YPVEHPDKFLKFGMT	ubiquitination	[1]
505	EHPDKFLKFGMTPSK	acetylation	[2, 3]
505	EHPDKFLKFGMTPSK	ubiquitination	[1]
512	KFGMTPSKGVLFYGP	acetylation	[2]
512	KFGMTPSKGVLFYGP	ubiquitination	[1]
524	YGPPGCGKTLLAKAI	ubiquitination	[1]
529	CGKTLLAKAIANECQ	acetylation	[2]
529	CGKTLLAKAIANECQ	ubiquitination	[1]
565	NVREIFDKARQAAPC	acetylation	[2]
584	DELDSIAKARGGNIG	ubiquitination	[1]
614	EMDGMSTKKNVFIIG	ubiquitination	[1]
615	MDGMSTKKNVFIIGA	ubiquitination	[1]
651	YIPLPDEKSRVAILK	acetylation	[2, 4]
651	YIPLPDEKSRVAILK	ubiquitination	[1]
658	KSRVAILKANLRKSP	acetylation	[2]
658	KSRVAILKANLRKSP	ubiquitination	[1]
668	LRKSPVAKDVDLEFL	acetylation	[2, 3]
668	LRKSPVAKDVDLEFL	succinylation	[3]
668	LRKSPVAKDVDLEFL	ubiquitination	[1, 5]
696	EICQRACKLAIRESI	ubiquitination	[1]
754	VSDNDIRKYEMFAQT	acetylation	[2, 3]
754	VSDNDIRKYEMFAQT	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144] 

Functional Description

 Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168- dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (By similarity). 

Sequence Annotation

 NP_BIND 247 253 ATP.
 REGION 797 806 Interaction with UBXN6 (By similarity).
 BINDING 348 348 ATP.
 BINDING 384 384 ATP.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 3 3 Phosphoserine (By similarity).
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 37 37 Phosphoserine (By similarity).
 MOD_RES 315 315 N6,N6,N6-trimethyllysine; by METTL21D.
 MOD_RES 436 436 Phosphothreonine (By similarity).
 MOD_RES 770 770 Phosphoserine (By similarity).
 MOD_RES 775 775 Phosphoserine (By similarity).
 MOD_RES 787 787 Phosphoserine (By similarity).  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Endoplasmic reticulum; Hydrolase; Lipid-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transport; Ubl conjugation; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 806 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000502; C:proteasome complex; IEA:Compara.
 GO:0043234; C:protein complex; IPI:MGI.
 GO:0035861; C:site of double-strand break; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:Compara.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0031593; F:polyubiquitin binding; IDA:BHF-UCL.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
 GO:0070842; P:aggresome assembly; IGI:MGI.
 GO:0006302; P:double-strand break repair; ISS:UniProtKB.
 GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Compara.
 GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
 GO:0031334; P:positive regulation of protein complex assembly; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
 GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
 GO:0030970; P:retrograde protein transport, ER to cytosol; ISS:UniProtKB.
 GO:0019985; P:translesion synthesis; ISS:UniProtKB. 

Interpro

 IPR003593; AAA+_ATPase.
 IPR009010; Asp_de-COase-like_dom.
 IPR005938; ATPase_AAA_CDC48.
 IPR003959; ATPase_AAA_core.
 IPR003960; ATPase_AAA_CS.
 IPR004201; Cdc48_dom2.
 IPR003338; CDC4_N-term_subdom.
 IPR027417; P-loop_NTPase.
 IPR015415; Vps4_C. 

Pfam

 PF00004; AAA
 PF02933; CDC48_2
 PF02359; CDC48_N
 PF09336; Vps4_C 

SMART

 SM00382; AAA
 SM01072; CDC48_2
 SM01073; CDC48_N 

PROSITE

 PS00674; AAA 

PRINTS