LipidDB ID

LipidDB-10090-01010

Entry Name

UniProt Accession

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

Theoretical PI

5.14

Molecular Weight

89321.8

Genbank Protein 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;

Genbank Nucleotide ID

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

Protein Name

Transitional endoplasmic reticulum ATPase

Protein Synonyms/Alias

TER ATPase; 3.6.4.6; 15S Mg(2+)-ATPase p97 subunit; Valosin-containing protein; VCP;

Gene Name

Vcp

Gene Synonyms/Alias

Created Date

01-JUL-1993

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Reference

[1] Predicted from GPS-Lipid

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. 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.

Sequence Annotation

Nucleotide-binding: 247 253 ATP.
Region: 797 806 Interaction with UBXN6.
Binding site: 348 348 ATP.
Binding site: 384 384 ATP.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 3 3 Phosphoserine.
Modified residue: 37 37 Phosphoserine.
Modified residue: 315 315 N6,N6,N6-trimethyllysine; by VCPKMT.
Modified residue: 436 436 Phosphothreonine.
Modified residue: 502 502 N6-acetyllysine.
Modified residue: 505 505 N6-acetyllysine.
Modified residue: 668 668 N6-acetyllysine; alternate.
Modified residue: 668 668 N6-succinyllysine; alternate.
Modified residue: 754 754 N6-acetyllysine.
Modified residue: 770 770 Phosphoserine.
Modified residue: 775 775 Phosphoserine.
Modified residue: 787 787 Phosphoserine.
Modified residue: 805 805 Phosphotyrosine.

Protein Length

806 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005829; C:cytosol; ISS:UniProtKB
GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0000836; C:Hrd1p ubiquitin ligase complex; IEA:Ensembl
GO:0005811; C:lipid particle; IEA:Ensembl
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0000502; C:proteasome complex; IEA:Ensembl
GO:0043234; C:protein complex; IPI:MGI
GO:0035861; C:site of double-strand break; ISS:UniProtKB
GO:0043531; F:ADP binding; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0016887; F:ATPase activity; IEA:Ensembl
GO:0035800; F:deubiquitinase activator activity; IEA:Ensembl
GO:0008289; F:lipid binding; IEA:UniProtKB-KW
GO:0044822; F:poly(A) RNA binding; IEA:Ensembl
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB
GO:0006302; P:double-strand break repair; ISS:UniProtKB
GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl
GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB
GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; IEA:Ensembl
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl
GO:0031334; P:positive regulation of protein complex assembly; IEA:Ensembl
GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IEA:Ensembl
GO:0051260; P:protein homooligomerization; IEA:Ensembl
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
GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:MGI

Interpro

InterPro; IPR003593; AAA+_ATPase
InterPro; IPR005938; AAA_ATPase_CDC48
InterPro; IPR009010; Asp_de-COase-like_dom
InterPro; IPR003959; ATPase_AAA_core
InterPro; IPR003960; ATPase_AAA_CS
InterPro; IPR004201; Cdc48_dom2
InterPro; IPR029067; CDC48_domain_2-like
InterPro; IPR003338; CDC4_N-term_subdom
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR015415; Vps4_C

Pfam

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

SMART

SMART; SM00382; AAA;
SMART; SM01072; CDC48_2;
SMART; SM01073; CDC48_N;

PROSITE

PROSITE; PS00674; AAA;

PRINTS