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Entry version 207 (05 Jun 2019)
Sequence version 4 (01 May 2007)
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Protein

Transitional endoplasmic reticulum ATPase

Gene

Vcp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 UFD1, 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-UFD1-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. Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. Plays a role in the regulation of stress granules (SGs) clearance process upon arsenite-induced response (By similarity). 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. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy. Acts as a negative regulator of type I interferon production by interacting with DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation. May more particularly play a role in caveolins sorting in cells. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei348ATP 1By similarity1
Binding sitei384ATP 12 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi247 – 253ATP 12 Publications7
Nucleotide bindingi521 – 526ATP 22 Publications6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAutophagy, DNA damage, DNA repair, Transport, Ubl conjugation pathway
LigandATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-110320 Translesion Synthesis by POLH
R-MMU-3371511 HSF1 activation
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6798695 Neutrophil degranulation
R-MMU-8876725 Protein methylation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transitional endoplasmic reticulum ATPase (EC:3.6.4.6By similarity)
Short name:
TER ATPase
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name:
VCP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Vcp
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:99919 Vcp

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi144R → A: Loss of phospholipid-binding. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3988606

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000845732 – 806Transitional endoplasmic reticulum ATPaseAdd BLAST805

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei3PhosphoserineBy similarity1
Modified residuei7PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei13PhosphoserineBy similarity1
Cross-linki18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei37PhosphoserineBy similarity1
Modified residuei315N6,N6,N6-trimethyllysine; by VCPKMT1 Publication1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei462PhosphoserineBy similarity1
Modified residuei502N6-acetyllysineCombined sources1
Modified residuei505N6-acetyllysineCombined sources1
Modified residuei668N6-acetyllysine; alternateCombined sources1
Modified residuei668N6-succinyllysine; alternateCombined sources1
Modified residuei702PhosphoserineBy similarity1
Modified residuei754N6-acetyllysineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei775PhosphoserineBy similarity1
Modified residuei787PhosphoserineBy similarity1
Modified residuei805PhosphotyrosineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphorylated in mitotic cells.By similarity
ISGylated.1 Publication
Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q01853

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q01853

MaxQB - The MaxQuant DataBase

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MaxQBi
Q01853

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q01853

PeptideAtlas

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PeptideAtlasi
Q01853

PRoteomics IDEntifications database

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PRIDEi
Q01853

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
Q01853

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
Q01853

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q01853

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q01853

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q01853

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000028452 Expressed in 277 organ(s), highest expression level in female gonad

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q01853 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter, that displays 6-fold radial symmetry. Part of a ternary complex containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer. The complex binds to membranes enriched in phosphatidylethanolamine-containing lipids and promotes Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1, binding to this heterodimer inhibits Golgi-membrane fusion. Interaction with VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to recruitment to stalled replication forks. Interacts with SELENOS and SYVN1, as well as with DERL1, DERL2 and DERL3; which probably transfer misfolded proteins from the ER to VCP. Interacts with SVIP. Component of a complex required to couple retrotranslocation, ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXN4 and RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of the endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with WASHC5. Interacts with UBOX5. Interacts (via N- terminus) with UBXN7, UBXN8, and probably several other UBX domain-containing proteins (via UBX domains); the interactions are mutually exclusive with VIM-dependent interactions such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and UBXN4 (By similarity). Interacts (via the PIM motif) with RNF31 (via the PUB domain) (By similarity). Interacts with DDX58/RIG-I and RNF125; interaction takes place when DDX58/RIG-I is ubiquitinated via'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of DDX58/RIG-I (By similarity). Interacts with BAG6 (By similarity). Interacts with UBXN10 (By similarity). Interacts with UBXN6; the interaction with UBXN6 is direct and competitive with UFD1 (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts with PLAA, UBXN6 and YOD1; may form a complex involved in macroautophagy (By similarity). Interacts with ANKZF1 (By similarity). Interacts with ubiquitin-binding protein FAF1 (By similarity). Interacts with ZFAND2B (via VIM motif); the interaction is direct (PubMed:24160817, PubMed:26337389). Interacts with ZFAND1 (via its ubiquitin-like region); this interaction occurs in an arsenite-dependent manner (By similarity).By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
234661, 54 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-136 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-264 Nsfl1c-Vcp complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q01853

Database of interacting proteins

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DIPi
DIP-29796N

Protein interaction database and analysis system

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IntActi
Q01853, 41 interactors

Molecular INTeraction database

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MINTi
Q01853

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000030164

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q01853

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1806
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00435

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q01853

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q01853

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni797 – 806Interaction with UBXN6By similarity10

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi802 – 806PIM motifBy similarity5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain shows evolutionary conservation with that of PEX1, and is able to bind phospholipids with a preference for phosphatidylinositol mono- and bisphosphates.
The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0730 Eukaryota
COG0464 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00900000141071

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q01853

KEGG Orthology (KO)

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KOi
K13525

Identification of Orthologs from Complete Genome Data

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OMAi
PIDDTTE

Database of Orthologous Groups

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OrthoDBi
194195at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q01853

TreeFam database of animal gene trees

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TreeFami
TF300542

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR005938 AAA_ATPase_CDC48
IPR041569 AAA_lid_3
IPR009010 Asp_de-COase-like_dom_sf
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR004201 Cdc48_dom2
IPR029067 CDC48_domain_2-like_sf
IPR003338 CDC4_N-term_subdom
IPR027417 P-loop_NTPase
IPR015415 Vps4_C

Pfam protein domain database

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Pfami
View protein in Pfam
PF00004 AAA, 2 hits
PF17862 AAA_lid_3, 2 hits
PF02933 CDC48_2, 1 hit
PF02359 CDC48_N, 1 hit
PF09336 Vps4_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 2 hits
SM01072 CDC48_2, 1 hit
SM01073 CDC48_N, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50692 SSF50692, 1 hit
SSF52540 SSF52540, 2 hits
SSF54585 SSF54585, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01243 CDC48, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00674 AAA, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q01853-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ
60 70 80 90 100
LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI
110 120 130 140 150
SIQPCPDVKY GKRIHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD
160 170 180 190 200
IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE
210 220 230 240 250
VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG
260 270 280 290 300
KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
310 320 330 340 350
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP
360 370 380 390 400
NSIDPALRRF GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA
410 420 430 440 450
NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD
460 470 480 490 500
DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP
510 520 530 540 550
DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM
560 570 580 590 600
WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
610 620 630 640 650
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE
660 670 680 690 700
KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR
710 720 730 740 750
ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN
760 770 780 790 800
DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGSVYTEDN

DDDLYG
Length:806
Mass (Da):89,322
Last modified:May 1, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i501B721D3A77BA8A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti73S → Y in BAC27119 (PubMed:16141072).Curated1
Sequence conflicti199N → Y in BAE39824 (PubMed:16141072).Curated1
Sequence conflicti206I → V in CAA78412 (PubMed:1382975).Curated1
Sequence conflicti359R → Q in BAC27119 (PubMed:16141072).Curated1
Sequence conflicti439A → T in BAE40919 (PubMed:16141072).Curated1
Sequence conflicti624N → S in BAE34876 (PubMed:16141072).Curated1
Sequence conflicti684G → V in BAC25849 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z14044 mRNA Translation: CAA78412.1
AK028264 mRNA Translation: BAC25849.1
AK030751 mRNA Translation: BAC27119.1
AK149931 mRNA Translation: BAE29175.1
AK151109 mRNA Translation: BAE30119.1
AK151418 mRNA Translation: BAE30383.1
AK153249 mRNA Translation: BAE31840.1
AK159177 mRNA Translation: BAE34876.1
AK159509 mRNA Translation: BAE35141.1
AK167794 mRNA Translation: BAE39824.1
AK169140 mRNA Translation: BAE40919.1
AL672276 Genomic DNA No translation available.
BC043053 mRNA Translation: AAH43053.1
BC049114 mRNA Translation: AAH49114.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS18086.1

Protein sequence database of the Protein Information Resource

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PIRi
S25197

NCBI Reference Sequences

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RefSeqi
NP_033529.3, NM_009503.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452

Database of genes from NCBI RefSeq genomes

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GeneIDi
269523

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:269523

UCSC genome browser

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UCSCi
uc008sor.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14044 mRNA Translation: CAA78412.1
AK028264 mRNA Translation: BAC25849.1
AK030751 mRNA Translation: BAC27119.1
AK149931 mRNA Translation: BAE29175.1
AK151109 mRNA Translation: BAE30119.1
AK151418 mRNA Translation: BAE30383.1
AK153249 mRNA Translation: BAE31840.1
AK159177 mRNA Translation: BAE34876.1
AK159509 mRNA Translation: BAE35141.1
AK167794 mRNA Translation: BAE39824.1
AK169140 mRNA Translation: BAE40919.1
AL672276 Genomic DNA No translation available.
BC043053 mRNA Translation: AAH43053.1
BC049114 mRNA Translation: AAH49114.1
CCDSiCCDS18086.1
PIRiS25197
RefSeqiNP_033529.3, NM_009503.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E32X-ray2.90A1-458[»]
1R7RX-ray3.60A1-806[»]
1S3SX-ray2.90A/B/C/D/E/F1-458[»]
2PJHNMR-B21-213[»]
3CF0X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N463-763[»]
3CF1X-ray4.40A/B/C1-806[»]
3CF2X-ray3.50A/B/C/D1-806[»]
3CF3X-ray4.25A/B/C1-806[»]
DisProtiDP00435
SMRiQ01853
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234661, 54 interactors
ComplexPortaliCPX-136 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-264 Nsfl1c-Vcp complex
CORUMiQ01853
DIPiDIP-29796N
IntActiQ01853, 41 interactors
MINTiQ01853
STRINGi10090.ENSMUSP00000030164

Chemistry databases

BindingDBiQ01853
ChEMBLiCHEMBL3988606

PTM databases

iPTMnetiQ01853
PhosphoSitePlusiQ01853
SwissPalmiQ01853

2D gel databases

REPRODUCTION-2DPAGEiQ01853
UCD-2DPAGEiQ01853

Proteomic databases

EPDiQ01853
jPOSTiQ01853
MaxQBiQ01853
PaxDbiQ01853
PeptideAtlasiQ01853
PRIDEiQ01853

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452
GeneIDi269523
KEGGimmu:269523
UCSCiuc008sor.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7415
MGIiMGI:99919 Vcp

Phylogenomic databases

eggNOGiKOG0730 Eukaryota
COG0464 LUCA
GeneTreeiENSGT00900000141071
InParanoidiQ01853
KOiK13525
OMAiPIDDTTE
OrthoDBi194195at2759
PhylomeDBiQ01853
TreeFamiTF300542

Enzyme and pathway databases

ReactomeiR-MMU-110320 Translesion Synthesis by POLH
R-MMU-3371511 HSF1 activation
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-6798695 Neutrophil degranulation
R-MMU-8876725 Protein methylation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Vcp mouse
EvolutionaryTraceiQ01853

Protein Ontology

More...
PROi
PR:Q01853

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028452 Expressed in 277 organ(s), highest expression level in female gonad
GenevisibleiQ01853 MM

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005938 AAA_ATPase_CDC48
IPR041569 AAA_lid_3
IPR009010 Asp_de-COase-like_dom_sf
IPR003959 ATPase_AAA_core
IPR003960 ATPase_AAA_CS
IPR004201 Cdc48_dom2
IPR029067 CDC48_domain_2-like_sf
IPR003338 CDC4_N-term_subdom
IPR027417 P-loop_NTPase
IPR015415 Vps4_C
PfamiView protein in Pfam
PF00004 AAA, 2 hits
PF17862 AAA_lid_3, 2 hits
PF02933 CDC48_2, 1 hit
PF02359 CDC48_N, 1 hit
PF09336 Vps4_C, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 2 hits
SM01072 CDC48_2, 1 hit
SM01073 CDC48_N, 1 hit
SUPFAMiSSF50692 SSF50692, 1 hit
SSF52540 SSF52540, 2 hits
SSF54585 SSF54585, 1 hit
TIGRFAMsiTIGR01243 CDC48, 1 hit
PROSITEiView protein in PROSITE
PS00674 AAA, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTERA_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01853
Secondary accession number(s): Q3TFH9
, Q3TIM2, Q3TXN9, Q6PI18, Q8BSR6, Q8CEG4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 1, 2007
Last modified: June 5, 2019
This is version 207 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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