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Entry version 185 (16 Oct 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Transitional endoplasmic reticulum ATPase

Gene

Vcp

Organism
Rattus norvegicus (Rat)
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) (PubMed:10930451, PubMed:12411482). Vesicle budding from the tER is an ATP-dependent process (PubMed:10930451, PubMed:12411482). 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 (PubMed:10930451, PubMed:12411482). 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 (By similarity). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (By similarity). May more particularly play a role in caveolins sorting in cells (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity).By similarity2 Publications

<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 1By similarity1

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 1By similarity7
Nucleotide bindingi521 – 526ATP 2By similarity6

<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
LigandATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.4.6 5301

Reactome - a knowledgebase of biological pathways and processes

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

<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 5

Organism-specific databases

Rat genome database

More...
RGDi
621595 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 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_00000845752 – 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 residuei3PhosphoserineCombined sources1
Modified residuei7PhosphoserineCombined sources1
<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 VCPKMTBy similarity1
Modified residuei436PhosphothreonineBy similarity1
Modified residuei462PhosphoserineBy similarity1
Modified residuei502N6-acetyllysineBy similarity1
Modified residuei505N6-acetyllysineBy similarity1
Modified residuei668N6-acetyllysine; alternateBy similarity1
Modified residuei668N6-succinyllysine; alternateBy similarity1
Modified residuei702PhosphoserineBy similarity1
Modified residuei754N6-acetyllysineBy similarity1
Modified residuei770PhosphoserineBy similarity1
Modified residuei775PhosphoserineBy similarity1
Modified residuei787PhosphoserineBy similarity1
Modified residuei805PhosphotyrosineBy similarity1

<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.1 Publication
ISGylated.By similarity
Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P46462

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

More...
PaxDbi
P46462

PRoteomics IDEntifications database

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PRIDEi
P46462

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P46462

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P46462

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

More...
PhosphoSitePlusi
P46462

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P46462

<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

More...
Bgeei
ENSRNOG00000034242 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P46462 RN

<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.

Interacts with NSFL1C-like protein p37; the complex has membrane fusion activity and is required for Golgi and endoplasmic reticulum biogenesis.

Interacts with RHBDD1 (via C-terminal domain).

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 SPRTN; leading to recruitment to stalled replication forks.

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 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 (By similarity).

Interacts with ZFAND1 (via its ubiquitin-like region); this interaction occurs in an arsenite-dependent manner (By similarity).

Interacts with CCDC47 (By similarity).

Interacts with LMBR1L and UBAC2 (By similarity).

Interacts with ATXN3 (By similarity).

By similarity4 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

WithEntry#Exp.IntActNotes
Nsfl1cO3598712EBI-399011,EBI-1993760

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
250528, 25 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-138 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-263 Nsfl1c-Vcp complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P46462

Protein interaction database and analysis system

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IntActi
P46462, 9 interactors

Molecular INTeraction database

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MINTi
P46462

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000040121

<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

3D structure databases

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

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SMRi
P46462

Database of comparative protein structure models

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ModBasei
Search...

<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 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

More...
eggNOGi
KOG0730 Eukaryota
COG0464 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00900000141071

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000223224

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P46462

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
P46462

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

More...
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

More...
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

More...
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.

P46462-1 [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 TGGNVYTEDN

DDDLYG
Length:806
Mass (Da):89,349
Last modified:January 23, 2007 - v3
<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:i501B721D205EBA8A
GO

Sequence databases

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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

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DDBJi
Links Updated
U11760 mRNA Translation: AAC52154.1
BC060518 mRNA Translation: AAH60518.1

Protein sequence database of the Protein Information Resource

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PIRi
A55190

NCBI Reference Sequences

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RefSeqi
NP_446316.1, NM_053864.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242

Database of genes from NCBI RefSeq genomes

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GeneIDi
116643

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:116643

UCSC genome browser

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UCSCi
RGD:621595 rat

<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
U11760 mRNA Translation: AAC52154.1
BC060518 mRNA Translation: AAH60518.1
PIRiA55190
RefSeqiNP_446316.1, NM_053864.2

3D structure databases

SMRiP46462
ModBaseiSearch...

Protein-protein interaction databases

BioGridi250528, 25 interactors
ComplexPortaliCPX-138 Vcp-Npl4-Ufd1 AAA ATPase complex
CPX-263 Nsfl1c-Vcp complex
CORUMiP46462
IntActiP46462, 9 interactors
MINTiP46462
STRINGi10116.ENSRNOP00000040121

PTM databases

iPTMnetiP46462
PhosphoSitePlusiP46462
SwissPalmiP46462

2D gel databases

World-2DPAGEi0004:P46462

Proteomic databases

jPOSTiP46462
PaxDbiP46462
PRIDEiP46462

Genome annotation databases

EnsembliENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242
GeneIDi116643
KEGGirno:116643
UCSCiRGD:621595 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7415
RGDi621595 Vcp

Phylogenomic databases

eggNOGiKOG0730 Eukaryota
COG0464 LUCA
GeneTreeiENSGT00900000141071
HOGENOMiHOG000223224
InParanoidiP46462
KOiK13525
OMAiPIDDTTE
OrthoDBi194195at2759
PhylomeDBiP46462
TreeFamiTF300542

Enzyme and pathway databases

BRENDAi3.6.4.6 5301
ReactomeiR-RNO-110320 Translesion Synthesis by POLH
R-RNO-3371511 HSF1 activation
R-RNO-382556 ABC-family proteins mediated transport
R-RNO-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-RNO-5358346 Hedgehog ligand biogenesis
R-RNO-5689877 Josephin domain DUBs
R-RNO-5689896 Ovarian tumor domain proteases
R-RNO-6798695 Neutrophil degranulation

Miscellaneous databases

Protein Ontology

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PROi
PR:P46462

Gene expression databases

BgeeiENSRNOG00000034242 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
GenevisibleiP46462 RN

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_RAT
<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: P46462
<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: November 1, 1995
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 185 of the entry and version 3 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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