UniProtKB - Q01853 (TERA_MOUSE)
Transitional endoplasmic reticulum ATPase
Vcp
Functioni
Catalytic activityi
- EC:3.6.4.6By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 348 | ATP 1By similarity | 1 | |
Binding sitei | 384 | ATP 12 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 247 – 253 | ATP 12 Publications | 7 | |
Nucleotide bindingi | 521 – 526 | ATP 22 Publications | 6 |
GO - Molecular functioni
- ADP binding Source: CAFA
- ATPase activity Source: ParkinsonsUK-UCL
- ATP binding Source: ParkinsonsUK-UCL
- BAT3 complex binding Source: MGI
- deubiquitinase activator activity Source: MGI
- identical protein binding Source: IntAct
- K48-linked polyubiquitin modification-dependent protein binding Source: ParkinsonsUK-UCL
- lipid binding Source: UniProtKB-KW
- MHC class I protein binding Source: ParkinsonsUK-UCL
- polyubiquitin modification-dependent protein binding Source: BHF-UCL
- protein-containing complex binding Source: MGI
- protein domain specific binding Source: MGI
- protein phosphatase binding Source: MGI
- signaling receptor binding Source: MGI
- ubiquitin-like protein ligase binding Source: MGI
- ubiquitin protein ligase binding Source: MGI
- ubiquitin-specific protease binding Source: ParkinsonsUK-UCL
GO - Biological processi
- activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
- aggresome assembly Source: MGI
- ATP metabolic process Source: ParkinsonsUK-UCL
- autophagosome maturation Source: UniProtKB
- autophagy Source: UniProtKB
- cellular response to arsenite ion Source: UniProtKB
- cellular response to DNA damage stimulus Source: UniProtKB
- cellular response to heat Source: UniProtKB
- DNA repair Source: UniProtKB
- double-strand break repair Source: UniProtKB
- endoplasmic reticulum stress-induced pre-emptive quality control Source: UniProtKB
- endoplasmic reticulum to Golgi vesicle-mediated transport Source: MGI
- endosome to lysosome transport via multivesicular body sorting pathway Source: UniProtKB
- ERAD pathway Source: UniProtKB
- ER-associated misfolded protein catabolic process Source: MGI
- flavin adenine dinucleotide catabolic process Source: MGI
- interstrand cross-link repair Source: UniProtKB
- macroautophagy Source: UniProtKB
- mitotic spindle disassembly Source: GO_Central
- NADH metabolic process Source: MGI
- negative regulation of smoothened signaling pathway Source: MGI
- positive regulation of ATP biosynthetic process Source: MGI
- positive regulation of canonical Wnt signaling pathway Source: MGI
- positive regulation of Lys63-specific deubiquitinase activity Source: MGI
- positive regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
- positive regulation of oxidative phosphorylation Source: MGI
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: MGI
- positive regulation of protein catabolic process Source: MGI
- positive regulation of protein-containing complex assembly Source: MGI
- positive regulation of protein K63-linked deubiquitination Source: MGI
- proteasomal protein catabolic process Source: UniProtKB
- proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
- protein ubiquitination Source: UniProtKB
- regulation of aerobic respiration Source: MGI
- regulation of protein localization to chromatin Source: UniProtKB
- regulation of synapse organization Source: MGI
- retrograde protein transport, ER to cytosol Source: ParkinsonsUK-UCL
- stress granule disassembly Source: UniProtKB
- translesion synthesis Source: UniProtKB
- ubiquitin-dependent ERAD pathway Source: UniProtKB
- ubiquitin-dependent protein catabolic process Source: MGI
- viral genome replication Source: MGI
Keywordsi
Molecular function | Hydrolase |
Biological process | Autophagy, DNA damage, DNA repair, Transport, Ubl conjugation pathway |
Ligand | ATP-binding, Lipid-binding, Nucleotide-binding |
Enzyme and pathway databases
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 |
Names & Taxonomyi
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 |
Gene namesi | Name:Vcp |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99919, Vcp |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Cytosol
- cytosol By similarity
Nucleus
- Nucleus By similarity
Other locations
- Stress granule By similarity
Note: Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN. Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains. Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to arsenite-induced stress treatment (By similarity).By similarity
Cytosol
- cytosol Source: UniProtKB
Endoplasmic reticulum
- Derlin-1 retrotranslocation complex Source: ParkinsonsUK-UCL
- endoplasmic reticulum Source: UniProtKB
- endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
- VCP-NPL4-UFD1 AAA ATPase complex Source: ParkinsonsUK-UCL
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- ATPase complex Source: CAFA
- cytoplasm Source: MGI
- cytoplasmic stress granule Source: UniProtKB
- glutamatergic synapse Source: MGI
- intracellular membrane-bounded organelle Source: MGI
- lipid droplet Source: MGI
- myelin sheath Source: UniProtKB
- perinuclear region of cytoplasm Source: MGI
- proteasome complex Source: MGI
- protein-containing complex Source: MGI
- site of double-strand break Source: UniProtKB
- synapse Source: SynGO
- VCP-NSFL1C complex Source: ParkinsonsUK-UCL
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 144 | R → A: Loss of phospholipid-binding. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3988606 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000084573 | 2 – 806 | Transitional endoplasmic reticulum ATPaseAdd BLAST | 805 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 3 | PhosphoserineBy similarity | 1 | |
Modified residuei | 7 | PhosphoserineBy similarity | 1 | |
Cross-linki | 8 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 13 | PhosphoserineBy similarity | 1 | |
Cross-linki | 18 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 37 | PhosphoserineBy similarity | 1 | |
Modified residuei | 315 | N6,N6,N6-trimethyllysine; by VCPKMT1 Publication | 1 | |
Modified residuei | 436 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 462 | PhosphoserineBy similarity | 1 | |
Modified residuei | 502 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 505 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 668 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 668 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 702 | PhosphoserineBy similarity | 1 | |
Modified residuei | 754 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 770 | PhosphoserineCombined sources | 1 | |
Modified residuei | 775 | PhosphoserineBy similarity | 1 | |
Modified residuei | 787 | PhosphoserineBy similarity | 1 | |
Modified residuei | 805 | PhosphotyrosineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
CPTACi | non-CPTAC-4013 |
EPDi | Q01853 |
jPOSTi | Q01853 |
MaxQBi | Q01853 |
PaxDbi | Q01853 |
PeptideAtlasi | Q01853 |
PRIDEi | Q01853 |
2D gel databases
REPRODUCTION-2DPAGEi | Q01853 |
UCD-2DPAGEi | Q01853 |
PTM databases
iPTMneti | Q01853 |
PhosphoSitePlusi | Q01853 |
SwissPalmi | Q01853 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000028452, Expressed in intestine and 292 other tissues |
Genevisiblei | Q01853, MM |
Interactioni
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).
Interacts with CCDC47 (PubMed:25009997).
Interacts with LMBR1L and UBAC2 (PubMed:31073040).
Interacts with ATXN3 (By similarity).
Interacts with TEX264; bridging VCP to covalent DNA-protein cross-links (DPCs) (By similarity).
By similarity9 PublicationsBinary interactionsi
Hide detailsQ01853
GO - Molecular functioni
- identical protein binding Source: IntAct
- K48-linked polyubiquitin modification-dependent protein binding Source: ParkinsonsUK-UCL
- MHC class I protein binding Source: ParkinsonsUK-UCL
- polyubiquitin modification-dependent protein binding Source: BHF-UCL
- protein domain specific binding Source: MGI
- protein phosphatase binding Source: MGI
- signaling receptor binding Source: MGI
- ubiquitin-like protein ligase binding Source: MGI
- ubiquitin protein ligase binding Source: MGI
- ubiquitin-specific protease binding Source: ParkinsonsUK-UCL
Protein-protein interaction databases
BioGRIDi | 234661, 135 interactors |
ComplexPortali | CPX-136, Vcp-Npl4-Ufd1 AAA ATPase complex CPX-264, Nsfl1c-Vcp complex |
CORUMi | Q01853 |
DIPi | DIP-29796N |
IntActi | Q01853, 42 interactors |
MINTi | Q01853 |
STRINGi | 10090.ENSMUSP00000030164 |
Chemistry databases
BindingDBi | Q01853 |
Miscellaneous databases
RNActi | Q01853, protein |
Structurei
Secondary structure
3D structure databases
SMRi | Q01853 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q01853 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 797 – 806 | Interaction with UBXN6By similarity | 10 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 802 – 806 | PIM motifBy similarity | 5 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0730, Eukaryota |
GeneTreei | ENSGT00900000141071 |
HOGENOMi | CLU_000688_12_3_1 |
InParanoidi | Q01853 |
OMAi | PIDDTTE |
OrthoDBi | 194195at2759 |
PhylomeDBi | Q01853 |
TreeFami | TF300542 |
Family and domain databases
DisProti | DP00435 |
IDEALi | IID50030 |
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 |
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 |
SMARTi | View protein in SMART SM00382, AAA, 2 hits SM01072, CDC48_2, 1 hit SM01073, CDC48_N, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit SSF52540, SSF52540, 2 hits SSF54585, SSF54585, 1 hit |
TIGRFAMsi | TIGR01243, CDC48, 1 hit |
PROSITEi | View protein in PROSITE PS00674, AAA, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 73 | S → Y in BAC27119 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 199 | N → Y in BAE39824 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 206 | I → V in CAA78412 (PubMed:1382975).Curated | 1 | |
Sequence conflicti | 359 | R → Q in BAC27119 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 439 | A → T in BAE40919 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 624 | N → S in BAE34876 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 684 | G → V in BAC25849 (PubMed:16141072).Curated | 1 |
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 |
CCDSi | CCDS18086.1 |
PIRi | S25197 |
RefSeqi | NP_033529.3, NM_009503.4 |
Genome annotation databases
Ensembli | ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452 |
GeneIDi | 269523 |
KEGGi | mmu:269523 |
UCSCi | uc008sor.2, mouse |
Similar proteinsi
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 |
CCDSi | CCDS18086.1 |
PIRi | S25197 |
RefSeqi | NP_033529.3, NM_009503.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1E32 | X-ray | 2.90 | A | 1-458 | [»] | |
1R7R | X-ray | 3.60 | A | 1-806 | [»] | |
1S3S | X-ray | 2.90 | A/B/C/D/E/F | 1-458 | [»] | |
2PJH | NMR | - | B | 21-213 | [»] | |
3CF0 | X-ray | 3.00 | A/B/C/D/E/F/G/H/I/J/K/L/M/N | 463-763 | [»] | |
3CF1 | X-ray | 4.40 | A/B/C | 1-806 | [»] | |
3CF2 | X-ray | 3.50 | A/B/C/D | 1-806 | [»] | |
3CF3 | X-ray | 4.25 | A/B/C | 1-806 | [»] | |
SMRi | Q01853 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 234661, 135 interactors |
ComplexPortali | CPX-136, Vcp-Npl4-Ufd1 AAA ATPase complex CPX-264, Nsfl1c-Vcp complex |
CORUMi | Q01853 |
DIPi | DIP-29796N |
IntActi | Q01853, 42 interactors |
MINTi | Q01853 |
STRINGi | 10090.ENSMUSP00000030164 |
Chemistry databases
BindingDBi | Q01853 |
ChEMBLi | CHEMBL3988606 |
PTM databases
iPTMneti | Q01853 |
PhosphoSitePlusi | Q01853 |
SwissPalmi | Q01853 |
2D gel databases
REPRODUCTION-2DPAGEi | Q01853 |
UCD-2DPAGEi | Q01853 |
Proteomic databases
CPTACi | non-CPTAC-4013 |
EPDi | Q01853 |
jPOSTi | Q01853 |
MaxQBi | Q01853 |
PaxDbi | Q01853 |
PeptideAtlasi | Q01853 |
PRIDEi | Q01853 |
Protocols and materials databases
Antibodypediai | 2215, 630 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452 |
GeneIDi | 269523 |
KEGGi | mmu:269523 |
UCSCi | uc008sor.2, mouse |
Organism-specific databases
CTDi | 7415 |
MGIi | MGI:99919, Vcp |
Phylogenomic databases
eggNOGi | KOG0730, Eukaryota |
GeneTreei | ENSGT00900000141071 |
HOGENOMi | CLU_000688_12_3_1 |
InParanoidi | Q01853 |
OMAi | PIDDTTE |
OrthoDBi | 194195at2759 |
PhylomeDBi | Q01853 |
TreeFami | TF300542 |
Enzyme and pathway databases
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 |
Miscellaneous databases
BioGRID-ORCSi | 269523, 8 hits in 18 CRISPR screens |
ChiTaRSi | Vcp, mouse |
EvolutionaryTracei | Q01853 |
PROi | PR:Q01853 |
RNActi | Q01853, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000028452, Expressed in intestine and 292 other tissues |
Genevisiblei | Q01853, MM |
Family and domain databases
DisProti | DP00435 |
IDEALi | IID50030 |
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 |
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 |
SMARTi | View protein in SMART SM00382, AAA, 2 hits SM01072, CDC48_2, 1 hit SM01073, CDC48_N, 1 hit |
SUPFAMi | SSF50692, SSF50692, 1 hit SSF52540, SSF52540, 2 hits SSF54585, SSF54585, 1 hit |
TIGRFAMsi | TIGR01243, CDC48, 1 hit |
PROSITEi | View protein in PROSITE PS00674, AAA, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TERA_MOUSE | |
Accessioni | Q01853Primary (citable) accession number: Q01853 Secondary accession number(s): Q3TFH9 Q8CEG4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | May 1, 2007 | |
Last modified: | December 2, 2020 | |
This is version 218 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families