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Q01853

- TERA_MOUSE

UniProt

Q01853 - TERA_MOUSE

Protein

Transitional endoplasmic reticulum ATPase

Gene

Vcp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    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 UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A By similarity. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei348 – 3481ATP
    Binding sitei384 – 3841ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi247 – 2537ATP

    GO - Molecular functioni

    1. ADP binding Source: Ensembl
    2. ATPase activity Source: Ensembl
    3. ATP binding Source: UniProtKB-KW
    4. lipid binding Source: UniProtKB-KW
    5. polyubiquitin binding Source: BHF-UCL
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. aggresome assembly Source: MGI
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. double-strand break repair Source: UniProtKB
    5. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    6. ER to Golgi vesicle-mediated transport Source: Ensembl
    7. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    8. positive regulation of protein complex assembly Source: Ensembl
    9. protein homooligomerization Source: Ensembl
    10. protein N-linked glycosylation via asparagine Source: UniProtKB
    11. protein ubiquitination Source: UniProtKB
    12. retrograde protein transport, ER to cytosol Source: UniProtKB
    13. translesion synthesis Source: UniProtKB
    14. ubiquitin-dependent protein catabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair, Transport, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_225256. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transitional endoplasmic reticulum ATPase (EC:3.6.4.6)
    Short name:
    TER ATPase
    Alternative name(s):
    15S Mg(2+)-ATPase p97 subunit
    Valosin-containing protein
    Short name:
    VCP
    Gene namesi
    Name:Vcp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:99919. Vcp.

    Subcellular locationi

    Cytoplasmcytosol. Nucleus. Endoplasmic reticulum 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 By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. endoplasmic reticulum Source: UniProtKB
    3. lipid particle Source: Ensembl
    4. nucleus Source: UniProtKB-SubCell
    5. proteasome complex Source: Ensembl
    6. protein complex Source: MGI
    7. site of double-strand break Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi144 – 1441R → A: Loss of phospholipid-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 806805Transitional endoplasmic reticulum ATPasePRO_0000084573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei3 – 31PhosphoserineBy similarity
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei315 – 3151N6,N6,N6-trimethyllysine; by VCPKMT1 Publication
    Modified residuei436 – 4361PhosphothreonineBy similarity
    Modified residuei502 – 5021N6-acetyllysine1 Publication
    Modified residuei505 – 5051N6-acetyllysine1 Publication
    Modified residuei668 – 6681N6-acetyllysine; alternate1 Publication
    Modified residuei668 – 6681N6-succinyllysine; alternate1 Publication
    Modified residuei754 – 7541N6-acetyllysine1 Publication
    Modified residuei770 – 7701PhosphoserineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity
    Modified residuei787 – 7871PhosphoserineBy similarity
    Modified residuei805 – 8051Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation.1 Publication
    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, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ01853.
    PaxDbiQ01853.
    PRIDEiQ01853.

    2D gel databases

    REPRODUCTION-2DPAGEQ01853.
    UCD-2DPAGEQ01853.

    PTM databases

    PhosphoSiteiQ01853.

    Expressioni

    Gene expression databases

    BgeeiQ01853.
    CleanExiMM_VCP.
    GenevestigatoriQ01853.

    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 UFD1L, 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, UFD1L 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 By similarity. Interacts with SELS/VIMP 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 UBXD2 and RNF19A. Interacts with CASR. Interacts with UBXN6, 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). Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP. Interacts with KIAA0196 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AmfrQ9R0494EBI-80597,EBI-3648125
    Ngly1Q9JI783EBI-80597,EBI-3648128
    Nsfl1cO359873EBI-80597,EBI-1993760From a different organism.
    VIMPQ9BQE44EBI-80597,EBI-398970From a different organism.

    Protein-protein interaction databases

    BioGridi234661. 51 interactions.
    DIPiDIP-29796N.
    IntActiQ01853. 32 interactions.
    MINTiMINT-220770.

    Structurei

    Secondary structure

    1
    806
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi25 – 295
    Beta strandi38 – 414
    Helixi43 – 486
    Beta strandi56 – 605
    Helixi62 – 643
    Beta strandi66 – 738
    Beta strandi75 – 773
    Beta strandi79 – 835
    Helixi86 – 916
    Beta strandi99 – 1046
    Beta strandi106 – 1105
    Beta strandi114 – 1196
    Helixi120 – 1223
    Turni123 – 1253
    Helixi130 – 1334
    Helixi135 – 1395
    Turni140 – 1423
    Beta strandi144 – 1474
    Beta strandi151 – 1566
    Beta strandi159 – 17618
    Beta strandi181 – 1833
    Beta strandi193 – 1953
    Beta strandi198 – 2003
    Helixi203 – 2053
    Helixi211 – 22515
    Helixi227 – 2326
    Beta strandi240 – 2445
    Helixi251 – 26111
    Beta strandi265 – 2695
    Helixi271 – 2744
    Helixi281 – 29515
    Beta strandi298 – 3058
    Helixi306 – 3083
    Helixi312 – 3154
    Helixi321 – 33313
    Helixi337 – 3393
    Beta strandi341 – 3488
    Helixi350 – 3523
    Helixi355 – 3573
    Beta strandi365 – 3684
    Helixi374 – 38310
    Turni384 – 3874
    Beta strandi388 – 3903
    Helixi396 – 4027
    Helixi408 – 43023
    Helixi439 – 4446
    Helixi449 – 4568
    Beta strandi457 – 4604
    Helixi476 – 4783
    Helixi483 – 49816
    Helixi500 – 5067
    Beta strandi512 – 5176
    Beta strandi519 – 5235
    Helixi524 – 53411
    Beta strandi538 – 5425
    Helixi544 – 5529
    Helixi558 – 56811
    Beta strandi571 – 5766
    Helixi581 – 5855
    Turni586 – 5905
    Helixi599 – 60911
    Beta strandi615 – 62410
    Helixi626 – 6283
    Helixi631 – 6344
    Turni636 – 6383
    Beta strandi641 – 6444
    Helixi650 – 66112
    Helixi672 – 6776
    Helixi684 – 70623
    Helixi733 – 7408
    Helixi749 – 76214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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.
    ProteinModelPortaliQ01853.
    SMRiQ01853. Positions 14-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01853.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni797 – 80610Interaction with UBXN6By similarity

    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.

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG0464.
    GeneTreeiENSGT00740000115575.
    HOVERGENiHBG001226.
    InParanoidiQ01853.
    KOiK13525.
    OMAiHKKVNLT.
    OrthoDBiEOG7H4DSW.
    PhylomeDBiQ01853.
    TreeFamiTF300542.

    Family and domain databases

    Gene3Di3.10.330.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR005938. AAA_ATPase_CDC48.
    IPR009010. Asp_de-COase-like_dom.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR004201. Cdc48_dom2.
    IPR029067. CDC48_domain_2-like.
    IPR003338. CDC4_N-term_subdom.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 2 hits.
    PF02933. CDC48_2. 1 hit.
    PF02359. CDC48_N. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 2 hits.
    SM01072. CDC48_2. 1 hit.
    SM01073. CDC48_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF54585. SSF54585. 1 hit.
    TIGRFAMsiTIGR01243. CDC48. 1 hit.
    PROSITEiPS00674. AAA. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q01853-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ    50
    LFRGDTVLLK GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI 100
    SIQPCPDVKY GKRIHVLPID DTVEGITGNL FEVYLKPYFL EAYRPIRKGD 150
    IFLVRGGMRA VEFKVVETDP SPYCIVAPDT VIHCEGEPIK REDEEESLNE 200
    VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG ILLYGPPGTG 250
    KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 300
    IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP 350
    NSIDPALRRF GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA 400
    NETHGHVGAD LAALCSEAAL QAIRKKMDLI DLEDETIDAE VMNSLAVTMD 450
    DFRWALSQSN PSALRETVVE VPQVTWEDIG GLEDVKRELQ ELVQYPVEHP 500
    DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI SIKGPELLTM 550
    WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 600
    INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE 650
    KSRVAILKAN LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR 700
    ESIESEIRRE RERQTNPSAM EVEEDDPVPE IRRDHFEEAM RFARRSVSDN 750
    DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG AGPSQGSGGG TGGSVYTEDN 800
    DDDLYG 806
    Length:806
    Mass (Da):89,322
    Last modified:May 1, 2007 - v4
    Checksum:i501B721D3A77BA8A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731S → Y in BAC27119. (PubMed:16141072)Curated
    Sequence conflicti199 – 1991N → Y in BAE39824. (PubMed:16141072)Curated
    Sequence conflicti206 – 2061I → V in CAA78412. (PubMed:1382975)Curated
    Sequence conflicti359 – 3591R → Q in BAC27119. (PubMed:16141072)Curated
    Sequence conflicti439 – 4391A → T in BAE40919. (PubMed:16141072)Curated
    Sequence conflicti624 – 6241N → S in BAE34876. (PubMed:16141072)Curated
    Sequence conflicti684 – 6841G → V in BAC25849. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAM14316.1.
    BC043053 mRNA. Translation: AAH43053.1.
    BC049114 mRNA. Translation: AAH49114.1.
    CCDSiCCDS18086.1.
    PIRiS25197.
    RefSeqiNP_033529.3. NM_009503.4.
    UniGeneiMm.245976.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Translation: CAM14316.1 .
    BC043053 mRNA. Translation: AAH43053.1 .
    BC049114 mRNA. Translation: AAH49114.1 .
    CCDSi CCDS18086.1.
    PIRi S25197.
    RefSeqi NP_033529.3. NM_009503.4.
    UniGenei Mm.245976.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    DisProti DP00435.
    ProteinModelPortali Q01853.
    SMRi Q01853. Positions 14-763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 234661. 51 interactions.
    DIPi DIP-29796N.
    IntActi Q01853. 32 interactions.
    MINTi MINT-220770.

    Chemistry

    BindingDBi Q01853.

    PTM databases

    PhosphoSitei Q01853.

    2D gel databases

    REPRODUCTION-2DPAGE Q01853.
    UCD-2DPAGE Q01853.

    Proteomic databases

    MaxQBi Q01853.
    PaxDbi Q01853.
    PRIDEi Q01853.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 COG0464.
    GeneTreei ENSGT00740000115575.
    HOVERGENi HBG001226.
    InParanoidi Q01853.
    KOi K13525.
    OMAi HKKVNLT.
    OrthoDBi EOG7H4DSW.
    PhylomeDBi Q01853.
    TreeFami TF300542.

    Enzyme and pathway databases

    Reactomei REACT_225256. HSF1 activation.

    Miscellaneous databases

    ChiTaRSi VCP. mouse.
    EvolutionaryTracei Q01853.
    NextBioi 392876.
    PROi Q01853.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q01853.
    CleanExi MM_VCP.
    Genevestigatori Q01853.

    Family and domain databases

    Gene3Di 3.10.330.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR005938. AAA_ATPase_CDC48.
    IPR009010. Asp_de-COase-like_dom.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR004201. Cdc48_dom2.
    IPR029067. CDC48_domain_2-like.
    IPR003338. CDC4_N-term_subdom.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 2 hits.
    PF02933. CDC48_2. 1 hit.
    PF02359. CDC48_N. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 2 hits.
    SM01072. CDC48_2. 1 hit.
    SM01073. CDC48_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50692. SSF50692. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF54585. SSF54585. 1 hit.
    TIGRFAMsi TIGR01243. CDC48. 1 hit.
    PROSITEi PS00674. AAA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation."
      Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H., Samelson L.E.
      EMBO J. 11:3533-3540(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-40; 295-309 AND 425-438.
      Strain: MRL/LPR.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c and C57BL/6J.
      Tissue: Bone marrow, Head and Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 9-18; 26-53; 87-93; 96-109; 148-155; 192-210; 218-231; 240-251; 278-287; 296-312; 324-336; 363-386; 454-502; 513-524; 530-560; 600-614; 639-651; 669-677; 701-709; 714-732 AND 754-766, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders."
      Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S., Kakizuka A., Tanaka K., Sobue G.
      J. Biol. Chem. 279:51376-51385(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF19A.
    7. Cited for: ISGYLATION.
    8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome."
      Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
      Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGLY1.
    10. Erratum
      Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006)
    11. "p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis."
      Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E., Dreveny I., Beuron F., Zhang X., Freemont P., Kondo H.
      Dev. Cell 11:803-816(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NSFL1C-LIKE PROTEIN P37.
    12. "The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97."
      Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N., Shirakawa M., Hiroaki H.
      FEBS J. 273:4959-4971(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHOLIPID BINDING, MUTAGENESIS OF ARG-144.
    13. "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor."
      Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1.
    14. "Lysine methylation of VCP by a member of a novel human protein methyltransferase family."
      Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S., Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.
      Nat. Commun. 3:1038-1038(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-315.
    15. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-502; LYS-505; LYS-668 AND LYS-754, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
    17. "Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains."
      DeLaBarre B., Brunger A.T.
      Nat. Struct. Biol. 10:856-863(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS).
    18. Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
    19. "Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47."
      Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.
      EMBO J. 23:1030-1039(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
    20. "Nucleotide dependent motion and mechanism of action of p97/VCP."
      DeLaBarre B., Brunger A.T.
      J. Mol. Biol. 347:437-452(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

    Entry informationi

    Entry nameiTERA_MOUSE
    AccessioniPrimary (citable) accession number: Q01853
    Secondary accession number(s): Q3TFH9
    , Q3TIM2, Q3TXN9, Q6PI18, Q8BSR6, Q8CEG4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3