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Q01853

- TERA_MOUSE

UniProt

Q01853 - TERA_MOUSE

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Protein

Transitional endoplasmic reticulum ATPase

Gene

Vcp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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

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. deubiquitinase activator activity Source: Ensembl
  5. lipid binding Source: UniProtKB-KW
  6. poly(A) RNA binding Source: Ensembl
  7. polyubiquitin binding Source: BHF-UCL

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 Lys63-specific deubiquitinase activity Source: Ensembl
  8. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  9. positive regulation of protein complex assembly Source: Ensembl
  10. positive regulation of protein K63-linked deubiquitination Source: Ensembl
  11. protein homooligomerization Source: Ensembl
  12. protein N-linked glycosylation via asparagine Source: UniProtKB
  13. protein ubiquitination Source: UniProtKB
  14. retrograde protein transport, ER to cytosol Source: UniProtKB
  15. translesion synthesis Source: UniProtKB
  16. ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  4. Hrd1p ubiquitin ligase complex Source: Ensembl
  5. lipid particle Source: Ensembl
  6. nucleus Source: UniProtKB-KW
  7. perinuclear region of cytoplasm Source: Ensembl
  8. proteasome complex Source: Ensembl
  9. protein complex Source: MGI
  10. site of double-strand break Source: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiQ01853. baseline and differential.
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. 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. Interacts with UBOX5.By similarity5 Publications

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. 55 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 10-763.
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

        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
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 10-763.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 234661. 55 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.
ExpressionAtlasi Q01853. baseline and differential.
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

« Hide 'large scale' publications
  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. "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones."
    Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.
    Genes Cells 9:533-548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBOX5.
  7. "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.
  8. Cited for: ISGYLATION.
  9. "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].
  10. "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.
  11. Erratum
    Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006)
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
  18. "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).
  19. Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
  20. "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.
  21. "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 29, 2014
This is version 157 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