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Q01853 (TERA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transitional endoplasmic reticulum ATPase

Short name=TER ATPase
EC=3.6.4.6
Alternative name(s):
15S Mg(2+)-ATPase p97 subunit
Valosin-containing protein
Short name=VCP
Gene names
Name:Vcp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.6 Ref.9 Ref.11 Ref.13

Subcellular location

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.

Domain

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.

Post-translational modification

Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation.

ISGylated. Ref.7

Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity By similarity. Ref.14

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
Endoplasmic reticulum
Nucleus
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

ER-associated ubiquitin-dependent protein catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 14561754. Source: MGI

aggresome assembly

Inferred from genetic interaction PubMed 16810319. Source: MGI

cellular response to DNA damage stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein N-linked glycosylation via asparagine

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

retrograde protein transport, ER to cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

translesion synthesis

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from genetic interaction PubMed 16810319. Source: MGI

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

lipid particle

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome complex

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from physical interaction PubMed 17785525. Source: MGI

site of double-strand break

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: Ensembl

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

polyubiquitin binding

Inferred from direct assay PubMed 11483959. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 12504083. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 806805Transitional endoplasmic reticulum ATPase
PRO_0000084573

Regions

Nucleotide binding247 – 2537ATP
Region797 – 80610Interaction with UBXN6 By similarity

Sites

Binding site3481ATP
Binding site3841ATP

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31Phosphoserine By similarity
Modified residue371Phosphoserine By similarity
Modified residue3151N6,N6,N6-trimethyllysine; by VCPKMT Ref.14
Modified residue4361Phosphothreonine By similarity
Modified residue5021N6-acetyllysine Ref.15
Modified residue5051N6-acetyllysine Ref.15
Modified residue6681N6-acetyllysine; alternate Ref.15
Modified residue6681N6-succinyllysine; alternate Ref.15
Modified residue7541N6-acetyllysine Ref.15
Modified residue7701Phosphoserine By similarity
Modified residue7751Phosphoserine By similarity
Modified residue7871Phosphoserine By similarity
Modified residue8051Phosphotyrosine Ref.8

Experimental info

Mutagenesis1441R → A: Loss of phospholipid-binding. Ref.12
Sequence conflict731S → Y in BAC27119. Ref.2
Sequence conflict1991N → Y in BAE39824. Ref.2
Sequence conflict2061I → V in CAA78412. Ref.1
Sequence conflict3591R → Q in BAC27119. Ref.2
Sequence conflict4391A → T in BAE40919. Ref.2
Sequence conflict6241N → S in BAE34876. Ref.2
Sequence conflict6841G → V in BAC25849. Ref.2

Secondary structure

...................................................................................................................................... 806
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01853 [UniParc].

Last modified May 1, 2007. Version 4.
Checksum: 501B721D3A77BA8A

FASTA80689,322
        10         20         30         40         50         60 
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK 

        70         80         90        100        110        120 
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID 

       130        140        150        160        170        180 
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT 

       190        200        210        220        230        240 
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG 

       250        260        270        280        290        300 
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI 

       310        320        330        340        350        360 
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF 

       370        380        390        400        410        420 
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL 

       430        440        450        460        470        480 
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG 

       490        500        510        520        530        540 
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI 

       550        560        570        580        590        600 
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV 

       610        620        630        640        650        660 
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN 

       670        680        690        700        710        720 
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM 

       730        740        750        760        770        780 
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG 

       790        800 
AGPSQGSGGG TGGSVYTEDN DDDLYG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
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]"Structure of the AAA ATPase p97."
Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E., Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H., van Heel M., Freemont P.S.
Mol. Cell 6:1473-1484(2000) [PubMed] [Europe PMC] [Abstract]
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]"The crystal structure of murine p97/VCP at 3.6A."
Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H., Ma J., Zhang X., Freemont P.S.
J. Struct. Biol. 144:337-348(2003) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS18086.1.
PIRS25197.
RefSeqNP_033529.3. NM_009503.4.
UniGeneMm.245976.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00435.
ProteinModelPortalQ01853.
SMRQ01853. Positions 14-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid234661. 51 interactions.
DIPDIP-29796N.
IntActQ01853. 32 interactions.
MINTMINT-220770.

Chemistry

BindingDBQ01853.

PTM databases

PhosphoSiteQ01853.

2D gel databases

REPRODUCTION-2DPAGEQ01853.
UCD-2DPAGEQ01853.

Proteomic databases

MaxQBQ01853.
PaxDbQ01853.
PRIDEQ01853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452.
GeneID269523.
KEGGmmu:269523.
UCSCuc008sor.2. mouse.

Organism-specific databases

CTD7415.
MGIMGI:99919. Vcp.

Phylogenomic databases

eggNOGCOG0464.
GeneTreeENSGT00740000115575.
HOVERGENHBG001226.
InParanoidQ01853.
KOK13525.
OMAHKKVNLT.
OrthoDBEOG7H4DSW.
PhylomeDBQ01853.
TreeFamTF300542.

Gene expression databases

BgeeQ01853.
CleanExMM_VCP.
GenevestigatorQ01853.

Family and domain databases

Gene3D3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. 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]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
TIGRFAMsTIGR01243. CDC48. 1 hit.
PROSITEPS00674. AAA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVCP. mouse.
EvolutionaryTraceQ01853.
NextBio392876.
PROQ01853.
SOURCESearch...

Entry information

Entry nameTERA_MOUSE
AccessionPrimary (citable) accession number: Q01853
Secondary accession number(s): Q3TFH9 expand/collapse secondary AC list , Q3TIM2, Q3TXN9, Q6PI18, Q8BSR6, Q8CEG4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot