Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2 )-ATPase p97 subunit) (Valosin-containing protein) (VCP)

 TERA_MOUSE              Reviewed;         806 AA.
Q01853; Q3TFH9; Q3TIM2; Q3TXN9; Q6PI18; Q8BSR6; Q8CEG4;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 4.
30-AUG-2017, entry version 188.
RecName: Full=Transitional endoplasmic reticulum ATPase;
Short=TER ATPase;
EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072};
AltName: Full=15S Mg(2+)-ATPase p97 subunit;
AltName: Full=Valosin-containing protein;
Short=VCP;
Name=Vcp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-40; 295-309 AND
425-438.
STRAIN=MRL/LPR;
PubMed=1382975;
Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H.,
Samelson L.E.;
"VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in
response to T cell antigen receptor activation.";
EMBO J. 11:3533-3540(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, Head, and Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[6]
INTERACTION WITH UBOX5.
PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x;
Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.;
"Interaction of U-box-type ubiquitin-protein ligases (E3s) with
molecular chaperones.";
Genes Cells 9:533-548(2004).
[7]
INTERACTION WITH RNF19A.
PubMed=15456787; DOI=10.1074/jbc.M406683200;
Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
Kakizuka A., Tanaka K., Sobue G.;
"Physical and functional interaction between dorfin and valosin-
containing protein that are colocalized in ubiquitylated inclusions in
neurodegenerative disorders.";
J. Biol. Chem. 279:51376-51385(2004).
[8]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
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.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
INTERACTION WITH NGLY1.
PubMed=16249333; DOI=10.1073/pnas.0507155102;
Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
"Multiple modes of interaction of the deglycosylation enzyme, mouse
peptide N-glycanase, with the proteasome.";
Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005).
[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]
INTERACTION WITH NSFL1C-LIKE PROTEIN P37.
PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016;
Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E.,
Dreveny I., Beuron F., Zhang X., Freemont P., Kondo H.;
"p37 is a p97 adaptor required for Golgi and ER biogenesis in
interphase and at the end of mitosis.";
Dev. Cell 11:803-816(2006).
[13]
PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-144.
PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x;
Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N.,
Shimozawa N., Shirakawa M., Hiroaki H.;
"The common phospholipid-binding activity of the N-terminal domains of
PEX1 and VCP/p97.";
FEBS J. 273:4959-4971(2006).
[14]
INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1.
PubMed=16709668; DOI=10.1073/pnas.0602747103;
Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
"The AAA ATPase p97 links peptide N-glycanase to the endoplasmic
reticulum-associated E3 ligase autocrine motility factor receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
METHYLATION AT LYS-315.
PubMed=22948820; DOI=10.1038/ncomms2041;
Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
"Lysine methylation of VCP by a member of a novel human protein
methyltransferase family.";
Nat. Commun. 3:1038-1038(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-502; LYS-505; LYS-668 AND
LYS-754, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-668, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
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.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[18]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP.
PubMed=11163219; DOI=10.1016/S1097-2765(00)00143-X;
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.;
"Structure of the AAA ATPase p97.";
Mol. Cell 6:1473-1484(2000).
[19]
X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS).
PubMed=12949490; DOI=10.1038/nsb972;
DeLaBarre B., Brunger A.T.;
"Complete structure of p97/valosin-containing protein reveals
communication between nucleotide domains.";
Nat. Struct. Biol. 10:856-863(2003).
[20]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
PubMed=14643202; DOI=10.1016/j.jsb.2003.10.007;
Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H.,
Ma J., Zhang X., Freemont P.S.;
"The crystal structure of murine p97/VCP at 3.6A.";
J. Struct. Biol. 144:337-348(2003).
[21]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP.
PubMed=14988733; DOI=10.1038/sj.emboj.7600139;
Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.;
"Structural basis of the interaction between the AAA ATPase p97/VCP
and its adaptor protein p47.";
EMBO J. 23:1030-1039(2004).
[22]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=15740751; DOI=10.1016/j.jmb.2005.01.060;
DeLaBarre B., Brunger A.T.;
"Nucleotide dependent motion and mechanism of action of p97/VCP.";
J. Mol. Biol. 347:437-452(2005).
-!- 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 UFD1, VCP
and NPLOC4 binds ubiquitinated proteins and is necessary for the
export of misfolded proteins from the ER to the cytoplasm, where
they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex
regulates spindle disassembly at the end of mitosis and is
necessary for the formation of a closed nuclear envelope.
Regulates E3 ubiquitin-protein ligase activity of RNF19A.
Component of the VCP/p97-AMFR/gp78 complex that participates in
the final step of the sterol-mediated ubiquitination and
endoplasmic reticulum-associated degradation (ERAD) of HMGCR.
Involved in endoplasmic reticulum stress-induced pre-emptive
quality control, a mechanism that selectively attenuates the
translocation of newly synthesized proteins into the endoplasmic
reticulum and reroutes them to the cytosol for proteasomal
degradation. Also involved in DNA damage response: recruited to
double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent
manner and promotes the recruitment of TP53BP1 at DNA damage
sites. Recruited to stalled replication forks by SPRTN: may act by
mediating extraction of DNA polymerase eta (POLH) to prevent
excessive translesion DNA synthesis and limit the incidence of
mutations induced by DNA damage. Required for cytoplasmic
retrotranslocation of stressed/damaged mitochondrial outer-
membrane proteins and their subsequent proteasomal degradation.
Essential for the maturation of ubiquitin-containing
autophagosomes and the clearance of ubiquitinated protein by
autophagy. Acts as a negative regulator of type I interferon
production by interacting with DDX58/RIG-I: interaction takes
place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked
ubiquitin on its CARD domains, leading to recruit RNF125 and
promote ubiquitination and degradation of DDX58/RIG-I. May play a
role in the ubiquitin-dependent sorting of membrane proteins to
lysosomes where they undergo degradation. May more particularly
play a role in caveolins sorting in cells.
{ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P55072}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072,
ECO:0000269|PubMed:15189447, ECO:0000269|PubMed:15456787,
ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16709668,
ECO:0000269|PubMed:17141156}.
-!- INTERACTION:
Q9R049:Amfr; NbExp=4; IntAct=EBI-80597, EBI-3648125;
Q80UU1:Ankzf1; NbExp=2; IntAct=EBI-80597, EBI-9510971;
Q9JI78:Ngly1; NbExp=3; IntAct=EBI-80597, EBI-3648128;
Q9ES54:Nploc4 (xeno); NbExp=5; IntAct=EBI-80597, EBI-1993990;
O35987:Nsfl1c (xeno); NbExp=8; IntAct=EBI-80597, EBI-1993760;
Q9BQE4:SELENOS (xeno); NbExp=4; IntAct=EBI-80597, EBI-398970;
P70362:Ufd1; NbExp=8; IntAct=EBI-80597, EBI-7961331;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P55072}. Nucleus
{ECO:0000250|UniProtKB:P55072}. 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. {ECO:0000250|UniProtKB:P55072}.
-!- 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.
-!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction
with the PUB domain of RNF31. {ECO:0000250|UniProtKB:P55072}.
-!- PTM: Phosphorylated by tyrosine kinases in response to T-cell
antigen receptor activation. Phosphorylated in mitotic cells.
{ECO:0000250|UniProtKB:P46462}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in
the presence of ASPSCR1. Lys-315 methylation may decrease ATPase
activity (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z14044; CAA78412.1; -; mRNA.
EMBL; AK028264; BAC25849.1; -; mRNA.
EMBL; AK030751; BAC27119.1; -; mRNA.
EMBL; AK149931; BAE29175.1; -; mRNA.
EMBL; AK151109; BAE30119.1; -; mRNA.
EMBL; AK151418; BAE30383.1; -; mRNA.
EMBL; AK153249; BAE31840.1; -; mRNA.
EMBL; AK159177; BAE34876.1; -; mRNA.
EMBL; AK159509; BAE35141.1; -; mRNA.
EMBL; AK167794; BAE39824.1; -; mRNA.
EMBL; AK169140; BAE40919.1; -; mRNA.
EMBL; AL672276; CAM14316.1; -; Genomic_DNA.
EMBL; BC043053; AAH43053.1; -; mRNA.
EMBL; BC049114; AAH49114.1; -; mRNA.
CCDS; CCDS18086.1; -.
PIR; S25197; S25197.
RefSeq; NP_033529.3; NM_009503.4.
UniGene; Mm.245976; -.
UniGene; Mm.262053; -.
UniGene; Mm.469106; -.
PDB; 1E32; X-ray; 2.90 A; A=1-458.
PDB; 1R7R; X-ray; 3.60 A; A=1-806.
PDB; 1S3S; X-ray; 2.90 A; A/B/C/D/E/F=1-458.
PDB; 2PJH; NMR; -; B=21-213.
PDB; 3CF0; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=463-763.
PDB; 3CF1; X-ray; 4.40 A; A/B/C=1-806.
PDB; 3CF2; X-ray; 3.50 A; A/B/C/D=1-806.
PDB; 3CF3; X-ray; 4.25 A; A/B/C=1-806.
PDBsum; 1E32; -.
PDBsum; 1R7R; -.
PDBsum; 1S3S; -.
PDBsum; 2PJH; -.
PDBsum; 3CF0; -.
PDBsum; 3CF1; -.
PDBsum; 3CF2; -.
PDBsum; 3CF3; -.
DisProt; DP00435; -.
ProteinModelPortal; Q01853; -.
SMR; Q01853; -.
BioGrid; 234661; 52.
DIP; DIP-29796N; -.
IntAct; Q01853; 36.
MINT; MINT-220770; -.
STRING; 10090.ENSMUSP00000030164; -.
BindingDB; Q01853; -.
iPTMnet; Q01853; -.
PhosphoSitePlus; Q01853; -.
SwissPalm; Q01853; -.
REPRODUCTION-2DPAGE; Q01853; -.
UCD-2DPAGE; Q01853; -.
EPD; Q01853; -.
MaxQB; Q01853; -.
PaxDb; Q01853; -.
PeptideAtlas; Q01853; -.
PRIDE; Q01853; -.
Ensembl; ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452.
GeneID; 269523; -.
KEGG; mmu:269523; -.
UCSC; uc008sor.2; mouse.
CTD; 7415; -.
MGI; MGI:99919; Vcp.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00890000139420; -.
HOVERGEN; HBG001226; -.
InParanoid; Q01853; -.
KO; K13525; -.
OMA; PIDDTTE; -.
OrthoDB; EOG091G024K; -.
PhylomeDB; Q01853; -.
TreeFam; TF300542; -.
Reactome; R-MMU-110320; Translesion Synthesis by POLH.
Reactome; R-MMU-3371511; HSF1 activation.
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
Reactome; R-MMU-5689877; Josephin domain DUBs.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8876725; Protein methylation.
ChiTaRS; Vcp; mouse.
EvolutionaryTrace; Q01853; -.
PRO; PR:Q01853; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028452; -.
CleanEx; MM_VCP; -.
Genevisible; Q01853; MM.
GO; GO:1904949; C:ATPase complex; IMP:CAFA.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005811; C:lipid particle; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0000502; C:proteasome complex; ISO:MGI.
GO; GO:0043234; C:protein complex; IPI:MGI.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL.
GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL.
GO; GO:0043531; F:ADP binding; IMP:CAFA.
GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL.
GO; GO:0016887; F:ATPase activity; IDA:ParkinsonsUK-UCL.
GO; GO:1904288; F:BAT3 complex binding; ISO:MGI.
GO; GO:0035800; F:deubiquitinase activator activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0036435; F:K48-linked polyubiquitin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0042288; F:MHC class I protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0031593; F:polyubiquitin binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0070842; P:aggresome assembly; IGI:MGI.
GO; GO:0046034; P:ATP metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI.
GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; ISO:MGI.
GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; ISO:MGI.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISO:MGI.
GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; ISO:MGI.
GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0034214; P:protein hexamerization; IDA:ParkinsonsUK-UCL.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:1903715; P:regulation of aerobic respiration; ISO:MGI.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL.
GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:MGI.
GO; GO:0019079; P:viral genome replication; ISO:MGI.
Gene3D; 3.10.330.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005938; AAA_ATPase_CDC48.
InterPro; IPR009010; Asp_de-COase-like_dom.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
Pfam; PF09336; Vps4_C; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
TIGRFAMs; TIGR01243; CDC48; 1.
PROSITE; PS00674; AAA; 2.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Autophagy; Complete proteome;
Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
Endoplasmic reticulum; Hydrolase; Isopeptide bond; Lipid-binding;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transport; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P55072}.
CHAIN 2 806 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000084573.
NP_BIND 247 253 ATP. {ECO:0000305|PubMed:11163219,
ECO:0000305|PubMed:14988733}.
NP_BIND 521 526 ATP. {ECO:0000305|PubMed:11163219,
ECO:0000305|PubMed:14988733}.
REGION 797 806 Interaction with UBXN6. {ECO:0000250}.
MOTIF 802 806 PIM motif.
{ECO:0000250|UniProtKB:P55072}.
BINDING 348 348 ATP. {ECO:0000250|UniProtKB:P55072}.
BINDING 384 384 ATP. {ECO:0000305|PubMed:11163219,
ECO:0000305|PubMed:14988733}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 315 315 N6,N6,N6-trimethyllysine; by VCPKMT.
{ECO:0000269|PubMed:22948820}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 502 502 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 505 505 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 668 668 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 668 668 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 754 754 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 805 805 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P55072}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P55072}.
MUTAGEN 144 144 R->A: Loss of phospholipid-binding.
{ECO:0000269|PubMed:17018057}.
CONFLICT 73 73 S -> Y (in Ref. 2; BAC27119).
{ECO:0000305}.
CONFLICT 199 199 N -> Y (in Ref. 2; BAE39824).
{ECO:0000305}.
CONFLICT 206 206 I -> V (in Ref. 1; CAA78412).
{ECO:0000305}.
CONFLICT 359 359 R -> Q (in Ref. 2; BAC27119).
{ECO:0000305}.
CONFLICT 439 439 A -> T (in Ref. 2; BAE40919).
{ECO:0000305}.
CONFLICT 624 624 N -> S (in Ref. 2; BAE34876).
{ECO:0000305}.
CONFLICT 684 684 G -> V (in Ref. 2; BAC25849).
{ECO:0000305}.
STRAND 25 29 {ECO:0000244|PDB:1E32}.
STRAND 38 41 {ECO:0000244|PDB:1E32}.
HELIX 43 48 {ECO:0000244|PDB:1E32}.
STRAND 56 60 {ECO:0000244|PDB:1E32}.
HELIX 62 64 {ECO:0000244|PDB:3CF2}.
STRAND 66 73 {ECO:0000244|PDB:1E32}.
STRAND 75 77 {ECO:0000244|PDB:1S3S}.
STRAND 79 83 {ECO:0000244|PDB:1E32}.
HELIX 86 91 {ECO:0000244|PDB:1E32}.
STRAND 99 104 {ECO:0000244|PDB:1E32}.
STRAND 106 110 {ECO:0000244|PDB:2PJH}.
STRAND 114 119 {ECO:0000244|PDB:1E32}.
HELIX 120 122 {ECO:0000244|PDB:1E32}.
TURN 123 125 {ECO:0000244|PDB:1E32}.
HELIX 130 133 {ECO:0000244|PDB:1E32}.
HELIX 135 139 {ECO:0000244|PDB:1E32}.
TURN 140 142 {ECO:0000244|PDB:1S3S}.
STRAND 144 147 {ECO:0000244|PDB:1E32}.
STRAND 151 156 {ECO:0000244|PDB:1E32}.
STRAND 159 176 {ECO:0000244|PDB:1E32}.
STRAND 181 183 {ECO:0000244|PDB:1S3S}.
STRAND 193 195 {ECO:0000244|PDB:2PJH}.
STRAND 198 200 {ECO:0000244|PDB:3CF2}.
HELIX 203 205 {ECO:0000244|PDB:1E32}.
HELIX 211 225 {ECO:0000244|PDB:1E32}.
HELIX 227 232 {ECO:0000244|PDB:1E32}.
STRAND 240 244 {ECO:0000244|PDB:1E32}.
HELIX 251 261 {ECO:0000244|PDB:1E32}.
STRAND 265 269 {ECO:0000244|PDB:1E32}.
HELIX 271 274 {ECO:0000244|PDB:1E32}.
HELIX 281 295 {ECO:0000244|PDB:1E32}.
STRAND 298 305 {ECO:0000244|PDB:1E32}.
HELIX 306 308 {ECO:0000244|PDB:1E32}.
HELIX 312 315 {ECO:0000244|PDB:1E32}.
HELIX 321 333 {ECO:0000244|PDB:1E32}.
HELIX 337 339 {ECO:0000244|PDB:1S3S}.
STRAND 341 348 {ECO:0000244|PDB:1E32}.
HELIX 350 352 {ECO:0000244|PDB:1E32}.
HELIX 355 357 {ECO:0000244|PDB:1E32}.
STRAND 365 368 {ECO:0000244|PDB:1E32}.
HELIX 374 383 {ECO:0000244|PDB:1E32}.
TURN 384 387 {ECO:0000244|PDB:1E32}.
STRAND 388 390 {ECO:0000244|PDB:1S3S}.
HELIX 396 402 {ECO:0000244|PDB:1E32}.
HELIX 408 430 {ECO:0000244|PDB:1E32}.
HELIX 439 444 {ECO:0000244|PDB:1E32}.
HELIX 449 456 {ECO:0000244|PDB:1E32}.
STRAND 457 460 {ECO:0000244|PDB:3CF2}.
HELIX 476 478 {ECO:0000244|PDB:3CF0}.
HELIX 483 498 {ECO:0000244|PDB:3CF0}.
HELIX 500 506 {ECO:0000244|PDB:3CF0}.
STRAND 512 517 {ECO:0000244|PDB:3CF0}.
STRAND 519 523 {ECO:0000244|PDB:3CF0}.
HELIX 524 534 {ECO:0000244|PDB:3CF0}.
STRAND 538 542 {ECO:0000244|PDB:3CF0}.
HELIX 544 552 {ECO:0000244|PDB:3CF0}.
HELIX 558 568 {ECO:0000244|PDB:3CF0}.
STRAND 571 576 {ECO:0000244|PDB:3CF0}.
HELIX 581 585 {ECO:0000244|PDB:3CF0}.
TURN 586 590 {ECO:0000244|PDB:3CF0}.
HELIX 599 609 {ECO:0000244|PDB:3CF0}.
STRAND 615 624 {ECO:0000244|PDB:3CF0}.
HELIX 626 628 {ECO:0000244|PDB:3CF0}.
HELIX 631 634 {ECO:0000244|PDB:3CF0}.
TURN 636 638 {ECO:0000244|PDB:3CF2}.
STRAND 641 644 {ECO:0000244|PDB:3CF0}.
HELIX 650 661 {ECO:0000244|PDB:3CF0}.
HELIX 672 677 {ECO:0000244|PDB:3CF0}.
HELIX 684 706 {ECO:0000244|PDB:3CF0}.
HELIX 733 740 {ECO:0000244|PDB:3CF0}.
HELIX 749 762 {ECO:0000244|PDB:3CF0}.
SEQUENCE 806 AA; 89322 MW; 501B721D3A77BA8A CRC64;
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG
AGPSQGSGGG TGGSVYTEDN DDDLYG


Related products :

Catalog number Product name Quantity
EIAAB41970 15S Mg(2+)-ATPase p97 subunit,Rat,Rattus norvegicus,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,Vcp
EIAAB41971 15S Mg(2+)-ATPase p97 subunit,Bos taurus,Bovine,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,VCP
EIAAB41972 15S Mg(2+)-ATPase p97 subunit,Mouse,Mus musculus,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,Vcp
EIAAB41968 15S Mg(2+)-ATPase p97 subunit,Pig,Sus scrofa,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,VCP
EIAAB41969 15S Mg(2+)-ATPase p97 subunit,Homo sapiens,Human,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,VCP
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
H7813 Transitional endoplasmic reticulum ATPase (VCP), Rat, ELISA Kit 96T
H7812 Transitional endoplasmic reticulum ATPase (VCP), Pig, ELISA Kit 96T
CSB-EL025813RA Rat Transitional endoplasmic reticulum ATPase(VCP) ELISA kit 96T
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45631 Atp6ap1,Atp6ip1,Atp6s1,Mouse,Mus musculus,Protein C7-1,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
CSB-EL025813RA Rat Transitional endoplasmic reticulum ATPase(VCP) ELISA kit SpeciesRat 96T
CSB-EL025813PI Pig Transitional endoplasmic reticulum ATPase(VCP) ELISA kit SpeciesPig 96T
H7809 Transitional endoplasmic reticulum ATPase (VCP), Bovine, ELISA Kit 96T
H7810 Transitional endoplasmic reticulum ATPase (VCP), Human, ELISA Kit 96T
CSB-EL025813BO Bovine Transitional endoplasmic reticulum ATPase(VCP) ELISA kit 96T
H7811 Transitional endoplasmic reticulum ATPase (VCP), Mouse, ELISA Kit 96T
CSB-EL025813MO Mouse Transitional endoplasmic reticulum ATPase(VCP) ELISA kit 96T
E1161r Mouse ELISA Kit FOR Transitional endoplasmic reticulum ATPase 96T
CSB-EL025813HU Human Transitional endoplasmic reticulum ATPase(VCP) ELISA kit 96T
CSB-EL025813BO Bovine Transitional endoplasmic reticulum ATPase(VCP) ELISA kit SpeciesBovine 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur