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

 TERA_RAT                Reviewed;         806 AA.
P46462;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 167.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7806566; DOI=10.1083/jcb.127.6.1871;
Zhang L., Ashendel C.L., Becker G.W., Morre D.J.;
"Isolation and characterization of the principal ATPase associated
with transitional endoplasmic reticulum of rat liver.";
J. Cell Biol. 127:1871-1883(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[3]
PROTEIN SEQUENCE OF 46-53; 149-155; 192-210; 218-225; 240-251;
296-312; 366-386; 454-465; 616-638; 669-677 AND 701-709, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Diao W.;
Submitted (APR-2007) to UniProtKB.
[4]
INTERACTION WITH STX5A.
PubMed=9506515; DOI=10.1016/S0092-8674(00)81128-9;
Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.;
"Syntaxin 5 is a common component of the NSF- and p97-mediated
reassembly pathways of Golgi cisternae from mitotic Golgi fragments in
vitro.";
Cell 92:603-610(1998).
[5]
INTERACTION WITH NPLOC4; UFD1; NSFL1C AND UBE4B, AND SUBCELLULAR
LOCATION.
PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
"A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
ubiquitin and nuclear transport pathways.";
EMBO J. 19:2181-2192(2000).
[6]
FUNCTION.
PubMed=10930451; DOI=10.1091/mbc.11.8.2529;
Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A.,
Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.;
"Role of p97 and syntaxin 5 in the assembly of transitional
endoplasmic reticulum.";
Mol. Biol. Cell 11:2529-2542(2000).
[7]
INTERACTION WITH MEMBRANES.
PubMed=12146947; DOI=10.1021/bi0259195;
Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M.,
Hoekstra D.;
"Phospholipid species act as modulators in p97/p47-mediated fusion of
Golgi membranes.";
Biochemistry 41:9813-9823(2002).
[8]
FUNCTION, AND INTERACTION WITH NSFL1C; NAP1L4 AND UFD1.
PubMed=12411482; DOI=10.1093/emboj/cdf579;
Meyer H.H., Wang Y., Warren G.;
"Direct binding of ubiquitin conjugates by the mammalian p97 adaptor
complexes, p47 and Ufd1-Npl4.";
EMBO J. 21:5645-5652(2002).
[9]
INTERACTION WITH VCIP135.
PubMed=12473691; DOI=10.1083/jcb.200208112;
Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B.,
Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.;
"VCIP135, a novel essential factor for p97/p47-mediated membrane
fusion, is required for Golgi and ER assembly in vivo.";
J. Cell Biol. 159:855-866(2002).
[10]
PHOSPHORYLATION.
PubMed=12810701; DOI=10.1083/jcb.200303048;
Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M.,
Zhang X., Kondo H.;
"The localization and phosphorylation of p47 are important for Golgi
disassembly-assembly during the cell cycle.";
J. Cell Biol. 161:1067-1079(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-7, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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) (PubMed:10930451, PubMed:12411482).
Vesicle budding from the tER is an ATP-dependent process
(PubMed:10930451, PubMed:12411482). 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 (PubMed:10930451,
PubMed:12411482). 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
(By similarity). May play a role in the ubiquitin-dependent
sorting of membrane proteins to lysosomes where they undergo
degradation (By similarity). May more particularly play a role in
caveolins sorting in cells (By similarity).
{ECO:0000250|UniProtKB:P55072, ECO:0000269|PubMed:10930451,
ECO:0000269|PubMed:12411482}.
-!- 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. Interacts with
NSFL1C-like protein p37; the complex has membrane fusion activity
and is required for Golgi and endoplasmic reticulum biogenesis.
Interacts with RHBDD1 (via C-terminal domain). 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 SPRTN; leading to
recruitment to stalled replication forks. 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 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:P55072, ECO:0000250|UniProtKB:Q01853,
ECO:0000269|PubMed:10811609, ECO:0000269|PubMed:12411482,
ECO:0000269|PubMed:12473691, ECO:0000269|PubMed:9506515}.
-!- INTERACTION:
O35987:Nsfl1c; NbExp=12; IntAct=EBI-399011, EBI-1993760;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10811609}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P55072}. Nucleus
{ECO:0000269|PubMed:10811609}. 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 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:0000269|PubMed:12810701}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.
-!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in
the presence of ASPSCR1. Lys-315 methylation may decrease ATPase
activity. {ECO:0000250|UniProtKB:P55072}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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EMBL; U11760; AAC52154.1; -; mRNA.
EMBL; BC060518; AAH60518.1; -; mRNA.
PIR; A55190; A55190.
RefSeq; NP_446316.1; NM_053864.2.
UniGene; Rn.98891; -.
ProteinModelPortal; P46462; -.
SMR; P46462; -.
BioGrid; 250528; 24.
IntAct; P46462; 9.
MINT; MINT-1954391; -.
STRING; 10116.ENSRNOP00000040121; -.
iPTMnet; P46462; -.
PhosphoSitePlus; P46462; -.
World-2DPAGE; 0004:P46462; -.
PaxDb; P46462; -.
PRIDE; P46462; -.
Ensembl; ENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242.
GeneID; 116643; -.
KEGG; rno:116643; -.
UCSC; RGD:621595; rat.
CTD; 7415; -.
RGD; 621595; Vcp.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00890000139420; -.
HOGENOM; HOG000223224; -.
HOVERGEN; HBG001226; -.
InParanoid; P46462; -.
KO; K13525; -.
OMA; PIDDTTE; -.
OrthoDB; EOG091G024K; -.
PhylomeDB; P46462; -.
TreeFam; TF300542; -.
BRENDA; 3.6.4.6; 5301.
Reactome; R-RNO-110320; Translesion Synthesis by POLH.
Reactome; R-RNO-3371511; HSF1 activation.
Reactome; R-RNO-382556; ABC-family proteins mediated transport.
Reactome; R-RNO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
Reactome; R-RNO-5689877; Josephin domain DUBs.
Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P46462; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000034242; -.
Genevisible; P46462; RN.
GO; GO:1904949; C:ATPase complex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005811; C:lipid particle; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0000502; C:proteasome complex; IEA:Ensembl.
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:RGD.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0016887; F:ATPase activity; IDA:RGD.
GO; GO:1904288; F:BAT3 complex binding; IEA:Ensembl.
GO; GO:0035800; F:deubiquitinase activator activity; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0036435; F:K48-linked polyubiquitin binding; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IDA:RGD.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
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; IMP:RGD.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:Ensembl.
GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IEA:Ensembl.
GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; IEA:Ensembl.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IEA:Ensembl.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:RGD.
GO; GO:0031334; P:positive regulation of protein complex assembly; IEA:Ensembl.
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:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
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; IEA:Ensembl.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
GO; GO:0019079; P:viral genome replication; IEA:Ensembl.
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;
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.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P55072}.
CHAIN 2 806 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000084575.
NP_BIND 247 253 ATP. {ECO:0000250|UniProtKB:P55072}.
NP_BIND 521 526 ATP. {ECO:0000250|UniProtKB:Q01853}.
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:0000250|UniProtKB:P55072}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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:0000250|UniProtKB:P55072}.
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:0000250|UniProtKB:Q01853}.
MOD_RES 505 505 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 668 668 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 668 668 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 754 754 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 805 805 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01853}.
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}.
SEQUENCE 806 AA; 89349 MW; 501B721D205EBA8A 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 TGGNVYTEDN DDDLYG


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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


 

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