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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_HUMAN              Reviewed;         806 AA.
P55072; B2R5T8; Q0V924; Q2TAI5; Q969G7; Q9UCD5;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 195.
RecName: Full=Transitional endoplasmic reticulum ATPase;
Short=TER ATPase;
EC=3.6.4.6 {ECO:0000269|PubMed:26471729};
AltName: Full=15S Mg(2+)-ATPase p97 subunit;
AltName: Full=Valosin-containing protein;
Short=VCP;
Name=VCP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W.,
Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S.,
Phan H., Velasco N., Garnes J., Danganan L., Poundstone P.,
Christensen M., Georgescu A., Avila J., Liu S., Attix C., Andreise T.,
Trankheim M., Amico-Keller G., Coefield J., Duarte S., Lucas S.,
Bruce R., Thomas P., Quan G., Kronmiller B., Arellano A.,
Montgomery M., Ow D., Nolan M., Trong S., Kobayashi A., Olsen A.O.,
Carrano A.V.;
"Sequence analysis of a human P1 clone containing the XRCC9 DNA repair
gene.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
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).
[7]
PROTEIN SEQUENCE OF 2-25.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PROTEIN SEQUENCE OF 2-18; 148-155; 278-287; 296-312; 366-377; 466-487;
587-599; 639-651 AND 669-677, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 27-41 AND 233-238, AND INTERACTION WITH CLATHRIN.
TISSUE=Glial tumor;
PubMed=8413590; DOI=10.1038/365459a0;
Pleasure I.T., Black M.M., Keen J.H.;
"Valosin-containing protein, VCP, is a ubiquitous clathrin-binding
protein.";
Nature 365:459-462(1993).
[10]
PROTEIN SEQUENCE OF 46-53; 66-81; 96-109; 148-155; 240-251; 323-336;
454-502; 530-560; 600-614; 639-651; 678-693; 714-732 AND 754-766, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 314-322, IDENTIFICATION BY MASS SPECTROMETRY,
METHYLATION AT LYS-315, MUTAGENESIS OF LYS-315, CHARACTERIZATION OF
VARIANTS IBMPFD1 HIS-155 AND GLN-191, AND CHARACTERIZATION OF VARIANT
ALS14 GLY-159.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 388-483.
TISSUE=Fetal brain;
Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
"Characterization of different mRNA types expressed in human brain.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[13]
INTERACTION WITH NGLY1.
PubMed=15362974; DOI=10.1042/BJ20041498;
McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.;
"A novel UBA and UBX domain protein that binds polyubiquitin and VCP
and is a substrate for SAPKs.";
Biochem. J. 384:391-400(2004).
[14]
FUNCTION, INTERACTION WITH RNF19A, IDENTIFICATION BY MASS
SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-524.
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).
[15]
INTERACTION WITH SELENOS, AND SUBCELLULAR LOCATION.
PubMed=15215856; DOI=10.1038/nature02656;
Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.;
"A membrane protein complex mediates retro-translocation from the ER
lumen into the cytosol.";
Nature 429:841-847(2004).
[16]
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).
[17]
INTERACTION WITH SYVN1 AND DERL1.
PubMed=16289116; DOI=10.1016/j.jmb.2005.10.020;
Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S.,
Wiertz E., Koning F., Kloetzel P.-M., Seeger M.;
"The ubiquitin-domain protein HERP forms a complex with components of
the endoplasmic reticulum associated degradation pathway.";
J. Mol. Biol. 354:1021-1027(2005).
[18]
INTERACTION WITH AMFR, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF LYS-251 AND LYS-524.
PubMed=16168377; DOI=10.1016/j.molcel.2005.08.009;
Song B.L., Sever N., DeBose-Boyd R.A.;
"Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1
and couples sterol-regulated ubiquitination to degradation of HMG CoA
reductase.";
Mol. Cell 19:829-840(2005).
[19]
FUNCTION, AND INTERACTION WITH DERL1; AMFR; SYVN1 AND SELENOS.
PubMed=16186510; DOI=10.1073/pnas.0505006102;
Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E.,
Rapoport T.A.;
"Recruitment of the p97 ATPase and ubiquitin ligases to the site of
retrotranslocation at the endoplasmic reticulum membrane.";
Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005).
[20]
INTERACTION WITH DERL1 AND DERL2.
PubMed=16186509; DOI=10.1073/pnas.0505014102;
Lilley B.N., Ploegh H.L.;
"Multiprotein complexes that link dislocation, ubiquitination, and
extraction of misfolded proteins from the endoplasmic reticulum
membrane.";
Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005).
[21]
INTERACTION WITH CASR AND RNF19A.
PubMed=16513638; DOI=10.1074/jbc.M513552200;
Huang Y., Niwa J., Sobue G., Breitwieser G.E.;
"Calcium-sensing receptor ubiquitination and degradation mediated by
the E3 ubiquitin ligase dorfin.";
J. Biol. Chem. 281:11610-11617(2006).
[22]
INTERACTION WITH DERL1; DERL2 AND DERL3.
PubMed=16449189; DOI=10.1083/jcb.200507057;
Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.;
"Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein
response and are required for ER-associated degradation.";
J. Cell Biol. 172:383-393(2006).
[23]
INTERACTION WITH UBXN4.
PubMed=16968747; DOI=10.1242/jcs.03163;
Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A.,
Monteiro M.J.;
"Characterization of erasin (UBXD2): a new ER protein that promotes
ER-associated protein degradation.";
J. Cell Sci. 119:4011-4024(2006).
[24]
INTERACTION WITH TRIM13.
PubMed=17314412; DOI=10.1091/mbc.E06-03-0248;
Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R.,
Ponten F., Uhlen M., Hober S., Grander D., Sangfelt O.;
"The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin
ligase involved in ERAD.";
Mol. Biol. Cell 18:1670-1682(2007).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[26]
INTERACTION WITH RNF103.
PubMed=18675248; DOI=10.1016/j.bbrc.2008.07.126;
Maruyama Y., Yamada M., Takahashi K., Yamada M.;
"Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-
associated degradation pathway.";
Biochem. Biophys. Res. Commun. 374:737-741(2008).
[27]
INTERACTION WITH UBXN6.
PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008;
Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M.,
Hartmann-Petersen R.;
"Ubxd1 is a novel co-factor of the human p97 ATPase.";
Int. J. Biochem. Cell Biol. 40:2927-2942(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-436 AND SER-787,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[29]
INTERACTION WITH TRIM21.
PubMed=18022694; DOI=10.1016/j.molimm.2007.10.023;
Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M.,
Hatakeyama S.;
"Ro52 functionally interacts with IgG1 and regulates its quality
control via the ERAD system.";
Mol. Immunol. 45:2045-2054(2008).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[31]
INTERACTION WITH UBXN6.
PubMed=19174149; DOI=10.1016/j.bbrc.2009.01.076;
Kern M., Fernandez-Saiz V., Schaefer Z., Buchberger A.;
"UBXD1 binds p97 through two independent binding sites.";
Biochem. Biophys. Res. Commun. 380:303-307(2009).
[32]
INTERACTION WITH UBXN6.
PubMed=19275885; DOI=10.1016/j.bbrc.2009.03.012;
Nagahama M., Ohnishi M., Kawate Y., Matsui T., Miyake H., Yuasa K.,
Tani K., Tagaya M., Tsuji A.;
"UBXD1 is a VCP-interacting protein that is involved in ER-associated
degradation.";
Biochem. Biophys. Res. Commun. 382:303-308(2009).
[33]
INTERACTION WITH UBXN4, AND IDENTIFICATION IN A COMPLEX WITH UBQLN1
AND UBXN4.
PubMed=19822669; DOI=10.1083/jcb.200903024;
Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
"Ubiquilin and p97/VCP bind erasin, forming a complex involved in
ERAD.";
J. Cell Biol. 187:201-217(2009).
[34]
INTERACTION WITH YOD1.
PubMed=19818707; DOI=10.1016/j.molcel.2009.09.016;
Ernst R., Mueller B., Ploegh H.L., Schlieker C.;
"The otubain YOD1 is a deubiquitinating enzyme that associates with
p97 to facilitate protein dislocation from the ER.";
Mol. Cell 36:28-38(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3 AND SER-37, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770 AND SER-775, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[37]
INTERACTION WITH WASHC5.
PubMed=20833645; DOI=10.1093/brain/awq222;
Clemen C.S., Tangavelou K., Strucksberg K.H., Just S., Gaertner L.,
Regus-Leidig H., Stumpf M., Reimann J., Coras R., Morgan R.O.,
Fernandez M.P., Hofmann A., Muller S., Schoser B., Hanisch F.G.,
Rottbauer W., Blumcke I., von Horsten S., Eichinger L., Schroder R.;
"Strumpellin is a novel valosin-containing protein binding partner
linking hereditary spastic paraplegia to protein aggregation
diseases.";
Brain 133:2920-2941(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
FUNCTION IN OMM PROTEIN TURNOVER.
PubMed=21118995; DOI=10.1091/mbc.E10-09-0748;
Xu S., Peng G., Wang Y., Fang S., Karbowski M.;
"The AAA-ATPase p97 is essential for outer mitochondrial membrane
protein turnover.";
Mol. Biol. Cell 22:291-300(2011).
[41]
INTERACTION WITH BAG6.
PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
"A ubiquitin ligase-associated chaperone holdase maintains
polypeptides in soluble states for proteasome degradation.";
Mol. Cell 42:758-770(2011).
[42]
FUNCTION, INTERACTION WITH CAV1 AND UBXN6, CHARACTERIZATION OF
VARIANTS IBMPFD1 GLY-95; HIS-155 AND GLU-232, AND MUTAGENESIS OF
GLU-578.
PubMed=21822278; DOI=10.1038/ncb2301;
Ritz D., Vuk M., Kirchner P., Bug M., Schuetz S., Hayer A., Bremer S.,
Lusk C., Baloh R.H., Lee H., Glatter T., Gstaiger M., Aebersold R.,
Weihl C.C., Meyer H.;
"Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP
and UBXD1 and impaired by VCP disease mutations.";
Nat. Cell Biol. 13:1116-1123(2011).
[43]
FUNCTION.
PubMed=22020440; DOI=10.1038/ncb2367;
Meerang M., Ritz D., Paliwal S., Garajova Z., Bosshard M., Mailand N.,
Janscak P., Hubscher U., Meyer H., Ramadan K.;
"The ubiquitin-selective segregase VCP/p97 orchestrates the response
to DNA double-strand breaks.";
Nat. Cell Biol. 13:1376-1382(2011).
[44]
FUNCTION, INTERACTION WITH L3MBTL1, AND SUBCELLULAR LOCATION.
PubMed=22120668; DOI=10.1038/nsmb.2188;
Acs K., Luijsterburg M.S., Ackermann L., Salomons F.A., Hoppe T.,
Dantuma N.P.;
"The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1
from DNA double-strand breaks.";
Nat. Struct. Mol. Biol. 18:1345-1350(2011).
[45]
INTERACTION WITH UBXN8.
PubMed=21949850; DOI=10.1371/journal.pone.0025061;
Madsen L., Kriegenburg F., Vala A., Best D., Prag S., Hofmann K.,
Seeger M., Adams I.R., Hartmann-Petersen R.;
"The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic
reticulum membrane for degradation of misfolded proteins.";
PLoS ONE 6:E25061-E25061(2011).
[46]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[47]
INTERACTION WITH UBXN7.
PubMed=22537386; DOI=10.1186/1741-7007-10-36;
Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G.;
"UBXN7 docks on neddylated cullin complexes using its UIM motif and
causes HIF1alpha accumulation.";
BMC Biol. 10:36-36(2012).
[48]
INTERACTION WITH RHBDD1, MUTAGENESIS OF LYS-251; LYS-524 AND GLU-578,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22795130; DOI=10.1016/j.molcel.2012.06.008;
Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L.,
Lemberg M.K.;
"Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of
membrane proteins.";
Mol. Cell 47:558-569(2012).
[49]
INTERACTION WITH SPRTN.
PubMed=22902628; DOI=10.1074/jbc.M112.400135;
Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.;
"Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is
a regulator of translesion synthesis.";
J. Biol. Chem. 287:34225-34233(2012).
[50]
FUNCTION IN ERAD PATHWAY.
PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015;
Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T.,
Nishitoh H., Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M.,
Chosa K., Koga T., Morino-Koga S., Wada I., Kai H.;
"STT3B-dependent posttranslational N-glycosylation as a surveillance
system for secretory protein.";
Mol. Cell 47:99-110(2012).
[51]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[52]
METHYLATION AT LYS-315, AND MUTAGENESIS OF LYS-312; ARG-313; GLU-314;
LYS-315; THR-316; HIS-317 AND GLY-318.
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).
[53]
FUNCTION, AND INTERACTION WITH SPRTN.
PubMed=23042607; DOI=10.1038/nsmb.2394;
Davis E.J., Lachaud C., Appleton P., Macartney T.J., Nathke I.,
Rouse J.;
"DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA
damage.";
Nat. Struct. Mol. Biol. 19:1093-1100(2012).
[54]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPRTN.
PubMed=23042605; DOI=10.1038/nsmb.2395;
Mosbech A., Gibbs-Seymour I., Kagias K., Thorslund T., Beli P.,
Povlsen L., Nielsen S.V., Smedegaard S., Sedgwick G., Lukas C.,
Hartmann-Petersen R., Lukas J., Choudhary C., Pocock R.,
Bekker-Jensen S., Mailand N.;
"DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes
ubiquitin-dependent responses to replication blocks.";
Nat. Struct. Mol. Biol. 19:1084-1092(2012).
[55]
FUNCTION.
PubMed=23335559; DOI=10.1074/jbc.M112.429076;
Kirchner P., Bug M., Meyer H.;
"Ubiquitination of the N-terminal region of caveolin-1 regulates
endosomal sorting by the VCP/p97 AAA-ATPase.";
J. Biol. Chem. 288:7363-7372(2013).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-7; SER-13;
SER-462 AND SER-702, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[57]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[58]
INTERACTION WITH RNF31.
PubMed=24726327; DOI=10.1016/j.molcel.2014.03.016;
Schaeffer V., Akutsu M., Olma M.H., Gomes L.C., Kawasaki M., Dikic I.;
"Binding of OTULIN to the PUB domain of HOIP controls NF-kappaB
signaling.";
Mol. Cell 54:349-361(2014).
[59]
FUNCTION.
PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047;
Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P.,
Kato H., Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H.,
Nishitoh H.;
"Pre-emptive quality control protects the ER from protein overload via
the proximity of ERAD components and SRP.";
Cell Rep. 13:944-956(2015).
[60]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DDX58 AND RNF125, AND
MUTAGENESIS OF 52-PHE--ASP-55; TYR-110; GLU-305 AND GLU-578.
PubMed=26471729; DOI=10.15252/embj.201591888;
Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
"A non-canonical role of the p97 complex in RIG-I antiviral
signaling.";
EMBO J. 34:2903-2920(2015).
[61]
INTERACTION WITH UBXN10.
PubMed=26389662; DOI=10.1038/ncb3238;
Raman M., Sergeev M., Garnaas M., Lydeard J.R., Huttlin E.L.,
Goessling W., Shah J.V., Harper J.W.;
"Systematic proteomics of the VCP-UBXD adaptor network identifies a
role for UBXN10 in regulating ciliogenesis.";
Nat. Cell Biol. 17:1356-1369(2015).
[62]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[63]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-18, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[64]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-481 IN COMPLEX WITH ATP
ANALOG, CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155,
MUTAGENESIS OF ARG-53 AND ARG-86, AND SUBUNIT.
PubMed=20512113; DOI=10.1038/emboj.2010.104;
Tang W.K., Li D., Li C.C., Esser L., Dai R., Guo L., Xia D.;
"A novel ATP-dependent conformation in p97 N-D1 fragment revealed by
crystal structures of disease-related mutants.";
EMBO J. 29:2217-2229(2010).
[65]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 797-806 IN COMPLEX WITH PLAA.
PubMed=19887378; DOI=10.1074/jbc.M109.044685;
Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A.,
Akutsu M., Piper R., Dhe-Paganon S.;
"Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.";
J. Biol. Chem. 285:365-372(2010).
[66]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-187 IN COMPLEX WITH AMFR.
PubMed=21914798; DOI=10.1074/jbc.M111.274506;
Hanzelmann P., Schindelin H.;
"The structural and functional basis of the p97/valosin-containing
protein (VCP)-interacting motif (VIM): mutually exclusive binding of
cofactors to the N-terminal domain of p97.";
J. Biol. Chem. 286:38679-38690(2011).
[67]
VARIANTS IBMPFD1 GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND
GLU-232.
PubMed=15034582; DOI=10.1038/ng1332;
Watts G.D.J., Wymer J., Kovach M.J., Mehta S.G., Mumm S., Darvish D.,
Pestronk A., Whyte M.P., Kimonis V.E.;
"Inclusion body myopathy associated with Paget disease of bone and
frontotemporal dementia is caused by mutant valosin-containing
protein.";
Nat. Genet. 36:377-381(2004).
[68]
VARIANT IBMPFD1 CYS-155.
PubMed=15732117; DOI=10.1002/ana.20407;
Schroeder R., Watts G.D.J., Mehta S.G., Evert B.O., Broich P.,
Fliessbach K., Pauls K., Hans V.H., Kimonis V., Thal D.R.;
"Mutant valosin-containing protein causes a novel type of
frontotemporal dementia.";
Ann. Neurol. 57:457-461(2005).
[69]
VARIANT IBMPFD1 HIS-159.
PubMed=16247064; DOI=10.1212/01.wnl.0000180407.15369.92;
Haubenberger D., Bittner R.E., Rauch-Shorny S., Zimprich F.,
Mannhalter C., Wagner L., Mineva I., Vass K., Auff E., Zimprich A.;
"Inclusion body myopathy and Paget disease is linked to a novel
mutation in the VCP gene.";
Neurology 65:1304-1305(2005).
[70]
CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155.
PubMed=16321991; DOI=10.1093/hmg/ddi426;
Weihl C.C., Dalal S., Pestronk A., Hanson P.I.;
"Inclusion body myopathy-associated mutations in p97/VCP impair
endoplasmic reticulum-associated degradation.";
Hum. Mol. Genet. 15:189-199(2006).
[71]
VARIANTS IBMPFD1 TRP-198 AND HIS-387.
PubMed=17935506; DOI=10.1111/j.1399-0004.2007.00887.x;
Watts G.D., Thomasova D., Ramdeen S.K., Fulchiero E.C., Mehta S.G.,
Drachman D.A., Weihl C.C., Jamrozik Z., Kwiecinski H., Kaminska A.,
Kimonis V.E.;
"Novel VCP mutations in inclusion body myopathy associated with Paget
disease of bone and frontotemporal dementia.";
Clin. Genet. 72:420-426(2007).
[72]
CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; SER-155 AND GLU-232,
MUTAGENESIS OF GLU-305 AND GLU-578, AND FUNCTION.
PubMed=20104022; DOI=10.4161/auto.6.2.11014;
Tresse E., Salomons F.A., Vesa J., Bott L.C., Kimonis V., Yao T.P.,
Dantuma N.P., Taylor J.P.;
"VCP/p97 is essential for maturation of ubiquitin-containing
autophagosomes and this function is impaired by mutations that cause
IBMPFD.";
Autophagy 6:217-227(2010).
[73]
VARIANTS IBMPFD1 LEU-155 AND TRP-198.
PubMed=20335036; DOI=10.1016/j.nmd.2010.03.002;
Kumar K.R., Needham M., Mina K., Davis M., Brewer J., Staples C.,
Ng K., Sue C.M., Mastaglia F.L.;
"Two Australian families with inclusion-body myopathy, Paget's disease
of bone and frontotemporal dementia: novel clinical and genetic
findings.";
Neuromuscul. Disord. 20:330-334(2010).
[74]
VARIANTS ALS14 HIS-155; GLY-159; GLN-191 AND ASN-592.
PubMed=21145000; DOI=10.1016/j.neuron.2010.11.036;
Johnson J.O., Mandrioli J., Benatar M., Abramzon Y., Van Deerlin V.M.,
Trojanowski J.Q., Gibbs J.R., Brunetti M., Gronka S., Wuu J., Ding J.,
McCluskey L., Martinez-Lage M., Falcone D., Hernandez D.G.,
Arepalli S., Chong S., Schymick J.C., Rothstein J., Landi F.,
Wang Y.D., Calvo A., Mora G., Sabatelli M., Monsurro M.R.,
Battistini S., Salvi F., Spataro R., Sola P., Borghero G., Galassi G.,
Scholz S.W., Taylor J.P., Restagno G., Chio A., Traynor B.J.;
"Exome sequencing reveals VCP mutations as a cause of familial ALS.";
Neuron 68:857-864(2010).
[75]
VARIANT CMT2Y LYS-185, CHARACTERIZATION OF VARIANT CMT2Y LYS-185, AND
CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155 AND GLU-232.
PubMed=25125609; DOI=10.1093/brain/awu224;
Gonzalez M.A., Feely S.M., Speziani F., Strickland A.V., Danzi M.,
Bacon C., Lee Y., Chou T.F., Blanton S.H., Weihl C.C., Zuchner S.,
Shy M.E.;
"A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease.";
Brain 137:2897-2902(2014).
[76]
VARIANT CMT2Y GLU-97, CHARACTERIZATION OF VARIANT CMT2Y GLU-97, AND
CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; TRP-198 AND GLU-232.
PubMed=25878907; DOI=10.1155/2015/239167;
Jerath N.U., Crockett C.D., Moore S.A., Shy M.E., Weihl C.C.,
Chou T.F., Grider T., Gonzalez M.A., Zuchner S., Swenson A.;
"Rare Manifestation of a c.290 C>T, p.Gly97Glu VCP Mutation.";
Case. Rep. Genet. 2015:239167-239167(2015).
[77]
VARIANT IBMPFD1 PHE-126.
PubMed=27209344; DOI=10.1016/j.nmd.2016.05.001;
Matsubara S., Shimizu T., Komori T., Mori-Yoshimura M., Minami N.,
Hayashi Y.K.;
"Nuclear inclusions mimicking poly(A)-binding protein nuclear 1
inclusions in a case of inclusion body myopathy associated with Paget
disease of bone and frontotemporal dementia with a novel mutation in
the valosin-containing protein gene.";
Neuromuscul. Disord. 26:436-440(2016).
[78]
FUNCTION, INTERACTION WITH PLAA; UBXN6 AND YOD1, SUBCELLULAR LOCATION,
CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; TRP-198 AND GLU-232, AND
MUTAGENESIS OF GLU-578.
PubMed=27753622; DOI=10.15252/embj.201695148;
Papadopoulos C., Kirchner P., Bug M., Grum D., Koerver L., Schulze N.,
Poehler R., Dressler A., Fengler S., Arhzaouy K., Lux V., Ehrmann M.,
Weihl C.C., Meyer H.;
"VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of
ruptured lysosomes by autophagy.";
EMBO J. 36:135-150(2017).
-!- 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 (PubMed:26565908). 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 (PubMed:22020440, PubMed:22120668).
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 (PubMed:23042607,
PubMed:23042605). Required for cytoplasmic retrotranslocation of
stressed/damaged mitochondrial outer-membrane proteins and their
subsequent proteasomal degradation (PubMed:16186510,
PubMed:21118995). Essential for the maturation of ubiquitin-
containing autophagosomes and the clearance of ubiquitinated
protein by autophagy (PubMed:20104022, PubMed:27753622). 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 (PubMed:26471729). May play a role in
the ubiquitin-dependent sorting of membrane proteins to lysosomes
where they undergo degradation (PubMed:21822278). May more
particularly play a role in caveolins sorting in cells
(PubMed:21822278, PubMed:23335559). {ECO:0000269|PubMed:15456787,
ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16186510,
ECO:0000269|PubMed:20104022, ECO:0000269|PubMed:21118995,
ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:22020440,
ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22607976,
ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607,
ECO:0000269|PubMed:23335559, ECO:0000269|PubMed:26471729,
ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:27753622}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:26471729}.
-!- 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 (PubMed:26471729). 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 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 RHBDD1 (via
C-terminal domain). Interacts with SPRTN; leading to recruitment
to stalled replication forks (PubMed:23042607, PubMed:23042605).
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.
Interacts (via the PIM motif) with RNF31 (via the PUB domain)
(PubMed:24726327). 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
(PubMed:26471729). Interacts with BAG6 (PubMed:21636303).
Interacts with UBXN10 (PubMed:26389662). Interacts with UBXN6; the
interaction with UBXN6 is direct and competitive with UFD1
(PubMed:19174149, PubMed:19275885). Forms a ternary complex with
CAV1 and UBXN6 (PubMed:21822278, PubMed:18656546,
PubMed:19174149). Interacts with PLAA, UBXN6 and YOD1; may form a
complex involved in macroautophagy (PubMed:27753622).
{ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:Q01853,
ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:15362974,
ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377,
ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16186510,
ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16449189,
ECO:0000269|PubMed:16513638, ECO:0000269|PubMed:16968747,
ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:18022694,
ECO:0000269|PubMed:18656546, ECO:0000269|PubMed:18675248,
ECO:0000269|PubMed:19174149, ECO:0000269|PubMed:19275885,
ECO:0000269|PubMed:19818707, ECO:0000269|PubMed:19822669,
ECO:0000269|PubMed:19887378, ECO:0000269|PubMed:20512113,
ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:21636303,
ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:21914798,
ECO:0000269|PubMed:21949850, ECO:0000269|PubMed:22120668,
ECO:0000269|PubMed:22537386, ECO:0000269|PubMed:22795130,
ECO:0000269|PubMed:22902628, ECO:0000269|PubMed:23042605,
ECO:0000269|PubMed:23042607, ECO:0000269|PubMed:24726327,
ECO:0000269|PubMed:26389662, ECO:0000269|PubMed:26471729,
ECO:0000269|PubMed:27753622, ECO:0000269|PubMed:8413590}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-355164, EBI-355164;
Q9UKV5:AMFR; NbExp=10; IntAct=EBI-355164, EBI-1046367;
Q9BZE9:ASPSCR1; NbExp=6; IntAct=EBI-355164, EBI-1993677;
P54252:ATXN3; NbExp=8; IntAct=EBI-355164, EBI-946046;
P54252-1:ATXN3; NbExp=10; IntAct=EBI-355164, EBI-946068;
O96017:CHEK2; NbExp=2; IntAct=EBI-355164, EBI-1180783;
Q9WTX6:Cul1 (xeno); NbExp=2; IntAct=EBI-355164, EBI-1551052;
Q13619:CUL4A; NbExp=2; IntAct=EBI-355164, EBI-456106;
Q9UNN5-1:FAF1; NbExp=4; IntAct=EBI-355164, EBI-15930546;
Q96CS3:FAF2; NbExp=3; IntAct=EBI-355164, EBI-1055805;
O94868:FCHSD2; NbExp=2; IntAct=EBI-355164, EBI-1215612;
P62993:GRB2; NbExp=3; IntAct=EBI-355164, EBI-401755;
Q9UNZ2:NSFL1C; NbExp=8; IntAct=EBI-355164, EBI-721577;
P07602-1:PSAP; NbExp=3; IntAct=EBI-355164, EBI-10635648;
P26045:PTPN3; NbExp=2; IntAct=EBI-355164, EBI-1047946;
P32969:RPL9P9; NbExp=4; IntAct=EBI-355164, EBI-358122;
B1AQ61:UBE4B; NbExp=4; IntAct=EBI-355164, EBI-7931266;
P68543:UBXN2A; NbExp=3; IntAct=EBI-355164, EBI-1993668;
Q14CS0:UBXN2B; NbExp=4; IntAct=EBI-355164, EBI-1993619;
Q92575:UBXN4; NbExp=2; IntAct=EBI-355164, EBI-723441;
Q9BZV1:UBXN6; NbExp=7; IntAct=EBI-355164, EBI-1993899;
O94888:UBXN7; NbExp=19; IntAct=EBI-355164, EBI-1993627;
Q92890:UFD1; NbExp=5; IntAct=EBI-355164, EBI-1994090;
P63104:YWHAZ; NbExp=2; IntAct=EBI-355164, EBI-347088;
P24278:ZBTB25; NbExp=4; IntAct=EBI-355164, EBI-739899;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:15456787}. Endoplasmic reticulum
{ECO:0000269|PubMed:15215856}. Nucleus
{ECO:0000269|PubMed:23042605}. Note=Present in the neuronal
hyaline inclusion bodies specifically found in motor neurons from
amyotrophic lateral sclerosis patients (PubMed:15456787). Present
in the Lewy bodies specifically found in neurons from Parkinson
disease patients (PubMed:15456787). Recruited to the cytoplasmic
surface of the endoplasmic reticulum via interaction with
AMFR/gp78 (PubMed:16168377). Following DNA double-strand breaks,
recruited to the sites of damage (PubMed:22120668). Recruited to
stalled replication forks via interaction with SPRTN
(PubMed:23042605). Recruited to damaged lysosomes decorated with
K48-linked ubiquitin chains (PubMed:27753622).
{ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377,
ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:23042605,
ECO:0000269|PubMed:27753622}.
-!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction
with the PUB domain of RNF31. {ECO:0000269|PubMed:24726327}.
-!- 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. {ECO:0000269|PubMed:22948820,
ECO:0000269|PubMed:23349634}.
-!- DISEASE: Inclusion body myopathy with early-onset Paget disease
with or without frontotemporal dementia 1 (IBMPFD1) [MIM:167320]:
An autosomal dominant disease characterized by disabling muscle
weakness clinically resembling to limb girdle muscular dystrophy,
osteolytic bone lesions consistent with Paget disease, and
premature frontotemporal dementia. Clinical features show
incomplete penetrance. {ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:15732117, ECO:0000269|PubMed:16247064,
ECO:0000269|PubMed:16321991, ECO:0000269|PubMed:17935506,
ECO:0000269|PubMed:20104022, ECO:0000269|PubMed:20335036,
ECO:0000269|PubMed:20512113, ECO:0000269|PubMed:21822278,
ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:25125609,
ECO:0000269|PubMed:25878907, ECO:0000269|PubMed:27209344,
ECO:0000269|PubMed:27753622}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Amyotrophic lateral sclerosis 14, with or without
frontotemporal dementia (ALS14) [MIM:613954]: A neurodegenerative
disorder affecting upper motor neurons in the brain and lower
motor neurons in the brain stem and spinal cord, resulting in
fatal paralysis. Sensory abnormalities are absent. The pathologic
hallmarks of the disease include pallor of the corticospinal tract
due to loss of motor neurons, presence of ubiquitin-positive
inclusions within surviving motor neurons, and deposition of
pathologic aggregates. The etiology of amyotrophic lateral
sclerosis is likely to be multifactorial, involving both genetic
and environmental factors. The disease is inherited in 5-10% of
the cases. Patients with ALS14 may develop frontotemporal
dementia. {ECO:0000269|PubMed:21145000,
ECO:0000269|PubMed:23349634}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2Y (CMT2Y) [MIM:616687]: An
autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Neuropathies of the CMT2 group are
characterized by signs of axonal degeneration in the absence of
obvious myelin alterations, normal or slightly reduced nerve
conduction velocities, and progressive distal muscle weakness and
atrophy. {ECO:0000269|PubMed:25125609,
ECO:0000269|PubMed:25878907}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- CAUTION: It is unclear how it participates in the recruitment of
TP53BP1 at DNA damage sites. According to a first report,
participates in the recruitment of TP53BP1 by promoting
ubiquitination and removal of L3MBTL1 from DNA damage sites
(PubMed:22120668). According to a second report, it acts by
removing 'Lys-48'-linked ubiquitination from sites of DNA damage
(PubMed:22020440). {ECO:0000305|PubMed:22020440,
ECO:0000305|PubMed:22120668}.
-----------------------------------------------------------------------
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EMBL; AC004472; AAC07984.1; -; Genomic_DNA.
EMBL; AF100752; AAD43016.1; -; mRNA.
EMBL; AK312310; BAG35235.1; -; mRNA.
EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58404.1; -; Genomic_DNA.
EMBL; BC110913; AAI10914.1; -; mRNA.
EMBL; BC121794; AAI21795.1; -; mRNA.
EMBL; Z70768; CAA94809.1; -; mRNA.
CCDS; CCDS6573.1; -.
PIR; T02243; T02243.
RefSeq; NP_009057.1; NM_007126.3.
UniGene; Hs.529782; -.
PDB; 3EBB; X-ray; 1.90 A; E/F/G/H=797-806.
PDB; 3HU1; X-ray; 2.81 A; A/B/C/D/E/F=1-481.
PDB; 3HU2; X-ray; 2.85 A; A/B/C/D/E/F=1-481.
PDB; 3HU3; X-ray; 2.20 A; A/B=1-481.
PDB; 3QC8; X-ray; 2.20 A; A=21-196.
PDB; 3QQ7; X-ray; 2.65 A; A=2-187.
PDB; 3QQ8; X-ray; 2.00 A; A=2-187.
PDB; 3QWZ; X-ray; 2.00 A; A=1-208.
PDB; 3TIW; X-ray; 1.80 A; A/B=1-187.
PDB; 4KDI; X-ray; 1.86 A; A/B=21-196.
PDB; 4KDL; X-ray; 1.81 A; A=21-196.
PDB; 4KLN; X-ray; 2.62 A; A/B/C/D/E/F=1-481.
PDB; 4KO8; X-ray; 1.98 A; A/B=1-481.
PDB; 4KOD; X-ray; 2.96 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
PDB; 4P0A; X-ray; 2.30 A; B/D=797-806.
PDB; 5B6C; X-ray; 1.55 A; A=21-191.
PDB; 5C18; X-ray; 3.30 A; A/B/C/D/E/F=2-806.
PDB; 5C19; X-ray; 4.20 A; A/B/C/D/E/F=2-806.
PDB; 5C1A; X-ray; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-806.
PDB; 5C1B; X-ray; 3.08 A; A/B/C/D/E/F=2-806.
PDB; 5DYG; X-ray; 2.20 A; A=1-460.
PDB; 5DYI; X-ray; 3.71 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
PDB; 5EPP; X-ray; 1.88 A; A=21-199.
PDB; 5FTJ; EM; 2.30 A; A/B/C/D/E/F=1-806.
PDB; 5FTK; EM; 2.40 A; A/B/C/D/E/F=1-806.
PDB; 5FTL; EM; 3.30 A; A/B/C/D/E/F=1-806.
PDB; 5FTM; EM; 3.20 A; A/B/C/D/E/F=1-806.
PDB; 5FTN; EM; 3.30 A; A/B/C/D/E/F=1-806.
PDB; 5GLF; X-ray; 2.25 A; A/C/E/G=21-199.
PDB; 5IFS; X-ray; 2.46 A; B/D=1-481.
PDB; 5IFW; X-ray; 3.40 A; B=2-806.
PDB; 5X4L; X-ray; 2.40 A; A/B=23-196.
PDBsum; 3EBB; -.
PDBsum; 3HU1; -.
PDBsum; 3HU2; -.
PDBsum; 3HU3; -.
PDBsum; 3QC8; -.
PDBsum; 3QQ7; -.
PDBsum; 3QQ8; -.
PDBsum; 3QWZ; -.
PDBsum; 3TIW; -.
PDBsum; 4KDI; -.
PDBsum; 4KDL; -.
PDBsum; 4KLN; -.
PDBsum; 4KO8; -.
PDBsum; 4KOD; -.
PDBsum; 4P0A; -.
PDBsum; 5B6C; -.
PDBsum; 5C18; -.
PDBsum; 5C19; -.
PDBsum; 5C1A; -.
PDBsum; 5C1B; -.
PDBsum; 5DYG; -.
PDBsum; 5DYI; -.
PDBsum; 5EPP; -.
PDBsum; 5FTJ; -.
PDBsum; 5FTK; -.
PDBsum; 5FTL; -.
PDBsum; 5FTM; -.
PDBsum; 5FTN; -.
PDBsum; 5GLF; -.
PDBsum; 5IFS; -.
PDBsum; 5IFW; -.
PDBsum; 5X4L; -.
ProteinModelPortal; P55072; -.
SMR; P55072; -.
BioGrid; 113258; 608.
CORUM; P55072; -.
DIP; DIP-33543N; -.
IntAct; P55072; 102.
MINT; MINT-272884; -.
STRING; 9606.ENSP00000351777; -.
BindingDB; P55072; -.
ChEMBL; CHEMBL1075145; -.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
iPTMnet; P55072; -.
PhosphoSitePlus; P55072; -.
SwissPalm; P55072; -.
BioMuta; VCP; -.
DMDM; 6094447; -.
DOSAC-COBS-2DPAGE; P55072; -.
OGP; P55072; -.
REPRODUCTION-2DPAGE; IPI00022774; -.
REPRODUCTION-2DPAGE; P55072; -.
EPD; P55072; -.
PaxDb; P55072; -.
PeptideAtlas; P55072; -.
PRIDE; P55072; -.
TopDownProteomics; P55072; -.
Ensembl; ENST00000358901; ENSP00000351777; ENSG00000165280.
GeneID; 7415; -.
KEGG; hsa:7415; -.
CTD; 7415; -.
DisGeNET; 7415; -.
EuPathDB; HostDB:ENSG00000165280.15; -.
GeneCards; VCP; -.
GeneReviews; VCP; -.
HGNC; HGNC:12666; VCP.
HPA; CAB005593; -.
HPA; HPA012728; -.
HPA; HPA012814; -.
MalaCards; VCP; -.
MIM; 167320; phenotype.
MIM; 601023; gene.
MIM; 613954; phenotype.
MIM; 616687; phenotype.
neXtProt; NX_P55072; -.
OpenTargets; ENSG00000165280; -.
Orphanet; 329478; Adult-onset distal myopathy due to VCP mutation.
Orphanet; 803; Amyotrophic lateral sclerosis.
Orphanet; 275864; Behavioral variant of frontotemporal dementia.
Orphanet; 275872; Frontotemporal dementia with motor neuron disease.
Orphanet; 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
Orphanet; 100070; Progressive non-fluent aphasia.
Orphanet; 100069; Semantic dementia.
Orphanet; 329475; Spastic paraplegia - Paget disease of bone.
PharmGKB; PA37289; -.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00900000141071; -.
HOGENOM; HOG000223224; -.
HOVERGEN; HBG001226; -.
InParanoid; P55072; -.
KO; K13525; -.
OMA; PIDDTTE; -.
OrthoDB; EOG091G024K; -.
PhylomeDB; P55072; -.
TreeFam; TF300542; -.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-3371511; HSF1 activation.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5689877; Josephin domain DUBs.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8876725; Protein methylation.
SignaLink; P55072; -.
SIGNOR; P55072; -.
ChiTaRS; VCP; human.
EvolutionaryTrace; P55072; -.
GeneWiki; Valosin-containing_protein; -.
GenomeRNAi; 7415; -.
PRO; PR:P55072; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000165280; -.
CleanEx; HS_VCP; -.
ExpressionAtlas; P55072; baseline and differential.
Genevisible; P55072; HS.
GO; GO:1904949; C:ATPase complex; IEA:Ensembl.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0005811; C:lipid droplet; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0000502; C:proteasome complex; IDA:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISS:ParkinsonsUK-UCL.
GO; GO:1990730; C:VCP-NSFL1C complex; ISS:ParkinsonsUK-UCL.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IMP:UniProtKB.
GO; GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0035800; F:deubiquitinase activator activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein 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:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL.
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; ISS:UniProtKB.
GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; IMP:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:UniProtKB.
GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0036503; P:ERAD pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0045184; P:establishment of protein localization; TAS:UniProtKB.
GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
GO; GO:0006734; P:NADH metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0034214; P:protein hexamerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0006479; P:protein methylation; TAS:Reactome.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:UniProtKB.
GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
GO; GO:0019079; P:viral genome replication; IMP:CACAO.
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; Amyotrophic lateral sclerosis; ATP-binding;
Autophagy; Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA damage; DNA repair;
Endoplasmic reticulum; Hydrolase; Isopeptide bond; Lipid-binding;
Methylation; Neurodegeneration; Neuropathy; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Transport;
Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.8}.
CHAIN 2 806 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000084572.
NP_BIND 247 253 ATP. {ECO:0000269|PubMed:20512113}.
NP_BIND 521 526 ATP. {ECO:0000250|UniProtKB:Q01853}.
REGION 797 806 Interaction with UBXN6.
{ECO:0000269|PubMed:18656546}.
MOTIF 802 806 PIM motif. {ECO:0000269|PubMed:24726327}.
BINDING 348 348 ATP. {ECO:0000269|PubMed:20512113}.
BINDING 384 384 ATP. {ECO:0000269|PubMed:20512113}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 315 315 N6,N6,N6-trimethyllysine; by VCPKMT.
{ECO:0000269|PubMed:22948820,
ECO:0000269|PubMed:23349634}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
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:0000244|PubMed:23186163}.
MOD_RES 754 754 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 805 805 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01853}.
CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 95 95 R -> G (in IBMPFD1; cultured cells
expressing the mutant protein show a
marked general increase in the level of
ubiquitin-conjugated proteins and
impaired protein degradation through the
endoplasmic reticulum-associated
degradation (ERAD) pathway; shows
strongly reduced affinity for ADP and
increased affinity for ATP; abolishes
enhancement of K-315 methylation by
ASPSCR1; decreased interaction with CAV1
and UBXN6; dbSNP:rs121909332).
{ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:16321991,
ECO:0000269|PubMed:20512113,
ECO:0000269|PubMed:21822278}.
/FTId=VAR_033016.
VARIANT 97 97 G -> E (in CMT2Y; increased ATPase
activity; dbSNP:rs864309502).
{ECO:0000269|PubMed:25878907}.
/FTId=VAR_076464.
VARIANT 126 126 I -> F (in IBMPFD1; unknown pathological
significance).
{ECO:0000269|PubMed:27209344}.
/FTId=VAR_076465.
VARIANT 155 155 R -> C (in IBMPFD1; also in one patient
without evidence of Paget disease of the
bone; dbSNP:rs121909330).
{ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:15732117}.
/FTId=VAR_033017.
VARIANT 155 155 R -> H (in ALS14 and IBMPFD1; ALS14
patients do not manifest frontotemporal
dementia; properly assembles into a
hexameric structure; cultured cells
expressing the mutant protein show a
marked general increase in the level of
ubiquitin-conjugated proteins and
impaired protein degradation through the
endoplasmic reticulum-associated
degradation (ERAD) pathway; shows
strongly reduced affinity for ADP and
increased affinity for ATP; shows normal
ATPase activity according to
PubMed:16321991 while according to
PubMed:25878907 and PubMed:25125609 shows
increased ATPase activity; no defect in
ubiquitin-dependent protein degradation
by the proteasome; impaired autophagic
function; defective maturation of
ubiquitin-containing autophagosomes;
decreased interaction with CAV1 and
UBXN6; decreased endosome to lysosome
transport via multivesicular body sorting
pathway of CAV1; dbSNP:rs121909329).
{ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:16321991,
ECO:0000269|PubMed:20104022,
ECO:0000269|PubMed:20512113,
ECO:0000269|PubMed:21145000,
ECO:0000269|PubMed:21822278,
ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:25125609,
ECO:0000269|PubMed:25878907,
ECO:0000269|PubMed:27753622}.
/FTId=VAR_033018.
VARIANT 155 155 R -> L (in IBMPFD1).
{ECO:0000269|PubMed:20335036}.
/FTId=VAR_078910.
VARIANT 155 155 R -> P (in IBMPFD1; dbSNP:rs121909329).
{ECO:0000269|PubMed:15034582}.
/FTId=VAR_033019.
VARIANT 155 155 R -> S (in IBMPFD1; impaired autophagic
function). {ECO:0000269|PubMed:20104022}.
/FTId=VAR_076466.
VARIANT 159 159 R -> G (in ALS14; dbSNP:rs387906789).
{ECO:0000269|PubMed:21145000,
ECO:0000269|PubMed:23349634}.
/FTId=VAR_065910.
VARIANT 159 159 R -> H (in IBMPFD1; without
frontotemporal dementia; abolishes
enhancement of K-315 methylation by
ASPSCR1; dbSNP:rs121909335).
{ECO:0000269|PubMed:16247064}.
/FTId=VAR_033020.
VARIANT 185 185 E -> K (in CMT2Y; normal ATPase activity;
impaired autophagic function;
dbSNP:rs864309501).
{ECO:0000269|PubMed:25125609}.
/FTId=VAR_076467.
VARIANT 191 191 R -> Q (in ALS14 and IBMPFD1; abolishes
enhancement of K-315 methylation by
ASPSCR1; dbSNP:rs121909334).
{ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:21145000,
ECO:0000269|PubMed:23349634}.
/FTId=VAR_033021.
VARIANT 198 198 L -> W (in IBMPFD1; increased ATPase
activity; impaired autophagic function).
{ECO:0000269|PubMed:17935506,
ECO:0000269|PubMed:20335036,
ECO:0000269|PubMed:25878907,
ECO:0000269|PubMed:27753622}.
/FTId=VAR_076468.
VARIANT 232 232 A -> E (in IBMPFD1; increased ATPase
activity; no defect in ubiquitin-
dependent protein degradation by the
proteasome; impaired autophagic function;
defect in maturation of ubiquitin-
containing autophagosomes; decreased
interaction with CAV1 and UBXN6;
dbSNP:rs121909331).
{ECO:0000269|PubMed:15034582,
ECO:0000269|PubMed:20104022,
ECO:0000269|PubMed:21822278,
ECO:0000269|PubMed:25125609,
ECO:0000269|PubMed:25878907,
ECO:0000269|PubMed:27753622}.
/FTId=VAR_033022.
VARIANT 387 387 N -> H (in IBMPFD1; unknown pathological
significance).
{ECO:0000269|PubMed:17935506}.
/FTId=VAR_078911.
VARIANT 592 592 D -> N (in ALS14; ALS14 patients do not
show frontotemporal dementia;
dbSNP:rs387906790).
{ECO:0000269|PubMed:21145000}.
/FTId=VAR_065911.
MUTAGEN 52 55 FRGD->ARGA: Abolishes interaction with
NPLOC4; when associated with A-110.
{ECO:0000269|PubMed:26471729}.
MUTAGEN 53 53 R->A: Minor effect on affinity for ATP
and ADP. {ECO:0000269|PubMed:20512113}.
MUTAGEN 86 86 R->A: Strongly increased affinity for
ATP. Strongly reduced affinity for ADP.
{ECO:0000269|PubMed:20512113}.
MUTAGEN 110 110 Y->A: Abolishes interaction with NPLOC4;
when associated with 52-A--A-55.
{ECO:0000269|PubMed:26471729}.
MUTAGEN 251 251 K->Q: Impairs ERAD degradation of HMGCR
and does not inhibit interaction with
RHBDD1; when associated with Q-524.
{ECO:0000269|PubMed:16168377,
ECO:0000269|PubMed:22795130}.
MUTAGEN 305 305 E->Q: Defect in ubiquitin-dependent
protein degradation by the proteasome;
when associated with Q-578.
{ECO:0000269|PubMed:20104022,
ECO:0000269|PubMed:26471729}.
MUTAGEN 312 312 K->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 313 313 R->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 314 314 E->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 314 314 Missing: Strongly impairs methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 315 315 K->L,Q,R: Abolishes methylation by
VCPKMT. {ECO:0000269|PubMed:22948820,
ECO:0000269|PubMed:23349634}.
MUTAGEN 316 316 T->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 317 317 H->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 318 318 G->A: Does not affect methylation by
VCPKMT. {ECO:0000269|PubMed:22948820}.
MUTAGEN 524 524 K->A: Impairs catalytic activity of
RNF19A toward SOD1 mutant. Does not
inhibit interaction with RHBDD1; when
associated with A-251.
{ECO:0000269|PubMed:15456787,
ECO:0000269|PubMed:16168377,
ECO:0000269|PubMed:22795130}.
MUTAGEN 524 524 K->Q: Impairs ERAD degradation of HMGCR;
when associated with Q-251.
{ECO:0000269|PubMed:15456787,
ECO:0000269|PubMed:16168377,
ECO:0000269|PubMed:22795130}.
MUTAGEN 578 578 E->Q: Does not inhibit interaction with
RHBDD1. Increased interaction with CAV1
and UBXN6. Impaired autophagic function.
Defect in ubiquitin-dependent protein
degradation by the proteasome; when
associated with Q-305.
{ECO:0000269|PubMed:20104022,
ECO:0000269|PubMed:21822278,
ECO:0000269|PubMed:22795130,
ECO:0000269|PubMed:26471729}.
CONFLICT 169 169 D -> H (in Ref. 6; AAI21795).
{ECO:0000305}.
CONFLICT 312 312 K -> I (in Ref. 3; BAG35235).
{ECO:0000305}.
TURN 15 17 {ECO:0000244|PDB:4KLN}.
HELIX 22 24 {ECO:0000244|PDB:5IFW}.
STRAND 25 29 {ECO:0000244|PDB:5B6C}.
STRAND 38 41 {ECO:0000244|PDB:5B6C}.
HELIX 43 48 {ECO:0000244|PDB:5B6C}.
STRAND 53 55 {ECO:0000244|PDB:5FTN}.
STRAND 56 60 {ECO:0000244|PDB:5B6C}.
HELIX 62 64 {ECO:0000244|PDB:3QQ8}.
STRAND 66 73 {ECO:0000244|PDB:5B6C}.
STRAND 75 77 {ECO:0000244|PDB:3HU1}.
STRAND 81 83 {ECO:0000244|PDB:5B6C}.
HELIX 86 92 {ECO:0000244|PDB:5B6C}.
STRAND 93 95 {ECO:0000244|PDB:5FTN}.
STRAND 99 104 {ECO:0000244|PDB:5B6C}.
STRAND 112 119 {ECO:0000244|PDB:5B6C}.
HELIX 120 123 {ECO:0000244|PDB:5B6C}.
STRAND 126 128 {ECO:0000244|PDB:5IFS}.
HELIX 130 133 {ECO:0000244|PDB:5B6C}.
HELIX 135 139 {ECO:0000244|PDB:5B6C}.
TURN 140 142 {ECO:0000244|PDB:5B6C}.
STRAND 144 147 {ECO:0000244|PDB:5B6C}.
STRAND 151 154 {ECO:0000244|PDB:5B6C}.
STRAND 157 159 {ECO:0000244|PDB:4KDI}.
STRAND 161 176 {ECO:0000244|PDB:5B6C}.
STRAND 181 183 {ECO:0000244|PDB:5B6C}.
HELIX 191 193 {ECO:0000244|PDB:4KDL}.
STRAND 198 200 {ECO:0000244|PDB:5FTJ}.
HELIX 203 205 {ECO:0000244|PDB:4KO8}.
HELIX 210 219 {ECO:0000244|PDB:4KO8}.
HELIX 221 225 {ECO:0000244|PDB:4KO8}.
HELIX 227 233 {ECO:0000244|PDB:4KO8}.
STRAND 240 244 {ECO:0000244|PDB:4KO8}.
STRAND 246 250 {ECO:0000244|PDB:4KLN}.
HELIX 251 261 {ECO:0000244|PDB:4KO8}.
STRAND 263 270 {ECO:0000244|PDB:4KO8}.
HELIX 271 275 {ECO:0000244|PDB:4KO8}.
HELIX 281 295 {ECO:0000244|PDB:4KO8}.
STRAND 298 305 {ECO:0000244|PDB:4KO8}.
HELIX 306 308 {ECO:0000244|PDB:4KO8}.
STRAND 313 315 {ECO:0000244|PDB:5FTK}.
HELIX 319 333 {ECO:0000244|PDB:4KO8}.
HELIX 335 337 {ECO:0000244|PDB:5DYG}.
STRAND 341 348 {ECO:0000244|PDB:4KO8}.
HELIX 350 352 {ECO:0000244|PDB:4KO8}.
HELIX 355 358 {ECO:0000244|PDB:4KO8}.
TURN 360 362 {ECO:0000244|PDB:5FTL}.
STRAND 365 368 {ECO:0000244|PDB:4KO8}.
HELIX 374 385 {ECO:0000244|PDB:4KO8}.
STRAND 388 390 {ECO:0000244|PDB:5DYG}.
HELIX 396 401 {ECO:0000244|PDB:4KO8}.
TURN 403 405 {ECO:0000244|PDB:5FTJ}.
HELIX 408 424 {ECO:0000244|PDB:4KO8}.
TURN 425 429 {ECO:0000244|PDB:4KO8}.
STRAND 432 436 {ECO:0000244|PDB:3HU1}.
HELIX 439 444 {ECO:0000244|PDB:4KO8}.
HELIX 449 457 {ECO:0000244|PDB:4KO8}.
STRAND 458 461 {ECO:0000244|PDB:4KO8}.
TURN 462 468 {ECO:0000244|PDB:4KO8}.
HELIX 476 478 {ECO:0000244|PDB:5FTK}.
HELIX 483 498 {ECO:0000244|PDB:5FTJ}.
HELIX 500 505 {ECO:0000244|PDB:5FTJ}.
STRAND 513 517 {ECO:0000244|PDB:5FTJ}.
HELIX 524 534 {ECO:0000244|PDB:5FTJ}.
STRAND 538 542 {ECO:0000244|PDB:5FTJ}.
HELIX 544 552 {ECO:0000244|PDB:5FTJ}.
HELIX 559 568 {ECO:0000244|PDB:5FTJ}.
STRAND 571 578 {ECO:0000244|PDB:5FTJ}.
HELIX 581 586 {ECO:0000244|PDB:5FTJ}.
STRAND 588 590 {ECO:0000244|PDB:5FTJ}.
HELIX 599 609 {ECO:0000244|PDB:5FTJ}.
STRAND 613 624 {ECO:0000244|PDB:5FTJ}.
STRAND 626 629 {ECO:0000244|PDB:5FTJ}.
HELIX 631 634 {ECO:0000244|PDB:5FTJ}.
STRAND 635 639 {ECO:0000244|PDB:5FTK}.
STRAND 641 644 {ECO:0000244|PDB:5FTJ}.
HELIX 650 661 {ECO:0000244|PDB:5FTJ}.
STRAND 662 664 {ECO:0000244|PDB:5C1B}.
HELIX 672 678 {ECO:0000244|PDB:5FTJ}.
HELIX 684 706 {ECO:0000244|PDB:5FTJ}.
STRAND 722 724 {ECO:0000244|PDB:5IFW}.
HELIX 735 741 {ECO:0000244|PDB:5FTJ}.
HELIX 749 762 {ECO:0000244|PDB:5FTJ}.
HELIX 763 765 {ECO:0000244|PDB:5FTM}.
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


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