TERA_HUMAN
ID TERA_HUMAN Reviewed; 806 AA.
AC P55072; B2R5T8; Q0V924; Q2TAI5; Q969G7; Q9UCD5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Transitional endoplasmic reticulum ATPase;
DE Short=TER ATPase;
DE EC=3.6.4.6 {ECO:0000269|PubMed:26471729};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE AltName: Full=Valosin-containing protein;
DE Short=VCP;
GN Name=VCP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W.,
RA Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S., Phan H.,
RA Velasco N., Garnes J., Danganan L., Poundstone P., Christensen M.,
RA Georgescu A., Avila J., Liu S., Attix C., Andreise T., Trankheim M.,
RA Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R., Thomas P.,
RA Quan G., Kronmiller B., Arellano A., Montgomery M., Ow D., Nolan M.,
RA Trong S., Kobayashi A., Olsen A.O., Carrano A.V.;
RT "Sequence analysis of a human P1 clone containing the XRCC9 DNA repair
RT gene.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-25.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-18; 148-155; 278-287; 296-312; 366-377; 466-487;
RP 587-599; 639-651 AND 669-677, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 27-41 AND 233-238, AND INTERACTION WITH CLATHRIN.
RC TISSUE=Glial tumor;
RX PubMed=8413590; DOI=10.1038/365459a0;
RA Pleasure I.T., Black M.M., Keen J.H.;
RT "Valosin-containing protein, VCP, is a ubiquitous clathrin-binding
RT protein.";
RL Nature 365:459-462(1993).
RN [10]
RP PROTEIN SEQUENCE OF 46-53; 66-81; 96-109; 148-155; 240-251; 323-336;
RP 454-502; 530-560; 600-614; 639-651; 678-693; 714-732 AND 754-766, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 314-322, IDENTIFICATION BY MASS SPECTROMETRY,
RP METHYLATION AT LYS-315, MUTAGENESIS OF LYS-315, CHARACTERIZATION OF
RP VARIANTS IBMPFD1 HIS-155 AND GLN-191, AND CHARACTERIZATION OF VARIANT
RP FTDALS6 GLY-159.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 388-483.
RC TISSUE=Fetal brain;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Characterization of different mRNA types expressed in human brain.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP INTERACTION WITH NGLY1.
RX PubMed=15362974; DOI=10.1042/bj20041498;
RA McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.;
RT "A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is
RT a substrate for SAPKs.";
RL Biochem. J. 384:391-400(2004).
RN [14]
RP FUNCTION, INTERACTION WITH RNF19A, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-524.
RX PubMed=15456787; DOI=10.1074/jbc.m406683200;
RA Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
RA Kakizuka A., Tanaka K., Sobue G.;
RT "Physical and functional interaction between dorfin and valosin-containing
RT protein that are colocalized in ubiquitylated inclusions in
RT neurodegenerative disorders.";
RL J. Biol. Chem. 279:51376-51385(2004).
RN [15]
RP INTERACTION WITH SELENOS, AND SUBCELLULAR LOCATION.
RX PubMed=15215856; DOI=10.1038/nature02656;
RA Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A.;
RT "A membrane protein complex mediates retro-translocation from the ER lumen
RT into the cytosol.";
RL Nature 429:841-847(2004).
RN [16]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [17]
RP INTERACTION WITH SYVN1 AND DERL1.
RX PubMed=16289116; DOI=10.1016/j.jmb.2005.10.020;
RA Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E.,
RA Koning F., Kloetzel P.-M., Seeger M.;
RT "The ubiquitin-domain protein HERP forms a complex with components of the
RT endoplasmic reticulum associated degradation pathway.";
RL J. Mol. Biol. 354:1021-1027(2005).
RN [18]
RP INTERACTION WITH AMFR, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-251 AND LYS-524.
RX PubMed=16168377; DOI=10.1016/j.molcel.2005.08.009;
RA Song B.L., Sever N., DeBose-Boyd R.A.;
RT "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and
RT couples sterol-regulated ubiquitination to degradation of HMG CoA
RT reductase.";
RL Mol. Cell 19:829-840(2005).
RN [19]
RP FUNCTION, AND INTERACTION WITH DERL1; AMFR; SYVN1 AND SELENOS.
RX PubMed=16186510; DOI=10.1073/pnas.0505006102;
RA Ye Y., Shibata Y., Kikkert M., van Voorden S., Wiertz E., Rapoport T.A.;
RT "Recruitment of the p97 ATPase and ubiquitin ligases to the site of
RT retrotranslocation at the endoplasmic reticulum membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14132-14138(2005).
RN [20]
RP INTERACTION WITH DERL1 AND DERL2.
RX PubMed=16186509; DOI=10.1073/pnas.0505014102;
RA Lilley B.N., Ploegh H.L.;
RT "Multiprotein complexes that link dislocation, ubiquitination, and
RT extraction of misfolded proteins from the endoplasmic reticulum membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14296-14301(2005).
RN [21]
RP INTERACTION WITH CASR AND RNF19A.
RX PubMed=16513638; DOI=10.1074/jbc.m513552200;
RA Huang Y., Niwa J., Sobue G., Breitwieser G.E.;
RT "Calcium-sensing receptor ubiquitination and degradation mediated by the E3
RT ubiquitin ligase dorfin.";
RL J. Biol. Chem. 281:11610-11617(2006).
RN [22]
RP INTERACTION WITH DERL1; DERL2 AND DERL3.
RX PubMed=16449189; DOI=10.1083/jcb.200507057;
RA Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., Mori K.;
RT "Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein
RT response and are required for ER-associated degradation.";
RL J. Cell Biol. 172:383-393(2006).
RN [23]
RP INTERACTION WITH UBXN4.
RX PubMed=16968747; DOI=10.1242/jcs.03163;
RA Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A.,
RA Monteiro M.J.;
RT "Characterization of erasin (UBXD2): a new ER protein that promotes ER-
RT associated protein degradation.";
RL J. Cell Sci. 119:4011-4024(2006).
RN [24]
RP INTERACTION WITH TRIM13.
RX PubMed=17314412; DOI=10.1091/mbc.e06-03-0248;
RA Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R., Ponten F.,
RA Uhlen M., Hober S., Grander D., Sangfelt O.;
RT "The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin
RT ligase involved in ERAD.";
RL Mol. Biol. Cell 18:1670-1682(2007).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [26]
RP INTERACTION WITH RNF103.
RX PubMed=18675248; DOI=10.1016/j.bbrc.2008.07.126;
RA Maruyama Y., Yamada M., Takahashi K., Yamada M.;
RT "Ubiquitin ligase Kf-1 is involved in the endoplasmic reticulum-associated
RT degradation pathway.";
RL Biochem. Biophys. Res. Commun. 374:737-741(2008).
RN [27]
RP INTERACTION WITH UBXN6.
RX PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008;
RA Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M.,
RA Hartmann-Petersen R.;
RT "Ubxd1 is a novel co-factor of the human p97 ATPase.";
RL Int. J. Biochem. Cell Biol. 40:2927-2942(2008).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-436 AND SER-787, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [29]
RP INTERACTION WITH TRIM21.
RX PubMed=18022694; DOI=10.1016/j.molimm.2007.10.023;
RA Takahata M., Bohgaki M., Tsukiyama T., Kondo T., Asaka M., Hatakeyama S.;
RT "Ro52 functionally interacts with IgG1 and regulates its quality control
RT via the ERAD system.";
RL Mol. Immunol. 45:2045-2054(2008).
RN [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [31]
RP INTERACTION WITH UBXN6.
RX PubMed=19174149; DOI=10.1016/j.bbrc.2009.01.076;
RA Kern M., Fernandez-Saiz V., Schaefer Z., Buchberger A.;
RT "UBXD1 binds p97 through two independent binding sites.";
RL Biochem. Biophys. Res. Commun. 380:303-307(2009).
RN [32]
RP INTERACTION WITH UBXN6.
RX PubMed=19275885; DOI=10.1016/j.bbrc.2009.03.012;
RA Nagahama M., Ohnishi M., Kawate Y., Matsui T., Miyake H., Yuasa K.,
RA Tani K., Tagaya M., Tsuji A.;
RT "UBXD1 is a VCP-interacting protein that is involved in ER-associated
RT degradation.";
RL Biochem. Biophys. Res. Commun. 382:303-308(2009).
RN [33]
RP INTERACTION WITH UBXN4, AND IDENTIFICATION IN A COMPLEX WITH UBQLN1 AND
RP UBXN4.
RX PubMed=19822669; DOI=10.1083/jcb.200903024;
RA Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
RA Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
RT "Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD.";
RL J. Cell Biol. 187:201-217(2009).
RN [34]
RP INTERACTION WITH YOD1.
RX PubMed=19818707; DOI=10.1016/j.molcel.2009.09.016;
RA Ernst R., Mueller B., Ploegh H.L., Schlieker C.;
RT "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to
RT facilitate protein dislocation from the ER.";
RL Mol. Cell 36:28-38(2009).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3 AND SER-37, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [36]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770 AND SER-775, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [37]
RP INTERACTION WITH WASHC5.
RX PubMed=20833645; DOI=10.1093/brain/awq222;
RA Clemen C.S., Tangavelou K., Strucksberg K.H., Just S., Gaertner L.,
RA Regus-Leidig H., Stumpf M., Reimann J., Coras R., Morgan R.O.,
RA Fernandez M.P., Hofmann A., Muller S., Schoser B., Hanisch F.G.,
RA Rottbauer W., Blumcke I., von Horsten S., Eichinger L., Schroder R.;
RT "Strumpellin is a novel valosin-containing protein binding partner linking
RT hereditary spastic paraplegia to protein aggregation diseases.";
RL Brain 133:2920-2941(2010).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [40]
RP FUNCTION IN OMM PROTEIN TURNOVER.
RX PubMed=21118995; DOI=10.1091/mbc.e10-09-0748;
RA Xu S., Peng G., Wang Y., Fang S., Karbowski M.;
RT "The AAA-ATPase p97 is essential for outer mitochondrial membrane protein
RT turnover.";
RL Mol. Biol. Cell 22:291-300(2011).
RN [41]
RP INTERACTION WITH BAG6.
RX PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
RA Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
RT "A ubiquitin ligase-associated chaperone holdase maintains polypeptides in
RT soluble states for proteasome degradation.";
RL Mol. Cell 42:758-770(2011).
RN [42]
RP FUNCTION, INTERACTION WITH CAV1 AND UBXN6, CHARACTERIZATION OF VARIANTS
RP IBMPFD1 GLY-95; HIS-155 AND GLU-232, AND MUTAGENESIS OF GLU-578.
RX PubMed=21822278; DOI=10.1038/ncb2301;
RA Ritz D., Vuk M., Kirchner P., Bug M., Schuetz S., Hayer A., Bremer S.,
RA Lusk C., Baloh R.H., Lee H., Glatter T., Gstaiger M., Aebersold R.,
RA Weihl C.C., Meyer H.;
RT "Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and
RT UBXD1 and impaired by VCP disease mutations.";
RL Nat. Cell Biol. 13:1116-1123(2011).
RN [43]
RP FUNCTION.
RX PubMed=22020440; DOI=10.1038/ncb2367;
RA Meerang M., Ritz D., Paliwal S., Garajova Z., Bosshard M., Mailand N.,
RA Janscak P., Hubscher U., Meyer H., Ramadan K.;
RT "The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA
RT double-strand breaks.";
RL Nat. Cell Biol. 13:1376-1382(2011).
RN [44]
RP FUNCTION, INTERACTION WITH L3MBTL1, AND SUBCELLULAR LOCATION.
RX PubMed=22120668; DOI=10.1038/nsmb.2188;
RA Acs K., Luijsterburg M.S., Ackermann L., Salomons F.A., Hoppe T.,
RA Dantuma N.P.;
RT "The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from
RT DNA double-strand breaks.";
RL Nat. Struct. Mol. Biol. 18:1345-1350(2011).
RN [45]
RP INTERACTION WITH UBXN8.
RX PubMed=21949850; DOI=10.1371/journal.pone.0025061;
RA Madsen L., Kriegenburg F., Vala A., Best D., Prag S., Hofmann K.,
RA Seeger M., Adams I.R., Hartmann-Petersen R.;
RT "The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum
RT membrane for degradation of misfolded proteins.";
RL PLoS ONE 6:E25061-E25061(2011).
RN [46]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [47]
RP INTERACTION WITH UBXN7.
RX PubMed=22537386; DOI=10.1186/1741-7007-10-36;
RA Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G.;
RT "UBXN7 docks on neddylated cullin complexes using its UIM motif and causes
RT HIF1alpha accumulation.";
RL BMC Biol. 10:36-36(2012).
RN [48]
RP INTERACTION WITH RHBDD1, MUTAGENESIS OF LYS-251; LYS-524 AND GLU-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22795130; DOI=10.1016/j.molcel.2012.06.008;
RA Fleig L., Bergbold N., Sahasrabudhe P., Geiger B., Kaltak L., Lemberg M.K.;
RT "Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of
RT membrane proteins.";
RL Mol. Cell 47:558-569(2012).
RN [49]
RP INTERACTION WITH SPRTN.
RX PubMed=22902628; DOI=10.1074/jbc.m112.400135;
RA Ghosal G., Leung J.W., Nair B.C., Fong K.W., Chen J.;
RT "Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a
RT regulator of translesion synthesis.";
RL J. Biol. Chem. 287:34225-34233(2012).
RN [50]
RP FUNCTION IN ERAD PATHWAY.
RX PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015;
RA Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H.,
RA Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T.,
RA Morino-Koga S., Wada I., Kai H.;
RT "STT3B-dependent posttranslational N-glycosylation as a surveillance system
RT for secretory protein.";
RL Mol. Cell 47:99-110(2012).
RN [51]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [52]
RP METHYLATION AT LYS-315, AND MUTAGENESIS OF LYS-312; ARG-313; GLU-314;
RP LYS-315; THR-316; HIS-317 AND GLY-318.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
RN [53]
RP FUNCTION, AND INTERACTION WITH SPRTN.
RX PubMed=23042607; DOI=10.1038/nsmb.2394;
RA Davis E.J., Lachaud C., Appleton P., Macartney T.J., Nathke I., Rouse J.;
RT "DVC1 (C1orf124) recruits the p97 protein segregase to sites of DNA
RT damage.";
RL Nat. Struct. Mol. Biol. 19:1093-1100(2012).
RN [54]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPRTN.
RX PubMed=23042605; DOI=10.1038/nsmb.2395;
RA Mosbech A., Gibbs-Seymour I., Kagias K., Thorslund T., Beli P., Povlsen L.,
RA Nielsen S.V., Smedegaard S., Sedgwick G., Lukas C., Hartmann-Petersen R.,
RA Lukas J., Choudhary C., Pocock R., Bekker-Jensen S., Mailand N.;
RT "DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes
RT ubiquitin-dependent responses to replication blocks.";
RL Nat. Struct. Mol. Biol. 19:1084-1092(2012).
RN [55]
RP FUNCTION.
RX PubMed=23335559; DOI=10.1074/jbc.m112.429076;
RA Kirchner P., Bug M., Meyer H.;
RT "Ubiquitination of the N-terminal region of caveolin-1 regulates endosomal
RT sorting by the VCP/p97 AAA-ATPase.";
RL J. Biol. Chem. 288:7363-7372(2013).
RN [56]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-7; SER-13; SER-462 AND
RP SER-702, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [57]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [58]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [59]
RP INTERACTION WITH RNF31.
RX PubMed=24726327; DOI=10.1016/j.molcel.2014.03.016;
RA Schaeffer V., Akutsu M., Olma M.H., Gomes L.C., Kawasaki M., Dikic I.;
RT "Binding of OTULIN to the PUB domain of HOIP controls NF-kappaB
RT signaling.";
RL Mol. Cell 54:349-361(2014).
RN [60]
RP FUNCTION.
RX PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047;
RA Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P., Kato H.,
RA Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H., Nishitoh H.;
RT "Pre-emptive quality control protects the ER from protein overload via the
RT proximity of ERAD components and SRP.";
RL Cell Rep. 13:944-956(2015).
RN [61]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DDX58 AND RNF125, AND
RP MUTAGENESIS OF 52-PHE--ASP-55; TYR-110; GLU-305 AND GLU-578.
RX PubMed=26471729; DOI=10.15252/embj.201591888;
RA Hao Q., Jiao S., Shi Z., Li C., Meng X., Zhang Z., Wang Y., Song X.,
RA Wang W., Zhang R., Zhao Y., Wong C.C., Zhou Z.;
RT "A non-canonical role of the p97 complex in RIG-I antiviral signaling.";
RL EMBO J. 34:2903-2920(2015).
RN [62]
RP INTERACTION WITH ZFAND2B.
RX PubMed=26337389; DOI=10.1091/mbc.e15-02-0085;
RA Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
RT "Proteasomal degradation of preemptive quality control (pQC) substrates is
RT mediated by an AIRAPL-p97 complex.";
RL Mol. Biol. Cell 26:3719-3727(2015).
RN [63]
RP INTERACTION WITH UBXN10.
RX PubMed=26389662; DOI=10.1038/ncb3238;
RA Raman M., Sergeev M., Garnaas M., Lydeard J.R., Huttlin E.L., Goessling W.,
RA Shah J.V., Harper J.W.;
RT "Systematic proteomics of the VCP-UBXD adaptor network identifies a role
RT for UBXN10 in regulating ciliogenesis.";
RL Nat. Cell Biol. 17:1356-1369(2015).
RN [64]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [65]
RP INTERACTION WITH FAF1, AND SUBCELLULAR LOCATION.
RX PubMed=26842564; DOI=10.1038/ncomms10612;
RA Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D., Kashkar H.,
RA Ramadan K., Hoppe T.;
RT "Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard
RT DNA replication fork progression.";
RL Nat. Commun. 7:10612-10612(2016).
RN [66]
RP FUNCTION.
RX PubMed=26692333; DOI=10.1038/nm.4013;
RA Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T.,
RA Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E., Vazquez J.,
RA Porta-de-la-Riva M., Ceron J., Fueyo A., Li J., Green A.R., Freije J.M.,
RA Lopez-Otin C.;
RT "Loss of the proteostasis factor AIRAPL causes myeloid transformation by
RT deregulating IGF-1 signaling.";
RL Nat. Med. 22:91-96(2016).
RN [67]
RP INTERACTION WITH ANKZF1.
RX PubMed=28302725; DOI=10.1074/jbc.m116.772038;
RA van Haaften-Visser D.Y., Harakalova M., Mocholi E., van Montfrans J.M.,
RA Elkadri A., Rieter E., Fiedler K., van Hasselt P.M., Triffaux E.M.M.,
RA van Haelst M.M., Nijman I.J., Kloosterman W.P., Nieuwenhuis E.E.S.,
RA Muise A.M., Cuppen E., Houwen R.H.J., Coffer P.J.;
RT "Ankyrin repeat and zinc-finger domain-containing 1 mutations are
RT associated with infantile-onset inflammatory bowel disease.";
RL J. Biol. Chem. 292:7904-7920(2017).
RN [68]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-18, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [69]
RP INTERACTION WITH ATXN3.
RX PubMed=30455355; DOI=10.1074/jbc.ra118.005801;
RA Weishaeupl D., Schneider J., Peixoto Pinheiro B., Ruess C., Dold S.M.,
RA von Zweydorf F., Gloeckner C.J., Schmidt J., Riess O., Schmidt T.;
RT "Physiological and pathophysiological characteristics of ataxin-3
RT isoforms.";
RL J. Biol. Chem. 294:644-661(2019).
RN [70]
RP INTERACTION WITH LMBR1L.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
RN [71]
RP FUNCTION, AND INTERACTION WITH TEX264.
RX PubMed=32152270; DOI=10.1038/s41467-020-15000-w;
RA Fielden J., Wiseman K., Torrecilla I., Li S., Hume S., Chiang S.C.,
RA Ruggiano A., Narayan Singh A., Freire R., Hassanieh S., Domingo E.,
RA Vendrell I., Fischer R., Kessler B.M., Maughan T.S., El-Khamisy S.F.,
RA Ramadan K.;
RT "TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-
RT DNA adducts.";
RL Nat. Commun. 11:1274-1274(2020).
RN [72]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-481 IN COMPLEX WITH ATP ANALOG,
RP CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155, MUTAGENESIS OF
RP ARG-53 AND ARG-86, AND SUBUNIT.
RX PubMed=20512113; DOI=10.1038/emboj.2010.104;
RA Tang W.K., Li D., Li C.C., Esser L., Dai R., Guo L., Xia D.;
RT "A novel ATP-dependent conformation in p97 N-D1 fragment revealed by
RT crystal structures of disease-related mutants.";
RL EMBO J. 29:2217-2229(2010).
RN [73]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 797-806 IN COMPLEX WITH PLAA.
RX PubMed=19887378; DOI=10.1074/jbc.m109.044685;
RA Qiu L., Pashkova N., Walker J.R., Winistorfer S., Allali-Hassani A.,
RA Akutsu M., Piper R., Dhe-Paganon S.;
RT "Structure and function of the PLAA/Ufd3-p97/Cdc48 complex.";
RL J. Biol. Chem. 285:365-372(2010).
RN [74]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-187 IN COMPLEX WITH AMFR.
RX PubMed=21914798; DOI=10.1074/jbc.m111.274506;
RA Hanzelmann P., Schindelin H.;
RT "The structural and functional basis of the p97/valosin-containing protein
RT (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to
RT the N-terminal domain of p97.";
RL J. Biol. Chem. 286:38679-38690(2011).
RN [75] {ECO:0007744|PDB:5GLF}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 21-199 IN COMPLEX WITH DERL1,
RP INTERACTION WITH DERL1, AND MUTAGENESIS OF 113-ARG--HIS-115; PHE-131;
RP LEU-140; ASP-179 AND HIS-183.
RX PubMed=27714797; DOI=10.1002/1873-3468.12447;
RA Lim J.J., Lee Y., Yoon S.Y., Ly T.T., Kang J.Y., Youn H.S., An J.Y.,
RA Lee J.G., Park K.R., Kim T.G., Yang J.K., Jun Y., Eom S.H.;
RT "Structural insights into the interaction of human p97 N-terminal domain
RT and SHP motif in Derlin-1 rhomboid pseudoprotease.";
RL FEBS Lett. 590:4402-4413(2016).
RN [76]
RP VARIANTS IBMPFD1 GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND GLU-232.
RX PubMed=15034582; DOI=10.1038/ng1332;
RA Watts G.D.J., Wymer J., Kovach M.J., Mehta S.G., Mumm S., Darvish D.,
RA Pestronk A., Whyte M.P., Kimonis V.E.;
RT "Inclusion body myopathy associated with Paget disease of bone and
RT frontotemporal dementia is caused by mutant valosin-containing protein.";
RL Nat. Genet. 36:377-381(2004).
RN [77]
RP VARIANT IBMPFD1 CYS-155.
RX PubMed=15732117; DOI=10.1002/ana.20407;
RA Schroeder R., Watts G.D.J., Mehta S.G., Evert B.O., Broich P.,
RA Fliessbach K., Pauls K., Hans V.H., Kimonis V., Thal D.R.;
RT "Mutant valosin-containing protein causes a novel type of frontotemporal
RT dementia.";
RL Ann. Neurol. 57:457-461(2005).
RN [78]
RP VARIANT IBMPFD1 HIS-159.
RX PubMed=16247064; DOI=10.1212/01.wnl.0000180407.15369.92;
RA Haubenberger D., Bittner R.E., Rauch-Shorny S., Zimprich F., Mannhalter C.,
RA Wagner L., Mineva I., Vass K., Auff E., Zimprich A.;
RT "Inclusion body myopathy and Paget disease is linked to a novel mutation in
RT the VCP gene.";
RL Neurology 65:1304-1305(2005).
RN [79]
RP CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155.
RX PubMed=16321991; DOI=10.1093/hmg/ddi426;
RA Weihl C.C., Dalal S., Pestronk A., Hanson P.I.;
RT "Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic
RT reticulum-associated degradation.";
RL Hum. Mol. Genet. 15:189-199(2006).
RN [80]
RP VARIANTS IBMPFD1 TRP-198 AND HIS-387.
RX PubMed=17935506; DOI=10.1111/j.1399-0004.2007.00887.x;
RA Watts G.D., Thomasova D., Ramdeen S.K., Fulchiero E.C., Mehta S.G.,
RA Drachman D.A., Weihl C.C., Jamrozik Z., Kwiecinski H., Kaminska A.,
RA Kimonis V.E.;
RT "Novel VCP mutations in inclusion body myopathy associated with Paget
RT disease of bone and frontotemporal dementia.";
RL Clin. Genet. 72:420-426(2007).
RN [81]
RP CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; SER-155 AND GLU-232,
RP MUTAGENESIS OF GLU-305 AND GLU-578, AND FUNCTION.
RX PubMed=20104022; DOI=10.4161/auto.6.2.11014;
RA Tresse E., Salomons F.A., Vesa J., Bott L.C., Kimonis V., Yao T.P.,
RA Dantuma N.P., Taylor J.P.;
RT "VCP/p97 is essential for maturation of ubiquitin-containing autophagosomes
RT and this function is impaired by mutations that cause IBMPFD.";
RL Autophagy 6:217-227(2010).
RN [82]
RP FUNCTION, INTERACTION WITH ZFAND1, MUTAGENESIS OF GLU-578, AND
RP CHARACTERIZATION OF VARIANT IBMPFD1 HIS-155.
RX PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
RA Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
RA Schlosser A., Hofmann K., Buchberger A.;
RT "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
RT arsenite-induced stress granules.";
RL Mol. Cell 70:906-919(2018).
RN [83]
RP VARIANTS IBMPFD1 LEU-155 AND TRP-198.
RX PubMed=20335036; DOI=10.1016/j.nmd.2010.03.002;
RA Kumar K.R., Needham M., Mina K., Davis M., Brewer J., Staples C., Ng K.,
RA Sue C.M., Mastaglia F.L.;
RT "Two Australian families with inclusion-body myopathy, Paget's disease of
RT bone and frontotemporal dementia: novel clinical and genetic findings.";
RL Neuromuscul. Disord. 20:330-334(2010).
RN [84]
RP VARIANTS FTDALS6 HIS-155; GLY-159; GLN-191 AND ASN-592.
RX PubMed=21145000; DOI=10.1016/j.neuron.2010.11.036;
RA Johnson J.O., Mandrioli J., Benatar M., Abramzon Y., Van Deerlin V.M.,
RA Trojanowski J.Q., Gibbs J.R., Brunetti M., Gronka S., Wuu J., Ding J.,
RA McCluskey L., Martinez-Lage M., Falcone D., Hernandez D.G., Arepalli S.,
RA Chong S., Schymick J.C., Rothstein J., Landi F., Wang Y.D., Calvo A.,
RA Mora G., Sabatelli M., Monsurro M.R., Battistini S., Salvi F., Spataro R.,
RA Sola P., Borghero G., Galassi G., Scholz S.W., Taylor J.P., Restagno G.,
RA Chio A., Traynor B.J.;
RT "Exome sequencing reveals VCP mutations as a cause of familial ALS.";
RL Neuron 68:857-864(2010).
RN [85]
RP VARIANT CMT2Y LYS-185, CHARACTERIZATION OF VARIANT CMT2Y LYS-185, AND
RP CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155 AND GLU-232.
RX PubMed=25125609; DOI=10.1093/brain/awu224;
RA Gonzalez M.A., Feely S.M., Speziani F., Strickland A.V., Danzi M.,
RA Bacon C., Lee Y., Chou T.F., Blanton S.H., Weihl C.C., Zuchner S.,
RA Shy M.E.;
RT "A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease.";
RL Brain 137:2897-2902(2014).
RN [86]
RP VARIANT CMT2Y GLU-97, CHARACTERIZATION OF VARIANT CMT2Y GLU-97, AND
RP CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; TRP-198 AND GLU-232.
RX PubMed=25878907; DOI=10.1155/2015/239167;
RA Jerath N.U., Crockett C.D., Moore S.A., Shy M.E., Weihl C.C., Chou T.F.,
RA Grider T., Gonzalez M.A., Zuchner S., Swenson A.;
RT "Rare Manifestation of a c.290 C>T, p.Gly97Glu VCP Mutation.";
RL Case Rep. Genet. 2015:239167-239167(2015).
RN [87]
RP VARIANT IBMPFD1 PHE-126.
RX PubMed=27209344; DOI=10.1016/j.nmd.2016.05.001;
RA Matsubara S., Shimizu T., Komori T., Mori-Yoshimura M., Minami N.,
RA Hayashi Y.K.;
RT "Nuclear inclusions mimicking poly(A)-binding protein nuclear 1 inclusions
RT in a case of inclusion body myopathy associated with Paget disease of bone
RT and frontotemporal dementia with a novel mutation in the valosin-containing
RT protein gene.";
RL Neuromuscul. Disord. 26:436-440(2016).
RN [88]
RP FUNCTION, INTERACTION WITH PLAA; UBXN6 AND YOD1, SUBCELLULAR LOCATION,
RP CHARACTERIZATION OF VARIANTS IBMPFD1 HIS-155; TRP-198 AND GLU-232, AND
RP MUTAGENESIS OF GLU-578.
RX PubMed=27753622; DOI=10.15252/embj.201695148;
RA Papadopoulos C., Kirchner P., Bug M., Grum D., Koerver L., Schulze N.,
RA Poehler R., Dressler A., Fengler S., Arhzaouy K., Lux V., Ehrmann M.,
RA Weihl C.C., Meyer H.;
RT "VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of
RT ruptured lysosomes by autophagy.";
RL EMBO J. 36:135-150(2017).
CC -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC mitosis and for their reassembly after mitosis. Involved in the
CC formation of the transitional endoplasmic reticulum (tER). The transfer
CC of membranes from the endoplasmic reticulum to the Golgi apparatus
CC occurs via 50-70 nm transition vesicles which derive from part-rough,
CC part-smooth transitional elements of the endoplasmic reticulum (tER).
CC Vesicle budding from the tER is an ATP-dependent process. The ternary
CC complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins
CC and is necessary for the export of misfolded proteins from the ER to
CC the cytoplasm, where they are degraded by the proteasome. The NPLOC4-
CC UFD1-VCP complex regulates spindle disassembly at the end of mitosis
CC and is necessary for the formation of a closed nuclear envelope.
CC Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of
CC the VCP/p97-AMFR/gp78 complex that participates in the final step of
CC the sterol-mediated ubiquitination and endoplasmic reticulum-associated
CC degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-
CC induced pre-emptive quality control, a mechanism that selectively
CC attenuates the translocation of newly synthesized proteins into the
CC endoplasmic reticulum and reroutes them to the cytosol for proteasomal
CC degradation (PubMed:26565908). Plays a role in the regulation of stress
CC granules (SGs) clearance process upon arsenite-induced response
CC (PubMed:29804830). Also involved in DNA damage response: recruited to
CC double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent
CC manner and promotes the recruitment of TP53BP1 at DNA damage sites
CC (PubMed:22020440, PubMed:22120668). Recruited to stalled replication
CC forks by SPRTN: may act by mediating extraction of DNA polymerase eta
CC (POLH) to prevent excessive translesion DNA synthesis and limit the
CC incidence of mutations induced by DNA damage (PubMed:23042607,
CC PubMed:23042605). Together with SPRTN metalloprotease, involved in the
CC repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis
CC (PubMed:32152270). Involved in interstrand cross-link repair in
CC response to replication stress by mediating unloading of the
CC ubiquitinated CMG helicase complex (By similarity). Required for
CC cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-
CC membrane proteins and their subsequent proteasomal degradation
CC (PubMed:16186510, PubMed:21118995). Essential for the maturation of
CC ubiquitin-containing autophagosomes and the clearance of ubiquitinated
CC protein by autophagy (PubMed:20104022, PubMed:27753622). Acts as a
CC negative regulator of type I interferon production by interacting with
CC DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated
CC via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit
CC RNF125 and promote ubiquitination and degradation of DDX58/RIG-I
CC (PubMed:26471729). May play a role in the ubiquitin-dependent sorting
CC of membrane proteins to lysosomes where they undergo degradation
CC (PubMed:21822278). May more particularly play a role in caveolins
CC sorting in cells (PubMed:21822278, PubMed:23335559). By controlling the
CC steady-state expression of the IGF1R receptor, indirectly regulates the
CC insulin-like growth factor receptor signaling pathway
CC (PubMed:26692333). {ECO:0000250|UniProtKB:P23787,
CC ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377,
CC ECO:0000269|PubMed:16186510, ECO:0000269|PubMed:20104022,
CC ECO:0000269|PubMed:21118995, ECO:0000269|PubMed:21822278,
CC ECO:0000269|PubMed:22020440, ECO:0000269|PubMed:22120668,
CC ECO:0000269|PubMed:22607976, ECO:0000269|PubMed:23042605,
CC ECO:0000269|PubMed:23042607, ECO:0000269|PubMed:23335559,
CC ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:26565908,
CC ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27753622,
CC ECO:0000269|PubMed:29804830, ECO:0000269|PubMed:32152270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000269|PubMed:26471729};
CC -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC that displays 6-fold radial symmetry. Part of a ternary complex
CC containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds
CC to one end of a VCP homohexamer. The complex binds to membranes
CC enriched in phosphatidylethanolamine-containing lipids and promotes
CC Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1,
CC binding to this heterodimer inhibits Golgi-membrane fusion
CC (PubMed:26471729). Interaction with VCIP135 leads to dissociation of
CC the complex via ATP hydrolysis by VCP. Part of a ternary complex
CC containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C-like protein
CC p37; the complex has membrane fusion activity and is required for Golgi
CC and endoplasmic reticulum biogenesis. Interacts with SELENOS and SYVN1,
CC as well as with DERL1 (via SHP-box motif), DERL2 and DERL3; which
CC probably transfer misfolded proteins from the ER to VCP
CC (PubMed:15215856, PubMed:16289116, PubMed:16186510, PubMed:16186509,
CC PubMed:16449189, PubMed:27714797). Interacts with SVIP. Component of a
CC complex required to couple retrotranslocation, ubiquitination and
CC deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B.
CC Directly interacts with UBXN4 and RNF19A. Interacts with CASR.
CC Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts with
CC RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-
CC AMFR/gp78 complex that participates in the final step of the
CC endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts
CC directly with AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-
CC terminal domain). Interacts with SPRTN; leading to recruitment to
CC stalled replication forks (PubMed:23042607, PubMed:23042605). Interacts
CC with WASHC5. Interacts with UBOX5. Interacts (via N-terminus) with
CC UBXN7, UBXN8, and probably several other UBX domain-containing proteins
CC (via UBX domains); the interactions are mutually exclusive with VIM-
CC dependent interactions such as those with AMFR and SELENOS. Forms a
CC complex with UBQLN1 and UBXN4. Interacts (via the PIM motif) with RNF31
CC (via the PUB domain) (PubMed:24726327). Interacts with DDX58/RIG-I and
CC RNF125; interaction takes place when DDX58/RIG-I is ubiquitinated via
CC 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit
CC RNF125 and promote ubiquitination and degradation of DDX58/RIG-I
CC (PubMed:26471729). Interacts with BAG6 (PubMed:21636303). Interacts
CC with UBXN10 (PubMed:26389662). Interacts with UBXN6; the interaction
CC with UBXN6 is direct and competitive with UFD1 (PubMed:19174149,
CC PubMed:19275885). Forms a ternary complex with CAV1 and UBXN6
CC (PubMed:21822278, PubMed:18656546, PubMed:19174149). Interacts with
CC PLAA, UBXN6 and YOD1; may form a complex involved in macroautophagy
CC (PubMed:27753622). Interacts with ANKZF1 (PubMed:28302725). Interacts
CC with ubiquitin-binding protein FAF1 (PubMed:26842564). Interacts with
CC ZFAND2B (via VIM motif); the interaction is direct (PubMed:24160817,
CC PubMed:26337389). Interacts with ZFAND1 (via its ubiquitin-like
CC region); this interaction occurs in an arsenite-dependent manner
CC (PubMed:29804830). Interacts with CCDC47 (By similarity). Interacts
CC with UBAC2 (By similarity). Interacts with LMBR1L (PubMed:31073040).
CC Interacts with ATXN3 (PubMed:30455355). Interacts with TEX264; bridging
CC VCP to covalent DNA-protein cross-links (DPCs) (PubMed:32152270).
CC {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:Q01853,
CC ECO:0000269|PubMed:15215856, ECO:0000269|PubMed:15362974,
CC ECO:0000269|PubMed:15456787, ECO:0000269|PubMed:16168377,
CC ECO:0000269|PubMed:16186509, ECO:0000269|PubMed:16186510,
CC ECO:0000269|PubMed:16289116, ECO:0000269|PubMed:16449189,
CC ECO:0000269|PubMed:16513638, ECO:0000269|PubMed:16968747,
CC ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:18022694,
CC ECO:0000269|PubMed:18656546, ECO:0000269|PubMed:18675248,
CC ECO:0000269|PubMed:19174149, ECO:0000269|PubMed:19275885,
CC ECO:0000269|PubMed:19818707, ECO:0000269|PubMed:19822669,
CC ECO:0000269|PubMed:19887378, ECO:0000269|PubMed:20512113,
CC ECO:0000269|PubMed:20833645, ECO:0000269|PubMed:21636303,
CC ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:21914798,
CC ECO:0000269|PubMed:21949850, ECO:0000269|PubMed:22120668,
CC ECO:0000269|PubMed:22537386, ECO:0000269|PubMed:22795130,
CC ECO:0000269|PubMed:22902628, ECO:0000269|PubMed:23042605,
CC ECO:0000269|PubMed:23042607, ECO:0000269|PubMed:24160817,
CC ECO:0000269|PubMed:24726327, ECO:0000269|PubMed:26337389,
CC ECO:0000269|PubMed:26389662, ECO:0000269|PubMed:26471729,
CC ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:27714797,
CC ECO:0000269|PubMed:27753622, ECO:0000269|PubMed:28302725,
CC ECO:0000269|PubMed:29804830, ECO:0000269|PubMed:30455355,
CC ECO:0000269|PubMed:32152270, ECO:0000269|PubMed:8413590,
CC ECO:0000305|PubMed:31073040}.
CC -!- INTERACTION:
CC P55072; Q9UKV5: AMFR; NbExp=12; IntAct=EBI-355164, EBI-1046367;
CC P55072; Q9BZE9: ASPSCR1; NbExp=28; IntAct=EBI-355164, EBI-1993677;
CC P55072; P54253: ATXN1; NbExp=3; IntAct=EBI-355164, EBI-930964;
CC P55072; P54252: ATXN3; NbExp=4; IntAct=EBI-355164, EBI-946046;
CC P55072; P54252-1: ATXN3; NbExp=16; IntAct=EBI-355164, EBI-946068;
CC P55072; Q96LK0: CEP19; NbExp=3; IntAct=EBI-355164, EBI-741885;
CC P55072; O96017: CHEK2; NbExp=2; IntAct=EBI-355164, EBI-1180783;
CC P55072; O75175: CNOT3; NbExp=3; IntAct=EBI-355164, EBI-743073;
CC P55072; Q13619: CUL4A; NbExp=2; IntAct=EBI-355164, EBI-456106;
CC P55072; O60941-5: DTNB; NbExp=3; IntAct=EBI-355164, EBI-11984733;
CC P55072; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-355164, EBI-21603100;
CC P55072; Q96J88-3: EPSTI1; NbExp=3; IntAct=EBI-355164, EBI-25885343;
CC P55072; Q9UNN5-1: FAF1; NbExp=4; IntAct=EBI-355164, EBI-15930546;
CC P55072; Q96CS3: FAF2; NbExp=13; IntAct=EBI-355164, EBI-1055805;
CC P55072; Q969W3: FAM104A; NbExp=6; IntAct=EBI-355164, EBI-10281506;
CC P55072; O94868: FCHSD2; NbExp=2; IntAct=EBI-355164, EBI-1215612;
CC P55072; P09471: GNAO1; NbExp=3; IntAct=EBI-355164, EBI-715087;
CC P55072; P62993: GRB2; NbExp=3; IntAct=EBI-355164, EBI-401755;
CC P55072; P42858: HTT; NbExp=10; IntAct=EBI-355164, EBI-466029;
CC P55072; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-355164, EBI-739832;
CC P55072; Q8WZA0: LZIC; NbExp=3; IntAct=EBI-355164, EBI-5774346;
CC P55072; Q9H7H0-2: METTL17; NbExp=3; IntAct=EBI-355164, EBI-11098807;
CC P55072; Q8TAT6: NPLOC4; NbExp=9; IntAct=EBI-355164, EBI-1994109;
CC P55072; Q9UNZ2: NSFL1C; NbExp=20; IntAct=EBI-355164, EBI-721577;
CC P55072; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-355164, EBI-741158;
CC P55072; Q9Y263: PLAA; NbExp=3; IntAct=EBI-355164, EBI-1994037;
CC P55072; Q07869: PPARA; NbExp=3; IntAct=EBI-355164, EBI-78615;
CC P55072; P62136: PPP1CA; NbExp=2; IntAct=EBI-355164, EBI-357253;
CC P55072; P07602-1: PSAP; NbExp=3; IntAct=EBI-355164, EBI-10635648;
CC P55072; P25786: PSMA1; NbExp=3; IntAct=EBI-355164, EBI-359352;
CC P55072; P62191: PSMC1; NbExp=3; IntAct=EBI-355164, EBI-357598;
CC P55072; P26045: PTPN3; NbExp=2; IntAct=EBI-355164, EBI-1047946;
CC P55072; Q9Y4L5: RNF115; NbExp=3; IntAct=EBI-355164, EBI-2129242;
CC P55072; P32969: RPL9P9; NbExp=3; IntAct=EBI-355164, EBI-358122;
CC P55072; Q9H0K1: SIK2; NbExp=4; IntAct=EBI-355164, EBI-1181664;
CC P55072; Q8NBI5: SLC43A3; NbExp=3; IntAct=EBI-355164, EBI-2855542;
CC P55072; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-355164, EBI-12938570;
CC P55072; P46977: STT3A; NbExp=3; IntAct=EBI-355164, EBI-719212;
CC P55072; P51668: UBE2D1; NbExp=3; IntAct=EBI-355164, EBI-743540;
CC P55072; B1AQ61: UBE4B; NbExp=4; IntAct=EBI-355164, EBI-7931266;
CC P55072; O94941: UBOX5; NbExp=3; IntAct=EBI-355164, EBI-751901;
CC P55072; Q96LJ8: UBXN10; NbExp=7; IntAct=EBI-355164, EBI-1993941;
CC P55072; Q5T124-6: UBXN11; NbExp=7; IntAct=EBI-355164, EBI-11524408;
CC P55072; P68543: UBXN2A; NbExp=17; IntAct=EBI-355164, EBI-1993668;
CC P55072; Q14CS0: UBXN2B; NbExp=11; IntAct=EBI-355164, EBI-1993619;
CC P55072; Q92575: UBXN4; NbExp=11; IntAct=EBI-355164, EBI-723441;
CC P55072; Q9BZV1: UBXN6; NbExp=20; IntAct=EBI-355164, EBI-1993899;
CC P55072; O94888: UBXN7; NbExp=18; IntAct=EBI-355164, EBI-1993627;
CC P55072; O00124: UBXN8; NbExp=8; IntAct=EBI-355164, EBI-1993850;
CC P55072; Q92890: UFD1; NbExp=5; IntAct=EBI-355164, EBI-1994090;
CC P55072; P63027: VAMP2; NbExp=3; IntAct=EBI-355164, EBI-520113;
CC P55072; P55072: VCP; NbExp=7; IntAct=EBI-355164, EBI-355164;
CC P55072; Q6GPH4: XAF1; NbExp=3; IntAct=EBI-355164, EBI-2815120;
CC P55072; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-355164, EBI-2510804;
CC P55072; P63104: YWHAZ; NbExp=2; IntAct=EBI-355164, EBI-347088;
CC P55072; P24278: ZBTB25; NbExp=3; IntAct=EBI-355164, EBI-739899;
CC P55072; Q9WTX6: Cul1; Xeno; NbExp=2; IntAct=EBI-355164, EBI-1551052;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15456787}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:15215856}. Nucleus
CC {ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:26842564}. Cytoplasm,
CC Stress granule {ECO:0000269|PubMed:29804830}. Note=Present in the
CC neuronal hyaline inclusion bodies specifically found in motor neurons
CC from amyotrophic lateral sclerosis patients (PubMed:15456787). Present
CC in the Lewy bodies specifically found in neurons from Parkinson disease
CC patients (PubMed:15456787). Recruited to the cytoplasmic surface of the
CC endoplasmic reticulum via interaction with AMFR/gp78 (PubMed:16168377).
CC Following DNA double-strand breaks, recruited to the sites of damage
CC (PubMed:22120668). Recruited to stalled replication forks via
CC interaction with SPRTN (PubMed:23042605). Recruited to damaged
CC lysosomes decorated with K48-linked ubiquitin chains (PubMed:27753622).
CC Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress granules
CC (SGs) in response to arsenite-induced stress treatment
CC (PubMed:29804830). {ECO:0000269|PubMed:15456787,
CC ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:22120668,
CC ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:27753622,
CC ECO:0000269|PubMed:29804830}.
CC -!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with
CC the PUB domain of RNF31. {ECO:0000269|PubMed:24726327}.
CC -!- PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen
CC receptor activation. Phosphorylated in mitotic cells.
CC {ECO:0000250|UniProtKB:P46462}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the
CC presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity.
CC {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634}.
CC -!- DISEASE: Inclusion body myopathy with early-onset Paget disease with or
CC without frontotemporal dementia 1 (IBMPFD1) [MIM:167320]: An autosomal
CC dominant disease characterized by disabling muscle weakness clinically
CC resembling to limb girdle muscular dystrophy, osteolytic bone lesions
CC consistent with Paget disease, and premature frontotemporal dementia.
CC Clinical features show incomplete penetrance.
CC {ECO:0000269|PubMed:15034582, ECO:0000269|PubMed:15732117,
CC ECO:0000269|PubMed:16247064, ECO:0000269|PubMed:16321991,
CC ECO:0000269|PubMed:17935506, ECO:0000269|PubMed:20104022,
CC ECO:0000269|PubMed:20335036, ECO:0000269|PubMed:20512113,
CC ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:25125609, ECO:0000269|PubMed:25878907,
CC ECO:0000269|PubMed:27209344, ECO:0000269|PubMed:27753622,
CC ECO:0000269|PubMed:29804830}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Frontotemporal dementia and/or amyotrophic lateral sclerosis 6
CC (FTDALS6) [MIM:613954]: A neurodegenerative disorder characterized by
CC frontotemporal dementia and/or amyotrophic lateral sclerosis in
CC affected individuals. There is high intrafamilial variation.
CC Frontotemporal dementia (FTD) is characterized by frontal and temporal
CC lobe atrophy associated with neuronal loss, gliosis, and dementia.
CC Patients exhibit progressive changes in social, behavioral, and/or
CC language function. Amyotrophic lateral sclerosis (ALS) is characterized
CC by the death of motor neurons in the brain, brainstem, and spinal cord,
CC resulting in fatal paralysis. FTDALS6 is an autosomal dominant form
CC characterized by onset of ALS or FTD in adulthood. Some patients with
CC the disorder may have features of both diseases.
CC {ECO:0000269|PubMed:21145000, ECO:0000269|PubMed:23349634}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2Y (CMT2Y) [MIM:616687]: An
CC autosomal dominant, axonal form of Charcot-Marie-Tooth disease, a
CC disorder of the peripheral nervous system, characterized by progressive
CC weakness and atrophy, initially of the peroneal muscles and later of
CC the distal muscles of the arms. Charcot-Marie-Tooth disease is
CC classified in two main groups on the basis of electrophysiologic
CC properties and histopathology: primary peripheral demyelinating
CC neuropathies (designated CMT1 when they are dominantly inherited) and
CC primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2
CC group are characterized by signs of axonal degeneration in the absence
CC of obvious myelin alterations, normal or slightly reduced nerve
CC conduction velocities, and progressive distal muscle weakness and
CC atrophy. {ECO:0000269|PubMed:25125609, ECO:0000269|PubMed:25878907}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: It is unclear how it participates in the recruitment of
CC TP53BP1 at DNA damage sites. According to a first report, participates
CC in the recruitment of TP53BP1 by promoting ubiquitination and removal
CC of L3MBTL1 from DNA damage sites (PubMed:22120668). According to a
CC second report, it acts by removing 'Lys-48'-linked ubiquitination from
CC sites of DNA damage (PubMed:22020440). {ECO:0000305|PubMed:22020440,
CC ECO:0000305|PubMed:22120668}.
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DR EMBL; AC004472; AAC07984.1; -; Genomic_DNA.
DR EMBL; AF100752; AAD43016.1; -; mRNA.
DR EMBL; AK312310; BAG35235.1; -; mRNA.
DR EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58404.1; -; Genomic_DNA.
DR EMBL; BC110913; AAI10914.1; -; mRNA.
DR EMBL; BC121794; AAI21795.1; -; mRNA.
DR EMBL; Z70768; CAA94809.1; -; mRNA.
DR CCDS; CCDS6573.1; -.
DR PIR; T02243; T02243.
DR RefSeq; NP_009057.1; NM_007126.3.
DR PDB; 3EBB; X-ray; 1.90 A; E/F/G/H=797-806.
DR PDB; 3HU1; X-ray; 2.81 A; A/B/C/D/E/F=1-481.
DR PDB; 3HU2; X-ray; 2.85 A; A/B/C/D/E/F=1-481.
DR PDB; 3HU3; X-ray; 2.20 A; A/B=1-481.
DR PDB; 3QC8; X-ray; 2.20 A; A=21-196.
DR PDB; 3QQ7; X-ray; 2.65 A; A=2-187.
DR PDB; 3QQ8; X-ray; 2.00 A; A=2-187.
DR PDB; 3QWZ; X-ray; 2.00 A; A=1-208.
DR PDB; 3TIW; X-ray; 1.80 A; A/B=1-187.
DR PDB; 4KDI; X-ray; 1.86 A; A/B=21-196.
DR PDB; 4KDL; X-ray; 1.81 A; A=21-196.
DR PDB; 4KLN; X-ray; 2.62 A; A/B/C/D/E/F=1-481.
DR PDB; 4KO8; X-ray; 1.98 A; A/B=1-481.
DR PDB; 4KOD; X-ray; 2.96 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
DR PDB; 4P0A; X-ray; 2.30 A; B/D=797-806.
DR PDB; 5B6C; X-ray; 1.55 A; A=21-191.
DR PDB; 5C18; X-ray; 3.30 A; A/B/C/D/E/F=2-806.
DR PDB; 5C19; X-ray; 4.20 A; A/B/C/D/E/F=2-806.
DR PDB; 5C1A; X-ray; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L=2-806.
DR PDB; 5C1B; X-ray; 3.08 A; A/B/C/D/E/F=2-806.
DR PDB; 5DYG; X-ray; 2.20 A; A=1-460.
DR PDB; 5DYI; X-ray; 3.71 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
DR PDB; 5EPP; X-ray; 1.88 A; A=21-199.
DR PDB; 5FTJ; EM; 2.30 A; A/B/C/D/E/F=1-806.
DR PDB; 5FTK; EM; 2.40 A; A/B/C/D/E/F=1-806.
DR PDB; 5FTL; EM; 3.30 A; A/B/C/D/E/F=1-806.
DR PDB; 5FTM; EM; 3.20 A; A/B/C/D/E/F=1-806.
DR PDB; 5FTN; EM; 3.30 A; A/B/C/D/E/F=1-806.
DR PDB; 5GLF; X-ray; 2.25 A; A/C/E/G=21-199.
DR PDB; 5IFS; X-ray; 2.46 A; B/D=1-481.
DR PDB; 5IFW; X-ray; 3.40 A; B=2-806.
DR PDB; 5KIW; X-ray; 3.41 A; A/B=1-460.
DR PDB; 5KIY; X-ray; 2.79 A; A=1-460.
DR PDB; 5X4L; X-ray; 2.40 A; A/B=23-196.
DR PDB; 6G2V; X-ray; 1.90 A; A=462-764.
DR PDB; 6G2W; X-ray; 2.68 A; A=462-764.
DR PDB; 6G2X; X-ray; 2.08 A; A=462-764.
DR PDB; 6G2Y; X-ray; 2.15 A; A=462-764.
DR PDB; 6G2Z; X-ray; 1.92 A; A=462-764.
DR PDB; 6G30; X-ray; 2.42 A; A=462-764.
DR PDB; 6HD0; X-ray; 3.73 A; A/B/C/T/U/V=1-481.
DR PDB; 6MCK; X-ray; 3.77 A; A/B/C/D/E/F/G/H/I/J/K/L=210-806.
DR PDB; 7BP8; EM; 3.90 A; A/B/C/D/E/F=1-806.
DR PDB; 7BP9; EM; 3.60 A; A/B/C/D/E/F=1-806.
DR PDB; 7BPA; EM; 3.30 A; A/B/C/D/E/F=1-806.
DR PDB; 7BPB; EM; 4.30 A; A/B/C/D/E/F=1-806.
DR PDB; 7JY5; EM; 2.89 A; A/B/C/D/E/F=1-806.
DR PDB; 7K56; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7K57; EM; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7K59; EM; 4.20 A; A/B/C/D/E/F=1-806.
DR PDB; 7L5W; EM; 3.34 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7L5X; EM; 6.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7LMY; EM; 2.40 A; A/B/C/D/E/F=1-806.
DR PDB; 7LMZ; EM; 3.06 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN0; EM; 2.98 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN1; EM; 3.40 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN2; EM; 3.63 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN3; EM; 3.45 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN4; EM; 3.00 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN5; EM; 3.09 A; A/B/C/D/E/F=1-806.
DR PDB; 7LN6; EM; 3.58 A; A/B/C/D/E/F=1-806.
DR PDB; 7MDM; EM; 4.86 A; A/B/C/D/E/F=1-806.
DR PDB; 7MDO; EM; 4.12 A; A/B/C/D/E/F=1-806.
DR PDB; 7R7S; EM; 4.23 A; A/B/C/D/E/F=1-806.
DR PDB; 7R7T; EM; 4.50 A; A/B/C/D/E/F=1-806.
DR PDB; 7R7U; EM; 4.30 A; A/B/C/D/E/F=1-806.
DR PDB; 7RL6; EM; 3.70 A; A/B/C/D/E/F=2-806.
DR PDB; 7RL7; EM; 3.00 A; A/B/C/D/E/F=2-806.
DR PDB; 7RL9; EM; 3.30 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLA; EM; 3.10 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLB; EM; 3.30 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLC; EM; 3.20 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLD; EM; 3.40 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLF; EM; 3.10 A; A/B/C/D/E/F=1-806.
DR PDB; 7RLG; EM; 3.70 A; A/B/C/D/E/F=2-806.
DR PDB; 7RLH; EM; 3.00 A; A/B/C/D/E/F=1-806.
DR PDB; 7RLI; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=2-806.
DR PDB; 7RLJ; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L=21-775.
DR PDB; 7VCS; EM; 3.32 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7VCT; EM; 3.21 A; A/B/C/D/E/F=1-806.
DR PDB; 7VCU; EM; 3.15 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806.
DR PDB; 7VCV; EM; 3.21 A; A/B/C/D/E/F=1-806.
DR PDB; 7VCX; EM; 3.24 A; A/B/C/D/E/F=1-806.
DR PDBsum; 3EBB; -.
DR PDBsum; 3HU1; -.
DR PDBsum; 3HU2; -.
DR PDBsum; 3HU3; -.
DR PDBsum; 3QC8; -.
DR PDBsum; 3QQ7; -.
DR PDBsum; 3QQ8; -.
DR PDBsum; 3QWZ; -.
DR PDBsum; 3TIW; -.
DR PDBsum; 4KDI; -.
DR PDBsum; 4KDL; -.
DR PDBsum; 4KLN; -.
DR PDBsum; 4KO8; -.
DR PDBsum; 4KOD; -.
DR PDBsum; 4P0A; -.
DR PDBsum; 5B6C; -.
DR PDBsum; 5C18; -.
DR PDBsum; 5C19; -.
DR PDBsum; 5C1A; -.
DR PDBsum; 5C1B; -.
DR PDBsum; 5DYG; -.
DR PDBsum; 5DYI; -.
DR PDBsum; 5EPP; -.
DR PDBsum; 5FTJ; -.
DR PDBsum; 5FTK; -.
DR PDBsum; 5FTL; -.
DR PDBsum; 5FTM; -.
DR PDBsum; 5FTN; -.
DR PDBsum; 5GLF; -.
DR PDBsum; 5IFS; -.
DR PDBsum; 5IFW; -.
DR PDBsum; 5KIW; -.
DR PDBsum; 5KIY; -.
DR PDBsum; 5X4L; -.
DR PDBsum; 6G2V; -.
DR PDBsum; 6G2W; -.
DR PDBsum; 6G2X; -.
DR PDBsum; 6G2Y; -.
DR PDBsum; 6G2Z; -.
DR PDBsum; 6G30; -.
DR PDBsum; 6HD0; -.
DR PDBsum; 6MCK; -.
DR PDBsum; 7BP8; -.
DR PDBsum; 7BP9; -.
DR PDBsum; 7BPA; -.
DR PDBsum; 7BPB; -.
DR PDBsum; 7JY5; -.
DR PDBsum; 7K56; -.
DR PDBsum; 7K57; -.
DR PDBsum; 7K59; -.
DR PDBsum; 7L5W; -.
DR PDBsum; 7L5X; -.
DR PDBsum; 7LMY; -.
DR PDBsum; 7LMZ; -.
DR PDBsum; 7LN0; -.
DR PDBsum; 7LN1; -.
DR PDBsum; 7LN2; -.
DR PDBsum; 7LN3; -.
DR PDBsum; 7LN4; -.
DR PDBsum; 7LN5; -.
DR PDBsum; 7LN6; -.
DR PDBsum; 7MDM; -.
DR PDBsum; 7MDO; -.
DR PDBsum; 7R7S; -.
DR PDBsum; 7R7T; -.
DR PDBsum; 7R7U; -.
DR PDBsum; 7RL6; -.
DR PDBsum; 7RL7; -.
DR PDBsum; 7RL9; -.
DR PDBsum; 7RLA; -.
DR PDBsum; 7RLB; -.
DR PDBsum; 7RLC; -.
DR PDBsum; 7RLD; -.
DR PDBsum; 7RLF; -.
DR PDBsum; 7RLG; -.
DR PDBsum; 7RLH; -.
DR PDBsum; 7RLI; -.
DR PDBsum; 7RLJ; -.
DR PDBsum; 7VCS; -.
DR PDBsum; 7VCT; -.
DR PDBsum; 7VCU; -.
DR PDBsum; 7VCV; -.
DR PDBsum; 7VCX; -.
DR AlphaFoldDB; P55072; -.
DR SMR; P55072; -.
DR BioGRID; 113258; 1043.
DR ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex.
DR ComplexPortal; CPX-262; NSFL1C-VCP complex.
DR CORUM; P55072; -.
DR DIP; DIP-33543N; -.
DR IntAct; P55072; 165.
DR MINT; P55072; -.
DR STRING; 9606.ENSP00000351777; -.
DR BindingDB; P55072; -.
DR ChEMBL; CHEMBL1075145; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DrugCentral; P55072; -.
DR MoonDB; P55072; Predicted.
DR TCDB; 3.A.16.1.1; the endoplasmic reticular retrotranslocon (er-rt) family.
DR CarbonylDB; P55072; -.
DR GlyGen; P55072; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55072; -.
DR MetOSite; P55072; -.
DR PhosphoSitePlus; P55072; -.
DR SwissPalm; P55072; -.
DR BioMuta; VCP; -.
DR DMDM; 6094447; -.
DR DOSAC-COBS-2DPAGE; P55072; -.
DR OGP; P55072; -.
DR REPRODUCTION-2DPAGE; IPI00022774; -.
DR REPRODUCTION-2DPAGE; P55072; -.
DR CPTAC; CPTAC-295; -.
DR CPTAC; CPTAC-296; -.
DR EPD; P55072; -.
DR jPOST; P55072; -.
DR MassIVE; P55072; -.
DR PaxDb; P55072; -.
DR PeptideAtlas; P55072; -.
DR PRIDE; P55072; -.
DR ProteomicsDB; 56776; -.
DR TopDownProteomics; P55072; -.
DR ABCD; P55072; 1 sequenced antibody.
DR Antibodypedia; 2215; 679 antibodies from 43 providers.
DR DNASU; 7415; -.
DR Ensembl; ENST00000358901.11; ENSP00000351777.6; ENSG00000165280.18.
DR GeneID; 7415; -.
DR KEGG; hsa:7415; -.
DR MANE-Select; ENST00000358901.11; ENSP00000351777.6; NM_007126.5; NP_009057.1.
DR CTD; 7415; -.
DR DisGeNET; 7415; -.
DR GeneCards; VCP; -.
DR GeneReviews; VCP; -.
DR HGNC; HGNC:12666; VCP.
DR HPA; ENSG00000165280; Low tissue specificity.
DR MalaCards; VCP; -.
DR MIM; 167320; phenotype.
DR MIM; 601023; gene.
DR MIM; 613954; phenotype.
DR MIM; 616687; phenotype.
DR neXtProt; NX_P55072; -.
DR OpenTargets; ENSG00000165280; -.
DR Orphanet; 329478; Adult-onset distal myopathy due to VCP mutation.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR Orphanet; 435387; Autosomal dominant Charcot-Marie-Tooth disease type 2Y.
DR Orphanet; 275864; Behavioral variant of frontotemporal dementia.
DR Orphanet; 275872; Frontotemporal dementia with motor neuron disease.
DR Orphanet; 52430; Inclusion body myopathy with Paget disease of bone and frontotemporal dementia.
DR Orphanet; 100070; Progressive non-fluent aphasia.
DR Orphanet; 329475; Spastic paraplegia-Paget disease of bone syndrome.
DR PharmGKB; PA37289; -.
DR VEuPathDB; HostDB:ENSG00000165280; -.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00900000141071; -.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; P55072; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; P55072; -.
DR TreeFam; TF300542; -.
DR BRENDA; 3.6.4.6; 2681.
DR PathwayCommons; P55072; -.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-3371511; HSF1 activation.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5689877; Josephin domain DUBs.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-8876725; Protein methylation.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9678110; Attachment and Entry.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; P55072; -.
DR SIGNOR; P55072; -.
DR BioGRID-ORCS; 7415; 813 hits in 1055 CRISPR screens.
DR ChiTaRS; VCP; human.
DR EvolutionaryTrace; P55072; -.
DR GeneWiki; Valosin-containing_protein; -.
DR GenomeRNAi; 7415; -.
DR Pharos; P55072; Tchem.
DR PRO; PR:P55072; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P55072; protein.
DR Bgee; ENSG00000165280; Expressed in stromal cell of endometrium and 208 other tissues.
DR ExpressionAtlas; P55072; baseline and differential.
DR Genevisible; P55072; HS.
DR GO; GO:1904949; C:ATPase complex; IEA:Ensembl.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000502; C:proteasome complex; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IPI:ComplexPortal.
DR GO; GO:1990730; C:VCP-NSFL1C complex; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
DR GO; GO:0046034; P:ATP metabolic process; IEA:Ensembl.
DR GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:UniProtKB.
DR GO; GO:1903843; P:cellular response to arsenite ion; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB.
DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; IMP:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:UniProtKB.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036503; P:ERAD pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045184; P:establishment of protein localization; TAS:UniProtKB.
DR GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; IMP:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
DR GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IDA:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:UniProtKB.
DR GO; GO:0035617; P:stress granule disassembly; IMP:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR GO; GO:0019079; P:viral genome replication; IMP:CACAO.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID00201; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amyotrophic lateral sclerosis; ATP-binding;
KW Autophagy; Charcot-Marie-Tooth disease; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA damage; DNA repair;
KW Endoplasmic reticulum; Hydrolase; Isopeptide bond; Lipid-binding;
KW Methylation; Neurodegeneration; Neuropathy; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transport; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..806
FT /note="Transitional endoplasmic reticulum ATPase"
FT /id="PRO_0000084572"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..806
FT /note="Interaction with UBXN6"
FT /evidence="ECO:0000269|PubMed:18656546"
FT MOTIF 802..806
FT /note="PIM motif"
FT /evidence="ECO:0000269|PubMed:24726327"
FT COMPBIAS 768..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20512113"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20512113"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:20512113"
FT BINDING 521..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 315
FT /note="N6,N6,N6-trimethyllysine; by VCPKMT"
FT /evidence="ECO:0000269|PubMed:22948820,
FT ECO:0000269|PubMed:23349634"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 502
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 505
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 668
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 668
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 805
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 95
FT /note="R -> G (in IBMPFD1; cultured cells expressing the
FT mutant protein show a marked general increase in the level
FT of ubiquitin-conjugated proteins and impaired protein
FT degradation through the endoplasmic reticulum-associated
FT degradation (ERAD) pathway; shows strongly reduced affinity
FT for ADP and increased affinity for ATP; abolishes
FT enhancement of K-315 methylation by ASPSCR1; decreased
FT interaction with CAV1 and UBXN6; dbSNP:rs121909332)"
FT /evidence="ECO:0000269|PubMed:15034582,
FT ECO:0000269|PubMed:16321991, ECO:0000269|PubMed:20512113,
FT ECO:0000269|PubMed:21822278"
FT /id="VAR_033016"
FT VARIANT 97
FT /note="G -> E (in CMT2Y; increased ATPase activity;
FT dbSNP:rs864309502)"
FT /evidence="ECO:0000269|PubMed:25878907"
FT /id="VAR_076464"
FT VARIANT 126
FT /note="I -> F (in IBMPFD1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27209344"
FT /id="VAR_076465"
FT VARIANT 155
FT /note="R -> C (in IBMPFD1; also in one patient without
FT evidence of Paget disease of the bone; dbSNP:rs121909330)"
FT /evidence="ECO:0000269|PubMed:15034582,
FT ECO:0000269|PubMed:15732117"
FT /id="VAR_033017"
FT VARIANT 155
FT /note="R -> H (in FTDALS6 and IBMPFD1; properly assembles
FT into a hexameric structure; cultured cells expressing the
FT mutant protein show a marked general increase in the level
FT of ubiquitin-conjugated proteins and impaired protein
FT degradation through the endoplasmic reticulum-associated
FT degradation (ERAD) pathway; shows strongly reduced affinity
FT for ADP and increased affinity for ATP; shows normal ATPase
FT activity according to PubMed:16321991 while according to
FT PubMed:25878907 and PubMed:25125609 shows increased ATPase
FT activity; no defect in ubiquitin-dependent protein
FT degradation by the proteasome; impaired autophagic
FT function; defective maturation of ubiquitin-containing
FT autophagosomes; decreased interaction with CAV1 and UBXN6;
FT decreased endosome to lysosome transport via multivesicular
FT body sorting pathway of CAV1; decreases the arsenite-
FT induced stress granules (SGs) clearance process;
FT dbSNP:rs121909329)"
FT /evidence="ECO:0000269|PubMed:15034582,
FT ECO:0000269|PubMed:16321991, ECO:0000269|PubMed:20104022,
FT ECO:0000269|PubMed:20512113, ECO:0000269|PubMed:21145000,
FT ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:23349634,
FT ECO:0000269|PubMed:25125609, ECO:0000269|PubMed:25878907,
FT ECO:0000269|PubMed:27753622, ECO:0000269|PubMed:29804830"
FT /id="VAR_033018"
FT VARIANT 155
FT /note="R -> L (in IBMPFD1; dbSNP:rs121909329)"
FT /evidence="ECO:0000269|PubMed:20335036"
FT /id="VAR_078910"
FT VARIANT 155
FT /note="R -> P (in IBMPFD1; dbSNP:rs121909329)"
FT /evidence="ECO:0000269|PubMed:15034582"
FT /id="VAR_033019"
FT VARIANT 155
FT /note="R -> S (in IBMPFD1; impaired autophagic function;
FT dbSNP:rs121909330)"
FT /evidence="ECO:0000269|PubMed:20104022"
FT /id="VAR_076466"
FT VARIANT 159
FT /note="R -> G (in FTDALS6; dbSNP:rs387906789)"
FT /evidence="ECO:0000269|PubMed:21145000,
FT ECO:0000269|PubMed:23349634"
FT /id="VAR_065910"
FT VARIANT 159
FT /note="R -> H (in IBMPFD1; without frontotemporal dementia;
FT abolishes enhancement of K-315 methylation by ASPSCR1;
FT dbSNP:rs121909335)"
FT /evidence="ECO:0000269|PubMed:16247064"
FT /id="VAR_033020"
FT VARIANT 185
FT /note="E -> K (in CMT2Y; normal ATPase activity; impaired
FT autophagic function; dbSNP:rs864309501)"
FT /evidence="ECO:0000269|PubMed:25125609"
FT /id="VAR_076467"
FT VARIANT 191
FT /note="R -> Q (in FTDALS6 and IBMPFD1; abolishes
FT enhancement of K-315 methylation by ASPSCR1;
FT dbSNP:rs121909334)"
FT /evidence="ECO:0000269|PubMed:15034582,
FT ECO:0000269|PubMed:21145000, ECO:0000269|PubMed:23349634"
FT /id="VAR_033021"
FT VARIANT 198
FT /note="L -> W (in IBMPFD1; increased ATPase activity;
FT impaired autophagic function; dbSNP:rs748447593)"
FT /evidence="ECO:0000269|PubMed:17935506,
FT ECO:0000269|PubMed:20335036, ECO:0000269|PubMed:25878907,
FT ECO:0000269|PubMed:27753622"
FT /id="VAR_076468"
FT VARIANT 232
FT /note="A -> E (in IBMPFD1; increased ATPase activity; no
FT defect in ubiquitin-dependent protein degradation by the
FT proteasome; impaired autophagic function; defect in
FT maturation of ubiquitin-containing autophagosomes;
FT decreased interaction with CAV1 and UBXN6;
FT dbSNP:rs121909331)"
FT /evidence="ECO:0000269|PubMed:15034582,
FT ECO:0000269|PubMed:20104022, ECO:0000269|PubMed:21822278,
FT ECO:0000269|PubMed:25125609, ECO:0000269|PubMed:25878907,
FT ECO:0000269|PubMed:27753622"
FT /id="VAR_033022"
FT VARIANT 387
FT /note="N -> H (in IBMPFD1; unknown pathological
FT significance; dbSNP:rs1554668420)"
FT /evidence="ECO:0000269|PubMed:17935506"
FT /id="VAR_078911"
FT VARIANT 592
FT /note="D -> N (in FTDALS6; dbSNP:rs387906790)"
FT /evidence="ECO:0000269|PubMed:21145000"
FT /id="VAR_065911"
FT MUTAGEN 52..55
FT /note="FRGD->ARGA: Abolishes interaction with NPLOC4; when
FT associated with A-110."
FT /evidence="ECO:0000269|PubMed:26471729"
FT MUTAGEN 53
FT /note="R->A: Minor effect on affinity for ATP and ADP."
FT /evidence="ECO:0000269|PubMed:20512113"
FT MUTAGEN 86
FT /note="R->A: Strongly increased affinity for ATP. Strongly
FT reduced affinity for ADP."
FT /evidence="ECO:0000269|PubMed:20512113"
FT MUTAGEN 110
FT /note="Y->A: Abolishes interaction with NPLOC4; when
FT associated with 52-A--A-55."
FT /evidence="ECO:0000269|PubMed:26471729"
FT MUTAGEN 113..115
FT /note="RIH->TIT: Severely reduced binding to DERL1."
FT /evidence="ECO:0000269|PubMed:27714797"
FT MUTAGEN 131
FT /note="F->R: Severely reduced binding to DERL1."
FT /evidence="ECO:0000269|PubMed:27714797"
FT MUTAGEN 140
FT /note="L->D: Severely reduced binding to DERL1."
FT /evidence="ECO:0000269|PubMed:27714797"
FT MUTAGEN 179
FT /note="D->R: No effect on binding to DERL1."
FT /evidence="ECO:0000269|PubMed:27714797"
FT MUTAGEN 183
FT /note="H->W: Severely reduced binding to DERL1."
FT /evidence="ECO:0000269|PubMed:27714797"
FT MUTAGEN 251
FT /note="K->Q: Impairs ERAD degradation of HMGCR and does not
FT inhibit interaction with RHBDD1; when associated with Q-
FT 524."
FT /evidence="ECO:0000269|PubMed:16168377,
FT ECO:0000269|PubMed:22795130"
FT MUTAGEN 305
FT /note="E->Q: Defect in ubiquitin-dependent protein
FT degradation by the proteasome; when associated with Q-578."
FT /evidence="ECO:0000269|PubMed:20104022,
FT ECO:0000269|PubMed:26471729"
FT MUTAGEN 312
FT /note="K->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 313
FT /note="R->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 314
FT /note="E->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 314
FT /note="Missing: Strongly impairs methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 315
FT /note="K->L,Q,R: Abolishes methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820,
FT ECO:0000269|PubMed:23349634"
FT MUTAGEN 316
FT /note="T->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 317
FT /note="H->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 318
FT /note="G->A: Does not affect methylation by VCPKMT."
FT /evidence="ECO:0000269|PubMed:22948820"
FT MUTAGEN 524
FT /note="K->A: Impairs catalytic activity of RNF19A toward
FT SOD1 mutant. Does not inhibit interaction with RHBDD1; when
FT associated with A-251."
FT /evidence="ECO:0000269|PubMed:15456787,
FT ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:22795130"
FT MUTAGEN 524
FT /note="K->Q: Impairs ERAD degradation of HMGCR; when
FT associated with Q-251."
FT /evidence="ECO:0000269|PubMed:15456787,
FT ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:22795130"
FT MUTAGEN 578
FT /note="E->Q: Does not inhibit interaction with RHBDD1.
FT Increased interaction with CAV1 and UBXN6. Impaired
FT autophagic function. Defect in ubiquitin-dependent protein
FT degradation by the proteasome; when associated with Q-305.
FT Increases interaction with ZFAND1 in an arsenite-dependent
FT manner."
FT /evidence="ECO:0000269|PubMed:20104022,
FT ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:22795130,
FT ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:29804830"
FT CONFLICT 169
FT /note="D -> H (in Ref. 6; AAI21795)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="K -> I (in Ref. 3; BAG35235)"
FT /evidence="ECO:0000305"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7LMY"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7BPA"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7RLD"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5FTN"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3QQ8"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3HU1"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7RL7"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5IFS"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:5B6C"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4KDI"
FT STRAND 161..176
FT /evidence="ECO:0007829|PDB:5B6C"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5B6C"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4KDL"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5FTJ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4KLN"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5FTK"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:5DYG"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:4KO8"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:7RL7"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5DYG"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:4KO8"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5FTJ"
FT HELIX 408..424
FT /evidence="ECO:0007829|PDB:4KO8"
FT TURN 425..429
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:3HU1"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 449..457
FT /evidence="ECO:0007829|PDB:4KO8"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:4KO8"
FT TURN 462..468
FT /evidence="ECO:0007829|PDB:4KO8"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 483..498
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:7LN0"
FT HELIX 557..568
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:6G2V"
FT TURN 584..586
FT /evidence="ECO:0007829|PDB:5FTN"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:5FTJ"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:7RL9"
FT HELIX 597..609
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 613..615
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 617..624
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 635..639
FT /evidence="ECO:0007829|PDB:5FTK"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 650..661
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:7LN0"
FT HELIX 672..677
FT /evidence="ECO:0007829|PDB:6G2V"
FT TURN 678..681
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 684..711
FT /evidence="ECO:0007829|PDB:6G2V"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:5IFW"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:7LMY"
FT HELIX 733..739
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 749..761
FT /evidence="ECO:0007829|PDB:6G2V"
FT HELIX 763..765
FT /evidence="ECO:0007829|PDB:7JY5"
FT STRAND 767..770
FT /evidence="ECO:0007829|PDB:7RLI"
SQ 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
