ID TERA_HUMAN Reviewed; 806 AA. AC P55072; B2R5T8; Q0V924; Q2TAI5; Q969G7; Q9UCD5; V9HW80; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 28-JAN-2026, entry version 248. 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; GN Synonyms=HEL-220 {ECO:0000312|EMBL:ACI46036.1}, GN HEL-S-70 {ECO:0000312|EMBL:ACI46044.1}; 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 [MRNA]. RA Li J., Wang H., Liu J., Liu F.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] RP INTERACTION WITH SVIP AND DERL1. RX PubMed=17872946; DOI=10.1074/jbc.m704446200; RA Ballar P., Zhong Y., Nagahama M., Tagaya M., Shen Y., Fang S.; RT "Identification of SVIP as an endogenous inhibitor of endoplasmic RT reticulum-associated degradation."; RL J. Biol. Chem. 282:33908-33914(2007). RN [26] 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 [47] 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 [48] 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 [49] 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 [50] 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 [51] 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 [52] 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 [53] 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 [54] 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 [55] 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 [56] 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 [57] 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 [58] 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 [59] 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 [60] 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 [61] 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 [62] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH STUB1; UBXN2A AND CHRNA3, AND RP INTERACTION WITH UBXN2A. RX PubMed=26265139; DOI=10.1016/j.bcp.2015.08.084; RA Teng Y., Rezvani K., De Biasi M.; RT "UBXN2A regulates nicotinic receptor degradation by modulating the E3 RT ligase activity of CHIP."; RL Biochem. Pharmacol. 97:518-530(2015). RN [63] 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 [64] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RIGI 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 [65] 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 [66] 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 [67] 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 [68] 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 [69] 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 [70] 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 [71] 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 [72] 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 [73] 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 [74] 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 [75] RP FUNCTION. RX PubMed=34739333; DOI=10.1126/science.abf6548; RA Gwon Y., Maxwell B.A., Kolaitis R.M., Zhang P., Kim H.J., Taylor J.P.; RT "Ubiquitination of G3BP1 mediates stress granule disassembly in a context- RT specific manner."; RL Science 372:eabf6548-eabf6548(2021). RN [76] RP FUNCTION. RX PubMed=35013556; DOI=10.1038/s41556-021-00807-6; RA Krastev D.B., Li S., Sun Y., Wicks A.J., Hoslett G., Weekes D., RA Badder L.M., Knight E.G., Marlow R., Pardo M.C., Yu L., Talele T.T., RA Bartek J., Choudhary J.S., Pommier Y., Pettitt S.J., Tutt A.N.J., RA Ramadan K., Lord C.J.; RT "The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from RT chromatin."; RL Nat. Cell Biol. 24:62-73(2022). RN [77] RP FUNCTION, UFMYLATION AT LYS-109, INTERACTION WITH NPLOC4, AND MUTAGENESIS RP OF LYS-109 AND TYR-110. RX PubMed=38762759; DOI=10.1080/15548627.2024.2356488; RA Wang Z., Xiong S., Wu Z., Wang X., Gong Y., Zhu W.G., Xu X.; RT "VCP/p97 UFMylation stabilizes BECN1 and facilitates the initiation of RT autophagy."; RL Autophagy 20:2041-2054(2024). RN [78] 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 [79] 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 [80] 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 [81] {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 [82] 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 [83] 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 [84] 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 [85] 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 [86] 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 [87] 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 [88] 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 [89] RP INTERACTION WITH FBXL4. RX PubMed=36896912; DOI=10.15252/embj.2022113033; RA Cao Y., Zheng J., Wan H., Sun Y., Fu S., Liu S., He B., Cai G., Cao Y., RA Huang H., Li Q., Ma Y., Chen S., Wang F., Jiang H.; RT "A mitochondrial SCF-FBXL4 ubiquitin E3 ligase complex degrades BNIP3 and RT NIX to restrain mitophagy and prevent mitochondrial disease."; RL EMBO J. 42:e113033-e113033(2023). RN [90] 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 [91] 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 [92] 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 [93] 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 [94] 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 [95] 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). RN [96] RP VARIANTS IBMPFD1 THR-160; PHE-254 AND THR-369. RX PubMed=36980948; DOI=10.3390/genes14030676; RA Columbres R.C.A., Chin Y., Pratti S., Quinn C., Gonzalez-Cuyar L.F., RA Weiss M., Quintero-Rivera F., Kimonis V.; RT "Novel Variants in the VCP Gene Causing Multisystem Proteinopathy 1."; RL Genes (Basel) 14:0-0(2023). 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. Mediates the endoplasmic reticulum- CC associated degradation of CHRNA3 in cortical neurons as part of the CC STUB1-VCP-UBXN2A complex (PubMed:26265139). Involved in endoplasmic CC reticulum stress-induced pre-emptive quality control, a mechanism that CC selectively attenuates the translocation of newly synthesized proteins CC into the endoplasmic reticulum and reroutes them to the cytosol for CC proteasomal degradation (PubMed:26565908). Involved in clearance CC process by mediating G3BP1 extraction from stress granules CC (PubMed:29804830, PubMed:34739333). Also involved in DNA damage CC response: recruited to double-strand breaks (DSBs) sites in a RNF8- and CC RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA CC damage sites (PubMed:22020440, PubMed:22120668). Recruited to stalled CC replication forks by SPRTN: may act by mediating extraction of DNA CC polymerase eta (POLH) to prevent excessive translesion DNA synthesis CC and limit the incidence of mutations induced by DNA damage CC (PubMed:23042605, PubMed:23042607). Together with SPRTN CC metalloprotease, involved in the repair of covalent DNA-protein cross- CC links (DPCs) during DNA synthesis (PubMed:32152270). Involved in CC interstrand cross-link repair in response to replication stress by CC mediating unloading of the ubiquitinated CMG helicase complex (By CC similarity). Mediates extraction of PARP1 trapped to chromatin: CC recognizes and binds ubiquitinated PARP1 and promotes its removal CC (PubMed:35013556). Required for cytoplasmic retrotranslocation of CC stressed/damaged mitochondrial outer-membrane proteins and their CC subsequent proteasomal degradation (PubMed:16186510, PubMed:21118995). CC Essential for the maturation of ubiquitin-containing autophagosomes and CC the clearance of ubiquitinated protein by autophagy (PubMed:20104022, CC PubMed:27753622, PubMed:38762759). Acts as a negative regulator of type CC I interferon production by interacting with RIGI: interaction takes CC place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CC CARD domains, leading to recruit RNF125 and promote ubiquitination and CC degradation of RIGI (PubMed:26471729). May play a role in the CC ubiquitin-dependent sorting of membrane proteins to lysosomes where CC they undergo degradation (PubMed:21822278). May more particularly play CC a role in caveolins sorting in cells (PubMed:21822278, CC PubMed:23335559). By controlling the steady-state expression of the CC IGF1R receptor, indirectly regulates the insulin-like growth factor CC receptor signaling pathway (PubMed:26692333). CC {ECO:0000250|UniProtKB:P23787, ECO:0000269|PubMed:15456787, CC ECO:0000269|PubMed:16168377, ECO:0000269|PubMed:16186510, CC ECO:0000269|PubMed:20104022, ECO:0000269|PubMed:21118995, CC ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:22020440, CC ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22607976, CC ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607, CC ECO:0000269|PubMed:23335559, ECO:0000269|PubMed:26265139, 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 ECO:0000269|PubMed:34739333, ECO:0000269|PubMed:35013556, CC ECO:0000269|PubMed:38762759}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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, PubMed:38762759). Interaction with VCIP135 leads to CC dissociation of the complex via ATP hydrolysis by VCP. Part of a CC ternary complex containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C- CC like protein p37; the complex has membrane fusion activity and is CC required for Golgi and endoplasmic reticulum biogenesis. Interacts with CC SELENOS and SYVN1, as well as with DERL1 (via SHP-box motif), DERL2 and CC DERL3; which probably transfer misfolded proteins from the ER to VCP CC (PubMed:15215856, PubMed:16186509, PubMed:16186510, PubMed:16289116, CC PubMed:16449189, PubMed:27714797). Interacts with SVIP and forms a CC complex with SVIP and DERL1 (PubMed:17872946). Component of a complex CC required to couple retrotranslocation, ubiquitination and CC deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Part of CC a complex composed of STUB1/CHIP, VCP/p97, CHRNA3, and UBXN2A that CC modulates the ubiquitination and endoplasmic reticulum-associated CC degradation (ERAD) of CHRNA3 (PubMed:26265139). Within the complex CC UBXN2A acts as a scaffold protein required for the interaction of CC CHRNA3 with VCP/p97, this interaction also inhibits CHRNA3 CC ubiquitination by STUB1/CHIP and subsequently ERAD (PubMed:26265139). CC Interacts with UBXN2A (via UBX domain); the interaction is required for CC the interaction of CHRNA3 in the STUB1-VCP-UBXN2A complex CC (PubMed:26265139). Directly interacts with UBXN4 and RNF19A. Interacts CC with CASR. Interacts with UBE4B and YOD1. Interacts with clathrin. CC Interacts with RNF103. Interacts with TRIM13 and TRIM21. Component of a CC VCP/p97-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:23042605, PubMed:23042607). 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 RIGI and RNF125; CC interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked CC ubiquitin on its CARD domains, leading to recruit RNF125 and promote CC ubiquitination and degradation of RIGI (PubMed:26471729). Interacts CC with BAG6 (PubMed:21636303). Interacts with UBXN10 (PubMed:26389662). CC Interacts with UBXN6; the interaction with UBXN6 is direct and CC competitive with UFD1 (PubMed:19174149, PubMed:19275885). Forms a CC ternary complex with CAV1 and UBXN6 (PubMed:18656546, PubMed:19174149, CC PubMed:21822278). Interacts with PLAA, UBXN6 and YOD1; may form a CC complex involved in macroautophagy (PubMed:27753622). Interacts with CC ANKZF1 (PubMed:28302725). Interacts with ubiquitin-binding protein FAF1 CC (PubMed:26842564). Interacts with ZFAND2B (via VIM motif); the CC interaction is direct (PubMed:24160817, PubMed:26337389). Interacts CC with ZFAND1 (via its ubiquitin-like region); this interaction occurs in CC an arsenite-dependent manner (PubMed:29804830). Interacts with CCDC47 CC (By similarity). Interacts with UBAC2 (By similarity). Interacts with CC LMBR1L (PubMed:31073040). Interacts with ATXN3 (PubMed:30455355). CC Interacts with TEX264; bridging VCP to covalent DNA-protein cross-links CC (DPCs) (PubMed:32152270). Interacts with FBXL4 (PubMed:36896912). 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:17872946, CC ECO:0000269|PubMed:18022694, ECO:0000269|PubMed:18656546, CC ECO:0000269|PubMed:18675248, ECO:0000269|PubMed:19174149, CC ECO:0000269|PubMed:19275885, ECO:0000269|PubMed:19818707, CC ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:19887378, CC ECO:0000269|PubMed:20512113, ECO:0000269|PubMed:20833645, CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21822278, CC ECO:0000269|PubMed:21914798, ECO:0000269|PubMed:21949850, CC ECO:0000269|PubMed:22120668, ECO:0000269|PubMed:22537386, CC ECO:0000269|PubMed:22795130, ECO:0000269|PubMed:22902628, CC ECO:0000269|PubMed:23042605, ECO:0000269|PubMed:23042607, CC ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:24726327, CC ECO:0000269|PubMed:26265139, 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:36896912, CC ECO:0000269|PubMed:38762759, 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=36; IntAct=EBI-355164, EBI-1993677; CC P55072; A9UGY9: ATG5; NbExp=3; IntAct=EBI-355164, EBI-10175276; 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=18; IntAct=EBI-355164, EBI-946068; CC P55072; Q96LK0: CEP19; NbExp=6; 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: DTNB; NbExp=4; IntAct=EBI-355164, EBI-740402; 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: FAF1; NbExp=3; IntAct=EBI-355164, EBI-718246; CC P55072; Q9UNN5-1: FAF1; NbExp=4; IntAct=EBI-355164, EBI-15930546; CC P55072; Q96CS3: FAF2; NbExp=16; IntAct=EBI-355164, EBI-1055805; CC P55072; O94868: FCHSD2; NbExp=2; IntAct=EBI-355164, EBI-1215612; CC P55072; P09471: GNAO1; NbExp=5; IntAct=EBI-355164, EBI-715087; CC P55072; P62993: GRB2; NbExp=5; IntAct=EBI-355164, EBI-401755; CC P55072; P04792: HSPB1; NbExp=3; IntAct=EBI-355164, EBI-352682; CC P55072; P42858: HTT; NbExp=10; IntAct=EBI-355164, EBI-466029; CC P55072; Q8TBB1: LNX1; NbExp=7; 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; Q9HC29: NOD2; NbExp=5; IntAct=EBI-355164, EBI-7445625; CC P55072; Q8TAT6: NPLOC4; NbExp=17; IntAct=EBI-355164, EBI-1994109; CC P55072; Q9UNZ2: NSFL1C; NbExp=28; IntAct=EBI-355164, EBI-721577; CC P55072; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-355164, EBI-741158; CC P55072; Q9Y263: PLAA; NbExp=9; IntAct=EBI-355164, EBI-1994037; CC P55072; Q07869: PPARA; NbExp=3; IntAct=EBI-355164, EBI-78615; CC P55072; P62136: PPP1CA; NbExp=3; IntAct=EBI-355164, EBI-357253; CC P55072; P07602-1: PSAP; NbExp=3; IntAct=EBI-355164, EBI-10635648; CC P55072; P25786: PSMA1; NbExp=8; IntAct=EBI-355164, EBI-359352; CC P55072; P62191: PSMC1; NbExp=5; 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; Q96EQ8: RNF125; NbExp=3; IntAct=EBI-355164, EBI-2339208; CC P55072; O76064: RNF8; NbExp=3; IntAct=EBI-355164, EBI-373337; CC P55072; P32969: RPL9P9; NbExp=7; 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; Q9Y4K3: TRAF6; NbExp=2; IntAct=EBI-355164, EBI-359276; 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=6; IntAct=EBI-355164, EBI-751901; CC P55072; Q04323: UBXN1; NbExp=9; IntAct=EBI-355164, EBI-1058647; 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=20; IntAct=EBI-355164, EBI-1993668; CC P55072; Q14CS0: UBXN2B; NbExp=16; IntAct=EBI-355164, EBI-1993619; CC P55072; Q92575: UBXN4; NbExp=12; IntAct=EBI-355164, EBI-723441; CC P55072; Q9BZV1: UBXN6; NbExp=26; IntAct=EBI-355164, EBI-1993899; CC P55072; Q9BZV1-2: UBXN6; NbExp=3; IntAct=EBI-355164, EBI-21851820; CC P55072; O94888: UBXN7; NbExp=19; IntAct=EBI-355164, EBI-1993627; CC P55072; O00124: UBXN8; NbExp=9; IntAct=EBI-355164, EBI-1993850; CC P55072; Q92890: UFD1; NbExp=10; IntAct=EBI-355164, EBI-1994090; CC P55072; P63027: VAMP2; NbExp=5; IntAct=EBI-355164, EBI-520113; CC P55072; Q969W3: VCF1; NbExp=10; IntAct=EBI-355164, EBI-10281506; CC P55072; P55072: VCP; NbExp=8; 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=4; 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 -!- PTM: UFMylated al Lys-109; UFMylation enhances the interactions between CC BECN1 and other components of the PtdIns3K complex and thereby promotes CC cellular autophagy initiation. {ECO:0000269|PubMed:38762759}. 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, ECO:0000269|PubMed:36980948}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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, axonal, type 2Y (CMT2Y) CC [MIM:616687]: An autosomal dominant, axonal form of Charcot-Marie-Tooth CC disease, a disorder of the peripheral nervous system, characterized by CC progressive weakness and atrophy, initially of the peroneal muscles and CC later of 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC004472; AAC07984.1; -; Genomic_DNA. DR EMBL; FJ224344; ACI46036.1; -; mRNA. DR EMBL; FJ224352; ACI46044.1; -; mRNA. 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_007126.5. 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; 7MHS; EM; 3.60 A; A/B/C/D/E=1-806. DR PDB; 7OAT; X-ray; 3.00 A; B=2-480. DR PDB; 7PUX; X-ray; 1.73 A; A=1-460. 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 PDB; 7Y4W; EM; 3.67 A; A/B/C/D/E/F=21-806. DR PDB; 7Y53; EM; 3.61 A; A/B/C/D/E/F=21-806. DR PDB; 7Y59; EM; 4.51 A; A/B/C/D/E/F=21-806. DR PDB; 8B5R; EM; 6.10 A; A/B/C/D/E/F=2-806. DR PDB; 8FCL; EM; 3.51 A; A/B/C/D/E/F=1-806. DR PDB; 8FCM; EM; 3.27 A; A/B/C/D/E/F=1-806. DR PDB; 8FCN; EM; 2.95 A; A/B/C/D/E/F=1-806. DR PDB; 8FCO; EM; 3.31 A; A/B/C/D/E/F=1-806. DR PDB; 8FCP; EM; 3.52 A; A/B/C/D/E/F=1-806. DR PDB; 8FCQ; EM; 3.93 A; A/B/C/D/E/F=1-806. DR PDB; 8FCR; EM; 4.12 A; A/B/C/D/E/F=1-806. DR PDB; 8FCT; EM; 3.42 A; A/B/C/D/E/F=1-806. DR PDB; 8HL7; X-ray; 2.80 A; B=23-458. DR PDB; 8HRZ; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=21-458. DR PDB; 8KG2; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=21-458. DR PDB; 8OOI; EM; 2.61 A; A/B/C/D/E/F=1-806. DR PDB; 8PQX; EM; 3.30 A; A/B/C/D/E/F=1-806. DR PDB; 8R0E; EM; 2.70 A; A/B/C/D/E/F=1-806. DR PDB; 8RS9; EM; 3.40 A; A/B/C/D/E/F=1-806. DR PDB; 8RSB; EM; 3.40 A; A/B/C/D/E/F=1-806. DR PDB; 8RSC; EM; 3.60 A; A/B/C/D/E/F=1-806. DR PDB; 8UV2; EM; 3.23 A; A/B/C/D/E/F=1-806. DR PDB; 8UVO; EM; 3.22 A; A/B/C/D/E/F=1-806. DR PDB; 8UVP; EM; 3.60 A; A/B/C/D/E/F=1-806. DR PDB; 8UVQ; EM; 3.42 A; A/B/C/D/E/F=1-806. DR PDB; 8VKU; EM; 3.50 A; A/B/C/D/E/F=1-806. DR PDB; 8VLS; EM; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806. DR PDB; 8VOV; EM; 3.60 A; A/B/C/D/E/F=1-806. DR PDB; 8YKA; EM; 3.45 A; A/B/C/D/E/F=12-775. DR PDB; 9BOQ; EM; 3.33 A; A/B/C/D/E/F/G/H/I/J/K/L=1-806. DR PDB; 9DIL; EM; 3.30 A; A/B=1-806. DR PDB; 9MQ6; EM; 3.30 A; A/B=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; 7MHS; -. DR PDBsum; 7OAT; -. DR PDBsum; 7PUX; -. 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 PDBsum; 7Y4W; -. DR PDBsum; 7Y53; -. DR PDBsum; 7Y59; -. DR PDBsum; 8B5R; -. DR PDBsum; 8FCL; -. DR PDBsum; 8FCM; -. DR PDBsum; 8FCN; -. DR PDBsum; 8FCO; -. DR PDBsum; 8FCP; -. DR PDBsum; 8FCQ; -. DR PDBsum; 8FCR; -. DR PDBsum; 8FCT; -. DR PDBsum; 8HL7; -. DR PDBsum; 8HRZ; -. DR PDBsum; 8KG2; -. DR PDBsum; 8OOI; -. DR PDBsum; 8PQX; -. DR PDBsum; 8R0E; -. DR PDBsum; 8RS9; -. DR PDBsum; 8RSB; -. DR PDBsum; 8RSC; -. DR PDBsum; 8UV2; -. DR PDBsum; 8UVO; -. DR PDBsum; 8UVP; -. DR PDBsum; 8UVQ; -. DR PDBsum; 8VKU; -. DR PDBsum; 8VLS; -. DR PDBsum; 8VOV; -. DR PDBsum; 8YKA; -. DR PDBsum; 9BOQ; -. DR PDBsum; 9DIL; -. DR PDBsum; 9MQ6; -. DR AlphaFoldDB; P55072; -. DR EMDB; EMD-15774; -. DR EMDB; EMD-15861; -. DR EMDB; EMD-16781; -. DR EMDB; EMD-17016; -. DR EMDB; EMD-17024; -. DR EMDB; EMD-17128; -. DR EMDB; EMD-17827; -. DR EMDB; EMD-17837; -. DR EMDB; EMD-18517; -. DR EMDB; EMD-18790; -. DR EMDB; EMD-19473; -. DR EMDB; EMD-19475; -. DR EMDB; EMD-19476; -. DR EMDB; EMD-22521; -. DR EMDB; EMD-22675; -. DR EMDB; EMD-22676; -. DR EMDB; EMD-22678; -. DR EMDB; EMD-23191; -. DR EMDB; EMD-23192; -. DR EMDB; EMD-23442; -. DR EMDB; EMD-23443; -. DR EMDB; EMD-23444; -. DR EMDB; EMD-23445; -. DR EMDB; EMD-23446; -. DR EMDB; EMD-23447; -. DR EMDB; EMD-23448; -. DR EMDB; EMD-23449; -. DR EMDB; EMD-23450; -. DR EMDB; EMD-23451; -. DR EMDB; EMD-23452; -. DR EMDB; EMD-23453; -. DR EMDB; EMD-23454; -. DR EMDB; EMD-23455; -. DR EMDB; EMD-23456; -. DR EMDB; EMD-23457; -. DR EMDB; EMD-23458; -. DR EMDB; EMD-23775; -. DR EMDB; EMD-23776; -. DR EMDB; EMD-23835; -. DR EMDB; EMD-24302; -. DR EMDB; EMD-24304; -. DR EMDB; EMD-24305; -. DR EMDB; EMD-24306; -. DR EMDB; EMD-24518; -. DR EMDB; EMD-24519; -. DR EMDB; EMD-24522; -. DR EMDB; EMD-24523; -. DR EMDB; EMD-24524; -. DR EMDB; EMD-24525; -. DR EMDB; EMD-24526; -. DR EMDB; EMD-24528; -. DR EMDB; EMD-24529; -. DR EMDB; EMD-24530; -. DR EMDB; EMD-24531; -. DR EMDB; EMD-24532; -. DR EMDB; EMD-28982; -. DR EMDB; EMD-28983; -. DR EMDB; EMD-28984; -. DR EMDB; EMD-28985; -. DR EMDB; EMD-28986; -. DR EMDB; EMD-28987; -. DR EMDB; EMD-28988; -. DR EMDB; EMD-28989; -. DR EMDB; EMD-28990; -. DR EMDB; EMD-28991; -. DR EMDB; EMD-28992; -. DR EMDB; EMD-30147; -. DR EMDB; EMD-30148; -. DR EMDB; EMD-30149; -. DR EMDB; EMD-30150; -. DR EMDB; EMD-31894; -. DR EMDB; EMD-31895; -. DR EMDB; EMD-31896; -. DR EMDB; EMD-31897; -. DR EMDB; EMD-31899; -. DR EMDB; EMD-32827; -. DR EMDB; EMD-3295; -. DR EMDB; EMD-3296; -. DR EMDB; EMD-3297; -. DR EMDB; EMD-3298; -. DR EMDB; EMD-3299; -. DR EMDB; EMD-3323; -. DR EMDB; EMD-3324; -. DR EMDB; EMD-3325; -. DR EMDB; EMD-3326; -. DR EMDB; EMD-3327; -. DR EMDB; EMD-3328; -. DR EMDB; EMD-33608; -. DR EMDB; EMD-33611; -. DR EMDB; EMD-33613; -. DR EMDB; EMD-38770; -. DR EMDB; EMD-38771; -. DR EMDB; EMD-38772; -. DR EMDB; EMD-39360; -. DR EMDB; EMD-42603; -. DR EMDB; EMD-42625; -. DR EMDB; EMD-42626; -. DR EMDB; EMD-42627; -. DR EMDB; EMD-43329; -. DR EMDB; EMD-43343; -. DR EMDB; EMD-43392; -. DR EMDB; EMD-44748; -. DR EMDB; EMD-46912; -. DR EMDB; EMD-48514; -. DR SMR; P55072; -. DR BioGRID; 113258; 1454. DR ComplexPortal; CPX-137; VCP-NPL4-UFD1 AAA ATPase complex. DR ComplexPortal; CPX-262; VCP-NSFL1C AAA ATPase complex. DR ComplexPortal; CPX-8095; VCP-FAF1 AAA ATPase complex. DR ComplexPortal; CPX-8096; VCP-NPL4-UFD1-FAF1 AAA ATPase complex. DR ComplexPortal; CPX-8101; VCP-NPL4-UFD1-UBXN7 AAA ATPase complex. DR ComplexPortal; CPX-8104; VCP-NPL4-UFD1-FAF2 AAA ATPase complex. DR ComplexPortal; CPX-8105; VCP-NPL4-UFD1-UBXN1 AAA ATPase complex. DR ComplexPortal; CPX-8121; VCP-UBXN2B AAA ATPase complex. DR ComplexPortal; CPX-8124; VCP-UBXN2A AAA ATPase complex. DR ComplexPortal; CPX-8128; VCP-YOD1 AAA ATPase complex. DR ComplexPortal; CPX-8129; VCP-PLAA AAA ATPase complex. DR ComplexPortal; CPX-8132; VCP-VCPIP1 AAA ATPase complex. DR ComplexPortal; CPX-8133; VCP-UBXN6 AAA ATPase complex. DR ComplexPortal; CPX-8134; VCP-AMFR AAA ATPase complex. DR ComplexPortal; CPX-8570; VCP-DERL1 AAA ATPase complex. DR ComplexPortal; CPX-8782; VCP-DERL2 AAA ATPase complex. DR ComplexPortal; CPX-8783; VCP-DERL3 AAA ATPase complex. DR CORUM; P55072; -. DR DIP; DIP-33543N; -. DR FunCoup; P55072; 2295. DR IntAct; P55072; 915. DR MINT; P55072; -. DR STRING; 9606.ENSP00000351777; -. DR BindingDB; P55072; -. DR ChEMBL; CHEMBL1075145; -. DR DrugBank; DB16874; CB-5083. 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; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P55072; -. DR MetOSite; P55072; -. DR PhosphoSitePlus; P55072; -. DR SwissPalm; P55072; -. DR BioMuta; VCP; -. DR DMDM; 6094447; -. DR OGP; P55072; -. DR REPRODUCTION-2DPAGE; IPI00022774; -. DR REPRODUCTION-2DPAGE; P55072; -. DR CPTAC; CPTAC-295; -. DR CPTAC; CPTAC-296; -. DR jPOST; P55072; -. DR MassIVE; P55072; -. DR PaxDb; 9606-ENSP00000351777; -. DR PeptideAtlas; P55072; -. DR PRIDE; P55072; -. DR ProteomicsDB; 56776; -. DR Pumba; P55072; -. DR TopDownProteomics; P55072; -. DR ABCD; P55072; 1 sequenced antibody. DR Antibodypedia; 2215; 680 antibodies from 44 providers. DR DNASU; 7415; -. DR Ensembl; ENST00000358901.11; ENSP00000351777.6; ENSG00000165280.19. DR GeneID; 7415; -. DR KEGG; hsa:7415; -. DR MANE-Select; ENST00000358901.11; ENSP00000351777.6; NM_007126.5; NP_009057.1. DR AGR; HGNC:12666; -. DR ClinPGx; PA37289; -. 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 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 VEuPathDB; HostDB:ENSG00000165280; -. DR eggNOG; KOG0730; Eukaryota. DR GeneTree; ENSGT00900000141071; -. DR HOGENOM; CLU_000688_12_3_1; -. DR InParanoid; P55072; -. DR OMA; VWPAYPE; -. DR OrthoDB; 27435at2759; -. DR PAN-GO; P55072; 10 GO annotations based on evolutionary models. DR PhylomeDB; P55072; -. 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 Agora; ENSG00000165280; Agora Nominated Target for Alzheimer's Disease. DR BioGRID-ORCS; 7415; 852 hits in 1138 CRISPR screens. DR CD-CODE; 550E224B; Proteasome condensate. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; B5B9A610; PML body. DR CD-CODE; DEE660B4; Stress granule. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 210 other cell types or tissues. DR ExpressionAtlas; P55072; baseline and differential. DR GO; GO:1904949; C:ATPase complex; IEA:Ensembl. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0036064; C:ciliary basal body; IDA:HPA. DR GO; GO:0097542; C:ciliary tip; IDA:HPA. DR GO; GO:0035869; C:ciliary transition zone; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IEA:Ensembl. 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; IPI:ComplexPortal. 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; IDA:UniProt. 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; IDA:UniProt. 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:0140036; F:ubiquitin-modified protein reader activity; IDA:UniProtKB. DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL. 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:0034605; P:cellular response to heat; IMP:UniProtKB. DR GO; GO:0071218; P:cellular response to misfolded protein; IMP:ParkinsonsUK-UCL. DR GO; GO:0140455; P:cytoplasm protein quality control; IDA:UniProt. DR GO; GO:0006974; P:DNA damage response; IDA: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:0036503; P:ERAD pathway; IDA:UniProtKB. 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:0019674; P:NAD+ metabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0035331; P:negative regulation of hippo signaling; IGI:FlyBase. DR GO; GO:0120186; P:negative regulation of protein localization to chromatin; IDA:UniProt. 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:0010918; P:positive regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IDA:UniProt. 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; IDA:UniProt. 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; IDA:UniProtKB. DR GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR GO; GO:0019079; P:viral genome replication; IMP:CACAO. DR CDD; cd19519; RecA-like_CDC48_r1-like; 1. DR CDD; cd19528; RecA-like_CDC48_r2-like; 1. DR DisProt; DP03238; -. DR FunFam; 1.10.8.60:FF:000004; Cell division control 48; 1. DR FunFam; 3.10.330.10:FF:000001; Cell division control 48; 1. DR FunFam; 2.40.40.20:FF:000003; Transitional endoplasmic reticulum ATPase; 1. DR FunFam; 3.40.50.300:FF:000012; Transitional endoplasmic reticulum ATPase; 1. DR FunFam; 3.40.50.300:FF:000048; Transitional endoplasmic reticulum ATPase; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 6.10.20.150; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR IDEAL; IID00201; -. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005938; AAA_ATPase_CDC48. DR InterPro; IPR050168; AAA_ATPase_domain. 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 NCBIfam; TIGR01243; CDC48; 1. DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1. DR PANTHER; PTHR23077:SF69; TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE; 1. 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 SMART; SM00382; AAA; 2. DR SMART; SM01072; CDC48_2; 1. DR SMART; SM01073; CDC48_N; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. 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; Proteomics identification; Reference proteome; Transport; KW Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.9, 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 777..793 FT /note="Gly 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.9, 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 CROSSLNK 109 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in UFM1)" FT /evidence="ECO:0000269|PubMed:38762759" 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; uncertain 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 160 FT /note="A -> T (in IBMPFD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:36980948" FT /id="VAR_088265" 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 254 FT /note="I -> F (in IBMPFD1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:36980948" FT /id="VAR_088266" FT VARIANT 369 FT /note="I -> T (in IBMPFD1; uncertain significance; FT dbSNP:rs1828723406)" FT /evidence="ECO:0000269|PubMed:36980948" FT /id="VAR_088267" FT VARIANT 387 FT /note="N -> H (in IBMPFD1; uncertain significance; FT 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 109 FT /note="K->R: Impaired UFMylation." FT /evidence="ECO:0000269|PubMed:38762759" FT MUTAGEN 110 FT /note="Y->A: Abolishes interaction with NPLOC4; when FT associated with 52-A--A-55. Impaired UFMylation." FT /evidence="ECO:0000269|PubMed:26471729, FT ECO:0000269|PubMed:38762759" 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. 7; AAI21795)" FT /evidence="ECO:0000305" FT CONFLICT 312 FT /note="K -> I (in Ref. 4; 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..37 FT /evidence="ECO:0007829|PDB:8R0E" 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:8OOI" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:5B6C" FT HELIX 86..92 FT /evidence="ECO:0007829|PDB:5B6C" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:8R0E" 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:7PUX" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5FTJ" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 210..225 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:4KLN" FT HELIX 251..262 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 271..275 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 278..280 FT /evidence="ECO:0007829|PDB:8OOI" FT HELIX 281..295 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 298..304 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 319..334 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:8HRZ" FT STRAND 341..348 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 355..358 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:8OOI" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 374..384 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 385..387 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:5DYG" FT HELIX 392..394 FT /evidence="ECO:0007829|PDB:8PQX" FT HELIX 396..402 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 403..405 FT /evidence="ECO:0007829|PDB:5FTJ" FT HELIX 408..427 FT /evidence="ECO:0007829|PDB:7PUX" FT TURN 428..430 FT /evidence="ECO:0007829|PDB:7PUX" FT STRAND 432..436 FT /evidence="ECO:0007829|PDB:3HU1" FT HELIX 439..444 FT /evidence="ECO:0007829|PDB:7PUX" FT HELIX 449..456 FT /evidence="ECO:0007829|PDB:7PUX" 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 STRAND 520..523 FT /evidence="ECO:0007829|PDB:8UV2" 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:8OOI" 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 718..721 FT /evidence="ECO:0007829|PDB:7VCU" 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 //