ID TERA_MOUSE Reviewed; 806 AA. AC Q01853; Q3TFH9; Q3TIM2; Q3TXN9; Q6PI18; Q8BSR6; Q8CEG4; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 4. DT 27-MAR-2024, entry version 234. DE RecName: Full=Transitional endoplasmic reticulum ATPase; DE Short=TER ATPase; DE EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072}; DE AltName: Full=15S Mg(2+)-ATPase p97 subunit; DE AltName: Full=Valosin-containing protein; DE Short=VCP; GN Name=Vcp {ECO:0000312|MGI:MGI:99919}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-40; 295-309 AND RP 425-438. RC STRAIN=MRL/LPR; RX PubMed=1382975; DOI=10.1002/j.1460-2075.1992.tb05436.x; RA Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H., Samelson L.E.; RT "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in RT response to T cell antigen receptor activation."; RL EMBO J. 11:3533-3540(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow, Head, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; 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 [5] RP PROTEIN SEQUENCE OF 9-18; 26-53; 87-93; 96-109; 148-155; 192-210; 218-231; RP 240-251; 278-287; 296-312; 324-336; 363-386; 454-502; 513-524; 530-560; RP 600-614; 639-651; 669-677; 701-709; 714-732 AND 754-766, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [6] RP INTERACTION WITH UBOX5. RX PubMed=15189447; DOI=10.1111/j.1356-9597.2004.00742.x; RA Hatakeyama S., Matsumoto M., Yada M., Nakayama K.I.; RT "Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular RT chaperones."; RL Genes Cells 9:533-548(2004). RN [7] RP INTERACTION WITH RNF19A. 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 [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-805, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP INTERACTION WITH NGLY1. RX PubMed=16249333; DOI=10.1073/pnas.0507155102; RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.; RT "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide RT N-glycanase, with the proteasome."; RL Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005). RN [11] RP ERRATUM OF PUBMED:16249333. RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.; RL Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006). RN [12] RP INTERACTION WITH NSFL1C-LIKE PROTEIN P37. RX PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016; RA Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E., Dreveny I., RA Beuron F., Zhang X., Freemont P., Kondo H.; RT "p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase RT and at the end of mitosis."; RL Dev. Cell 11:803-816(2006). RN [13] RP PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-144. RX PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x; RA Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N., Shimozawa N., RA Shirakawa M., Hiroaki H.; RT "The common phospholipid-binding activity of the N-terminal domains of PEX1 RT and VCP/p97."; RL FEBS J. 273:4959-4971(2006). RN [14] RP INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1. RX PubMed=16709668; DOI=10.1073/pnas.0602747103; RA Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.; RT "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum- RT associated E3 ligase autocrine motility factor receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [16] RP METHYLATION AT LYS-315. 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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-502; LYS-505; LYS-668 AND RP LYS-754, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-668, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [18] 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 [19] RP INTERACTION WITH CCDC47. RX PubMed=25009997; DOI=10.1016/j.ydbio.2014.06.024; RA Yamamoto S., Yamazaki T., Komazaki S., Yamashita T., Osaki M., RA Matsubayashi M., Kidoya H., Takakura N., Yamazaki D., Kakizawa S.; RT "Contribution of calumin to embryogenesis through participation in the RT endoplasmic reticulum-associated degradation activity."; RL Dev. Biol. 393:33-43(2014). RN [20] RP TISSUE SPECIFICITY. 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 [21] 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 [22] RP INTERACTION WITH LMBR1L AND UBAC2. 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 [23] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=33590678; DOI=10.15252/embr.202052164; RA Villa F., Fujisawa R., Ainsworth J., Nishimura K., Lie-A-Ling M., RA Lacaud G., Labib K.P.; RT "CUL2LRR1, TRAIP and p97 control CMG helicase disassembly in the mammalian RT cell cycle."; RL EMBO Rep. 22:e52164-e52164(2021). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP. RX PubMed=11163219; DOI=10.1016/s1097-2765(00)00143-x; RA Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E., RA Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H., RA van Heel M., Freemont P.S.; RT "Structure of the AAA ATPase p97."; RL Mol. Cell 6:1473-1484(2000). RN [25] RP X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS). RX PubMed=12949490; DOI=10.1038/nsb972; RA DeLaBarre B., Brunger A.T.; RT "Complete structure of p97/valosin-containing protein reveals communication RT between nucleotide domains."; RL Nat. Struct. Biol. 10:856-863(2003). RN [26] RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS). RX PubMed=14643202; DOI=10.1016/j.jsb.2003.10.007; RA Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H., Ma J., RA Zhang X., Freemont P.S.; RT "The crystal structure of murine p97/VCP at 3.6A."; RL J. Struct. Biol. 144:337-348(2003). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-458 IN COMPLEX WITH ADP. RX PubMed=14988733; DOI=10.1038/sj.emboj.7600139; RA Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.; RT "Structural basis of the interaction between the AAA ATPase p97/VCP and its RT adaptor protein p47."; RL EMBO J. 23:1030-1039(2004). RN [28] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX PubMed=15740751; DOI=10.1016/j.jmb.2005.01.060; RA DeLaBarre B., Brunger A.T.; RT "Nucleotide dependent motion and mechanism of action of p97/VCP."; RL J. Mol. Biol. 347:437-452(2005). 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 (By similarity). 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. Involved in clearance process by mediating CC G3BP1 extraction from stress granules (By similarity). Also involved in CC DNA damage response: recruited to double-strand breaks (DSBs) sites in CC a RNF8- and RNF168-dependent manner and promotes the recruitment of CC TP53BP1 at DNA damage sites. Recruited to stalled replication forks by CC SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to CC prevent excessive translesion DNA synthesis and limit the incidence of CC mutations induced by DNA damage. Together with SPRTN metalloprotease, CC involved in the repair of covalent DNA-protein cross-links (DPCs) CC during DNA synthesis (By similarity). Involved in interstrand cross- CC link repair in response to replication stress by mediating unloading of CC the ubiquitinated CMG helicase complex (PubMed:33590678). Mediates CC extraction of PARP1 trapped to chromatin: recognizes and binds CC ubiquitinated PARP1 and promotes its removal (By similarity). Required CC for cytoplasmic retrotranslocation of stressed/damaged mitochondrial CC outer-membrane proteins and their subsequent proteasomal degradation. CC Essential for the maturation of ubiquitin-containing autophagosomes and CC the clearance of ubiquitinated protein by autophagy. Acts as a negative CC regulator of type I interferon production by interacting with RIGI: 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. May play a role in the CC ubiquitin-dependent sorting of membrane proteins to lysosomes where CC they undergo degradation. May more particularly play a role in CC caveolins sorting in cells. By controlling the steady-state expression CC of the IGF1R receptor, indirectly regulates the insulin-like growth CC factor receptor signaling pathway. {ECO:0000250|UniProtKB:P23787, CC ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072, CC ECO:0000269|PubMed:33590678}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; CC Evidence={ECO:0000250|UniProtKB:P55072}; 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. Interaction CC with VCIP135 leads to dissociation of the complex via ATP hydrolysis by CC VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP. CC Interacts with NSFL1C-like protein p37; the complex has membrane fusion CC activity and is required for Golgi and endoplasmic reticulum CC biogenesis. Interacts with RNF103. Interacts with TRIM13 and TRIM21. CC Component of a VCP/p97-AMFR/gp78 complex that participates in the final CC step of the endoplasmic reticulum-associated degradation (ERAD) of CC HMGCR. Interacts directly with AMFR/gp78 (via its VIM). Interacts with CC RHBDD1 (via C-terminal domain). Interacts with SPRTN; leading to CC recruitment to stalled replication forks. Interacts with SELENOS and CC SYVN1, as well as with DERL1 (via SHP-box motif), DERL2 and DERL3; CC which probably transfer misfolded proteins from the ER to VCP. CC Interacts with SVIP. Component of a complex required to couple CC retrotranslocation, ubiquitination and deglycosylation composed of CC NGLY1, SAKS1, AMFR, VCP and RAD23B. Part of a complex composed of CC STUB1/CHIP, VCP/p97, CHRNA3, and UBXN2A that modulates the CC ubiquitination and endoplasmic reticulum-associated degradation (ERAD) CC of CHRNA3 (By similarity). Within the complex UBXN2A acts as a scaffold CC protein required for the interaction of CHRNA3 with VCP/p97, this CC interaction also inhibits CHRNA3 ubiquitination by STUB1/CHIP and CC subsequently ERAD (By similarity). Interacts with UBXN2A (via UBX CC domain); the interaction is required for the interaction of CHRNA3 in CC the STUB1-VCP-UBXN2A complex (By similarity). Directly interacts with CC UBXN4 and RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1. CC Interacts with clathrin. Interacts with RNF103. Interacts with TRIM13 CC and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that participates CC in the final step of the endoplasmic reticulum-associated degradation CC (ERAD) of HMGCR. Interacts directly with AMFR/gp78 (via its VIM). CC Interacts with WASHC5. Interacts with UBOX5. Interacts (via CC N- terminus) with UBXN7, UBXN8, and probably several other UBX domain- CC containing proteins (via UBX domains); the interactions are mutually CC exclusive with VIM-dependent interactions such as those with AMFR and CC SELENOS. Forms a complex with UBQLN1 and UBXN4 (By similarity). CC Interacts (via the PIM motif) with RNF31 (via the PUB domain) (By CC similarity). Interacts with RIGI and RNF125; interaction takes place CC when RIGI is ubiquitinated via'Lys-63'-linked ubiquitin on its CARD CC domains, leading to recruit RNF125 and promote ubiquitination and CC degradation of RIGI (By similarity). Interacts with BAG6 (By CC similarity). Interacts with UBXN10 (By similarity). Interacts with CC UBXN6; the interaction with UBXN6 is direct and competitive with UFD1 CC (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts CC with PLAA, UBXN6 and YOD1; may form a complex involved in CC macroautophagy (By similarity). Interacts with ANKZF1 (By similarity). CC Interacts with ubiquitin-binding protein FAF1 (By similarity). CC Interacts with ZFAND2B (via VIM motif); the interaction is direct CC (PubMed:24160817, PubMed:26337389). Interacts with ZFAND1 (via its CC ubiquitin-like region); this interaction occurs in an arsenite- CC dependent manner (By similarity). Interacts with CCDC47 CC (PubMed:25009997). Interacts with LMBR1L and UBAC2 (PubMed:31073040). CC Interacts with ATXN3 (By similarity). Interacts with TEX264; bridging CC VCP to covalent DNA-protein cross-links (DPCs) (By similarity). CC {ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072, CC ECO:0000269|PubMed:15189447, ECO:0000269|PubMed:15456787, CC ECO:0000269|PubMed:16249333, ECO:0000269|PubMed:16709668, CC ECO:0000269|PubMed:17141156, ECO:0000269|PubMed:24160817, CC ECO:0000269|PubMed:25009997, ECO:0000269|PubMed:26337389, CC ECO:0000269|PubMed:31073040}. CC -!- INTERACTION: CC Q01853; Q9R049: Amfr; NbExp=4; IntAct=EBI-80597, EBI-3648125; CC Q01853; Q80UU1: Ankzf1; NbExp=2; IntAct=EBI-80597, EBI-9510971; CC Q01853; Q9JI78: Ngly1; NbExp=9; IntAct=EBI-80597, EBI-3648128; CC Q01853; P70362: Ufd1; NbExp=9; IntAct=EBI-80597, EBI-7961331; CC Q01853; Q01853: Vcp; NbExp=3; IntAct=EBI-80597, EBI-80597; CC Q01853; P36037: DOA1; Xeno; NbExp=2; IntAct=EBI-80597, EBI-6017; CC Q01853; Q9ES54: Nploc4; Xeno; NbExp=11; IntAct=EBI-80597, EBI-1993990; CC Q01853; O35987: Nsfl1c; Xeno; NbExp=8; IntAct=EBI-80597, EBI-1993760; CC Q01853; Q9BQE4: SELENOS; Xeno; NbExp=4; IntAct=EBI-80597, EBI-398970; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}. CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}. Nucleus CC {ECO:0000269|PubMed:33590678}. Note=Recruited to the cytoplasmic CC surface of the endoplasmic reticulum via interaction with AMFR/gp78. CC Following DNA double-strand breaks, recruited to the sites of damage. CC Recruited to stalled replication forks via interaction with SPRTN. CC Recruited to damaged lysosomes decorated with K48-linked ubiquitin CC chains. Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress CC granules (SGs) in response to arsenite-induced stress treatment (By CC similarity). {ECO:0000250|UniProtKB:P55072}. CC -!- TISSUE SPECIFICITY: Expressed in the prefrontal cortex (at protein CC level). {ECO:0000269|PubMed:26265139}. CC -!- DOMAIN: The N-terminal domain shows evolutionary conservation with that CC of PEX1, and is able to bind phospholipids with a preference for CC phosphatidylinositol mono- and bisphosphates. CC -!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with CC the PUB domain of RNF31. {ECO:0000250|UniProtKB:P55072}. 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 (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. 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; Z14044; CAA78412.1; -; mRNA. DR EMBL; AK028264; BAC25849.1; -; mRNA. DR EMBL; AK030751; BAC27119.1; -; mRNA. DR EMBL; AK149931; BAE29175.1; -; mRNA. DR EMBL; AK151109; BAE30119.1; -; mRNA. DR EMBL; AK151418; BAE30383.1; -; mRNA. DR EMBL; AK153249; BAE31840.1; -; mRNA. DR EMBL; AK159177; BAE34876.1; -; mRNA. DR EMBL; AK159509; BAE35141.1; -; mRNA. DR EMBL; AK167794; BAE39824.1; -; mRNA. DR EMBL; AK169140; BAE40919.1; -; mRNA. DR EMBL; AL672276; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC043053; AAH43053.1; -; mRNA. DR EMBL; BC049114; AAH49114.1; -; mRNA. DR CCDS; CCDS18086.1; -. DR PIR; S25197; S25197. DR RefSeq; NP_033529.3; NM_009503.4. DR PDB; 1E32; X-ray; 2.90 A; A=1-458. DR PDB; 1R7R; X-ray; 3.60 A; A=1-806. DR PDB; 1S3S; X-ray; 2.90 A; A/B/C/D/E/F=1-458. DR PDB; 2PJH; NMR; -; B=21-213. DR PDB; 3CF0; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=463-763. DR PDB; 3CF1; X-ray; 4.40 A; A/B/C=1-806. DR PDB; 3CF2; X-ray; 3.50 A; A/B/C/D=1-806. DR PDB; 3CF3; X-ray; 4.25 A; A/B/C=1-806. DR PDBsum; 1E32; -. DR PDBsum; 1R7R; -. DR PDBsum; 1S3S; -. DR PDBsum; 2PJH; -. DR PDBsum; 3CF0; -. DR PDBsum; 3CF1; -. DR PDBsum; 3CF2; -. DR PDBsum; 3CF3; -. DR AlphaFoldDB; Q01853; -. DR EMDB; EMD-2319; -. DR EMDB; EMD-2589; -. DR EMDB; EMD-2590; -. DR EMDB; EMD-2591; -. DR EMDB; EMD-2592; -. DR EMDB; EMD-2593; -. DR SMR; Q01853; -. DR BioGRID; 234661; 158. DR ComplexPortal; CPX-136; Vcp-Npl4-Ufd1 AAA ATPase complex. DR ComplexPortal; CPX-264; Vcp-Nsfl1c AAA ATPase complex. DR CORUM; Q01853; -. DR DIP; DIP-29796N; -. DR IntAct; Q01853; 41. DR MINT; Q01853; -. DR STRING; 10090.ENSMUSP00000030164; -. DR BindingDB; Q01853; -. DR ChEMBL; CHEMBL3988606; -. DR GlyGen; Q01853; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q01853; -. DR MetOSite; Q01853; -. DR PhosphoSitePlus; Q01853; -. DR SwissPalm; Q01853; -. DR REPRODUCTION-2DPAGE; Q01853; -. DR CPTAC; non-CPTAC-4013; -. DR EPD; Q01853; -. DR jPOST; Q01853; -. DR MaxQB; Q01853; -. DR PaxDb; 10090-ENSMUSP00000030164; -. DR PeptideAtlas; Q01853; -. DR ProteomicsDB; 263105; -. DR Pumba; Q01853; -. DR Antibodypedia; 2215; 808 antibodies from 43 providers. DR DNASU; 269523; -. DR Ensembl; ENSMUST00000030164.8; ENSMUSP00000030164.8; ENSMUSG00000028452.8. DR GeneID; 269523; -. DR KEGG; mmu:269523; -. DR UCSC; uc008sor.2; mouse. DR AGR; MGI:99919; -. DR CTD; 7415; -. DR MGI; MGI:99919; Vcp. DR VEuPathDB; HostDB:ENSMUSG00000028452; -. DR eggNOG; KOG0730; Eukaryota. DR GeneTree; ENSGT00900000141071; -. DR HOGENOM; CLU_000688_12_3_1; -. DR InParanoid; Q01853; -. DR OMA; HACHDIK; -. DR OrthoDB; 168438at2759; -. DR PhylomeDB; Q01853; -. DR TreeFam; TF300542; -. DR Reactome; R-MMU-110320; Translesion Synthesis by POLH. DR Reactome; R-MMU-3371511; HSF1 activation. DR Reactome; R-MMU-382556; ABC-family proteins mediated transport. DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle. DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis. DR Reactome; R-MMU-5689877; Josephin domain DUBs. DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-8876725; Protein methylation. DR Reactome; R-MMU-8951664; Neddylation. DR Reactome; R-MMU-9013407; RHOH GTPase cycle. DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway. DR BioGRID-ORCS; 269523; 35 hits in 113 CRISPR screens. DR ChiTaRS; Vcp; mouse. DR EvolutionaryTrace; Q01853; -. DR PRO; PR:Q01853; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q01853; Protein. DR Bgee; ENSMUSG00000028452; Expressed in hindlimb stylopod muscle and 239 other cell types or tissues. DR GO; GO:1904949; C:ATPase complex; IMP:CAFA. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0005811; C:lipid droplet; ISO:MGI. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0000502; C:proteasome complex; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; IPI:MGI. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:SynGO. DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL. DR GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL. DR GO; GO:0043531; F:ADP binding; IMP:CAFA. DR GO; GO:0005524; F:ATP binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:ParkinsonsUK-UCL. DR GO; GO:1904288; F:BAT3 complex binding; ISO:MGI. DR GO; GO:0035800; F:deubiquitinase activator activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0042288; F:MHC class I protein binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:BHF-UCL. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0140036; F:ubiquitin-dependent protein binding; ISO:MGI. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI. DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0070842; P:aggresome assembly; IGI:MGI. DR GO; GO:0046034; P:ATP metabolic process; IDA:ParkinsonsUK-UCL. DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB. DR GO; GO:0006914; P:autophagy; ISS:UniProtKB. DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB. DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB. DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI. DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB. DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI. DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB. DR GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; ISO:MGI. DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB. DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB. DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central. DR GO; GO:0006734; P:NADH metabolic process; ISO:MGI. DR GO; GO:0120186; P:negative regulation of protein localization to chromatin; ISO:MGI. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:MGI. DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI. 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; IEA:Ensembl. DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:MGI. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI. DR GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; ISO:MGI. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI. DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB. DR GO; GO:1903715; P:regulation of aerobic respiration; ISO:MGI. DR GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB. DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB. DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; EXP:ComplexPortal. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:MGI. DR GO; GO:0019079; P:viral genome replication; ISO:MGI. DR CDD; cd19519; RecA-like_CDC48_r1-like; 1. DR CDD; cd19528; RecA-like_CDC48_r2-like; 1. DR DisProt; DP00435; -. 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; IID50030; -. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005938; AAA_ATPase_CDC48. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR004201; Cdc48_dom2. DR InterPro; IPR029067; CDC48_domain_2-like_sf. DR InterPro; IPR003338; CDC4_N-term_subdom. DR InterPro; IPR027417; P-loop_NTPase. DR 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. DR UCD-2DPAGE; Q01853; -. DR Genevisible; Q01853; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Autophagy; Cytoplasm; KW Direct protein sequencing; DNA damage; DNA repair; Endoplasmic reticulum; KW Hydrolase; Isopeptide bond; Lipid-binding; Methylation; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Transport; Ubl conjugation; KW Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P55072" FT CHAIN 2..806 FT /note="Transitional endoplasmic reticulum ATPase" FT /id="PRO_0000084573" 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:0000250" FT MOTIF 802..806 FT /note="PIM motif" FT /evidence="ECO:0000250|UniProtKB:P55072" FT COMPBIAS 768..794 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 247..253 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:11163219, FT ECO:0000305|PubMed:14988733" FT BINDING 348 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P55072" FT BINDING 384 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000305|PubMed:11163219, FT ECO:0000305|PubMed:14988733" FT BINDING 521..526 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000305|PubMed:11163219, FT ECO:0000305|PubMed:14988733" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 315 FT /note="N6,N6,N6-trimethyllysine; by VCPKMT" FT /evidence="ECO:0000269|PubMed:22948820" FT MOD_RES 436 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 462 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 502 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 505 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 668 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 668 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 754 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 775 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 787 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MOD_RES 805 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT CROSSLNK 8 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P55072" FT CROSSLNK 18 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P55072" FT MUTAGEN 144 FT /note="R->A: Loss of phospholipid-binding." FT /evidence="ECO:0000269|PubMed:17018057" FT CONFLICT 73 FT /note="S -> Y (in Ref. 2; BAC27119)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="N -> Y (in Ref. 2; BAE39824)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="I -> V (in Ref. 1; CAA78412)" FT /evidence="ECO:0000305" FT CONFLICT 359 FT /note="R -> Q (in Ref. 2; BAC27119)" FT /evidence="ECO:0000305" FT CONFLICT 439 FT /note="A -> T (in Ref. 2; BAE40919)" FT /evidence="ECO:0000305" FT CONFLICT 624 FT /note="N -> S (in Ref. 2; BAE34876)" FT /evidence="ECO:0000305" FT CONFLICT 684 FT /note="G -> V (in Ref. 2; BAC25849)" FT /evidence="ECO:0000305" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 43..48 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:3CF2" FT STRAND 66..73 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1S3S" FT STRAND 79..83 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 86..91 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 99..104 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:2PJH" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:1E32" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 130..133 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 135..139 FT /evidence="ECO:0007829|PDB:1E32" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:1S3S" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 159..176 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:1S3S" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:2PJH" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:3CF2" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 211..225 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 227..232 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 251..261 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 281..295 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 298..305 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 312..315 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 321..333 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:1S3S" FT STRAND 341..348 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 374..383 FT /evidence="ECO:0007829|PDB:1E32" FT TURN 384..387 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:1S3S" FT HELIX 396..402 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 408..430 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 439..444 FT /evidence="ECO:0007829|PDB:1E32" FT HELIX 449..456 FT /evidence="ECO:0007829|PDB:1E32" FT STRAND 457..460 FT /evidence="ECO:0007829|PDB:3CF2" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 483..498 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 500..506 FT /evidence="ECO:0007829|PDB:3CF0" FT STRAND 512..517 FT /evidence="ECO:0007829|PDB:3CF0" FT STRAND 519..523 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 524..534 FT /evidence="ECO:0007829|PDB:3CF0" FT STRAND 538..542 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 544..552 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 558..568 FT /evidence="ECO:0007829|PDB:3CF0" FT STRAND 571..576 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 581..585 FT /evidence="ECO:0007829|PDB:3CF0" FT TURN 586..590 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 599..609 FT /evidence="ECO:0007829|PDB:3CF0" FT STRAND 615..624 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 626..628 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 631..634 FT /evidence="ECO:0007829|PDB:3CF0" FT TURN 636..638 FT /evidence="ECO:0007829|PDB:3CF2" FT STRAND 641..644 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 650..661 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 672..677 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 684..706 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 733..740 FT /evidence="ECO:0007829|PDB:3CF0" FT HELIX 749..762 FT /evidence="ECO:0007829|PDB:3CF0" 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 //