ID ATAD2_HUMAN Reviewed; 1390 AA. AC Q6PL18; Q14CR1; Q658P2; Q68CQ0; Q6PJV6; Q8N890; Q9UHS5; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-SEP-2026, entry version 178. DE RecName: Full=ATPase family AAA domain-containing protein 2; DE EC=3.6.1.-; DE AltName: Full=AAA nuclear coregulator cancer-associated protein; DE Short=ANCCA; GN Name=ATAD2; ORFNames=L16, PRO2000; 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 [MRNA] (ISOFORM 1), AND INDUCTION. RX PubMed=15334068; DOI=10.1038/sj.onc.1207921; RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., RA Cerveny C., Law C.-L., Wahl A., Carter P.; RT "Suppression subtractive hybridization and expression profiling identifies RT a unique set of genes overexpressed in non-small-cell lung cancer."; RL Oncogene 23:7734-7745(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 47-1390 (ISOFORM 1). RC TISSUE=Lymph node, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum, Cervix, and Eye; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-978 (ISOFORM 1). RC TISSUE=Spleen; 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 MRNA] OF 813-1390. RC TISSUE=Fetal liver; RX PubMed=11483580; DOI=10.1101/gr.175501; RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.; RT "Gene expression profiling in human fetal liver and identification of RT tissue- and developmental-stage-specific genes through compiled expression RT profiles and efficient cloning of full-length cDNAs."; RL Genome Res. 11:1392-1403(2001). RN [6] RP TISSUE SPECIFICITY. RX PubMed=15721472; DOI=10.1016/s0140-6736(05)17947-1; RA Wang Y., Klijn J.G., Zhang Y., Sieuwerts A.M., Look M.P., Yang F., RA Talantov D., Timmermans M., Meijer-van Gelder M.E., Yu J., Jatkoe T., RA Berns E.M.J.J., Atkins D., Foekens J.A.; RT "Gene-expression profiles to predict distant metastasis of lymph-node- RT negative primary breast cancer."; RL Lancet 365:671-679(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP TISSUE SPECIFICITY. RX PubMed=17076897; DOI=10.1186/gb-2006-7-10-r101; RA Teschendorff A.E., Naderi A., Barbosa-Morais N.L., Pinder S.E., Ellis I.O., RA Aparicio S., Brenton J.D., Caldas C.; RT "A consensus prognostic gene expression classifier for ER positive breast RT cancer."; RL Genome Biol. 7:R101.1-R101.13(2006). RN [9] RP INDUCTION. RX PubMed=16709241; DOI=10.1186/1476-4598-5-20; RA De Angelis P.M., Svendsrud D.H., Kravik K.L., Stokke T.; RT "Cellular response to 5-fluorouracil (5-FU) in 5-FU-resistant colon cancer RT cell lines during treatment and recovery."; RL Mol. Cancer 5:20-20(2006). RN [10] RP TISSUE SPECIFICITY. RX PubMed=17660802; DOI=10.1038/modpathol.3800937; RA Fellenberg J., Bernd L., Delling G., Witte D., Zahlten-Hinguranage A.; RT "Prognostic significance of drug-regulated genes in high-grade RT osteosarcoma."; RL Mod. Pathol. 20:1085-1094(2007). RN [11] RP FUNCTION, INTERACTION WITH ESR1 AND NCOA3, SUBCELLULAR LOCATION, INDUCTION, RP AND MUTAGENESIS OF LYS-473 AND GLU-532. RX PubMed=17998543; DOI=10.1073/pnas.0705814104; RA Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W.; RT "ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is RT required for coregulator occupancy and chromatin modification."; RL Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746; SER-751; THR-1149; RP THR-1152 AND SER-1302, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-1302, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-337 AND SER-1302, RP AND 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND IDENTIFICATION BY RP 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-61; SER-165; SER-170; RP SER-327; SER-337; SER-342; SER-410; SER-1139; THR-1176; SER-1200; SER-1233; RP SER-1235; SER-1243; SER-1302 AND THR-1323, AND IDENTIFICATION BY MASS RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1200, AND IDENTIFICATION BY RP 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 [19] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-317; LYS-1128; LYS-1148 RP AND LYS-1236, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 981-1108, AND SUBUNIT. RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013; RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., RA Gingras A.C., Arrowsmith C.H., Knapp S.; RT "Histone recognition and large-scale structural analysis of the human RT bromodomain family."; RL Cell 149:214-231(2012). CC -!- FUNCTION: May be a transcriptional coactivator of the nuclear receptor CC ESR1 required to induce the expression of a subset of estradiol target CC genes, such as CCND1, MYC and E2F1. May play a role in the recruitment CC or occupancy of CREBBP at some ESR1 target gene promoters. May be CC required for histone hyperacetylation. Involved in the estrogen-induced CC cell proliferation and cell cycle progression of breast cancer cells. CC {ECO:0000269|PubMed:17998543}. 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; CC -!- SUBUNIT: Interacts with ESR1 and NCOA3 and these interactions are CC enhanced by estradiol. Interacts with acetylated lysine residues on CC histone H1.4, H2A, H2B and H3 (in vitro). {ECO:0000269|PubMed:17998543, CC ECO:0000269|PubMed:22464331}. CC -!- INTERACTION: CC Q6PL18; P03372: ESR1; NbExp=5; IntAct=EBI-6598454, EBI-78473; CC Q6PL18; Q9Y6Q9: NCOA3; NbExp=2; IntAct=EBI-6598454, EBI-81196; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17998543, CC ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6PL18-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6PL18-2; Sequence=VSP_015633, VSP_015634, VSP_015635; CC -!- TISSUE SPECIFICITY: Highly expressed in estrogen receptor positive CC breast tumors and in osteosarcoma tumors. {ECO:0000269|PubMed:15721472, CC ECO:0000269|PubMed:17076897, ECO:0000269|PubMed:17660802}. CC -!- INDUCTION: Up-regulated in breast, uterus, colon, ovary, and stomach CC tumors. Induced in breast cancer cells overexpressing NCOA3 or treated CC with estrogen. Down-regulated in 5-fluorouracil-resistant derivatives CC of the colon cancer cell line HCT 116. {ECO:0000269|PubMed:15334068, CC ECO:0000269|PubMed:16709241, ECO:0000269|PubMed:17998543}. CC -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform. May be produced at very CC low levels due to a premature stop codon in the mRNA, leading to CC nonsense-mediated mRNA decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF22032.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH10686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part (676-679).; Evidence={ECO:0000305}; CC Sequence=AAH19909.1; Type=Erroneous initiation; Evidence={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; AY598335; AAT06746.1; -; mRNA. DR EMBL; CR749832; CAH18688.1; -; mRNA. DR EMBL; AL833653; CAH56229.1; -; mRNA. DR EMBL; BC010686; AAH10686.1; ALT_SEQ; mRNA. DR EMBL; BC019909; AAH19909.1; ALT_INIT; mRNA. DR EMBL; BC113656; AAI13657.1; -; mRNA. DR EMBL; AK097133; BAC04959.1; -; mRNA. DR EMBL; AF118088; AAF22032.1; ALT_INIT; mRNA. DR CCDS; CCDS6343.1; -. [Q6PL18-1] DR RefSeq; NP_054828.2; NM_014109.4. [Q6PL18-1] DR PDB; 3DAI; X-ray; 1.95 A; A=981-1108. DR PDB; 4QSP; X-ray; 1.60 A; A=981-1108. DR PDB; 4QSQ; X-ray; 1.80 A; A=981-1108. DR PDB; 4QSR; X-ray; 2.00 A; A=981-1108. DR PDB; 4QSS; X-ray; 2.00 A; A=981-1108. DR PDB; 4QST; X-ray; 2.05 A; A=981-1108. DR PDB; 4QSU; X-ray; 1.90 A; A=981-1108. DR PDB; 4QSV; X-ray; 1.90 A; A=981-1108. DR PDB; 4QSW; X-ray; 1.80 A; A=981-1108. DR PDB; 4QSX; X-ray; 1.93 A; A=981-1108. DR PDB; 4QUT; X-ray; 1.70 A; A=981-1108. DR PDB; 4QUU; X-ray; 1.80 A; A=981-1108. DR PDB; 4TT2; X-ray; 2.50 A; A=981-1108. DR PDB; 4TT4; X-ray; 2.70 A; A/B=981-1108. DR PDB; 4TT6; X-ray; 2.00 A; A=981-1108. DR PDB; 4TTE; X-ray; 1.80 A; A=981-1108. DR PDB; 4TU4; X-ray; 1.73 A; A=981-1108. DR PDB; 4TU6; X-ray; 2.27 A; A/B/C/D=981-1108. DR PDB; 4TYL; X-ray; 1.85 A; A=981-1108. DR PDB; 4TZ2; X-ray; 1.70 A; A=981-1108. DR PDB; 4TZ8; X-ray; 2.15 A; A=981-1108. DR PDB; 5A5N; X-ray; 1.95 A; A=981-1108. DR PDB; 5A5O; X-ray; 2.04 A; A=981-1108. DR PDB; 5A5P; X-ray; 2.03 A; A=981-1108. DR PDB; 5A5Q; X-ray; 1.97 A; A=981-1108. DR PDB; 5A5R; X-ray; 2.01 A; A=981-1108. DR PDB; 5A81; X-ray; 2.03 A; A=981-1108. DR PDB; 5A82; X-ray; 1.86 A; A=981-1108. DR PDB; 5A83; X-ray; 2.09 A; A=981-1108. DR PDB; 5EPB; X-ray; 1.50 A; A=981-1108. DR PDB; 5F36; X-ray; 1.50 A; A=981-1108. DR PDB; 5F3A; X-ray; 1.60 A; A=981-1108. DR PDB; 5LJ0; X-ray; 1.82 A; A=981-1108. DR PDB; 5QXI; X-ray; 1.64 A; A=981-1108. DR PDB; 5QXJ; X-ray; 1.46 A; A=981-1108. DR PDB; 5QXK; X-ray; 1.72 A; A=981-1108. DR PDB; 5QXL; X-ray; 1.57 A; A=981-1108. DR PDB; 5QXM; X-ray; 1.50 A; A=981-1108. DR PDB; 5QXN; X-ray; 1.41 A; A=981-1108. DR PDB; 5QXO; X-ray; 1.47 A; A=981-1108. DR PDB; 5QXP; X-ray; 1.41 A; A=981-1108. DR PDB; 5QXQ; X-ray; 1.55 A; A=981-1108. DR PDB; 5QXR; X-ray; 1.66 A; A=981-1108. DR PDB; 5QXS; X-ray; 1.62 A; A=981-1108. DR PDB; 5QXT; X-ray; 1.55 A; A=981-1108. DR PDB; 5QXU; X-ray; 1.65 A; A=981-1108. DR PDB; 5QXV; X-ray; 1.74 A; A=981-1108. DR PDB; 5QXW; X-ray; 1.78 A; A=981-1108. DR PDB; 5QXX; X-ray; 1.58 A; A=981-1108. DR PDB; 5QXY; X-ray; 1.54 A; A=981-1108. DR PDB; 5QXZ; X-ray; 1.64 A; A=981-1108. DR PDB; 5QY0; X-ray; 1.89 A; A=981-1108. DR PDB; 5R4E; X-ray; 1.83 A; A=981-1108. DR PDB; 5R4F; X-ray; 1.44 A; A=981-1108. DR PDB; 5R4V; X-ray; 1.29 A; A=981-1108. DR PDB; 5R4W; X-ray; 1.47 A; A=981-1108. DR PDB; 5R4X; X-ray; 1.40 A; A=981-1108. DR PDB; 5R4Y; X-ray; 1.84 A; A=981-1108. DR PDB; 5R4Z; X-ray; 1.46 A; A=981-1108. DR PDB; 6CPS; X-ray; 1.93 A; A=981-1108. DR PDB; 6EPJ; X-ray; 1.65 A; A=981-1108. DR PDB; 6EPR; X-ray; 2.05 A; A=981-1108. DR PDB; 6EPS; X-ray; 2.08 A; A=981-1108. DR PDB; 6EPT; X-ray; 1.65 A; A=981-1108. DR PDB; 6EPU; X-ray; 1.80 A; A=981-1108. DR PDB; 6EPV; X-ray; 1.79 A; A=981-1108. DR PDB; 6EPW; X-ray; 1.92 A; A=981-1108. DR PDB; 6EPX; X-ray; 1.84 A; A=981-1108. DR PDB; 6HDN; X-ray; 1.90 A; A=981-1108. DR PDB; 6HDO; X-ray; 2.61 A; A=981-1108. DR PDB; 6HI3; X-ray; 2.40 A; A=981-1108. DR PDB; 6HI4; X-ray; 1.69 A; A=981-1108. DR PDB; 6HI5; X-ray; 1.59 A; A=981-1108. DR PDB; 6HI6; X-ray; 1.64 A; A=981-1108. DR PDB; 6HI7; X-ray; 1.74 A; A=981-1108. DR PDB; 6HI8; X-ray; 1.90 A; A=981-1108. DR PDB; 6HIA; X-ray; 1.90 A; A=981-1108. DR PDB; 6HIB; X-ray; 2.03 A; A=981-1108. DR PDB; 6HIC; X-ray; 1.77 A; A=981-1108. DR PDB; 6HID; X-ray; 1.77 A; A=981-1108. DR PDB; 6HIE; X-ray; 2.05 A; A=981-1108. DR PDB; 6S55; X-ray; 2.09 A; A=981-1108. DR PDB; 6S56; X-ray; 2.01 A; A=981-1108. DR PDB; 6S57; X-ray; 1.82 A; A=981-1108. DR PDB; 6YB4; X-ray; 1.85 A; AAA=981-1108. DR PDB; 7M98; X-ray; 1.60 A; A=966-1112. DR PDB; 7PPX; X-ray; 1.35 A; AAA=981-1108. DR PDB; 7PX5; X-ray; 2.18 A; AAA=981-1108. DR PDB; 7Q6T; X-ray; 2.05 A; A=981-1108. DR PDB; 7Q6U; X-ray; 1.95 A; A=981-1108. DR PDB; 7Q6V; X-ray; 1.96 A; A=981-1108. DR PDB; 7Q6W; X-ray; 1.96 A; A=981-1108. DR PDB; 7QU7; X-ray; 2.13 A; AAA=981-1108. DR PDB; 7QUK; X-ray; 1.47 A; AAA=981-1108. DR PDB; 7QUM; X-ray; 1.50 A; AAA=981-1108. DR PDB; 7QWO; X-ray; 1.50 A; AAA=981-1108. DR PDB; 7QX1; X-ray; 1.49 A; AAA=981-1108. DR PDB; 7QXT; X-ray; 1.51 A; AAA=981-1108. DR PDB; 7QYK; X-ray; 1.43 A; AAA=981-1108. DR PDB; 7QYL; X-ray; 1.44 A; AAA=981-1108. DR PDB; 7QZM; X-ray; 1.45 A; AAA=981-1108. DR PDB; 7QZY; X-ray; 1.93 A; AAA=981-1108. DR PDB; 7QZZ; X-ray; 2.52 A; AAA=981-1108. DR PDB; 7R00; X-ray; 1.48 A; AAA=981-1108. DR PDB; 7R05; X-ray; 1.53 A; AAA=981-1108. DR PDB; 7R0Y; X-ray; 1.43 A; AAA=981-1108. DR PDB; 7Z9H; X-ray; 1.34 A; AAA=981-1108. DR PDB; 7Z9I; X-ray; 1.50 A; AAA=981-1108. DR PDB; 7Z9J; X-ray; 1.90 A; AAA=981-1108. DR PDB; 7Z9N; X-ray; 1.34 A; AAA=981-1108. DR PDB; 7Z9O; X-ray; 1.47 A; AAA=981-1108. DR PDB; 7Z9S; X-ray; 1.50 A; AAA=981-1108. DR PDB; 7Z9U; X-ray; 1.76 A; AAA=981-1108. DR PDB; 8H3H; EM; 3.15 A; A/B/C/D/E/F=403-1390. DR PDB; 8JUW; EM; 3.79 A; A/B/C/D/E/F=403-1390. DR PDB; 8JUY; EM; 4.34 A; A/B/C/D/E/F=403-1390. DR PDB; 8JUZ; EM; 4.29 A; A/B/C/D/E/F=403-1390. DR PDB; 8RU5; X-ray; 1.36 A; A=981-1108. DR PDB; 8SDO; X-ray; 2.01 A; A=966-1112. DR PDB; 8SDQ; X-ray; 1.85 A; A=966-1112. DR AlphaFoldDB; Q6PL18; -. DR EMDB; EMD-34468; -. DR EMDB; EMD-36665; -. DR EMDB; EMD-36666; -. DR EMDB; EMD-36667; -. DR MDposit; Q6PL18; -. DR SMR; Q6PL18; -. DR BioGRID; 118827; 67. DR DIP; DIP-46197N; -. DR FunCoup; Q6PL18; 2711. DR IntAct; Q6PL18; 43. DR MINT; Q6PL18; -. DR NDEx; IQUERY-CP-ATAD2; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000287394; -. DR BindingDB; Q6PL18; -. DR ChEMBL; CHEMBL2150837; -. DR GuidetoPHARMACOLOGY; 2719; -. DR GlyGen; Q6PL18; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q6PL18; -. DR PhosphoSitePlus; Q6PL18; -. DR SwissPalm; Q6PL18; -. DR BioMuta; ATAD2; -. DR DMDM; 74762365; -. DR jPOST; Q6PL18; -. DR MassIVE; Q6PL18; -. DR PaxDb; 9606-ENSP00000287394; -. DR PeptideAtlas; Q6PL18; -. DR ProteomicsDB; 67248; -. [Q6PL18-1] DR ProteomicsDB; 67249; -. [Q6PL18-2] DR Pumba; Q6PL18; -. DR Antibodypedia; 13822; 181 antibodies from 31 providers. DR DNASU; 29028; -. DR Ensembl; ENST00000287394.10; ENSP00000287394.5; ENSG00000156802.14. [Q6PL18-1] DR GeneID; 29028; -. DR KEGG; hsa:29028; -. DR MANE-Select; ENST00000287394.10; ENSP00000287394.5; NM_014109.4; NP_054828.2. DR UCSC; uc003yqh.5; human. [Q6PL18-1] DR AGR; HGNC:30123; -. DR ClinPGx; PA134895566; -. DR CTD; 29028; -. DR DisGeNET; 29028; -. DR GeneCards; ATAD2; -. DR HGNC; HGNC:30123; ATAD2. DR HPA; ENSG00000156802; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 611941; gene. DR OpenTargets; ENSG00000156802; -. DR VEuPathDB; HostDB:ENSG00000156802; -. DR eggNOG; KOG0732; Eukaryota. DR GeneTree; ENSGT00550000074694; -. DR HOGENOM; CLU_001448_3_2_1; -. DR InParanoid; Q6PL18; -. DR OMA; NRNACHQ; -. DR OrthoDB; 5421at2759; -. DR PAN-GO; Q6PL18; 7 GO annotations based on evolutionary models. DR PhylomeDB; Q6PL18; -. DR PathwayCommons; Q6PL18; -. DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors. DR SignaLink; Q6PL18; -. DR Agora; ENSG00000156802; -. DR BioGRID-ORCS; 29028; 37 hits in 1174 CRISPR screens. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; ATAD2; human. DR EvolutionaryTrace; Q6PL18; -. DR GenomeRNAi; 29028; -. DR Pharos; Q6PL18; Tchem. DR PRO; PR:Q6PL18; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q6PL18; protein. DR Bgee; ENSG00000156802; Expressed in secondary oocyte and 146 other cell types or tissues. DR ExpressionAtlas; Q6PL18; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central. DR GO; GO:0006337; P:nucleosome disassembly; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IBA:GO_Central. DR CDD; cd05528; Bromo_AAA; 1. DR CDD; cd19517; RecA-like_Yta7-like; 1. DR FunFam; 1.20.920.10:FF:000021; ATPase family AAA domain-containing protein 2; 1. DR FunFam; 1.10.8.60:FF:000016; ATPase family AAA domain-containing protein 2B; 1. DR FunFam; 3.40.50.300:FF:000734; ATPase family, AAA domain containing 2; 1. DR FunFam; 3.40.50.300:FF:000061; ATPase family, AAA domain-containing 2; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR IDEAL; IID00570; -. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR045199; ATAD2-like. DR InterPro; IPR061960; ATAD2_C. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23069:SF4; ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 2; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF31015; ATAD2_C; 1. DR Pfam; PF00439; Bromodomain; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00382; AAA; 1. DR SMART; SM00297; BROMO; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00674; AAA; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PDBsum; 3DAI; -. DR PDBsum; 4QSP; -. DR PDBsum; 4QSQ; -. DR PDBsum; 4QSR; -. DR PDBsum; 4QSS; -. DR PDBsum; 4QST; -. DR PDBsum; 4QSU; -. DR PDBsum; 4QSV; -. DR PDBsum; 4QSW; -. DR PDBsum; 4QSX; -. DR PDBsum; 4QUT; -. DR PDBsum; 4QUU; -. DR PDBsum; 4TT2; -. DR PDBsum; 4TT4; -. DR PDBsum; 4TT6; -. DR PDBsum; 4TTE; -. DR PDBsum; 4TU4; -. DR PDBsum; 4TU6; -. DR PDBsum; 4TYL; -. DR PDBsum; 4TZ2; -. DR PDBsum; 4TZ8; -. DR PDBsum; 5A5N; -. DR PDBsum; 5A5O; -. DR PDBsum; 5A5P; -. DR PDBsum; 5A5Q; -. DR PDBsum; 5A5R; -. DR PDBsum; 5A81; -. DR PDBsum; 5A82; -. DR PDBsum; 5A83; -. DR PDBsum; 5EPB; -. DR PDBsum; 5F36; -. DR PDBsum; 5F3A; -. DR PDBsum; 5LJ0; -. DR PDBsum; 5QXI; -. DR PDBsum; 5QXJ; -. DR PDBsum; 5QXK; -. DR PDBsum; 5QXL; -. DR PDBsum; 5QXM; -. DR PDBsum; 5QXN; -. DR PDBsum; 5QXO; -. DR PDBsum; 5QXP; -. DR PDBsum; 5QXQ; -. DR PDBsum; 5QXR; -. DR PDBsum; 5QXS; -. DR PDBsum; 5QXT; -. DR PDBsum; 5QXU; -. DR PDBsum; 5QXV; -. DR PDBsum; 5QXW; -. DR PDBsum; 5QXX; -. DR PDBsum; 5QXY; -. DR PDBsum; 5QXZ; -. DR PDBsum; 5QY0; -. DR PDBsum; 5R4E; -. DR PDBsum; 5R4F; -. DR PDBsum; 5R4V; -. DR PDBsum; 5R4W; -. DR PDBsum; 5R4X; -. DR PDBsum; 5R4Y; -. DR PDBsum; 5R4Z; -. DR PDBsum; 6CPS; -. DR PDBsum; 6EPJ; -. DR PDBsum; 6EPR; -. DR PDBsum; 6EPS; -. DR PDBsum; 6EPT; -. DR PDBsum; 6EPU; -. DR PDBsum; 6EPV; -. DR PDBsum; 6EPW; -. DR PDBsum; 6EPX; -. DR PDBsum; 6HDN; -. DR PDBsum; 6HDO; -. DR PDBsum; 6HI3; -. DR PDBsum; 6HI4; -. DR PDBsum; 6HI5; -. DR PDBsum; 6HI6; -. DR PDBsum; 6HI7; -. DR PDBsum; 6HI8; -. DR PDBsum; 6HIA; -. DR PDBsum; 6HIB; -. DR PDBsum; 6HIC; -. DR PDBsum; 6HID; -. DR PDBsum; 6HIE; -. DR PDBsum; 6S55; -. DR PDBsum; 6S56; -. DR PDBsum; 6S57; -. DR PDBsum; 6YB4; -. DR PDBsum; 7M98; -. DR PDBsum; 7PPX; -. DR PDBsum; 7PX5; -. DR PDBsum; 7Q6T; -. DR PDBsum; 7Q6U; -. DR PDBsum; 7Q6V; -. DR PDBsum; 7Q6W; -. DR PDBsum; 7QU7; -. DR PDBsum; 7QUK; -. DR PDBsum; 7QUM; -. DR PDBsum; 7QWO; -. DR PDBsum; 7QX1; -. DR PDBsum; 7QXT; -. DR PDBsum; 7QYK; -. DR PDBsum; 7QYL; -. DR PDBsum; 7QZM; -. DR PDBsum; 7QZY; -. DR PDBsum; 7QZZ; -. DR PDBsum; 7R00; -. DR PDBsum; 7R05; -. DR PDBsum; 7R0Y; -. DR PDBsum; 7Z9H; -. DR PDBsum; 7Z9I; -. DR PDBsum; 7Z9J; -. DR PDBsum; 7Z9N; -. DR PDBsum; 7Z9O; -. DR PDBsum; 7Z9S; -. DR PDBsum; 7Z9U; -. DR PDBsum; 8H3H; -. DR PDBsum; 8JUW; -. DR PDBsum; 8JUY; -. DR PDBsum; 8JUZ; -. DR PDBsum; 8RU5; -. DR PDBsum; 8SDO; -. DR PDBsum; 8SDQ; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; ATP-binding; Bromodomain; KW Coiled coil; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..1390 FT /note="ATPase family AAA domain-containing protein 2" FT /id="PRO_0000084796" FT DOMAIN 980..1092 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 40..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 216..380 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1124..1163 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1181..1242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 970..994 FT /evidence="ECO:0000255" FT COILED 1086..1112 FT /evidence="ECO:0000255" FT COMPBIAS 42..57 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 223..232 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 244..288 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1135..1148 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1149..1160 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1185..1200 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1229..1242 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 467..474 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 170 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 327 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 410 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 746 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 751 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1139 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1149 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1152 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1176 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1200 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1233 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1235 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1243 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1302 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1323 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 125 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 317 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1148 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1236 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..170 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_015633" FT VAR_SEQ 551..582 FT /note="IVSTLLALMDGLDSRGEIVVIGATNRLDSIDP -> YGWIGQQRGNCGHWCY FT EQARFYRSCFTKAWSL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_015634" FT VAR_SEQ 583..1390 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_015635" FT VARIANT 1280 FT /note="I -> T (in dbSNP:rs3758122)" FT /id="VAR_047625" FT MUTAGEN 473 FT /note="K->T: Reduces the ability to mediate FT estradiol-dependent induction of CCND1 and E2F1; when FT associated with Q-532." FT /evidence="ECO:0000269|PubMed:17998543" FT MUTAGEN 532 FT /note="E->Q: Reduces the ability to mediate FT estradiol-dependent induction of CCND1 and E2F1; when FT associated with T-473." FT /evidence="ECO:0000269|PubMed:17998543" FT STRAND 424..427 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 435..438 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 439..442 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 444..447 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 451..454 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 462..468 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 471..473 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 474..484 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 485..487 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 492..501 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 508..523 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 525..531 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 533..535 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 549..559 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 567..575 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 577..579 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 587..589 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 597..599 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 601..611 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 621..630 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 637..654 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 680..684 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 690..693 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 700..702 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 703..705 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 706..716 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 721..723 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 725..728 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 794..798 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 805..809 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 810..816 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 817..819 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 820..824 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 828..832 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 838..851 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 854..859 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 862..865 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 866..868 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 871..880 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 890..898 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 900..902 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 905..908 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 913..915 FT /evidence="ECO:0007829|PDB:8H3H" FT STRAND 918..920 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 923..925 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 926..937 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 940..942 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 981..1001 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1004..1009 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1012..1014 FT /evidence="ECO:0007829|PDB:5R4V" FT TURN 1015..1017 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1021..1024 FT /evidence="ECO:0007829|PDB:5R4V" FT STRAND 1025..1027 FT /evidence="ECO:0007829|PDB:6S56" FT HELIX 1031..1039 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1046..1063 FT /evidence="ECO:0007829|PDB:5R4V" FT STRAND 1066..1068 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1069..1092 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1095..1107 FT /evidence="ECO:0007829|PDB:5R4V" FT HELIX 1332..1343 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 1349..1352 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 1353..1359 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 1360..1365 FT /evidence="ECO:0007829|PDB:8H3H" FT TURN 1372..1375 FT /evidence="ECO:0007829|PDB:8H3H" FT HELIX 1376..1383 FT /evidence="ECO:0007829|PDB:8H3H" SQ SEQUENCE 1390 AA; 158554 MW; F43B30C77BB0F4BA CRC64; MVVLRSSLEL HNHSAASATG SLDLSSDFLS LEHIGRRRLR SAGAAQKKPA ATTAKAGDGS SVKEVETYHR TRALRSLRKD AQNSSDSSFE KNVEITEQLA NGRHFTRQLA RQQADKKKEE HREDKVIPVT RSLRARNIVQ STEHLHEDNG DVEVRRSCRI RSRYSGVNQS MLFDKLITNT AEAVLQKMDD MKKMRRQRMR ELEDLGVFNE TEESNLNMYT RGKQKDIQRT DEETTDNQEG SVESSEEGED QEHEDDGEDE DDEDDDDDDD DDDDDDDEDD EDEEDGEEEN QKRYYLRQRK ATVYYQAPLE KPRHQRKPNI FYSGPASPAR PRYRLSSAGP RSPYCKRMNR RRHAIHSSDS TSSSSSEDEQ HFERRRKRSR NRAINRCLPL NFRKDELKGI YKDRMKIGAS LADVDPMQLD SSVRFDSVGG LSNHIAALKE MVVFPLLYPE VFEKFKIQPP RGCLFYGPPG TGKTLVARAL ANECSQGDKR VAFFMRKGAD CLSKWVGESE RQLRLLFDQA YQMRPSIIFF DEIDGLAPVR SSRQDQIHSS IVSTLLALMD GLDSRGEIVV IGATNRLDSI DPALRRPGRF DREFLFSLPD KEARKEILKI HTRDWNPKPL DTFLEELAEN CVGYCGADIK SICAEAALCA LRRRYPQIYT TSEKLQLDLS SINISAKDFE VAMQKMIPAS QRAVTSPGQA LSTVVKPLLQ NTVDKILEAL QRVFPHAEFR TNKTLDSDIS CPLLESDLAY SDDDVPSVYE NGLSQKSSHK AKDNFNFLHL NRNACYQPMS FRPRILIVGE PGFGQGSHLA PAVIHALEKF TVYTLDIPVL FGVSTTSPEE TCAQVIREAK RTAPSIVYVP HIHVWWEIVG PTLKATFTTL LQNIPSFAPV LLLATSDKPH SALPEEVQEL FIRDYGEIFN VQLPDKEERT KFFEDLILKQ AAKPPISKKK AVLQALEVLP VAPPPEPRSL TAEEVKRLEE QEEDTFRELR IFLRNVTHRL AIDKRFRVFT KPVDPDEVPD YVTVIKQPMD LSSVISKIDL HKYLTVKDYL RDIDLICSNA LEYNPDRDPG DRLIRHRACA LRDTAYAIIK EELDEDFEQL CEEIQESRKK RGCSSSKYAP SYYHVMPKQN STLVGDKRSD PEQNEKLKTP STPVACSTPA QLKRKIRKKS NWYLGTIKKR RKISQAKDDS QNAIDHKIES DTEETQDTSV DHNETGNTGE SSVEENEKQQ NASESKLELR NNSNTCNIEN ELEDSRKTTA CTELRDKIAC NGDASSSQII HISDENEGKE MCVLRMTRAR RSQVEQQQLI TVEKALAILS QPTPSLVVDH ERLKNLLKTV VKKSQNYNIF QLENLYAVIS QCIYRHRKDH DKTSLIQKME QEVENFSCSR //