ATAD2_HUMAN
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 03-AUG-2022, entry version 159.
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)70933-8;
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 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 [20]
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 + H(+) + phosphate; 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 -!- 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};
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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_014109.3. [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; 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 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; 7Q6T; -.
DR PDBsum; 7Q6U; -.
DR PDBsum; 7Q6V; -.
DR PDBsum; 7Q6W; -.
DR AlphaFoldDB; Q6PL18; -.
DR SMR; Q6PL18; -.
DR BioGRID; 118827; 44.
DR DIP; DIP-46197N; -.
DR IntAct; Q6PL18; 12.
DR MINT; Q6PL18; -.
DR STRING; 9606.ENSP00000287394; -.
DR BindingDB; Q6PL18; -.
DR ChEMBL; CHEMBL2150837; -.
DR GuidetoPHARMACOLOGY; 2719; -.
DR iPTMnet; Q6PL18; -.
DR PhosphoSitePlus; Q6PL18; -.
DR BioMuta; ATAD2; -.
DR DMDM; 74762365; -.
DR EPD; Q6PL18; -.
DR jPOST; Q6PL18; -.
DR MassIVE; Q6PL18; -.
DR MaxQB; Q6PL18; -.
DR PaxDb; Q6PL18; -.
DR PeptideAtlas; Q6PL18; -.
DR PRIDE; Q6PL18; -.
DR ProteomicsDB; 67248; -. [Q6PL18-1]
DR ProteomicsDB; 67249; -. [Q6PL18-2]
DR Antibodypedia; 13822; 171 antibodies from 28 providers.
DR DNASU; 29028; -.
DR Ensembl; ENST00000287394.10; ENSP00000287394.5; ENSG00000156802.13. [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 CTD; 29028; -.
DR DisGeNET; 29028; -.
DR GeneCards; ATAD2; -.
DR HGNC; HGNC:30123; ATAD2.
DR HPA; ENSG00000156802; Tissue enhanced (lymphoid).
DR MIM; 611941; gene.
DR neXtProt; NX_Q6PL18; -.
DR OpenTargets; ENSG00000156802; -.
DR PharmGKB; PA134895566; -.
DR VEuPathDB; HostDB:ENSG00000156802; -.
DR eggNOG; KOG0732; Eukaryota.
DR GeneTree; ENSGT00550000074694; -.
DR HOGENOM; CLU_001448_3_2_1; -.
DR InParanoid; Q6PL18; -.
DR OMA; RRKSKWY; -.
DR PhylomeDB; Q6PL18; -.
DR TreeFam; TF314783; -.
DR PathwayCommons; Q6PL18; -.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR SignaLink; Q6PL18; -.
DR BioGRID-ORCS; 29028; 37 hits in 1094 CRISPR screens.
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 145 other tissues.
DR ExpressionAtlas; Q6PL18; baseline and differential.
DR Genevisible; Q6PL18; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR IDEAL; IID00570; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR031252; ANCCA.
DR InterPro; IPR045199; ATAD2-like.
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; PTHR23069; 1.
DR PANTHER; PTHR23069:SF4; PTHR23069:SF4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
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; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1390
FT /note="ATPase family AAA domain-containing protein 2"
FT /id="PRO_0000084796"
FT DOMAIN 1001..1071
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 237..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1226
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 estradiol-
FT dependent induction of CCND1 and E2F1; when associated with
FT Q-532."
FT /evidence="ECO:0000269|PubMed:17998543"
FT MUTAGEN 532
FT /note="E->Q: Reduces the ability to mediate estradiol-
FT dependent induction of CCND1 and E2F1; when associated with
FT T-473."
FT /evidence="ECO:0000269|PubMed:17998543"
FT HELIX 981..1001
FT /evidence="ECO:0007829|PDB:5R4V"
FT HELIX 1004..1009
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 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"
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
