NCOA2_HUMAN
ID NCOA2_HUMAN Reviewed; 1464 AA.
AC Q15596; Q14CD2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 2.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Nuclear receptor coactivator 2;
DE Short=NCoA-2;
DE AltName: Full=Class E basic helix-loop-helix protein 75;
DE Short=bHLHe75;
DE AltName: Full=Transcriptional intermediary factor 2 {ECO:0000303|PubMed:8670870};
DE Short=hTIF2 {ECO:0000303|PubMed:8670870};
GN Name=NCOA2; Synonyms=BHLHE75, SRC2, TIF2 {ECO:0000303|PubMed:8670870};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=8670870; DOI=10.1002/j.1460-2075.1996.tb00736.x;
RA Voegel J.J., Heine M.J.S., Zechel C., Chambon P., Gronemeyer H.;
RT "TIF2, a 160 kDa transcriptional mediator for the ligand-dependent
RT activation function AF-2 of nuclear receptors.";
RL EMBO J. 15:3667-3675(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-1282.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 870-939, AND CHROMOSOMAL TRANSLOCATION WITH
RP KAT6A.
RX PubMed=9558366;
RA Carapeti M., Aguiar R.C.T., Goldman J.M., Cross N.C.P.;
RT "A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in
RT acute myeloid leukemia.";
RL Blood 91:3127-3133(1998).
RN [4]
RP FUNCTION, INTERACTION WITH CREBBP; ESR1; RARA AND RXRA, DOMAIN, AND
RP MUTAGENESIS OF 644-LEU-LEU-645; 693-LEU-LEU-694; 748-LEU-LEU-749;
RP 1079-LEU--LEU-1083 AND 1081-ASP-GLN-1082.
RX PubMed=9430642; DOI=10.1093/emboj/17.2.507;
RA Voegel J.J., Heine M.J.S., Tini M., Vivat V., Chambon P., Gronemeyer H.;
RT "The coactivator TIF2 contains three nuclear receptor-binding motifs and
RT mediates transactivation through CBP binding-dependent and -independent
RT pathways.";
RL EMBO J. 17:507-519(1998).
RN [5]
RP INTERACTION WITH NR3C1.
RX PubMed=9590696; DOI=10.1038/30032;
RA Fryer C.J., Archer T.K.;
RT "Chromatin remodelling by the glucocorticoid receptor requires the BRG1
RT complex.";
RL Nature 393:88-91(1998).
RN [6]
RP INTERACTION WITH RORA.
RX PubMed=10478845; DOI=10.1210/mend.13.9.0343;
RA Atkins G.B., Hu X., Guenther M.G., Rachez C., Freedman L.P., Lazar M.A.;
RT "Coactivators for the orphan nuclear receptor RORalpha.";
RL Mol. Endocrinol. 13:1550-1557(1999).
RN [7]
RP INTERACTION WITH HIF1A; NCOA1 AND APEX1.
RX PubMed=10594042; DOI=10.1128/mcb.20.1.402-415.2000;
RA Carrero P., Okamoto K., Coumailleau P., O'Brien S., Tanaka H.,
RA Poellinger L.;
RT "Redox-regulated recruitment of the transcriptional coactivators CREB-
RT binding protein and SRC-1 to hypoxia-inducible factor 1alpha.";
RL Mol. Cell. Biol. 20:402-415(2000).
RN [8]
RP INTERACTION WITH DDX5.
RX PubMed=11250900; DOI=10.1093/emboj/20.6.1341;
RA Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y.,
RA Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S.;
RT "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor
RT alpha coactivator through the N-terminal activation domain (AF-1) with an
RT RNA coactivator, SRA.";
RL EMBO J. 20:1341-1352(2001).
RN [9]
RP IDENTIFICATION IN A COACTIVATOR COMPLEX CONTAINING CREBBP; NCOA3; IKKA;
RP IKKB AND IKBKG.
RX PubMed=11971985; DOI=10.1128/mcb.22.10.3549-3561.2002;
RA Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J.,
RA O'Malley B.W.;
RT "Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by
RT I kappa B kinase.";
RL Mol. Cell. Biol. 22:3549-3561(2002).
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH KAT6A.
RX PubMed=12676584; DOI=10.1016/s1535-6108(03)00051-5;
RA Deguchi K., Ayton P.M., Carapeti M., Kutok J.L., Snyder C.S.,
RA Williams I.R., Cross N.C.P., Glass C.K., Cleary M.L., Gilliland D.G.;
RT "MOZ-TIF2-induced acute myeloid leukemia requires the MOZ nucleosome
RT binding motif and TIF2-mediated recruitment of CBP.";
RL Cancer Cell 3:259-271(2003).
RN [11]
RP CHROMOSOMAL TRANSLOCATION WITH KAT6A.
RX PubMed=15657427; DOI=10.1128/mcb.25.3.988-1002.2005;
RA Kindle K.B., Troke P.J.F., Collins H.M., Matsuda S., Bossi D., Bellodi C.,
RA Kalkhoven E., Salomoni P., Pelicci P.G., Minucci S., Heery D.M.;
RT "MOZ-TIF2 inhibits transcription by nuclear receptors and p53 by impairment
RT of CBP function.";
RL Mol. Cell. Biol. 25:988-1002(2005).
RN [12]
RP INTERACTION WITH PSMB9.
RX PubMed=16957778; DOI=10.1038/sj.emboj.7601306;
RA Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R.,
RA Sun X., Shang Y.;
RT "The catalytic subunit of the proteasome is engaged in the entire process
RT of estrogen receptor-regulated transcription.";
RL EMBO J. 25:4223-4233(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [14]
RP INTERACTION WITH TTLL5.
RC TISSUE=Testis;
RX PubMed=17116691; DOI=10.1128/mcb.01360-06;
RA He Y., Simons S.S. Jr.;
RT "STAMP, a novel predicted factor assisting TIF2 actions in glucocorticoid
RT receptor-mediated induction and repression.";
RL Mol. Cell. Biol. 27:1467-1485(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH NR1H3.
RX PubMed=19481530; DOI=10.1016/j.molcel.2009.05.006;
RA Jakobsson T., Venteclef N., Toresson G., Damdimopoulos A.E., Ehrlund A.,
RA Lou X., Sanyal S., Steffensen K.R., Gustafsson J.A., Treuter E.;
RT "GPS2 is required for cholesterol efflux by triggering histone
RT demethylation, LXR recruitment, and coregulator assembly at the ABCG1
RT locus.";
RL Mol. Cell 34:510-518(2009).
RN [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-640; LYS-780 AND LYS-785, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-493 AND SER-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-493; SER-565;
RP SER-682; SER-699; SER-736 AND SER-771, 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 [24]
RP FUNCTION, AND INTERACTION WITH RWDD3 AND NR3C1.
RX PubMed=23508108; DOI=10.1128/mcb.01470-12;
RA Druker J., Liberman A.C., Antunica-Noguerol M., Gerez J., Paez-Pereda M.,
RA Rein T., Iniguez-Lluhi J.A., Holsboer F., Arzt E.;
RT "RSUME enhances glucocorticoid receptor SUMOylation and transcriptional
RT activity.";
RL Mol. Cell. Biol. 33:2116-2127(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-554; SER-565 AND
RP SER-699, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [26]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1173; ARG-1177; ARG-1190;
RP ARG-1196; ARG-1203; ARG-1221; ARG-1261 AND ARG-1266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-785, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-648; LYS-705; LYS-731;
RP LYS-785 AND LYS-1454, 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).
CC -!- FUNCTION: Transcriptional coactivator for steroid receptors and nuclear
CC receptors (PubMed:8670870, PubMed:23508108, PubMed:9430642).
CC Coactivator of the steroid binding domain (AF-2) but not of the
CC modulating N-terminal domain (AF-1) (PubMed:8670870, PubMed:23508108,
CC PubMed:9430642). Required with NCOA1 to control energy balance between
CC white and brown adipose tissues (PubMed:8670870, PubMed:23508108,
CC PubMed:9430642). Critical regulator of glucose metabolism regulation,
CC acts as RORA coactivator to specifically modulate G6PC1 expression
CC (PubMed:8670870, PubMed:23508108, PubMed:9430642). Involved in the
CC positive regulation of the transcriptional activity of the
CC glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3
CC (PubMed:23508108). Positively regulates the circadian clock by acting
CC as a transcriptional coactivator for the CLOCK-ARNTL/BMAL1 heterodimer
CC (By similarity). {ECO:0000250|UniProtKB:Q61026,
CC ECO:0000269|PubMed:23508108, ECO:0000269|PubMed:8670870,
CC ECO:0000269|PubMed:9430642}.
CC -!- SUBUNIT: Present in a complex containing NCOA3, IKKA, IKKB, IKBKG and
CC CREBBP. Interacts (via C-terminus) with CREBBP. Interacts with ESR1,
CC HIF1A, NCOA1, APEX1, NR3C1, NR3C2, CARM1, RARA, and RXRA. Present in a
CC complex containing CARM1 and EP300/P300. Interacts with CASP8AP2 and
CC TTLL5/STAMP. Interacts with PSMB9 and DDX5. Interacts (via LXXLL 1, 2
CC and 3 motifs) with RORA and RORC (via AF-2 motif). Interacts with
CC RWDD3. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Interacts
CC with NR4A3; potentiates the activity of the NR4A3 (By similarity).
CC Interacts with NR1H3 (PubMed:19481530). {ECO:0000250|UniProtKB:Q61026,
CC ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:10594042,
CC ECO:0000269|PubMed:11250900, ECO:0000269|PubMed:11971985,
CC ECO:0000269|PubMed:16957778, ECO:0000269|PubMed:17116691,
CC ECO:0000269|PubMed:19481530, ECO:0000269|PubMed:23508108,
CC ECO:0000269|PubMed:9430642, ECO:0000269|PubMed:9590696}.
CC -!- INTERACTION:
CC Q15596; P10275: AR; NbExp=3; IntAct=EBI-81236, EBI-608057;
CC Q15596; P03372: ESR1; NbExp=5; IntAct=EBI-81236, EBI-78473;
CC Q15596; O00482-1: NR5A2; NbExp=2; IntAct=EBI-81236, EBI-15960777;
CC Q15596; P19793: RXRA; NbExp=5; IntAct=EBI-81236, EBI-78598;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8670870}.
CC -!- DOMAIN: Contains four Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. The LXXLL
CC motifs are essential for the association with nuclear receptors and
CC are, at least in part, functionally redundant.
CC {ECO:0000269|PubMed:9430642}.
CC -!- DOMAIN: The LLXXLXXXL motif is involved in transcriptional coactivation
CC and CREBBP/CBP binding. {ECO:0000269|PubMed:9430642}.
CC -!- DOMAIN: Contains 2 C-terminal transcription activation domains (AD1 and
CC AD2) that can function independently. {ECO:0000269|PubMed:9430642}.
CC -!- PTM: Acetylated. Deacetylation at Lys-780 by SIRT6 stimulates its
CC ability to coactivate PPARA. {ECO:0000250|UniProtKB:Q61026}.
CC -!- DISEASE: Note=Chromosomal aberrations involving NCOA2 may be a cause of
CC acute myeloid leukemias. Inversion inv(8)(p11;q13) generates the KAT6A-
CC NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the
CC C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts
CC its function in transcription activation. {ECO:0000269|PubMed:12676584,
CC ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366}.
CC -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC family. {ECO:0000305}.
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DR EMBL; X97674; CAA66263.1; -; mRNA.
DR EMBL; BC114383; AAI14384.1; -; mRNA.
DR CCDS; CCDS47872.1; -.
DR RefSeq; NP_001308632.1; NM_001321703.1.
DR RefSeq; NP_001308636.1; NM_001321707.1.
DR RefSeq; NP_001308640.1; NM_001321711.1.
DR RefSeq; NP_001308641.1; NM_001321712.1.
DR RefSeq; NP_001308642.1; NM_001321713.1.
DR RefSeq; NP_006531.1; NM_006540.3.
DR PDB; 1GWQ; X-ray; 2.45 A; C/D=688-696.
DR PDB; 1GWR; X-ray; 2.40 A; C/D=742-750.
DR PDB; 1M2Z; X-ray; 2.50 A; B/E=734-754.
DR PDB; 1MV9; X-ray; 1.90 A; B=686-698.
DR PDB; 1MVC; X-ray; 1.90 A; B=686-698.
DR PDB; 1MZN; X-ray; 1.90 A; B/D/F/H=686-698.
DR PDB; 1P93; X-ray; 2.70 A; E/F/G/H=740-751.
DR PDB; 1T63; X-ray; 2.07 A; B=740-753.
DR PDB; 1T65; X-ray; 1.66 A; B=686-698.
DR PDB; 1UHL; X-ray; 2.90 A; C/D=687-696.
DR PDB; 1YOK; X-ray; 2.50 A; B/C=740-753.
DR PDB; 1ZDT; X-ray; 2.10 A; P/Q=741-752.
DR PDB; 1ZDU; X-ray; 2.50 A; P/Q=741-751.
DR PDB; 1ZKY; X-ray; 2.25 A; C/D=686-698.
DR PDB; 2AO6; X-ray; 1.89 A; B=740-753.
DR PDB; 2B1V; X-ray; 1.80 A; C/D=686-698.
DR PDB; 2B1Z; X-ray; 1.78 A; C/D=686-698.
DR PDB; 2B23; X-ray; 2.10 A; C/D=686-698.
DR PDB; 2FAI; X-ray; 2.10 A; C/D=686-698.
DR PDB; 2G44; X-ray; 2.65 A; C/D=686-698.
DR PDB; 2G5O; X-ray; 2.30 A; C/D=686-698.
DR PDB; 2LDC; NMR; -; A=687-697.
DR PDB; 2P15; X-ray; 1.94 A; C/D=686-698.
DR PDB; 2P1T; X-ray; 1.80 A; B=686-698.
DR PDB; 2P1U; X-ray; 2.20 A; B=686-698.
DR PDB; 2P1V; X-ray; 2.20 A; B=686-698.
DR PDB; 2Q7J; X-ray; 1.90 A; B=740-753.
DR PDB; 2Q7L; X-ray; 1.92 A; B=740-753.
DR PDB; 2YJD; X-ray; 1.93 A; C/D=687-697.
DR PDB; 2ZXZ; X-ray; 3.00 A; B=686-698.
DR PDB; 2ZY0; X-ray; 2.90 A; B/D=686-698.
DR PDB; 3A9E; X-ray; 2.75 A; I=686-698.
DR PDB; 3CLD; X-ray; 2.84 A; C/H=740-751.
DR PDB; 3DZU; X-ray; 3.20 A; E/G=685-697.
DR PDB; 3DZY; X-ray; 3.10 A; E/G=685-697.
DR PDB; 3E00; X-ray; 3.10 A; E/G=685-697.
DR PDB; 3E7C; X-ray; 2.15 A; D/H=741-751.
DR PDB; 3E94; X-ray; 1.90 A; B=686-698.
DR PDB; 3ERD; X-ray; 2.03 A; C/D=686-698.
DR PDB; 3FUG; X-ray; 2.00 A; B=686-698.
DR PDB; 3GN8; X-ray; 2.50 A; C/E=734-754.
DR PDB; 3K22; X-ray; 2.10 A; D/H=740-751.
DR PDB; 3K23; X-ray; 3.00 A; D/E/F=740-751.
DR PDB; 3KWY; X-ray; 2.30 A; B=686-698.
DR PDB; 3KYT; X-ray; 2.35 A; C=686-697.
DR PDB; 3L0E; X-ray; 2.30 A; B=740-751.
DR PDB; 3L0J; X-ray; 2.40 A; C=688-697.
DR PDB; 3L0L; X-ray; 1.74 A; C/E=685-697.
DR PDB; 3O1D; X-ray; 2.40 A; B=686-698.
DR PDB; 3O1E; X-ray; 2.50 A; B=686-698.
DR PDB; 3OAP; X-ray; 2.05 A; B=686-696.
DR PDB; 3OZJ; X-ray; 2.10 A; B/D=686-696.
DR PDB; 3PCU; X-ray; 2.00 A; B=687-696.
DR PDB; 3PLZ; X-ray; 1.75 A; C/D=740-753.
DR PDB; 3Q95; X-ray; 2.05 A; C/D=686-698.
DR PDB; 3R5M; X-ray; 2.80 A; B/D=687-696.
DR PDB; 3UP0; X-ray; 1.60 A; P/Q=740-753.
DR PDB; 3UP3; X-ray; 1.25 A; P=741-754.
DR PDB; 4CSJ; X-ray; 2.30 A; B=741-753.
DR PDB; 4DOS; X-ray; 2.00 A; B/C=740-753.
DR PDB; 4E2J; X-ray; 2.50 A; C/E=741-752.
DR PDB; 4FHH; X-ray; 2.33 A; B=686-698.
DR PDB; 4FHI; X-ray; 2.40 A; B=686-698.
DR PDB; 4IA1; X-ray; 2.44 A; B=686-698.
DR PDB; 4IA2; X-ray; 2.95 A; B=686-698.
DR PDB; 4IA3; X-ray; 2.70 A; B=686-698.
DR PDB; 4IA7; X-ray; 2.70 A; B=686-698.
DR PDB; 4IQR; X-ray; 2.90 A; I/J/K/L=685-697.
DR PDB; 4IU7; X-ray; 2.29 A; C/D=687-696.
DR PDB; 4IUI; X-ray; 2.30 A; C/D=687-696.
DR PDB; 4IV2; X-ray; 2.14 A; C/D=687-696.
DR PDB; 4IV4; X-ray; 2.30 A; C/D=687-696.
DR PDB; 4IVW; X-ray; 2.06 A; C/D=687-696.
DR PDB; 4IVY; X-ray; 1.95 A; C/D=687-696.
DR PDB; 4IW6; X-ray; 1.98 A; C/D=687-696.
DR PDB; 4IW8; X-ray; 2.04 A; C/D=687-696.
DR PDB; 4IWC; X-ray; 2.24 A; C/D=687-696.
DR PDB; 4IWF; X-ray; 1.93 A; C/D=687-696.
DR PDB; 4K4J; X-ray; 2.00 A; B=686-698.
DR PDB; 4K6I; X-ray; 2.10 A; B=686-698.
DR PDB; 4M8E; X-ray; 2.40 A; B=686-696.
DR PDB; 4M8H; X-ray; 2.20 A; B=686-696.
DR PDB; 4NIE; X-ray; 2.01 A; C/D=686-697.
DR PDB; 4NQA; X-ray; 3.10 A; C/D/J/K=686-698.
DR PDB; 4OC7; X-ray; 2.50 A; B=686-698.
DR PDB; 4P6W; X-ray; 1.95 A; B=741-752.
DR PDB; 4P6X; X-ray; 2.50 A; B/D/F/H/J/L=740-753.
DR PDB; 4PLD; X-ray; 1.75 A; B=740-753.
DR PDB; 4PLE; X-ray; 1.75 A; B/D/F/H=740-753.
DR PDB; 4POH; X-ray; 2.30 A; B=686-698.
DR PDB; 4POJ; X-ray; 2.00 A; B=686-698.
DR PDB; 4PP3; X-ray; 2.00 A; B=686-698.
DR PDB; 4PP5; X-ray; 2.00 A; B=686-698.
DR PDB; 4PP6; X-ray; 2.20 A; C/D=688-696.
DR PDB; 4PPP; X-ray; 2.69 A; C/D=688-696.
DR PDB; 4PPS; X-ray; 1.93 A; C/D=687-698.
DR PDB; 4PXM; X-ray; 1.90 A; C/D=686-698.
DR PDB; 4Q0A; X-ray; 1.90 A; D=687-695.
DR PDB; 4Q13; X-ray; 2.24 A; C/D=686-698.
DR PDB; 4QE6; X-ray; 1.65 A; B=740-752.
DR PDB; 4QE8; X-ray; 2.62 A; C/D=740-752.
DR PDB; 4RFW; X-ray; 2.40 A; G=686-698.
DR PDB; 4RMC; X-ray; 2.70 A; B=686-698.
DR PDB; 4RMD; X-ray; 1.90 A; B=686-698.
DR PDB; 4RME; X-ray; 2.30 A; B=686-698.
DR PDB; 4RUO; X-ray; 2.81 A; B=686-698.
DR PDB; 4UDC; X-ray; 2.50 A; B=740-753.
DR PDB; 4UDD; X-ray; 1.80 A; B=740-753.
DR PDB; 4WG0; X-ray; 1.82 A; A/B/C/D/E/F/G/H/I/J/K/L/M=742-752.
DR PDB; 4ZN7; X-ray; 1.93 A; C/D=686-698.
DR PDB; 4ZN9; X-ray; 2.21 A; C/D=686-698.
DR PDB; 4ZNH; X-ray; 1.93 A; C/D=686-698.
DR PDB; 4ZNS; X-ray; 1.86 A; C/D=686-698.
DR PDB; 4ZNT; X-ray; 1.90 A; C/D=686-698.
DR PDB; 4ZNU; X-ray; 2.40 A; C/D=686-698.
DR PDB; 4ZNV; X-ray; 1.77 A; C/D=686-698.
DR PDB; 4ZNW; X-ray; 2.31 A; C/D=686-698.
DR PDB; 4ZO1; X-ray; 3.22 A; A=686-694.
DR PDB; 4ZSH; X-ray; 1.80 A; B=686-698.
DR PDB; 5APH; X-ray; 1.54 A; C=686-697.
DR PDB; 5APJ; X-ray; 2.08 A; C=686-697.
DR PDB; 5DI7; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DID; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DIE; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DIG; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DK9; X-ray; 2.28 A; C/D=686-699.
DR PDB; 5DKB; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5DKE; X-ray; 2.60 A; C/D=686-699.
DR PDB; 5DKG; X-ray; 2.15 A; C/D=686-699.
DR PDB; 5DKS; X-ray; 2.60 A; C/D=686-699.
DR PDB; 5DL4; X-ray; 2.10 A; C/D=686-699.
DR PDB; 5DLR; X-ray; 2.26 A; C/D=686-699.
DR PDB; 5DMC; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5DMF; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5DP0; X-ray; 2.38 A; C/D=686-699.
DR PDB; 5DRJ; X-ray; 2.07 A; C/D=686-699.
DR PDB; 5DRM; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DTV; X-ray; 2.29 A; C/D=686-699.
DR PDB; 5DU5; X-ray; 2.19 A; C/D=686-699.
DR PDB; 5DUE; X-ray; 2.09 A; C/D=686-699.
DR PDB; 5DUG; X-ray; 2.25 A; C/D=686-699.
DR PDB; 5DUH; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DVS; X-ray; 2.28 A; C/D=686-699.
DR PDB; 5DVV; X-ray; 2.50 A; C/D=686-699.
DR PDB; 5DWE; X-ray; 1.92 A; C/D=686-699.
DR PDB; 5DWG; X-ray; 2.30 A; C/D=686-699.
DR PDB; 5DWI; X-ray; 2.43 A; C/D=686-699.
DR PDB; 5DWJ; X-ray; 2.00 A; C/D=686-699.
DR PDB; 5DX3; X-ray; 2.09 A; C/D=687-697.
DR PDB; 5DXB; X-ray; 2.08 A; D/E=687-697.
DR PDB; 5DXE; X-ray; 1.50 A; C/D=687-697.
DR PDB; 5DXG; X-ray; 1.86 A; C/D=687-697.
DR PDB; 5DXK; X-ray; 2.23 A; C/D=686-699.
DR PDB; 5DXM; X-ray; 2.37 A; C/D=686-699.
DR PDB; 5DXP; X-ray; 2.20 A; C/D=686-699.
DR PDB; 5DXQ; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5DXR; X-ray; 2.28 A; C/D=686-699.
DR PDB; 5DY8; X-ray; 2.03 A; C/D=686-699.
DR PDB; 5DYB; X-ray; 2.27 A; C/D=686-699.
DR PDB; 5DYD; X-ray; 2.48 A; C/D=686-699.
DR PDB; 5DZ0; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5DZ1; X-ray; 2.20 A; C/D=686-699.
DR PDB; 5DZ3; X-ray; 2.15 A; C/D=686-699.
DR PDB; 5DZH; X-ray; 2.11 A; C/D=686-699.
DR PDB; 5DZI; X-ray; 1.90 A; C/D=686-699.
DR PDB; 5E0W; X-ray; 2.00 A; C/D=686-699.
DR PDB; 5E0X; X-ray; 2.01 A; C/D=686-699.
DR PDB; 5E14; X-ray; 2.22 A; C/D=686-699.
DR PDB; 5E15; X-ray; 2.10 A; C/D=686-699.
DR PDB; 5E19; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5E1C; X-ray; 1.98 A; C/D=686-699.
DR PDB; 5EC9; X-ray; 2.30 A; B=686-696.
DR PDB; 5EGV; X-ray; 2.86 A; C/D=686-699.
DR PDB; 5EHJ; X-ray; 2.50 A; C/D=686-699.
DR PDB; 5EI1; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5EIT; X-ray; 2.68 A; C/D=686-699.
DR PDB; 5G3J; X-ray; 2.40 A; B=740-753.
DR PDB; 5G42; X-ray; 1.72 A; C=688-697.
DR PDB; 5G43; X-ray; 2.58 A; C=686-697.
DR PDB; 5G44; X-ray; 1.84 A; C=686-697.
DR PDB; 5G45; X-ray; 2.07 A; C=688-697.
DR PDB; 5G46; X-ray; 1.76 A; C=688-697.
DR PDB; 5G5W; X-ray; 2.20 A; B=740-753.
DR PDB; 5H1E; X-ray; 2.60 A; C=740-752.
DR PDB; 5HYR; X-ray; 2.27 A; F/G=687-697.
DR PDB; 5I4V; X-ray; 2.61 A; A/B/E/F=687-699.
DR PDB; 5IAW; X-ray; 2.58 A; C/D=742-751.
DR PDB; 5ICK; X-ray; 2.47 A; C/D=742-752.
DR PDB; 5KCC; X-ray; 2.39 A; C/D=686-699.
DR PDB; 5KCD; X-ray; 1.82 A; C/D=686-699.
DR PDB; 5KCE; X-ray; 1.85 A; C/D=686-698, C/D=687-696.
DR PDB; 5KCF; X-ray; 2.07 A; C/D=686-699.
DR PDB; 5KCT; X-ray; 1.60 A; C/D=686-699.
DR PDB; 5KCU; X-ray; 2.03 A; C/D=686-699.
DR PDB; 5KCW; X-ray; 1.91 A; C/D=686-699.
DR PDB; 5KD9; X-ray; 1.78 A; C/D=686-699.
DR PDB; 5KR9; X-ray; 2.25 A; C/D=686-699.
DR PDB; 5KRA; X-ray; 2.40 A; C/D/G/H=686-699.
DR PDB; 5KRC; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5KRF; X-ray; 2.19 A; C/D=686-699.
DR PDB; 5KRH; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5KRI; X-ray; 2.25 A; C/D=686-699.
DR PDB; 5KRJ; X-ray; 2.70 A; C/D=686-699.
DR PDB; 5KRK; X-ray; 2.39 A; C/D=686-699.
DR PDB; 5KRL; X-ray; 2.40 A; C/D=686-699.
DR PDB; 5KRM; X-ray; 2.24 A; C/D=686-699.
DR PDB; 5KRO; X-ray; 2.10 A; C/D=686-699.
DR PDB; 5L11; X-ray; 1.85 A; C=740-753.
DR PDB; 5LGA; X-ray; 2.50 A; B=686-698.
DR PDB; 5LYQ; X-ray; 2.17 A; B=686-698.
DR PDB; 5MK4; X-ray; 2.00 A; B/D=686-696.
DR PDB; 5NFP; X-ray; 2.10 A; B=740-753.
DR PDB; 5NFT; X-ray; 2.30 A; B=740-753.
DR PDB; 5NI5; X-ray; 2.30 A; C=684-698.
DR PDB; 5NI7; X-ray; 2.45 A; C=684-698.
DR PDB; 5NI8; X-ray; 1.94 A; C=684-698.
DR PDB; 5NIB; X-ray; 1.82 A; C=684-698.
DR PDB; 5Q17; X-ray; 2.10 A; B=741-752.
DR PDB; 5SYZ; X-ray; 1.93 A; C=740-754.
DR PDB; 5T1Z; X-ray; 2.10 A; C/D=686-698.
DR PDB; 5TLD; X-ray; 2.38 A; C/D=686-698.
DR PDB; 5TLF; X-ray; 2.20 A; C/D=686-698.
DR PDB; 5TLG; X-ray; 2.23 A; C/D=686-698.
DR PDB; 5TLL; X-ray; 2.42 A; C/D=686-698.
DR PDB; 5TLM; X-ray; 2.50 A; C/D=686-698.
DR PDB; 5TLO; X-ray; 2.28 A; C/D=686-698.
DR PDB; 5TLP; X-ray; 2.08 A; C/D=686-698.
DR PDB; 5TLT; X-ray; 1.90 A; C/D=686-698.
DR PDB; 5TLU; X-ray; 2.22 A; C/D=686-698.
DR PDB; 5TLV; X-ray; 2.32 A; C/D=686-698.
DR PDB; 5TLX; X-ray; 2.10 A; C/D=686-698.
DR PDB; 5TLY; X-ray; 2.14 A; C/D=686-698.
DR PDB; 5TM1; X-ray; 2.23 A; C/D=686-698.
DR PDB; 5TM2; X-ray; 2.60 A; C/D=686-698.
DR PDB; 5TM3; X-ray; 2.19 A; C/D=686-698.
DR PDB; 5TM4; X-ray; 2.25 A; C/D=686-698.
DR PDB; 5TM5; X-ray; 2.24 A; C/D=686-698.
DR PDB; 5TM6; X-ray; 2.54 A; C/D=686-698.
DR PDB; 5TM7; X-ray; 2.40 A; C/D=686-698.
DR PDB; 5TM8; X-ray; 1.99 A; C/D=686-698.
DR PDB; 5TM9; X-ray; 2.50 A; C/D=686-698.
DR PDB; 5TML; X-ray; 2.25 A; C/D=686-698.
DR PDB; 5TMM; X-ray; 2.20 A; C/D=686-698.
DR PDB; 5TMO; X-ray; 2.17 A; C/D=686-698.
DR PDB; 5TMQ; X-ray; 2.24 A; C/D=686-698.
DR PDB; 5TMR; X-ray; 2.30 A; C/D=686-698.
DR PDB; 5TMS; X-ray; 2.24 A; C/D=686-698.
DR PDB; 5TMT; X-ray; 2.05 A; C/D=686-698.
DR PDB; 5TMU; X-ray; 2.43 A; C/D=686-698.
DR PDB; 5TMV; X-ray; 2.38 A; C/D=686-698.
DR PDB; 5TMW; X-ray; 2.29 A; C/D=686-698.
DR PDB; 5TMZ; X-ray; 2.21 A; C/D=686-698.
DR PDB; 5TN1; X-ray; 2.06 A; C/D=686-698.
DR PDB; 5TN3; X-ray; 2.54 A; C/D=686-698.
DR PDB; 5TN4; X-ray; 1.86 A; C/D=686-698.
DR PDB; 5TN5; X-ray; 1.89 A; C/D=686-698.
DR PDB; 5TN6; X-ray; 2.09 A; C/D=686-698.
DR PDB; 5TN7; X-ray; 2.24 A; C/D=686-698.
DR PDB; 5TN8; X-ray; 2.65 A; C/D=686-698.
DR PDB; 5U2D; X-ray; 1.86 A; C/D=686-698.
DR PDB; 5UAN; X-ray; 3.51 A; C/D=687-696.
DR PDB; 5VB3; X-ray; 1.95 A; A=685-697.
DR PDB; 5VB5; X-ray; 2.23 A; A=685-697.
DR PDB; 5VB6; X-ray; 2.04 A; A=685-697.
DR PDB; 5VB7; X-ray; 2.33 A; A=685-697.
DR PDB; 5VQK; X-ray; 3.10 A; A=685-697.
DR PDB; 5VQL; X-ray; 2.70 A; A=685-697.
DR PDB; 5WGQ; X-ray; 2.30 A; E/F=687-697.
DR PDB; 5WZX; X-ray; 2.95 A; C/D=741-752.
DR PDB; 5XPL; X-ray; 2.05 A; C=740-752.
DR PDB; 5Y1J; X-ray; 2.00 A; U=742-751.
DR PDB; 5Y49; X-ray; 2.40 A; D/E=741-751.
DR PDB; 5YP5; X-ray; 2.65 A; B=688-695.
DR PDB; 5YXB; X-ray; 2.95 A; B=741-751.
DR PDB; 5YXD; X-ray; 2.98 A; B=741-751.
DR PDB; 5YXJ; X-ray; 2.62 A; C/D=741-751.
DR PDB; 5YXL; X-ray; 2.24 A; B/D=743-750.
DR PDB; 5Z12; X-ray; 2.75 A; F/I=687-695, H/J=687-692.
DR PDB; 6CZN; X-ray; 2.50 A; C/D=686-698.
DR PDB; 6D0F; X-ray; 2.50 A; C/D=687-696.
DR PDB; 6EL6; X-ray; 2.40 A; B=740-753.
DR PDB; 6EL7; X-ray; 2.18 A; B=740-753.
DR PDB; 6EL9; X-ray; 2.19 A; B=740-753.
DR PDB; 6ESN; X-ray; 1.84 A; C=686-697.
DR PDB; 6KKB; X-ray; 1.70 A; D=741-751.
DR PDB; 6KKE; X-ray; 2.58 A; C=741-751.
DR PDB; 6KNU; X-ray; 2.70 A; C=741-751.
DR PDB; 6KNV; X-ray; 2.80 A; C=741-751.
DR PDB; 6KNW; X-ray; 2.67 A; C=741-751.
DR PDB; 6LB4; X-ray; 1.50 A; B=686-698.
DR PDB; 6LB5; X-ray; 2.40 A; B/D=686-698.
DR PDB; 6LB6; X-ray; 2.40 A; B=686-698.
DR PDB; 6LIT; X-ray; 2.00 A; D/E=686-696.
DR PDB; 6OQX; X-ray; 2.00 A; C=740-754.
DR PDB; 6OQY; X-ray; 2.23 A; C=740-754.
DR PDB; 6OR1; X-ray; 2.17 A; C=740-754.
DR PDB; 6R7A; X-ray; 2.13 A; C=684-698.
DR PDB; 6R7J; X-ray; 1.84 A; C=684-698.
DR PDB; 6R7K; X-ray; 1.54 A; C=684-698.
DR PDB; 6SJM; X-ray; 2.52 A; B=686-699.
DR PDB; 6STI; X-ray; 1.89 A; B=686-698.
DR PDB; 6VC2; X-ray; 1.70 A; C=740-754.
DR PDB; 6VIF; X-ray; 2.26 A; B=740-753.
DR PDB; 7A77; X-ray; 1.50 A; B=686-699.
DR PDB; 7A78; X-ray; 1.72 A; B=686-699.
DR PDB; 7A79; X-ray; 2.05 A; C/D=686-699.
DR PDB; 7APO; X-ray; 2.40 A; C/D=686-713.
DR PDB; 7B88; X-ray; 2.38 A; B=686-699.
DR PDB; 7B9O; X-ray; 2.05 A; C=686-699.
DR PDB; 7BK4; X-ray; 2.80 A; B/D=686-713.
DR PDB; 7D42; X-ray; 2.70 A; B=740-753.
DR PDB; 7JHD; X-ray; 2.40 A; C/D=686-698.
DR PDB; 7JYD; X-ray; 2.30 A; C=740-751.
DR PDB; 7JYE; X-ray; 2.55 A; C=740-751.
DR PDB; 7KCO; X-ray; 1.86 A; C/D=685-697.
DR PDB; 7NEL; X-ray; 1.45 A; C/D=686-699.
DR PDB; 7NFB; X-ray; 1.33 A; C/D=686-699.
DR PDB; 7NKE; X-ray; 2.35 A; B/D=686-698.
DR PDB; 7OFI; X-ray; 1.95 A; C=684-698.
DR PDB; 7OFK; X-ray; 1.61 A; C=684-698.
DR PDB; 7VUE; X-ray; 2.60 A; B=740-753.
DR PDBsum; 1GWQ; -.
DR PDBsum; 1GWR; -.
DR PDBsum; 1M2Z; -.
DR PDBsum; 1MV9; -.
DR PDBsum; 1MVC; -.
DR PDBsum; 1MZN; -.
DR PDBsum; 1P93; -.
DR PDBsum; 1T63; -.
DR PDBsum; 1T65; -.
DR PDBsum; 1UHL; -.
DR PDBsum; 1YOK; -.
DR PDBsum; 1ZDT; -.
DR PDBsum; 1ZDU; -.
DR PDBsum; 1ZKY; -.
DR PDBsum; 2AO6; -.
DR PDBsum; 2B1V; -.
DR PDBsum; 2B1Z; -.
DR PDBsum; 2B23; -.
DR PDBsum; 2FAI; -.
DR PDBsum; 2G44; -.
DR PDBsum; 2G5O; -.
DR PDBsum; 2LDC; -.
DR PDBsum; 2P15; -.
DR PDBsum; 2P1T; -.
DR PDBsum; 2P1U; -.
DR PDBsum; 2P1V; -.
DR PDBsum; 2Q7J; -.
DR PDBsum; 2Q7L; -.
DR PDBsum; 2YJD; -.
DR PDBsum; 2ZXZ; -.
DR PDBsum; 2ZY0; -.
DR PDBsum; 3A9E; -.
DR PDBsum; 3CLD; -.
DR PDBsum; 3DZU; -.
DR PDBsum; 3DZY; -.
DR PDBsum; 3E00; -.
DR PDBsum; 3E7C; -.
DR PDBsum; 3E94; -.
DR PDBsum; 3ERD; -.
DR PDBsum; 3FUG; -.
DR PDBsum; 3GN8; -.
DR PDBsum; 3K22; -.
DR PDBsum; 3K23; -.
DR PDBsum; 3KWY; -.
DR PDBsum; 3KYT; -.
DR PDBsum; 3L0E; -.
DR PDBsum; 3L0J; -.
DR PDBsum; 3L0L; -.
DR PDBsum; 3O1D; -.
DR PDBsum; 3O1E; -.
DR PDBsum; 3OAP; -.
DR PDBsum; 3OZJ; -.
DR PDBsum; 3PCU; -.
DR PDBsum; 3PLZ; -.
DR PDBsum; 3Q95; -.
DR PDBsum; 3R5M; -.
DR PDBsum; 3UP0; -.
DR PDBsum; 3UP3; -.
DR PDBsum; 4CSJ; -.
DR PDBsum; 4DOS; -.
DR PDBsum; 4E2J; -.
DR PDBsum; 4FHH; -.
DR PDBsum; 4FHI; -.
DR PDBsum; 4IA1; -.
DR PDBsum; 4IA2; -.
DR PDBsum; 4IA3; -.
DR PDBsum; 4IA7; -.
DR PDBsum; 4IQR; -.
DR PDBsum; 4IU7; -.
DR PDBsum; 4IUI; -.
DR PDBsum; 4IV2; -.
DR PDBsum; 4IV4; -.
DR PDBsum; 4IVW; -.
DR PDBsum; 4IVY; -.
DR PDBsum; 4IW6; -.
DR PDBsum; 4IW8; -.
DR PDBsum; 4IWC; -.
DR PDBsum; 4IWF; -.
DR PDBsum; 4K4J; -.
DR PDBsum; 4K6I; -.
DR PDBsum; 4M8E; -.
DR PDBsum; 4M8H; -.
DR PDBsum; 4NIE; -.
DR PDBsum; 4NQA; -.
DR PDBsum; 4OC7; -.
DR PDBsum; 4P6W; -.
DR PDBsum; 4P6X; -.
DR PDBsum; 4PLD; -.
DR PDBsum; 4PLE; -.
DR PDBsum; 4POH; -.
DR PDBsum; 4POJ; -.
DR PDBsum; 4PP3; -.
DR PDBsum; 4PP5; -.
DR PDBsum; 4PP6; -.
DR PDBsum; 4PPP; -.
DR PDBsum; 4PPS; -.
DR PDBsum; 4PXM; -.
DR PDBsum; 4Q0A; -.
DR PDBsum; 4Q13; -.
DR PDBsum; 4QE6; -.
DR PDBsum; 4QE8; -.
DR PDBsum; 4RFW; -.
DR PDBsum; 4RMC; -.
DR PDBsum; 4RMD; -.
DR PDBsum; 4RME; -.
DR PDBsum; 4RUO; -.
DR PDBsum; 4UDC; -.
DR PDBsum; 4UDD; -.
DR PDBsum; 4WG0; -.
DR PDBsum; 4ZN7; -.
DR PDBsum; 4ZN9; -.
DR PDBsum; 4ZNH; -.
DR PDBsum; 4ZNS; -.
DR PDBsum; 4ZNT; -.
DR PDBsum; 4ZNU; -.
DR PDBsum; 4ZNV; -.
DR PDBsum; 4ZNW; -.
DR PDBsum; 4ZO1; -.
DR PDBsum; 4ZSH; -.
DR PDBsum; 5APH; -.
DR PDBsum; 5APJ; -.
DR PDBsum; 5DI7; -.
DR PDBsum; 5DID; -.
DR PDBsum; 5DIE; -.
DR PDBsum; 5DIG; -.
DR PDBsum; 5DK9; -.
DR PDBsum; 5DKB; -.
DR PDBsum; 5DKE; -.
DR PDBsum; 5DKG; -.
DR PDBsum; 5DKS; -.
DR PDBsum; 5DL4; -.
DR PDBsum; 5DLR; -.
DR PDBsum; 5DMC; -.
DR PDBsum; 5DMF; -.
DR PDBsum; 5DP0; -.
DR PDBsum; 5DRJ; -.
DR PDBsum; 5DRM; -.
DR PDBsum; 5DTV; -.
DR PDBsum; 5DU5; -.
DR PDBsum; 5DUE; -.
DR PDBsum; 5DUG; -.
DR PDBsum; 5DUH; -.
DR PDBsum; 5DVS; -.
DR PDBsum; 5DVV; -.
DR PDBsum; 5DWE; -.
DR PDBsum; 5DWG; -.
DR PDBsum; 5DWI; -.
DR PDBsum; 5DWJ; -.
DR PDBsum; 5DX3; -.
DR PDBsum; 5DXB; -.
DR PDBsum; 5DXE; -.
DR PDBsum; 5DXG; -.
DR PDBsum; 5DXK; -.
DR PDBsum; 5DXM; -.
DR PDBsum; 5DXP; -.
DR PDBsum; 5DXQ; -.
DR PDBsum; 5DXR; -.
DR PDBsum; 5DY8; -.
DR PDBsum; 5DYB; -.
DR PDBsum; 5DYD; -.
DR PDBsum; 5DZ0; -.
DR PDBsum; 5DZ1; -.
DR PDBsum; 5DZ3; -.
DR PDBsum; 5DZH; -.
DR PDBsum; 5DZI; -.
DR PDBsum; 5E0W; -.
DR PDBsum; 5E0X; -.
DR PDBsum; 5E14; -.
DR PDBsum; 5E15; -.
DR PDBsum; 5E19; -.
DR PDBsum; 5E1C; -.
DR PDBsum; 5EC9; -.
DR PDBsum; 5EGV; -.
DR PDBsum; 5EHJ; -.
DR PDBsum; 5EI1; -.
DR PDBsum; 5EIT; -.
DR PDBsum; 5G3J; -.
DR PDBsum; 5G42; -.
DR PDBsum; 5G43; -.
DR PDBsum; 5G44; -.
DR PDBsum; 5G45; -.
DR PDBsum; 5G46; -.
DR PDBsum; 5G5W; -.
DR PDBsum; 5H1E; -.
DR PDBsum; 5HYR; -.
DR PDBsum; 5I4V; -.
DR PDBsum; 5IAW; -.
DR PDBsum; 5ICK; -.
DR PDBsum; 5KCC; -.
DR PDBsum; 5KCD; -.
DR PDBsum; 5KCE; -.
DR PDBsum; 5KCF; -.
DR PDBsum; 5KCT; -.
DR PDBsum; 5KCU; -.
DR PDBsum; 5KCW; -.
DR PDBsum; 5KD9; -.
DR PDBsum; 5KR9; -.
DR PDBsum; 5KRA; -.
DR PDBsum; 5KRC; -.
DR PDBsum; 5KRF; -.
DR PDBsum; 5KRH; -.
DR PDBsum; 5KRI; -.
DR PDBsum; 5KRJ; -.
DR PDBsum; 5KRK; -.
DR PDBsum; 5KRL; -.
DR PDBsum; 5KRM; -.
DR PDBsum; 5KRO; -.
DR PDBsum; 5L11; -.
DR PDBsum; 5LGA; -.
DR PDBsum; 5LYQ; -.
DR PDBsum; 5MK4; -.
DR PDBsum; 5NFP; -.
DR PDBsum; 5NFT; -.
DR PDBsum; 5NI5; -.
DR PDBsum; 5NI7; -.
DR PDBsum; 5NI8; -.
DR PDBsum; 5NIB; -.
DR PDBsum; 5Q17; -.
DR PDBsum; 5SYZ; -.
DR PDBsum; 5T1Z; -.
DR PDBsum; 5TLD; -.
DR PDBsum; 5TLF; -.
DR PDBsum; 5TLG; -.
DR PDBsum; 5TLL; -.
DR PDBsum; 5TLM; -.
DR PDBsum; 5TLO; -.
DR PDBsum; 5TLP; -.
DR PDBsum; 5TLT; -.
DR PDBsum; 5TLU; -.
DR PDBsum; 5TLV; -.
DR PDBsum; 5TLX; -.
DR PDBsum; 5TLY; -.
DR PDBsum; 5TM1; -.
DR PDBsum; 5TM2; -.
DR PDBsum; 5TM3; -.
DR PDBsum; 5TM4; -.
DR PDBsum; 5TM5; -.
DR PDBsum; 5TM6; -.
DR PDBsum; 5TM7; -.
DR PDBsum; 5TM8; -.
DR PDBsum; 5TM9; -.
DR PDBsum; 5TML; -.
DR PDBsum; 5TMM; -.
DR PDBsum; 5TMO; -.
DR PDBsum; 5TMQ; -.
DR PDBsum; 5TMR; -.
DR PDBsum; 5TMS; -.
DR PDBsum; 5TMT; -.
DR PDBsum; 5TMU; -.
DR PDBsum; 5TMV; -.
DR PDBsum; 5TMW; -.
DR PDBsum; 5TMZ; -.
DR PDBsum; 5TN1; -.
DR PDBsum; 5TN3; -.
DR PDBsum; 5TN4; -.
DR PDBsum; 5TN5; -.
DR PDBsum; 5TN6; -.
DR PDBsum; 5TN7; -.
DR PDBsum; 5TN8; -.
DR PDBsum; 5U2D; -.
DR PDBsum; 5UAN; -.
DR PDBsum; 5VB3; -.
DR PDBsum; 5VB5; -.
DR PDBsum; 5VB6; -.
DR PDBsum; 5VB7; -.
DR PDBsum; 5VQK; -.
DR PDBsum; 5VQL; -.
DR PDBsum; 5WGQ; -.
DR PDBsum; 5WZX; -.
DR PDBsum; 5XPL; -.
DR PDBsum; 5Y1J; -.
DR PDBsum; 5Y49; -.
DR PDBsum; 5YP5; -.
DR PDBsum; 5YXB; -.
DR PDBsum; 5YXD; -.
DR PDBsum; 5YXJ; -.
DR PDBsum; 5YXL; -.
DR PDBsum; 5Z12; -.
DR PDBsum; 6CZN; -.
DR PDBsum; 6D0F; -.
DR PDBsum; 6EL6; -.
DR PDBsum; 6EL7; -.
DR PDBsum; 6EL9; -.
DR PDBsum; 6ESN; -.
DR PDBsum; 6KKB; -.
DR PDBsum; 6KKE; -.
DR PDBsum; 6KNU; -.
DR PDBsum; 6KNV; -.
DR PDBsum; 6KNW; -.
DR PDBsum; 6LB4; -.
DR PDBsum; 6LB5; -.
DR PDBsum; 6LB6; -.
DR PDBsum; 6LIT; -.
DR PDBsum; 6OQX; -.
DR PDBsum; 6OQY; -.
DR PDBsum; 6OR1; -.
DR PDBsum; 6R7A; -.
DR PDBsum; 6R7J; -.
DR PDBsum; 6R7K; -.
DR PDBsum; 6SJM; -.
DR PDBsum; 6STI; -.
DR PDBsum; 6VC2; -.
DR PDBsum; 6VIF; -.
DR PDBsum; 7A77; -.
DR PDBsum; 7A78; -.
DR PDBsum; 7A79; -.
DR PDBsum; 7APO; -.
DR PDBsum; 7B88; -.
DR PDBsum; 7B9O; -.
DR PDBsum; 7BK4; -.
DR PDBsum; 7D42; -.
DR PDBsum; 7JHD; -.
DR PDBsum; 7JYD; -.
DR PDBsum; 7JYE; -.
DR PDBsum; 7KCO; -.
DR PDBsum; 7NEL; -.
DR PDBsum; 7NFB; -.
DR PDBsum; 7NKE; -.
DR PDBsum; 7OFI; -.
DR PDBsum; 7OFK; -.
DR PDBsum; 7VUE; -.
DR AlphaFoldDB; Q15596; -.
DR SASBDB; Q15596; -.
DR SMR; Q15596; -.
DR BioGRID; 115761; 112.
DR ComplexPortal; CPX-513; RXRalpha-NCOA2 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-5156; ERalpha-NCOA2 activated estrogen receptor complex.
DR ComplexPortal; CPX-666; RARalpha-NCOA2 activated retinoic acid receptor complex.
DR ComplexPortal; CPX-702; PPARgamma-NCOA2 activated nuclear receptor complex.
DR ComplexPortal; CPX-816; RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex.
DR CORUM; Q15596; -.
DR DIP; DIP-5997N; -.
DR ELM; Q15596; -.
DR IntAct; Q15596; 54.
DR MINT; Q15596; -.
DR STRING; 9606.ENSP00000399968; -.
DR BindingDB; Q15596; -.
DR DrugBank; DB08175; (2E,4E)-11-METHOXY-3,7,11-TRIMETHYLDODECA-2,4-DIENOIC ACID.
DR DrugBank; DB07678; (9ALPHA,13BETA,17BETA)-2-[(1Z)-BUT-1-EN-1-YL]ESTRA-1,3,5(10)-TRIENE-3,17-DIOL.
DR DrugBank; DB07707; (9BETA,11ALPHA,13ALPHA,14BETA,17ALPHA)-11-(METHOXYMETHYL)ESTRA-1(10),2,4-TRIENE-3,17-DIOL.
DR DrugBank; DB06871; 17-METHYL-17-ALPHA-DIHYDROEQUILENIN.
DR DrugBank; DB08773; 2-(4-hydroxyphenyl)benzo[b]thiophen-6-ol.
DR DrugBank; DB08402; 2-[(2,4-DICHLOROBENZOYL)AMINO]-5-(PYRIMIDIN-2-YLOXY)BENZOIC ACID.
DR DrugBank; DB08398; 2-Amino-1-methyl-6-phenylimidazo(4,5-b)pyridine.
DR DrugBank; DB07863; 2-chloro-5-nitro-N-phenylbenzamide.
DR DrugBank; DB07708; 3-CHLORO-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DR DrugBank; DB07712; 3-ETHYL-2-(4-HYDROXYPHENYL)-2H-INDAZOL-5-OL.
DR DrugBank; DB06898; 4-(2-amino-1-methyl-1H-imidazo[4,5-b]pyridin-6-yl)phenol.
DR DrugBank; DB08048; 4-(6-HYDROXY-1H-INDAZOL-3-YL)BENZENE-1,3-DIOL.
DR DrugBank; DB08595; 4-[(1S,2R,5S)-4,4,8-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07195; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-6,8,9-TRIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07086; 4-[(1S,2S,5S)-5-(HYDROXYMETHYL)-8-METHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB07087; 4-[(1S,2S,5S,9R)-5-(HYDROXYMETHYL)-8,9-DIMETHYL-3-OXABICYCLO[3.3.1]NON-7-EN-2-YL]PHENOL.
DR DrugBank; DB08047; 4-[1-allyl-7-(trifluoromethyl)-1H-indazol-3-yl]benzene-1,3-diol.
DR DrugBank; DB08320; DIETHYL (1R,2S,3R,4S)-5,6-BIS(4-HYDROXYPHENYL)-7-OXABICYCLO[2.2.1]HEPT-5-ENE-2,3-DICARBOXYLATE.
DR DrugBank; DB00255; Diethylstilbestrol.
DR DrugBank; DB07932; dimethyl (1R,4S)-5,6-bis(4-hydroxyphenyl)-7-oxabicyclo[2.2.1]hepta-2,5-diene-2,3-dicarboxylate.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB02998; Metribolone.
DR DrugBank; DB07080; TO-901317.
DR DrugBank; DB08601; Tributyltin.
DR GlyGen; Q15596; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15596; -.
DR PhosphoSitePlus; Q15596; -.
DR BioMuta; NCOA2; -.
DR DMDM; 13626594; -.
DR EPD; Q15596; -.
DR jPOST; Q15596; -.
DR MassIVE; Q15596; -.
DR MaxQB; Q15596; -.
DR PaxDb; Q15596; -.
DR PeptideAtlas; Q15596; -.
DR PRIDE; Q15596; -.
DR ProteomicsDB; 60649; -.
DR Antibodypedia; 6252; 322 antibodies from 32 providers.
DR DNASU; 10499; -.
DR Ensembl; ENST00000452400.7; ENSP00000399968.2; ENSG00000140396.13.
DR GeneID; 10499; -.
DR KEGG; hsa:10499; -.
DR MANE-Select; ENST00000452400.7; ENSP00000399968.2; NM_006540.4; NP_006531.1.
DR UCSC; uc003xyn.2; human.
DR CTD; 10499; -.
DR DisGeNET; 10499; -.
DR GeneCards; NCOA2; -.
DR HGNC; HGNC:7669; NCOA2.
DR HPA; ENSG00000140396; Low tissue specificity.
DR MIM; 601993; gene.
DR neXtProt; NX_Q15596; -.
DR OpenTargets; ENSG00000140396; -.
DR PharmGKB; PA31471; -.
DR VEuPathDB; HostDB:ENSG00000140396; -.
DR eggNOG; KOG3561; Eukaryota.
DR GeneTree; ENSGT00950000183021; -.
DR HOGENOM; CLU_001988_0_0_1; -.
DR InParanoid; Q15596; -.
DR OMA; DSNMPPV; -.
DR OrthoDB; 59971at2759; -.
DR PhylomeDB; Q15596; -.
DR TreeFam; TF332652; -.
DR PathwayCommons; Q15596; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-HSA-193807; Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-211976; Endogenous sterols.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q15596; -.
DR SIGNOR; Q15596; -.
DR BioGRID-ORCS; 10499; 25 hits in 1096 CRISPR screens.
DR ChiTaRS; NCOA2; human.
DR EvolutionaryTrace; Q15596; -.
DR GeneWiki; Nuclear_receptor_coactivator_2; -.
DR GenomeRNAi; 10499; -.
DR Pharos; Q15596; Tbio.
DR PRO; PR:Q15596; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15596; protein.
DR Bgee; ENSG00000140396; Expressed in corpus epididymis and 210 other tissues.
DR ExpressionAtlas; Q15596; baseline and differential.
DR Genevisible; Q15596; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:BHF-UCL.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IBA:GO_Central.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IC:ComplexPortal.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR CDD; cd00130; PAS; 1.
DR DisProt; DP01880; -.
DR Gene3D; 4.10.280.10; -; 1.
DR Gene3D; 6.10.140.20; -; 1.
DR IDEAL; IID00082; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR010011; NCO_DUF1518.
DR InterPro; IPR028822; NCOA2.
DR InterPro; IPR032565; NCOA2/3_DUF4927.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR InterPro; IPR037077; Nuc_rcpt_coact_Ncoa_int_sf.
DR InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR014935; SRC/p160_LXXLL.
DR PANTHER; PTHR10684; PTHR10684; 1.
DR PANTHER; PTHR10684:SF2; PTHR10684:SF2; 1.
DR Pfam; PF07469; DUF1518; 1.
DR Pfam; PF16279; DUF4927; 1.
DR Pfam; PF08815; Nuc_rec_co-act; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08832; SRC-1; 1.
DR PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR SMART; SM01151; DUF1518; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF69125; SSF69125; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Biological rhythms; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1464
FT /note="Nuclear receptor coactivator 2"
FT /id="PRO_0000094402"
FT DOMAIN 26..83
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 119..183
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..743
FT /note="CASP8AP2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT REGION 709..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..1121
FT /note="Interaction with ARNTL"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT REGION 973..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 641..645
FT /note="LXXLL motif 1"
FT MOTIF 690..694
FT /note="LXXLL motif 2"
FT MOTIF 745..749
FT /note="LXXLL motif 3"
FT MOTIF 878..882
FT /note="LXXLL motif 4"
FT MOTIF 1079..1087
FT /note="LLXXLXXXL motif"
FT COMPBIAS 11..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 869..870
FT /note="Breakpoint for translocation to form KAT6A-NCOA2"
FT /evidence="ECO:0000269|PubMed:12676584,
FT ECO:0000269|PubMed:15657427, ECO:0000269|PubMed:9558366"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 636
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 785
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 864
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 874
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 1173
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1177
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1190
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1196
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1203
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1221
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1240
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61026"
FT MOD_RES 1261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1266
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 648
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 705
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 785
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 1282
FT /note="M -> I (in dbSNP:rs2228591)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024546"
FT MUTAGEN 644..645
FT /note="LL->AA: By itself, does not affect nuclear receptor
FT binding or transcriptional coactivation. Abrogates ligand-
FT induced nuclear receptor binding and transactivation; when
FT associated with 693-A-A-694 and 748-A-A-749."
FT /evidence="ECO:0000269|PubMed:9430642"
FT MUTAGEN 693..694
FT /note="LL->AA: By itself, does not affect nuclear receptor
FT binding or transcriptional coactivation. Abrogates ligand-
FT induced nuclear receptor binding and transactivation; when
FT associated with 644-A-A-665 and 748-A-A-749."
FT /evidence="ECO:0000269|PubMed:9430642"
FT MUTAGEN 748..749
FT /note="LL->AA: By itself, does not affect nuclear receptor
FT binding or transcriptional coactivation. Abrogates ligand-
FT induced nuclear receptor binding and transactivation; when
FT associated with 644-A-A-665 and 693-A-A-694."
FT /evidence="ECO:0000269|PubMed:9430642"
FT MUTAGEN 1079..1083
FT /note="LLDQL->AADQA: Reduces transcriptional coactivation
FT and disrupts interaction with CREBBP/CBP."
FT /evidence="ECO:0000269|PubMed:9430642"
FT MUTAGEN 1081..1082
FT /note="DQ->AA: Has little effect on transcriptional
FT coactivation."
FT /evidence="ECO:0000269|PubMed:9430642"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:5VB7"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:7NFB"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:1M2Z"
FT HELIX 743..750
FT /evidence="ECO:0007829|PDB:3UP3"
SQ SEQUENCE 1464 AA; 159157 MW; 0A61AA5D1878304B CRC64;
MSGMGENTSD PSRAETRKRK ECPDQLGPSP KRNTEKRNRE QENKYIEELA ELIFANFNDI
DNFNFKPDKC AILKETVKQI RQIKEQEKAA AANIDEVQKS DVSSTGQGVI DKDALGPMML
EALDGFFFVV NLEGNVVFVS ENVTQYLRYN QEELMNKSVY SILHVGDHTE FVKNLLPKSI
VNGGSWSGEP PRRNSHTFNC RMLVKPLPDS EEEGHDNQEA HQKYETMQCF AVSQPKSIKE
EGEDLQSCLI CVARRVPMKE RPVLPSSESF TTRQDLQGKI TSLDTSTMRA AMKPGWEDLV
RRCIQKFHAQ HEGESVSYAK RHHHEVLRQG LAFSQIYRFS LSDGTLVAAQ TKSKLIRSQT
TNEPQLVISL HMLHREQNVC VMNPDLTGQT MGKPLNPISS NSPAHQALCS GNPGQDMTLS
SNINFPINGP KEQMGMPMGR FGGSGGMNHV SGMQATTPQG SNYALKMNSP SQSSPGMNPG
QPTSMLSPRH RMSPGVAGSP RIPPSQFSPA GSLHSPVGVC SSTGNSHSYT NSSLNALQAL
SEGHGVSLGS SLASPDLKMG NLQNSPVNMN PPPLSKMGSL DSKDCFGLYG EPSEGTTGQA
ESSCHPGEQK ETNDPNLPPA VSSERADGQS RLHDSKGQTK LLQLLTTKSD QMEPSPLASS
LSDTNKDSTG SLPGSGSTHG TSLKEKHKIL HRLLQDSSSP VDLAKLTAEA TGKDLSQESS
STAPGSEVTI KQEPVSPKKK ENALLRYLLD KDDTKDIGLP EITPKLERLD SKTDPASNTK
LIAMKTEKEE MSFEPGDQPG SELDNLEEIL DDLQNSQLPQ LFPDTRPGAP AGSVDKQAII
NDLMQLTAEN SPVTPVGAQK TALRISQSTF NNPRPGQLGR LLPNQNLPLD ITLQSPTGAG
PFPPIRNSSP YSVIPQPGMM GNQGMIGNQG NLGNSSTGMI GNSASRPTMP SGEWAPQSSA
VRVTCAATTS AMNRPVQGGM IRNPAASIPM RPSSQPGQRQ TLQSQVMNIG PSELEMNMGG
PQYSQQQAPP NQTAPWPESI LPIDQASFAS QNRQPFGSSP DDLLCPHPAA ESPSDEGALL
DQLYLALRNF DGLEEIDRAL GIPELVSQSQ AVDPEQFSSQ DSNIMLEQKA PVFPQQYASQ
AQMAQGSYSP MQDPNFHTMG QRPSYATLRM QPRPGLRPTG LVQNQPNQLR LQLQHRLQAQ
QNRQPLMNQI SNVSNVNLTL RPGVPTQAPI NAQMLAQRQR EILNQHLRQR QMHQQQQVQQ
RTLMMRGQGL NMTPSMVAPS GMPATMSNPR IPQANAQQFP FPPNYGISQQ PDPGFTGATT
PQSPLMSPRM AHTQSPMMQQ SQANPAYQAP SDINGWAQGN MGGNSMFSQQ SPPHFGQQAN
TSMYSNNMNI NVSMATNTGG MSSMNQMTGQ ISMTSVTSVP TSGLSSMGPE QVNDPALRGG
NLFPNQLPGM DMIKQEGDTT RKYC
