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Database: UniProt
Entry: Q15596
LinkDB: Q15596
Original site: Q15596 
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   07-APR-2021, entry version 227.
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;
DE            Short=hTIF2;
GN   Name=NCOA2; Synonyms=BHLHE75, SRC2, TIF2;
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].
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. Coactivator of the steroid binding domain (AF-2) but not of
CC       the modulating N-terminal domain (AF-1). Required with NCOA1 to control
CC       energy balance between white and brown adipose tissues. Critical
CC       regulator of glucose metabolism regulation, acts as RORA coactivator to
CC       specifically modulate G6PC1 expression. Involved in the positive
CC       regulation of the transcriptional activity of the glucocorticoid
CC       receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the
CC       circadian clock by acting as a transcriptional coactivator for the
CC       CLOCK-ARNTL/BMAL1 heterodimer (By similarity).
CC       {ECO:0000250|UniProtKB:Q61026, ECO:0000269|PubMed:23508108,
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=2; 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.
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   -!- 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; 7B88; X-ray; 2.38 A; B=686-699.
DR   PDB; 7D42; X-ray; 2.70 A; B=740-753.
DR   PDB; 7JHD; X-ray; 2.40 A; C/D=686-698.
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; 7B88; -.
DR   PDBsum; 7D42; -.
DR   PDBsum; 7JHD; -.
DR   SMR; Q15596; -.
DR   BioGRID; 115761; 84.
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; 30.
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   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; 297 antibodies.
DR   Ensembl; ENST00000452400; ENSP00000399968; ENSG00000140396.
DR   GeneID; 10499; -.
DR   KEGG; hsa:10499; -.
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:ENSG00000140396.12; -.
DR   eggNOG; KOG3561; Eukaryota.
DR   GeneTree; ENSGT00950000183021; -.
DR   HOGENOM; CLU_001988_0_0_1; -.
DR   InParanoid; Q15596; -.
DR   OMA; MRTEKEE; -.
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   SignaLink; Q15596; -.
DR   SIGNOR; Q15596; -.
DR   BioGRID-ORCS; 10499; 17 hits in 1002 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 epithelium of mammary gland and 248 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:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
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:0015721; P:bile acid and bile salt transport; TAS:Reactome.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
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; 1.10.287.1070; -; 1.
DR   Gene3D; 4.10.280.10; -; 1.
DR   IDEAL; IID00082; -.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR010011; DUF1518.
DR   InterPro; IPR032565; DUF4927.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR028822; NCOA2.
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          691..743
FT                   /note="CASP8AP2-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          730..1121
FT                   /note="Interaction with ARNTL"
FT                   /evidence="ECO:0000250|UniProtKB:Q61026"
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        1254..1260
FT                   /note="Poly-Gln"
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; alternate"
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:0007744|PDB:5VB7"
FT   HELIX           689..693
FT                   /evidence="ECO:0007744|PDB:5DXE"
FT   STRAND          739..741
FT                   /evidence="ECO:0007744|PDB:1M2Z"
FT   HELIX           743..750
FT                   /evidence="ECO:0007744|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
//
DBGET integrated database retrieval system