ID   BAZ2A_MOUSE             Reviewed;        1889 AA.
AC   Q91YE5; Q3U235; Q80U42;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Bromodomain adjacent to zinc finger domain protein 2A;
DE   AltName: Full=Transcription termination factor I-interacting protein 5;
DE            Short=TTF-I-interacting protein 5;
DE            Short=Tip5;
GN   Name=Baz2a; Synonyms=Kiaa0314, Tip5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-703 (ISOFORM 3).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 40-1889 (ISOFORM 1), FUNCTION, IDENTIFICATION
RP   IN THE NORC-5 ISWI CHROMATIN REMODELING COMPLEX, INTERACTION WITH SMARCA5
RP   AND TTF1, AND SUBCELLULAR LOCATION.
RX   PubMed=11532953; DOI=10.1093/emboj/20.17.4892;
RA   Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R.,
RA   Laengst G., Grummt I.;
RT   "NoRC -- a novel member of mammalian ISWI-containing chromatin remodeling
RT   machines.";
RL   EMBO J. 20:4892-4900(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1889 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HDAC1 AND SIN3A, AND
RP   MUTAGENESIS OF TYR-1814.
RX   PubMed=12198165; DOI=10.1093/emboj/cdf460;
RA   Zhou Y., Santoro R., Grummt I.;
RT   "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene
RT   promoter and represses RNA polymerase I transcription.";
RL   EMBO J. 21:4632-4640(2002).
RN   [5]
RP   INTERACTION WITH TTF1.
RX   PubMed=15292447; DOI=10.1093/nar/gkh732;
RA   Nemeth A., Strohner R., Grummt I., Laengst G.;
RT   "The chromatin remodeling complex NoRC and TTF-I cooperate in the
RT   regulation of the mammalian rRNA genes in vivo.";
RL   Nucleic Acids Res. 32:4091-4099(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH DNMT1; DNM3B;
RP   HDAC1 AND SMARCA5.
RX   PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
RA   Zhou Y., Grummt I.;
RT   "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16
RT   and is sufficient for rDNA silencing.";
RL   Curr. Biol. 15:1434-1438(2005).
RN   [7]
RP   FUNCTION, RNA-BINDING, DOMAIN, AND MUTAGENESIS OF 570-TRP-TYR-571.
RX   PubMed=16678107; DOI=10.1016/j.molcel.2006.03.028;
RA   Mayer C., Schmitz K.-M., Li J., Grummt I., Santoro R.;
RT   "Intergenic transcripts regulate the epigenetic state of rRNA genes.";
RL   Mol. Cell 22:351-361(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=18600236; DOI=10.1038/embor.2008.109;
RA   Mayer C., Neubert M., Grummt I.;
RT   "The structure of NoRC-associated RNA is crucial for targeting the
RT   chromatin remodelling complex NoRC to the nucleolus.";
RL   EMBO Rep. 9:774-780(2008).
RN   [10]
RP   ACETYLATION AT LYS-672, RNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF 570-TRP-TYR-571 AND LYS-672.
RX   PubMed=19578370; DOI=10.1038/ncb1914;
RA   Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.;
RT   "Reversible acetylation of the chromatin remodelling complex NoRC is
RT   required for non-coding RNA-dependent silencing.";
RL   Nat. Cell Biol. 11:1010-1016(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1042; SER-1174; SER-1374;
RP   SER-1377; SER-1383 AND THR-1738, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Regulatory subunit of the ATP-dependent NoRC-1 and NoRC-5
CC       ISWI chromatin remodeling complexes, which form ordered nucleosome
CC       arrays on chromatin and facilitate access to DNA during DNA-templated
CC       processes such as DNA replication, transcription, and repair
CC       (PubMed:11532953). Both complexes regulate the spacing of nucleosomes
CC       along the chromatin and have the ability to slide mononucleosomes to
CC       the center of a DNA template (PubMed:11532953). Directly stimulates the
CC       ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling
CC       complex (By similarity). The NoRC-1 ISWI chromatin remodeling complex
CC       has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin
CC       remodeling complex (By similarity). Within the NoRC-5 ISWI chromatin
CC       remodeling complex, mediates silencing of a fraction of rDNA by
CC       recruiting histone-modifying enzymes and DNA methyltransferases,
CC       leading to heterochromatin formation and transcriptional silencing
CC       (PubMed:11532953). In the complex, it plays a central role by being
CC       recruited to rDNA and by targeting chromatin modifying enzymes such as
CC       HDAC1, leading to repress RNA polymerase I transcription
CC       (PubMed:12198165, PubMed:16085498). Recruited to rDNA via its
CC       interaction with TTF1 and its ability to recognize and bind histone H4
CC       acetylated on 'Lys-16' (H4K16ac), leading to deacetylation of H4K5ac,
CC       H4K8ac, H4K12ac but not H4K16ac (PubMed:11532953, PubMed:16085498).
CC       Specifically binds pRNAs, 150-250 nucleotide RNAs that are
CC       complementary in sequence to the rDNA promoter; pRNA-binding is
CC       required for heterochromatin formation and rDNA silencing
CC       (PubMed:16678107, PubMed:18600236). {ECO:0000250|UniProtKB:Q9UIF9,
CC       ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:12198165,
CC       ECO:0000269|PubMed:16085498, ECO:0000269|PubMed:16678107,
CC       ECO:0000269|PubMed:18600236}.
CC   -!- SUBUNIT: Component of the NoRC-1 ISWI chromatin remodeling complex at
CC       least composed of SMARCA1 and BAZ2A/TIP5, which regulates the spacing
CC       of histone octamers on the DNA template to facilitate access to DNA (By
CC       similarity). Within the NoRC-1 ISWI chromatin remodeling complex
CC       interacts with SMARCA1; the interaction is direct (By similarity).
CC       Component of the NoRC-5 ISWI chromatin remodeling complex (also called
CC       the NoRC nucleolar-remodeling complex), at least composed of
CC       SMARCA5/SNF2H and BAZ2A/TIP5, which regulates the spacing of histone
CC       octamers on the DNA template to facilitate access to DNA
CC       (PubMed:11532953). Within the NoRC-5 ISWI chromatin remodeling
CC       complexes interacts with SMARCA5/SNF2H; the interaction is direct
CC       (PubMed:11532953, PubMed:16085498). Interacts with TTF1; the
CC       interaction is required for recruitment of the NoRC-5 ISWI chromatin
CC       remodeling complex to rDNA (PubMed:11532953, PubMed:15292447).
CC       Interacts with HDAC1 (PubMed:12198165, PubMed:16085498). Interacts with
CC       SIN3A (PubMed:12198165). Interacts with DNMT1 and DNM3B
CC       (PubMed:16085498). Interacts with BEND3 and USP21 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UIF9, ECO:0000269|PubMed:11532953,
CC       ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:15292447,
CC       ECO:0000269|PubMed:16085498}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11532953,
CC       ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:16085498,
CC       ECO:0000269|PubMed:18600236, ECO:0000269|PubMed:19578370}. Note=Co-
CC       localizes with the basal RNA polymerase I transcription factor UBF in
CC       the nucleolus. {ECO:0000269|PubMed:11532953}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q91YE5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YE5-2; Sequence=VSP_037963;
CC       Name=3;
CC         IsoId=Q91YE5-3; Sequence=VSP_037962;
CC   -!- DOMAIN: The bromo domain and the PHD-type zinc finger recognize and
CC       bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2 domains play
CC       a central role in the recruitment of chromatin silencing proteins such
CC       as DNMT1, DNMT3B and HDAC1. {ECO:0000269|PubMed:16085498}.
CC   -!- DOMAIN: The MBD (methyl-CpG-binding) domain, also named TAM domain,
CC       specifically recognizes and binds a conserved stem-loop structure the
CC       association within pRNA. Binding to pRNA induces a conformational
CC       change of BAZ2A/TIP5 and is essential for targeting the NoRC complex to
CC       the nucleolus. {ECO:0000269|PubMed:16678107}.
CC   -!- PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its
CC       stabilization. {ECO:0000250|UniProtKB:Q9UIF9}.
CC   -!- PTM: Acetylation at Lys-672 by KAT8/MOF promotes its dissociation from
CC       pRNA, affecting heterochromatin formation, nucleosome positioning and
CC       rDNA silencing. Deacetylation by SIRT1 in late S phase enhances pRNA-
CC       binding, allowing de novo DNA methylation and heterochromatin
CC       formation. Acetylation is high during S phase and declines to
CC       background levels in late S phase when the silent copies of rRNA genes
CC       are replicated. {ECO:0000269|PubMed:19578370}.
CC   -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
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DR   EMBL; AK155523; BAE33307.1; -; mRNA.
DR   EMBL; AJ309544; CAC69992.1; -; mRNA.
DR   EMBL; AK122243; BAC65525.1; -; mRNA.
DR   AlphaFoldDB; Q91YE5; -.
DR   BMRB; Q91YE5; -.
DR   SMR; Q91YE5; -.
DR   ComplexPortal; CPX-424; NoRC chromatin remodelling complex.
DR   CORUM; Q91YE5; -.
DR   IntAct; Q91YE5; 1.
DR   STRING; 10090.ENSMUSP00000151961; -.
DR   iPTMnet; Q91YE5; -.
DR   PhosphoSitePlus; Q91YE5; -.
DR   EPD; Q91YE5; -.
DR   jPOST; Q91YE5; -.
DR   MaxQB; Q91YE5; -.
DR   PaxDb; 10090-ENSMUSP00000129803; -.
DR   ProteomicsDB; 273542; -. [Q91YE5-1]
DR   ProteomicsDB; 273543; -. [Q91YE5-2]
DR   ProteomicsDB; 273544; -. [Q91YE5-3]
DR   AGR; MGI:2151152; -.
DR   MGI; MGI:2151152; Baz2a.
DR   eggNOG; KOG1245; Eukaryota.
DR   InParanoid; Q91YE5; -.
DR   PhylomeDB; Q91YE5; -.
DR   ChiTaRS; Baz2a; mouse.
DR   PRO; PR:Q91YE5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q91YE5; Protein.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0090536; C:NoRC complex; IPI:ComplexPortal.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
DR   GO; GO:0140463; F:chromatin-protein adaptor activity; IDA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0042393; F:histone binding; ISO:MGI.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
DR   GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin formation; IDA:ComplexPortal.
DR   GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:ComplexPortal.
DR   GO; GO:0031062; P:positive regulation of histone methylation; IDA:ComplexPortal.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IDA:UniProtKB.
DR   GO; GO:0044030; P:regulation of DNA methylation; IDA:ComplexPortal.
DR   GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC.
DR   CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR   CDD; cd01397; HAT_MBD; 1.
DR   CDD; cd15629; PHD_BAZ2A; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR037374; BAZ2A/B_Bromo.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   InterPro; IPR028940; PHD_BAZ2A.
DR   InterPro; IPR028942; WHIM1_dom.
DR   InterPro; IPR028941; WHIM2_dom.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45915:SF5; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A; 1.
DR   PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF01429; MBD; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF15612; WHIM1; 1.
DR   Pfam; PF15613; WSD; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00384; AT_hook; 4.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00391; MBD; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS50982; MBD; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW   Coiled coil; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1889
FT                   /note="Bromodomain adjacent to zinc finger domain protein
FT                   2A"
FT                   /id="PRO_0000211173"
FT   DOMAIN          538..609
FT                   /note="MBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT   DOMAIN          839..904
FT                   /note="DDT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT   DOMAIN          1794..1864
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DNA_BIND        641..653
FT                   /note="A.T hook 1"
FT   DNA_BIND        662..674
FT                   /note="A.T hook 2"
FT   DNA_BIND        1176..1188
FT                   /note="A.T hook 3"
FT   DNA_BIND        1390..1402
FT                   /note="A.T hook 4"
FT   ZN_FING         1662..1712
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..726
FT                   /note="Required for TTF1 binding"
FT                   /evidence="ECO:0000269|PubMed:11532953"
FT   REGION          384..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1147..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1269..1397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1720..1778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          686..813
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        28..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..704
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        728..791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1147..1177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1190..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1332..1368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         499
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         540
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         605
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         672
FT                   /note="N6-acetyllysine; by KAT8"
FT                   /evidence="ECO:0000269|PubMed:19578370"
FT   MOD_RES         790
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         1042
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1374
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         1733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         1738
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   MOD_RES         1767
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   CROSSLNK        857
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   CROSSLNK        1141
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   CROSSLNK        1163
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   CROSSLNK        1662
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   CROSSLNK        1695
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UIF9"
FT   VAR_SEQ         305
FT                   /note="L -> LA (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_037962"
FT   VAR_SEQ         1712
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12693553"
FT                   /id="VSP_037963"
FT   MUTAGEN         570..571
FT                   /note="WY->GA: Impairs interaction with pRNA and
FT                   heterochromatin formation but retains ability to trigger
FT                   DNA methylation and silence rDNA transcription."
FT                   /evidence="ECO:0000269|PubMed:16678107,
FT                   ECO:0000269|PubMed:19578370"
FT   MUTAGEN         672
FT                   /note="K->R: Abolishes acetylation by KAT8/MOF, leading to
FT                   increase interaction with TTF1 and association with pRNA."
FT                   /evidence="ECO:0000269|PubMed:19578370"
FT   MUTAGEN         1814
FT                   /note="Y->F: Impairs binding to chromatin."
FT                   /evidence="ECO:0000269|PubMed:12198165"
FT   CONFLICT        41..42
FT                   /note="NF -> SL (in Ref. 1; CAC69992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1889 AA;  209618 MW;  14E7A817877EB114 CRC64;
     MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST
     VSHTTTSGIL NSAPHSSSTS HLHHPNVAYD CLWNYSQYPS ANPGNNLKDP PLLSQFPGGQ
     YPLNGILGGN RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP
     NGPPSFFTSP QTSPMLGSSI QTFAPSQDVS SDIHPDEAAE KELTSVVAEN GTGLVGSLEL
     EEEQPELKMC GYNGSVSSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE
     PFDSLAAEPV SGSLYGIDDA ELMGAEDKLP LEGNPVISAL DCPALSNANA FSLLADDSQT
     SASIFVSPTS PPVLGESVLQ DNSFGLNSCS DSEQEEIETQ SSNFQRPLTE PAPDQPPSTQ
     LHPAVSPTAS PAASLTASAE ISPAVSPVAS SPVPPEVFVA VSPASSPALP AISLEASMTT
     PVTSPQGSPE PSPAAAFQTV SPARKNVSSA PKARADREET TGGAVAVSGS GDVLKRRIAT
     PEEVRLPLQH GWRREVRIKK GSHRWQGETW YYGPCGKRMK QFPEVIKYLS RNVVHSVRRE
     HFSFSPRMPV GDFFEERDTP EGLQWVQLSA EEIPSRIQAI TGKRGRPRNN EKAKNKEVPK
     VKRGRGRPPK IKMPELLNKT DNRLPKKLET QEILSEDDKA KMTKNKKKMR QKVQRGESQT
     PVQGQARNKR KQDTKSLKQK DTKKKLKAEK EKMKTKQEKL KEKVKREKKE KVKAKGKEGP
     RARPSCRADK TLATQKRLEE QQRQQAILEE MKKPTEGMCL SDHQPLPDFT RIPGLTLSSR
     AFSDCLTIVE FLHSFGKVLG FDLTKDVPSL GVLQEGLLCQ GDSLDKVQDL LVRLLKAALH
     DPGLPPYCQS LKILGEKMSE IPLTRDNVSE ILRCFLMAYR VEPPFCDSLR TQPFQAQPPQ
     QKAAILAFLV HELNSSTIII NEIDKTLESV SSCRKNKWIV EGRLRRLKTA LAKRTGRPEV
     MMEGAEDGLG RRRSSRIMEE TSGIEEEEEE ENTTAVHGRR GRKEGEIDVA ASSIPELERH
     IEKLSKRQLF FRKKLLHSSQ MLRAVSLGQD RYRRHYWVLP YLAGIFVEGS EGSTVTEDEI
     KQETESLMEV VTSTPSSARA SVKRELTGSN ASTSPARSRG RPRKPKPGSL QPQHLQSTIR
     ECDSEQAQTQ VHPEPQPQLQ APTQPHLQPS SGFLEPEGSP FSLGQSQHDL SQSAFLSWLS
     QTQSHNSLLS SSVLTPDSSP GKLDSAPSQS LEEPEPDEAQ SCPGPQGPWF NFSAQIPCDA
     APTPPPAVSE DQPTPSLQLL ASSKPMNTPG AANPCSPVQL SSTHLPGGTP KRLSGDSEEM
     SQSPTGLGQP KRRGRPPSKF FKQVEQHYLT QLTAQPIPPE MCSGWWWIRD PETLDVLLKA
     LHPRGIREKA LHKHLSKHKD FLQEVCLQPL TDPIFEPNEL PALEEGVMSW SPKEKTYETD
     LAVLQWVEEL EQRVVLSDLQ IRGWTCPTPD STREDLTYCE HLPDSPEDIP WRGRGREGTV
     PQRQNNNPLD LAVMRLAVLE QNVERRYLRE PLWAAHEVVV EKALLSTPNG APDGTSTEIS
     YEITPRVRVW RQTLERCRSA AQVCLCMGQL ERSIAWEKSV NKVTCLVCRK GDNDEFLLLC
     DGCDRGCHIY CHRPKMEAVP EGDWFCAVCL SQQVEEEYTQ RPGFPKRGQK RKSSFPLTFP
     EGDSRRRMLS RSRDSPAVPR YPEDGLSPPK RRRHSMRSHH SDLTFCEIIL MEMESHDAAW
     PFLEPVNPRL VSGYRRVIKN PMDFSTMRER LLRGGYTSSE EFAADALLVF DNCQTFNEDD
     SEVGKAGHVM RRFFESRWEE FYQGKQANL
//