BAZ2A_MOUSE
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 03-AUG-2022, entry version 165.
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 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 complex.
DR CORUM; Q91YE5; -.
DR IntAct; Q91YE5; 1.
DR STRING; 10090.ENSMUSP00000129803; -.
DR iPTMnet; Q91YE5; -.
DR PhosphoSitePlus; Q91YE5; -.
DR EPD; Q91YE5; -.
DR jPOST; Q91YE5; -.
DR MaxQB; Q91YE5; -.
DR PaxDb; Q91YE5; -.
DR PRIDE; Q91YE5; -.
DR ProteomicsDB; 273542; -. [Q91YE5-1]
DR ProteomicsDB; 273543; -. [Q91YE5-2]
DR ProteomicsDB; 273544; -. [Q91YE5-3]
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:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
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:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
DR GO; GO:0006306; P:DNA methylation; IDA:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR GO; GO:0051567; P:histone H3-K9 methylation; IDA:MGI.
DR GO; GO:0070933; P:histone H4 deacetylation; IDA:MGI.
DR GO; GO:0034770; P:histone H4-K20 methylation; IDA:MGI.
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 assembly; IDA:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IDA:ComplexPortal.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 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; TIP5.
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; PTHR45915:SF5; 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; SSF47370; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR SUPFAM; SSF57903; SSF57903; 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
