ID BAZ2A_HUMAN Reviewed; 1905 AA. AC Q9UIF9; B3KN66; O00536; O15030; Q68DI8; Q96H26; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 4. DT 27-MAR-2024, entry version 213. 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; DE AltName: Full=hWALp3; GN Name=BAZ2A; Synonyms=KIAA0314, TIP5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=10662543; DOI=10.1006/geno.1999.6071; RA Jones M.H., Hamana N., Nezu J., Shimane M.; RT "A novel family of bromodomain genes."; RL Genomics 63:40-45(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Fetal kidney; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1905 (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [5] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-1905 (ISOFORMS 1/2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 359-753. RC TISSUE=Lung; RA Jansa P., Grummt I.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1905. RC TISSUE=Lymph; 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1559, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747; SER-1770 AND SER-1783, RP AND 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION AT SER-1184, AND ACETYLATION AT LYS-680. 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1397 AND SER-1783, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-1397; SER-1770 AND RP SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-1397; SER-1783 AND RP SER-1785, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; THR-548; SER-613; RP SER-1051; SER-1397 AND SER-1783, ACETYLATION AT LYS-799, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1150, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [20] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [21] RP INTERACTION WITH BEND3 AND USP21, UBIQUITINATION, AND DEUBIQUITINATION. RX PubMed=26100909; DOI=10.1073/pnas.1424705112; RA Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K., Anantharaman A., RA Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V., Prasanth S.G.; RT "BEND3 represses rDNA transcription by stabilizing a NoRC component via RT USP21 deubiquitinase."; RL Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015). RN [22] RP FUNCTION, IDENTIFICATION IN THE NORC-1 ISWI CHROMATIN REMODELING COMPLEX, RP IDENTIFICATION IN THE NORC-5 CHROMATIN REMODELING COMPLEX, AND INTERACTION RP WITH SMARCA1 AND SMARCA5. RX PubMed=28801535; DOI=10.15252/embr.201744011; RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C., RA Cochran A.G.; RT "Expansion of the ISWI chromatin remodeler family with new active RT complexes."; RL EMBO Rep. 18:1697-1706(2017). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-866; LYS-1150; LYS-1172; LYS-1676 RP AND LYS-1709, 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: 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:28801535). 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:28801535). Directly stimulates the CC ATPase activity of SMARCA5 in the NoRC-5 ISWI chromatin remodeling CC complex (PubMed:28801535). The NoRC-1 ISWI chromatin remodeling complex CC has a lower ATP hydrolysis rate than the NoRC-5 ISWI chromatin CC remodeling complex (PubMed:28801535). 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 (By CC similarity). In the complex, it plays a central role by being recruited CC to rDNA and by targeting chromatin modifying enzymes such as HDAC1, CC leading to repress RNA polymerase I transcription (By similarity). CC Recruited to rDNA via its interaction with TTF1 and its ability to CC recognize and bind histone H4 acetylated on 'Lys-16' (H4K16ac), leading CC to deacetylation of H4K5ac, H4K8ac, H4K12ac but not H4K16ac (By CC similarity). 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 (By CC similarity). {ECO:0000250|UniProtKB:Q91YE5, CC ECO:0000269|PubMed:28801535}. 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 CC (PubMed:28801535). Within the NoRC-1 ISWI chromatin remodeling complex CC interacts with SMARCA1; the interaction is direct (PubMed:28801535). 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:28801535). Within the NoRC-5 ISWI chromatin remodeling CC complexes interacts with SMARCA5/SNF2H; the interaction is direct CC (PubMed:28801535). Interacts with TTF1; the interaction is required for CC recruitment of the NoRC-5 ISWI chromatin remodeling complex to rDNA (By CC similarity). Interacts with HDAC1 (By similarity). Interacts with SIN3A CC (By similarity). Interacts with DNMT1 and DNM3B (By similarity). CC Interacts with BEND3 and USP21 (PubMed:26100909). CC {ECO:0000250|UniProtKB:Q91YE5, ECO:0000269|PubMed:26100909, CC ECO:0000269|PubMed:28801535}. CC -!- INTERACTION: CC Q9UIF9; P16333: NCK1; NbExp=2; IntAct=EBI-934890, EBI-389883; CC Q9UIF9; Q62187: Ttf1; Xeno; NbExp=3; IntAct=EBI-934890, EBI-11705418; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q91YE5, CC ECO:0000305|PubMed:25593309}. Note=Colocalizes with the basal RNA CC polymerase I transcription factor UBF in the nucleolus. CC {ECO:0000250|UniProtKB:Q91YE5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=2; CC IsoId=Q9UIF9-1; Sequence=Displayed; CC Name=1; CC IsoId=Q9UIF9-2; Sequence=VSP_037960, VSP_019111; CC Name=3; CC IsoId=Q9UIF9-3; Sequence=VSP_037961; CC -!- TISSUE SPECIFICITY: Expressed at moderate levels in most tissues CC analyzed, including heart, brain, placenta, lung, skeletal muscle, CC kidney and pancreas. 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:0000250|UniProtKB:Q91YE5}. 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:0000250|UniProtKB:Q91YE5}. CC -!- PTM: Acetylation at Lys-680 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 (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its CC stabilization. {ECO:0000269|PubMed:26100909}. CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB60864.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAG51228.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB032254; BAA89211.1; -; mRNA. DR EMBL; CR749379; CAH18232.1; -; mRNA. DR EMBL; AC090681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB002312; BAA20773.2; -; mRNA. DR EMBL; AK023830; BAG51228.1; ALT_SEQ; mRNA. DR EMBL; AF000422; AAB60864.1; ALT_SEQ; mRNA. DR EMBL; BC008965; AAH08965.2; -; mRNA. DR CCDS; CCDS44924.1; -. [Q9UIF9-1] DR RefSeq; NP_038477.2; NM_013449.3. [Q9UIF9-1] DR PDB; 4LZ2; X-ray; 1.76 A; A=1796-1899. DR PDB; 4Q6F; X-ray; 1.91 A; A/B/C/D=1673-1728. DR PDB; 4QBM; X-ray; 1.65 A; A/B=1796-1899. DR PDB; 4QF2; X-ray; 1.70 A; A/B/C/D=1673-1728. DR PDB; 5AGQ; NMR; -; A=543-650. DR PDB; 5MGJ; X-ray; 2.10 A; A=1796-1898. DR PDB; 5MGK; X-ray; 2.30 A; A=1796-1898. DR PDB; 5MGL; X-ray; 2.65 A; A=1796-1898. DR PDB; 5MGM; X-ray; 2.80 A; A=1796-1898. DR PDB; 5OR8; X-ray; 2.40 A; A=1796-1899. DR PDB; 5T8R; X-ray; 2.40 A; A/B/C/D=1673-1728. DR PDB; 6FAP; X-ray; 2.70 A; A/B/C/D=1673-1728. DR PDB; 6FG6; X-ray; 2.40 A; A=1796-1898. DR PDB; 6FGF; X-ray; 2.80 A; A=1796-1898. DR PDB; 6FGG; X-ray; 1.10 A; A=1796-1899. DR PDB; 6FGH; X-ray; 2.10 A; A=1796-1898. DR PDB; 6FGI; X-ray; 2.55 A; A=1796-1898. DR PDB; 6FGL; X-ray; 2.10 A; A=1796-1898. DR PDB; 6FGV; X-ray; 2.50 A; A=1796-1899. DR PDB; 6FGW; X-ray; 2.73 A; A=1796-1899. DR PDB; 6FHU; X-ray; 2.00 A; A/B/C/D=1673-1728. DR PDB; 6FI0; X-ray; 1.90 A; A/B/C/D=1673-1728. DR PDB; 6FKP; X-ray; 2.00 A; A/B/C/D=1673-1728. DR PDB; 7B7B; X-ray; 1.40 A; A=1796-1898. DR PDB; 7B7G; X-ray; 1.43 A; A=1796-1898. DR PDB; 7B7I; X-ray; 1.15 A; A=1796-1898. DR PDB; 7B82; X-ray; 1.25 A; A=1796-1898. DR PDB; 7BC2; X-ray; 2.00 A; A=1796-1898. DR PDB; 7BL8; X-ray; 2.50 A; A=1796-1898. DR PDB; 7BL9; X-ray; 1.30 A; A=1796-1898. DR PDB; 7BLA; X-ray; 1.09 A; A=1796-1898. DR PDB; 7BLB; X-ray; 2.30 A; A=1796-1898. DR PDB; 7BLC; X-ray; 2.30 A; A=1796-1898. DR PDB; 7BLD; X-ray; 2.35 A; A=1796-1898. DR PDB; 7FHJ; X-ray; 2.28 A; A/B=536-653. DR PDB; 7MWH; X-ray; 2.28 A; A/B=536-653. DR PDB; 7MWI; X-ray; 1.80 A; A=536-653. DR PDB; 7MWL; X-ray; 1.84 A; A/B=536-653. DR PDB; 7QVT; X-ray; 2.60 A; A=1796-1898. DR PDB; 7QVU; X-ray; 2.40 A; A=1796-1898. DR PDB; 7QVV; X-ray; 2.60 A; A=1796-1898. DR PDB; 7QWF; X-ray; 2.25 A; A=1796-1898. DR PDB; 7QWU; X-ray; 1.60 A; A=1796-1898. DR PDB; 7QWY; X-ray; 2.44 A; A=1796-1898. DR PDB; 7QX2; X-ray; 1.43 A; A=1796-1898. DR PDB; 7QX9; X-ray; 1.50 A; A=1796-1898. DR PDB; 7QXL; X-ray; 1.15 A; A=1796-1898. DR PDB; 7QYE; X-ray; 1.65 A; A=1796-1898. DR PDB; 7QYO; X-ray; 0.98 A; A=1796-1899. DR PDB; 7QYT; X-ray; 2.60 A; A=1796-1898. DR PDB; 7QYU; X-ray; 1.50 A; A=1796-1898. DR PDB; 7QYV; X-ray; 2.25 A; A=1796-1898. DR PDB; 7QYW; X-ray; 2.10 A; A=1796-1898. DR PDB; 7QZ0; X-ray; 2.10 A; A=1796-1898. DR PDB; 7QZ4; X-ray; 2.30 A; A=1796-1898. DR PDB; 7QZB; X-ray; 2.15 A; A=1796-1898. DR PDB; 7QZC; X-ray; 2.10 A; A=1796-1898. DR PDB; 7QZI; X-ray; 1.98 A; A=1796-1898. DR PDB; 7QZT; X-ray; 2.18 A; A=1796-1898. DR PDB; 7R01; X-ray; 2.26 A; A=1796-1898. DR PDB; 7R0B; X-ray; 2.35 A; A=1796-1898. DR PDBsum; 4LZ2; -. DR PDBsum; 4Q6F; -. DR PDBsum; 4QBM; -. DR PDBsum; 4QF2; -. DR PDBsum; 5AGQ; -. DR PDBsum; 5MGJ; -. DR PDBsum; 5MGK; -. DR PDBsum; 5MGL; -. DR PDBsum; 5MGM; -. DR PDBsum; 5OR8; -. DR PDBsum; 5T8R; -. DR PDBsum; 6FAP; -. DR PDBsum; 6FG6; -. DR PDBsum; 6FGF; -. DR PDBsum; 6FGG; -. DR PDBsum; 6FGH; -. DR PDBsum; 6FGI; -. DR PDBsum; 6FGL; -. DR PDBsum; 6FGV; -. DR PDBsum; 6FGW; -. DR PDBsum; 6FHU; -. DR PDBsum; 6FI0; -. DR PDBsum; 6FKP; -. DR PDBsum; 7B7B; -. DR PDBsum; 7B7G; -. DR PDBsum; 7B7I; -. DR PDBsum; 7B82; -. DR PDBsum; 7BC2; -. DR PDBsum; 7BL8; -. DR PDBsum; 7BL9; -. DR PDBsum; 7BLA; -. DR PDBsum; 7BLB; -. DR PDBsum; 7BLC; -. DR PDBsum; 7BLD; -. DR PDBsum; 7FHJ; -. DR PDBsum; 7MWH; -. DR PDBsum; 7MWI; -. DR PDBsum; 7MWL; -. DR PDBsum; 7QVT; -. DR PDBsum; 7QVU; -. DR PDBsum; 7QVV; -. DR PDBsum; 7QWF; -. DR PDBsum; 7QWU; -. DR PDBsum; 7QWY; -. DR PDBsum; 7QX2; -. DR PDBsum; 7QX9; -. DR PDBsum; 7QXL; -. DR PDBsum; 7QYE; -. DR PDBsum; 7QYO; -. DR PDBsum; 7QYT; -. DR PDBsum; 7QYU; -. DR PDBsum; 7QYV; -. DR PDBsum; 7QYW; -. DR PDBsum; 7QZ0; -. DR PDBsum; 7QZ4; -. DR PDBsum; 7QZB; -. DR PDBsum; 7QZC; -. DR PDBsum; 7QZI; -. DR PDBsum; 7QZT; -. DR PDBsum; 7R01; -. DR PDBsum; 7R0B; -. DR AlphaFoldDB; Q9UIF9; -. DR BMRB; Q9UIF9; -. DR SMR; Q9UIF9; -. DR BioGRID; 116346; 70. DR ComplexPortal; CPX-432; NoRC chromatin remodelling complex. DR CORUM; Q9UIF9; -. DR IntAct; Q9UIF9; 21. DR MINT; Q9UIF9; -. DR STRING; 9606.ENSP00000446880; -. DR BindingDB; Q9UIF9; -. DR ChEMBL; CHEMBL3108642; -. DR GuidetoPHARMACOLOGY; 2721; -. DR GlyCosmos; Q9UIF9; 1 site, 1 glycan. DR GlyGen; Q9UIF9; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9UIF9; -. DR PhosphoSitePlus; Q9UIF9; -. DR SwissPalm; Q9UIF9; -. DR BioMuta; BAZ2A; -. DR DMDM; 257051081; -. DR EPD; Q9UIF9; -. DR jPOST; Q9UIF9; -. DR MassIVE; Q9UIF9; -. DR MaxQB; Q9UIF9; -. DR PaxDb; 9606-ENSP00000446880; -. DR PeptideAtlas; Q9UIF9; -. DR ProteomicsDB; 84511; -. [Q9UIF9-1] DR ProteomicsDB; 84512; -. [Q9UIF9-2] DR ProteomicsDB; 84513; -. [Q9UIF9-3] DR Pumba; Q9UIF9; -. DR Antibodypedia; 28282; 111 antibodies from 22 providers. DR DNASU; 11176; -. DR Ensembl; ENST00000551812.5; ENSP00000446880.1; ENSG00000076108.12. [Q9UIF9-1] DR GeneID; 11176; -. DR KEGG; hsa:11176; -. DR UCSC; uc001slq.2; human. [Q9UIF9-1] DR AGR; HGNC:962; -. DR CTD; 11176; -. DR DisGeNET; 11176; -. DR GeneCards; BAZ2A; -. DR HGNC; HGNC:962; BAZ2A. DR HPA; ENSG00000076108; Low tissue specificity. DR MIM; 605682; gene. DR neXtProt; NX_Q9UIF9; -. DR OpenTargets; ENSG00000076108; -. DR PharmGKB; PA25272; -. DR VEuPathDB; HostDB:ENSG00000076108; -. DR eggNOG; KOG1245; Eukaryota. DR GeneTree; ENSGT00940000159490; -. DR InParanoid; Q9UIF9; -. DR OrthoDB; 2912910at2759; -. DR PhylomeDB; Q9UIF9; -. DR TreeFam; TF329083; -. DR PathwayCommons; Q9UIF9; -. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR SignaLink; Q9UIF9; -. DR BioGRID-ORCS; 11176; 41 hits in 1171 CRISPR screens. DR ChiTaRS; BAZ2A; human. DR GeneWiki; BAZ2A; -. DR GenomeRNAi; 11176; -. DR Pharos; Q9UIF9; Tchem. DR PRO; PR:Q9UIF9; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9UIF9; Protein. DR Bgee; ENSG00000076108; Expressed in sural nerve and 210 other cell types or tissues. DR ExpressionAtlas; Q9UIF9; baseline and differential. DR GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0090536; C:NoRC complex; ISO:ComplexPortal. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IPI:UniProtKB. DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016922; F:nuclear receptor binding; NAS:BHF-UCL. DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB. DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; ISO:ComplexPortal. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISO:ComplexPortal. DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:ComplexPortal. DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:ComplexPortal. DR GO; GO:0000183; P:rDNA heterochromatin formation; ISS:UniProtKB. DR GO; GO:0044030; P:regulation of DNA methylation; ISO:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. 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. DR Genevisible; Q9UIF9; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Bromodomain; KW Chromatin regulator; Coiled coil; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Repressor; RNA-binding; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..1905 FT /note="Bromodomain adjacent to zinc finger domain protein FT 2A" FT /id="PRO_0000211172" FT DOMAIN 546..617 FT /note="MBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338" FT DOMAIN 848..913 FT /note="DDT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063" FT DOMAIN 1810..1880 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DNA_BIND 649..661 FT /note="A.T hook 1" FT DNA_BIND 670..682 FT /note="A.T hook 2" FT DNA_BIND 1186..1198 FT /note="A.T hook 3" FT DNA_BIND 1404..1416 FT /note="A.T hook 4" FT ZN_FING 1676..1726 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 362..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..792 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1178..1220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1283..1318 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1330..1412 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1734..1755 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1769..1789 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 693..792 FT /evidence="ECO:0000255" FT COMPBIAS 28..59 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 653..712 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 736..792 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1347..1377 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 507 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 548 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 680 FT /note="N6-acetyllysine; by KAT8" FT /evidence="ECO:0000269|PubMed:19578370" FT MOD_RES 799 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91YE5" FT MOD_RES 1051 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91YE5" FT MOD_RES 1184 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q91YE5" FT MOD_RES 1397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1559 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 1747 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1783 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1785 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT CROSSLNK 866 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1150 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1172 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1676 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1709 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 6 FT /note="N -> NEAN (in isoform 1)" FT /evidence="ECO:0000303|PubMed:10662543" FT /id="VSP_037960" FT VAR_SEQ 178..207 FT /note="Missing (in isoform 1)" FT /evidence="ECO:0000303|PubMed:10662543" FT /id="VSP_019111" FT VAR_SEQ 1434..1437 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_037961" FT VARIANT 498 FT /note="V -> E (in dbSNP:rs2230579)" FT /id="VAR_055548" FT CONFLICT 106 FT /note="N -> S (in Ref. 2; CAH18232)" FT /evidence="ECO:0000305" FT CONFLICT 148 FT /note="E -> K (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="Q -> H (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="Q -> P (in Ref. 2; CAH18232)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="G -> C (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="G -> C (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 503 FT /note="A -> T (in Ref. 2; CAH18232)" FT /evidence="ECO:0000305" FT CONFLICT 601 FT /note="V -> L (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 727 FT /note="Q -> L (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 747 FT /note="Q -> H (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 812 FT /note="R -> K (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 978 FT /note="L -> P (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1032..1033 FT /note="EG -> GR (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1190 FT /note="G -> S (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1193 FT /note="R -> L (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1199 FT /note="S -> F (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1205 FT /note="L -> F (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1229 FT /note="A -> V (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1274 FT /note="S -> N (in Ref. 2; CAH18232)" FT /evidence="ECO:0000305" FT CONFLICT 1319 FT /note="P -> L (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1322 FT /note="L -> F (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1340 FT /note="P -> L (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1443 FT /note="R -> P (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1568 FT /note="R -> P (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1598 FT /note="E -> K (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1643 FT /note="V -> I (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1649 FT /note="E -> Q (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1656 FT /note="Q -> H (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1663 FT /note="Q -> H (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1766 FT /note="R -> K (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT CONFLICT 1781 FT /note="G -> R (in Ref. 1; BAA89211)" FT /evidence="ECO:0000305" FT HELIX 549..553 FT /evidence="ECO:0007829|PDB:7MWI" FT HELIX 554..557 FT /evidence="ECO:0007829|PDB:7MWI" FT STRAND 561..568 FT /evidence="ECO:0007829|PDB:7MWI" FT STRAND 570..580 FT /evidence="ECO:0007829|PDB:7MWI" FT STRAND 582..584 FT /evidence="ECO:0007829|PDB:5AGQ" FT HELIX 590..599 FT /evidence="ECO:0007829|PDB:7MWI" FT HELIX 607..609 FT /evidence="ECO:0007829|PDB:7MWI" FT STRAND 619..627 FT /evidence="ECO:0007829|PDB:7MWI" FT STRAND 630..635 FT /evidence="ECO:0007829|PDB:7MWI" FT TURN 638..640 FT /evidence="ECO:0007829|PDB:7MWI" FT HELIX 641..647 FT /evidence="ECO:0007829|PDB:7MWI" FT HELIX 1674..1676 FT /evidence="ECO:0007829|PDB:4Q6F" FT TURN 1680..1682 FT /evidence="ECO:0007829|PDB:4QF2" FT HELIX 1688..1690 FT /evidence="ECO:0007829|PDB:4QF2" FT STRAND 1691..1693 FT /evidence="ECO:0007829|PDB:4QF2" FT STRAND 1695..1698 FT /evidence="ECO:0007829|PDB:4QF2" FT STRAND 1700..1702 FT /evidence="ECO:0007829|PDB:4QF2" FT TURN 1703..1705 FT /evidence="ECO:0007829|PDB:4QF2" FT HELIX 1721..1724 FT /evidence="ECO:0007829|PDB:4QF2" FT HELIX 1799..1810 FT /evidence="ECO:0007829|PDB:7BLA" FT HELIX 1813..1818 FT /evidence="ECO:0007829|PDB:7BLA" FT TURN 1824..1826 FT /evidence="ECO:0007829|PDB:7BLA" FT HELIX 1830..1833 FT /evidence="ECO:0007829|PDB:7BLA" FT HELIX 1840..1847 FT /evidence="ECO:0007829|PDB:7BLA" FT TURN 1848..1850 FT /evidence="ECO:0007829|PDB:7BLA" FT HELIX 1855..1872 FT /evidence="ECO:0007829|PDB:7BLA" FT HELIX 1878..1897 FT /evidence="ECO:0007829|PDB:7BLA" SQ SEQUENCE 1905 AA; 211198 MW; F364E2AC4BF89EA2 CRC64; MEMEANDHFN FTGLPPAPAA SGLKPSPSSG EGLYTNGSPM NFPQQGKSLN GDVNVNGLST VSHTTTSGIL NSAPHSSSTS HLHHPSVAYD CLWNYSQYPS ANPGSNLKDP PLLSQFSGGQ YPLNGILGGS RQPSSPSHNT NLRAGSQEFW ANGTQSPMGL NFDSQELYDS FPDQNFEVMP NGPPSFFTSP QTSPMLGSSI QTFAPSQEVG SGIHPDEAAE KEMTSVVAEN GTGLVGSLEL EEEQPELKMC GYNGSVPSVE SLHQEVSVLV PDPTVSCLDD PSHLPDQLED TPILSEDSLE PFNSLAPEPV SGGLYGIDDT ELMGAEDKLP LEDSPVISAL DCPSLNNATA FSLLADDSQT STSIFASPTS PPVLGESVLQ DNSFDLNNGS DAEQEEMETQ SSDFPPSLTQ PAPDQSSTIQ LHPATSPAVS PTTSPAVSLV VSPAASPEIS PEVCPAASTV VSPAVFSVVS PASSAVLPAV SLEVPLTASV TSPKASPVTS PAAAFPTASP ANKDVSSFLE TTADVEEITG EGLTASGSGD VMRRRIATPE EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG KRGRPRNTEK AKTKEVPKVK RGRGRPPKVK ITELLNKTDN RPLKKLEAQE TLNEEDKAKI AKSKKKMRQK VQRGECQTTI QGQARNKRKQ ETKSLKQKEA KKKSKAEKEK GKTKQEKLKE KVKREKKEKV KMKEKEEVTK AKPACKADKT LATQRRLEER QRQQMILEEM KKPTEDMCLT DHQPLPDFSR VPGLTLPSGA FSDCLTIVEF LHSFGKVLGF DPAKDVPSLG VLQEGLLCQG DSLGEVQDLL VRLLKAALHD PGFPSYCQSL KILGEKVSEI PLTRDNVSEI LRCFLMAYGV EPALCDRLRT QPFQAQPPQQ KAAVLAFLVH ELNGSTLIIN EIDKTLESMS SYRKNKWIVE GRLRRLKTVL AKRTGRSEVE MEGPEECLGR RRSSRIMEET SGMEEEEEEE SIAAVPGRRG RRDGEVDATA SSIPELERQI EKLSKRQLFF RKKLLHSSQM LRAVSLGQDR YRRRYWVLPY LAGIFVEGTE GNLVPEEVIK KETDSLKVAA HASLNPALFS MKMELAGSNT TASSPARARG RPRKTKPGSM QPRHLKSPVR GQDSEQPQAQ LQPEAQLHAP AQPQPQLQLQ LQSHKGFLEQ EGSPLSLGQS QHDLSQSAFL SWLSQTQSHS SLLSSSVLTP DSSPGKLDPA PSQPPEEPEP DEAESSPDPQ ALWFNISAQM PCNAAPTPPP AVSEDQPTPS PQQLASSKPM NRPSAANPCS PVQFSSTPLA GLAPKRRAGD PGEMPQSPTG LGQPKRRGRP PSKFFKQMEQ RYLTQLTAQP VPPEMCSGWW WIRDPEMLDA MLKALHPRGI REKALHKHLN KHRDFLQEVC LRPSADPIFE PRQLPAFQEG IMSWSPKEKT YETDLAVLQW VEELEQRVIM SDLQIRGWTC PSPDSTREDL AYCEHLSDSQ EDITWRGRGR EGLAPQRKTT NPLDLAVMRL AALEQNVERR YLREPLWPTH EVVLEKALLS TPNGAPEGTT TEISYEITPR IRVWRQTLER CRSAAQVCLC LGQLERSIAW EKSVNKVTCL VCRKGDNDEF LLLCDGCDRG CHIYCHRPKM EAVPEGDWFC TVCLAQQVEG EFTQKPGFPK RGQKRKSGYS LNFSEGDGRR RRVLLRGRES PAAGPRYSEE GLSPSKRRRL SMRNHHSDLT FCEIILMEME SHDAAWPFLE PVNPRLVSGY RRIIKNPMDF STMRERLLRG GYTSSEEFAA DALLVFDNCQ TFNEDDSEVG KAGHIMRRFF ESRWEEFYQG KQANL //