BAZ2A_HUMAN
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 03-AUG-2022, entry version 204.
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 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 [21]
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 [22]
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
CC {ECO:0000250|UniProtKB:Q91YE5}. 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};
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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; 7MWI; X-ray; 1.80 A; A=536-653.
DR PDB; 7MWL; X-ray; 1.84 A; A/B=536-653.
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; 7MWI; -.
DR PDBsum; 7MWL; -.
DR AlphaFoldDB; Q9UIF9; -.
DR BMRB; Q9UIF9; -.
DR SMR; Q9UIF9; -.
DR BioGRID; 116346; 58.
DR ComplexPortal; CPX-432; NoRC complex.
DR CORUM; Q9UIF9; -.
DR IntAct; Q9UIF9; 17.
DR MINT; Q9UIF9; -.
DR STRING; 9606.ENSP00000446880; -.
DR BindingDB; Q9UIF9; -.
DR ChEMBL; CHEMBL3108642; -.
DR GuidetoPHARMACOLOGY; 2721; -.
DR GlyGen; Q9UIF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UIF9; -.
DR PhosphoSitePlus; Q9UIF9; -.
DR BioMuta; BAZ2A; -.
DR DMDM; 257051081; -.
DR EPD; Q9UIF9; -.
DR jPOST; Q9UIF9; -.
DR MassIVE; Q9UIF9; -.
DR MaxQB; Q9UIF9; -.
DR PaxDb; Q9UIF9; -.
DR PeptideAtlas; Q9UIF9; -.
DR PRIDE; Q9UIF9; -.
DR ProteomicsDB; 84511; -. [Q9UIF9-1]
DR ProteomicsDB; 84512; -. [Q9UIF9-2]
DR ProteomicsDB; 84513; -. [Q9UIF9-3]
DR Antibodypedia; 28282; 100 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 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; 200493at2759; -.
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; 39 hits in 1094 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 208 other tissues.
DR ExpressionAtlas; Q9UIF9; baseline and differential.
DR Genevisible; Q9UIF9; HS.
DR GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; ISS: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:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC.
DR GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
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; 2.
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 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 1797..1799
FT /evidence="ECO:0007829|PDB:7B7I"
FT HELIX 1800..1810
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1813..1815
FT /evidence="ECO:0007829|PDB:5MGJ"
FT HELIX 1816..1818
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1824..1826
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1830..1833
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1840..1848
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1855..1872
FT /evidence="ECO:0007829|PDB:6FGG"
FT HELIX 1878..1897
FT /evidence="ECO:0007829|PDB:6FGG"
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
