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Bromodomain adjacent to zinc finger domain protein 2A (Transcription termination factor I-interacting protein 5) (TTF-I-interacting protein 5) (Tip5) (hWALp3)

 BAZ2A_HUMAN             Reviewed;        1905 AA.
Q9UIF9; B3KN66; O00536; O15030; Q68DI8; Q96H26;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 4.
18-JUL-2018, entry version 179.
RecName: Full=Bromodomain adjacent to zinc finger domain protein 2A;
AltName: Full=Transcription termination factor I-interacting protein 5;
Short=TTF-I-interacting protein 5;
Short=Tip5;
AltName: Full=hWALp3;
Name=BAZ2A; Synonyms=KIAA0314, TIP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=10662543; DOI=10.1006/geno.1999.6071;
Jones M.H., Hamana N., Nezu J., Shimane M.;
"A novel family of bromodomain genes.";
Genomics 63:40-45(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-1905 (ISOFORM 2).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[5]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-1905 (ISOFORMS 1/2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 359-753.
TISSUE=Lung;
Jansa P., Grummt I.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1065-1905.
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1559, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1747; SER-1770 AND
SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION AT LYS-680.
PubMed=19578370; DOI=10.1038/ncb1914;
Zhou Y., Schmitz K.M., Mayer C., Yuan X., Akhtar A., Grummt I.;
"Reversible acetylation of the chromatin remodelling complex NoRC is
required for non-coding RNA-dependent silencing.";
Nat. Cell Biol. 11:1010-1016(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1397 AND SER-1783, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-1397; SER-1770
AND SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-1397; SER-1783
AND SER-1785, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; THR-548; SER-613;
SER-1397 AND SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1150, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[20]
INTERACTION WITH BEND3 AND USP21, UBIQUITINATION, AND
DEUBIQUITINATION.
PubMed=26100909; DOI=10.1073/pnas.1424705112;
Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K.,
Anantharaman A., Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V.,
Prasanth S.G.;
"BEND3 represses rDNA transcription by stabilizing a NoRC component
via USP21 deubiquitinase.";
Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-866; LYS-1150; LYS-1172;
LYS-1676 AND LYS-1709, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Essential component of the NoRC (nucleolar remodeling
complex) complex, a complex that mediates silencing of a fraction
of rDNA by recruiting histone-modifying enzymes and DNA
methyltransferases, leading to heterochromatin formation and
transcriptional silencing. In the complex, it plays a central role
by being recruited to rDNA and by targeting chromatin modifying
enzymes such as HDAC1, leading to repress RNA polymerase I
transcription. Recruited to rDNA via its interaction with TTF1 and
its ability to recognize and bind histone H4 acetylated on 'Lys-
16' (H4K16ac), leading to deacetylation of H4K5ac, H4K8ac, H4K12ac
but not H4K16ac. Specifically binds pRNAs, 150-250 nucleotide RNAs
that are complementary in sequence to the rDNA promoter; pRNA-
binding is required for heterochromatin formation and rDNA
silencing (By similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the NoRC complex, at least composed of
SMARCA5/SNF2H and BAZ2A/TIP5. Interacts with TTF1; required for
recruitment of the NoRC complex to rDNA. Interacts with DNMT1,
DNM3B, HDAC1 and SIN3A (By similarity). Interacts with BEND3 and
USP21. {ECO:0000250|UniProtKB:Q91YE5,
ECO:0000269|PubMed:26100909}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-934890, EBI-389883;
Q62187:Ttf1 (xeno); NbExp=3; IntAct=EBI-934890, EBI-11705418;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
Note=Colocalizes with the basal RNA polymerase I transcription
factor UBF in the nucleolus. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2;
IsoId=Q9UIF9-1; Sequence=Displayed;
Name=1;
IsoId=Q9UIF9-2; Sequence=VSP_037960, VSP_019111;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9UIF9-3; Sequence=VSP_037961;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at moderate levels in most tissues
analyzed, including heart, brain, placenta, lung, skeletal muscle,
kidney and pancreas.
-!- DOMAIN: The bromo domain and the PHD-type zinc finger recognize
and bind histone H4 acetylated on 'Lys-16' (H4K16ac). These 2
domains play a central role in the recruitment of chromatin
silencing proteins such as DNMT1, DNMT3B and HDAC1.
-!- DOMAIN: The MBD (methyl-CpG-binding) domain, also named TAM
domain, specifically recognizes and binds a conserved stem-loop
structure the association within pRNA. Binding to pRNA induces a
conformational change of BAZ2A/TIP5 and is essential for targeting
the NoRC complex to the nucleolus (By similarity). {ECO:0000250}.
-!- PTM: Acetylation at Lys-680 by KAT8/MOF promotes its dissociation
from pRNA, affecting heterochromatin formation, nucleosome
positioning and rDNA silencing. Deacetylation by SIRT1 in late S
phase enhances pRNA-binding, allowing de novo DNA methylation and
heterochromatin formation. Acetylation is high during S phase and
declines to background levels in late S phase when the silent
copies of rRNA genes are replicated (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated. Deubiquitinated by USP21 leading to its
stabilization. {ECO:0000269|PubMed:26100909}.
-!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB60864.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAG51228.1; Type=Erroneous termination; Positions=168; Note=Translated as Tyr.; Evidence={ECO:0000305};
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EMBL; AB032254; BAA89211.1; -; mRNA.
EMBL; CR749379; CAH18232.1; -; mRNA.
EMBL; AC090681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB002312; BAA20773.2; -; mRNA.
EMBL; AK023830; BAG51228.1; ALT_SEQ; mRNA.
EMBL; AF000422; AAB60864.1; ALT_SEQ; mRNA.
EMBL; BC008965; AAH08965.2; -; mRNA.
CCDS; CCDS44924.1; -. [Q9UIF9-1]
RefSeq; NP_038477.2; NM_013449.3. [Q9UIF9-1]
UniGene; Hs.314263; -.
PDB; 4LZ2; X-ray; 1.76 A; A=1796-1899.
PDB; 4Q6F; X-ray; 1.91 A; A/B/C/D=1673-1728.
PDB; 4QBM; X-ray; 1.65 A; A/B=1796-1899.
PDB; 4QF2; X-ray; 1.70 A; A/B/C/D=1673-1728.
PDB; 5AGQ; NMR; -; A=543-650.
PDB; 5MGJ; X-ray; 2.10 A; A=1796-1898.
PDB; 5MGK; X-ray; 2.30 A; A=1796-1898.
PDB; 5MGL; X-ray; 2.65 A; A=1796-1898.
PDB; 5MGM; X-ray; 2.80 A; A=1796-1898.
PDB; 5OR8; X-ray; 2.40 A; A=1796-1899.
PDB; 5T8R; X-ray; 2.40 A; A/B/C/D=1673-1728.
PDB; 6FAP; X-ray; 2.70 A; A/B/C/D=1673-1728.
PDB; 6FG6; X-ray; 2.40 A; A=1796-1898.
PDB; 6FGF; X-ray; 2.80 A; A=1796-1898.
PDB; 6FGG; X-ray; 1.10 A; A=1796-1899.
PDB; 6FGH; X-ray; 2.10 A; A=1796-1898.
PDB; 6FGI; X-ray; 2.55 A; A=1796-1898.
PDB; 6FGL; X-ray; 2.10 A; A=1796-1898.
PDB; 6FGV; X-ray; 2.50 A; A=1796-1899.
PDB; 6FGW; X-ray; 2.73 A; A=1796-1899.
PDB; 6FHU; X-ray; 2.00 A; A/B/C/D=1673-1728.
PDB; 6FI0; X-ray; 1.90 A; A/B/C/D=1673-1728.
PDB; 6FKP; X-ray; 2.00 A; A/B/C/D=1673-1728.
PDBsum; 4LZ2; -.
PDBsum; 4Q6F; -.
PDBsum; 4QBM; -.
PDBsum; 4QF2; -.
PDBsum; 5AGQ; -.
PDBsum; 5MGJ; -.
PDBsum; 5MGK; -.
PDBsum; 5MGL; -.
PDBsum; 5MGM; -.
PDBsum; 5OR8; -.
PDBsum; 5T8R; -.
PDBsum; 6FAP; -.
PDBsum; 6FG6; -.
PDBsum; 6FGF; -.
PDBsum; 6FGG; -.
PDBsum; 6FGH; -.
PDBsum; 6FGI; -.
PDBsum; 6FGL; -.
PDBsum; 6FGV; -.
PDBsum; 6FGW; -.
PDBsum; 6FHU; -.
PDBsum; 6FI0; -.
PDBsum; 6FKP; -.
ProteinModelPortal; Q9UIF9; -.
SMR; Q9UIF9; -.
BioGrid; 116346; 18.
ComplexPortal; CPX-432; NoRC complex.
CORUM; Q9UIF9; -.
IntAct; Q9UIF9; 9.
MINT; Q9UIF9; -.
STRING; 9606.ENSP00000446880; -.
BindingDB; Q9UIF9; -.
ChEMBL; CHEMBL3108642; -.
GuidetoPHARMACOLOGY; 2721; -.
iPTMnet; Q9UIF9; -.
PhosphoSitePlus; Q9UIF9; -.
BioMuta; BAZ2A; -.
DMDM; 257051081; -.
EPD; Q9UIF9; -.
PaxDb; Q9UIF9; -.
PeptideAtlas; Q9UIF9; -.
PRIDE; Q9UIF9; -.
ProteomicsDB; 84511; -.
ProteomicsDB; 84512; -. [Q9UIF9-2]
ProteomicsDB; 84513; -. [Q9UIF9-3]
DNASU; 11176; -.
Ensembl; ENST00000551812; ENSP00000446880; ENSG00000076108. [Q9UIF9-1]
GeneID; 11176; -.
KEGG; hsa:11176; -.
UCSC; uc001slq.2; human. [Q9UIF9-1]
CTD; 11176; -.
DisGeNET; 11176; -.
EuPathDB; HostDB:ENSG00000076108.11; -.
GeneCards; BAZ2A; -.
H-InvDB; HIX0010736; -.
HGNC; HGNC:962; BAZ2A.
HPA; HPA005782; -.
HPA; HPA063806; -.
MIM; 605682; gene.
neXtProt; NX_Q9UIF9; -.
OpenTargets; ENSG00000076108; -.
PharmGKB; PA25272; -.
eggNOG; KOG1245; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00920000148952; -.
HOGENOM; HOG000169644; -.
HOVERGEN; HBG107494; -.
InParanoid; Q9UIF9; -.
KO; K15224; -.
OMA; NYSQYPS; -.
OrthoDB; EOG091G00WO; -.
PhylomeDB; Q9UIF9; -.
TreeFam; TF329083; -.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
ChiTaRS; BAZ2A; human.
GeneWiki; BAZ2A; -.
GenomeRNAi; 11176; -.
PRO; PR:Q9UIF9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000076108; -.
CleanEx; HS_BAZ2A; -.
ExpressionAtlas; Q9UIF9; baseline and differential.
Genevisible; Q9UIF9; HS.
GO; GO:0005677; C:chromatin silencing complex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0033553; C:rDNA heterochromatin; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; NAS:BHF-UCL.
GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
GO; GO:0000183; P:chromatin silencing at rDNA; ISS:UniProtKB.
GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
CDD; cd05503; Bromo_BAZ2A_B_like; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR037374; BAZ2A/B_Bromo.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR018501; DDT_dom.
InterPro; IPR016177; DNA-bd_dom_sf.
InterPro; IPR001739; Methyl_CpG_DNA-bd.
InterPro; IPR028940; TIP5.
InterPro; IPR028942; WHIM1_dom.
InterPro; IPR028941; WHIM2_dom.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR22880:SF141; PTHR22880:SF141; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF02791; DDT; 1.
Pfam; PF01429; MBD; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF15612; WHIM1; 1.
Pfam; PF15613; WSD; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00384; AT_hook; 4.
SMART; SM00297; BROMO; 1.
SMART; SM00571; DDT; 1.
SMART; SM00391; MBD; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF54171; SSF54171; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS50827; DDT; 1.
PROSITE; PS50982; MBD; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Bromodomain;
Chromatin regulator; Coiled coil; Complete proteome; DNA-binding;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Repressor; RNA-binding; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1905 Bromodomain adjacent to zinc finger
domain protein 2A.
/FTId=PRO_0000211172.
DOMAIN 546 617 MBD. {ECO:0000255|PROSITE-
ProRule:PRU00338}.
DOMAIN 848 913 DDT. {ECO:0000255|PROSITE-
ProRule:PRU00063}.
DOMAIN 1810 1880 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DNA_BIND 649 661 A.T hook 1.
DNA_BIND 670 682 A.T hook 2.
DNA_BIND 1186 1198 A.T hook 3.
DNA_BIND 1404 1416 A.T hook 4.
ZN_FING 1676 1726 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
COILED 693 792 {ECO:0000255}.
COMPBIAS 660 799 Lys-rich.
COMPBIAS 1212 1277 Glu-rich.
COMPBIAS 1290 1411 Pro-rich.
COMPBIAS 1759 1762 Poly-Arg.
MOD_RES 507 507 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 509 509 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 548 548 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 680 680 N6-acetyllysine; by KAT8.
{ECO:0000269|PubMed:19578370}.
MOD_RES 799 799 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91YE5}.
MOD_RES 1051 1051 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE5}.
MOD_RES 1184 1184 Phosphoserine.
{ECO:0000250|UniProtKB:Q91YE5}.
MOD_RES 1397 1397 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1559 1559 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 1747 1747 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1770 1770 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1783 1783 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1785 1785 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 866 866 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1150 1150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1172 1172 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1676 1676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1709 1709 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 6 6 N -> NEAN (in isoform 1).
{ECO:0000303|PubMed:10662543}.
/FTId=VSP_037960.
VAR_SEQ 178 207 Missing (in isoform 1).
{ECO:0000303|PubMed:10662543}.
/FTId=VSP_019111.
VAR_SEQ 1434 1437 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_037961.
VARIANT 498 498 V -> E (in dbSNP:rs2230579).
/FTId=VAR_055548.
CONFLICT 106 106 N -> S (in Ref. 2; CAH18232).
{ECO:0000305}.
CONFLICT 148 148 E -> K (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 155 155 Q -> H (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 207 207 Q -> P (in Ref. 2; CAH18232).
{ECO:0000305}.
CONFLICT 210 210 G -> C (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 236 236 G -> C (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 503 503 A -> T (in Ref. 2; CAH18232).
{ECO:0000305}.
CONFLICT 601 601 V -> L (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 727 727 Q -> L (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 747 747 Q -> H (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 812 812 R -> K (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 978 978 L -> P (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1032 1033 EG -> GR (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1190 1190 G -> S (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1193 1193 R -> L (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1199 1199 S -> F (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1205 1205 L -> F (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1229 1229 A -> V (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1274 1274 S -> N (in Ref. 2; CAH18232).
{ECO:0000305}.
CONFLICT 1319 1319 P -> L (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1322 1322 L -> F (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1340 1340 P -> L (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1443 1443 R -> P (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1568 1568 R -> P (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1598 1598 E -> K (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1643 1643 V -> I (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1649 1649 E -> Q (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1656 1656 Q -> H (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1663 1663 Q -> H (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1766 1766 R -> K (in Ref. 1; BAA89211).
{ECO:0000305}.
CONFLICT 1781 1781 G -> R (in Ref. 1; BAA89211).
{ECO:0000305}.
HELIX 549 558 {ECO:0000244|PDB:5AGQ}.
STRAND 561 568 {ECO:0000244|PDB:5AGQ}.
STRAND 570 580 {ECO:0000244|PDB:5AGQ}.
STRAND 582 584 {ECO:0000244|PDB:5AGQ}.
HELIX 590 599 {ECO:0000244|PDB:5AGQ}.
HELIX 607 609 {ECO:0000244|PDB:5AGQ}.
STRAND 618 627 {ECO:0000244|PDB:5AGQ}.
STRAND 630 636 {ECO:0000244|PDB:5AGQ}.
TURN 638 640 {ECO:0000244|PDB:5AGQ}.
HELIX 641 648 {ECO:0000244|PDB:5AGQ}.
HELIX 1674 1676 {ECO:0000244|PDB:4Q6F}.
TURN 1680 1682 {ECO:0000244|PDB:4QF2}.
HELIX 1688 1690 {ECO:0000244|PDB:4QF2}.
STRAND 1691 1693 {ECO:0000244|PDB:4QF2}.
STRAND 1695 1698 {ECO:0000244|PDB:4QF2}.
STRAND 1700 1702 {ECO:0000244|PDB:4QF2}.
TURN 1703 1705 {ECO:0000244|PDB:4QF2}.
HELIX 1721 1724 {ECO:0000244|PDB:4QF2}.
HELIX 1796 1811 {ECO:0000244|PDB:4QBM}.
HELIX 1813 1818 {ECO:0000244|PDB:4QBM}.
TURN 1824 1826 {ECO:0000244|PDB:4QBM}.
HELIX 1830 1833 {ECO:0000244|PDB:4QBM}.
HELIX 1840 1848 {ECO:0000244|PDB:4QBM}.
HELIX 1855 1872 {ECO:0000244|PDB:4QBM}.
HELIX 1878 1894 {ECO:0000244|PDB:4QBM}.
HELIX 1895 1898 {ECO:0000244|PDB:4QBM}.
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


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