BAZ2B_HUMAN
ID BAZ2B_HUMAN Reviewed; 2168 AA.
AC Q9UIF8; D3DPA8; Q96EA1; Q96SQ8; Q9P252; Q9Y4N8;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 2B;
DE AltName: Full=hWALp4;
GN Name=BAZ2B; Synonyms=KIAA1476;
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 4).
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 5).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-967 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1720-2168 (ISOFORMS 1/2/3/4/5), AND VARIANTS
RP THR-71 AND SER-422.
RC TISSUE=Melanoma, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-986 (ISOFORM 2), AND VARIANT
RP SER-422.
RC TISSUE=Skeletal muscle;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 670-1411 (ISOFORM 3).
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 [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1462, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1680; THR-2014 AND SER-2019,
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1465 AND SER-1467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP FUNCTION, IDENTIFICATION IN THE BRF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE BRF-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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1425, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
RN [14]
RP STRUCTURE BY NMR OF 2062-2166.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the bromodomain from human bromodomain adjacent to
RT zinc finger domain 2B.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2054-2168, AND SUBUNIT.
RX PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA Gingras A.C., Arrowsmith C.H., Knapp S.;
RT "Histone recognition and large-scale structural analysis of the human
RT bromodomain family.";
RL Cell 149:214-231(2012).
CC -!- FUNCTION: Regulatory subunit of the ATP-dependent BRF-1 and BRF-5 ISWI
CC chromatin remodeling complexes, which form ordered nucleosome arrays on
CC chromatin and facilitate access to DNA during DNA-templated processes
CC such as DNA replication, transcription, and repair (PubMed:28801535).
CC Both complexes regulate the spacing of nucleosomes along the chromatin
CC and have the ability to slide mononucleosomes to the center of a DNA
CC template (PubMed:28801535). The BRF-1 ISWI chromatin remodeling complex
CC has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin
CC remodeling complex (PubMed:28801535). Chromatin reader protein, which
CC may play a role in transcriptional regulation via interaction with ISWI
CC (By similarity) (PubMed:10662543). Involved in positively modulating
CC the rate of age-related behavioral deterioration (By similarity).
CC Represses the expression of mitochondrial function-related genes,
CC perhaps by occupying their promoter regions, working in concert with
CC histone methyltransferase EHMT1 (By similarity).
CC {ECO:0000250|UniProtKB:A2AUY4, ECO:0000269|PubMed:28801535,
CC ECO:0000303|PubMed:10662543}.
CC -!- SUBUNIT: Component of the BRF-1 ISWI chromatin remodeling complex, at
CC least composed of SMARCA1 and BAZ2B, which regulates the spacing of
CC histone octamers on the DNA template to facilitate access to DNA
CC (PubMed:28801535). Within the BRF-1 ISWI chromatin remodeling complex
CC interacts with SMARCA1; the interaction is direct (PubMed:28801535).
CC Component of the BRF-5 ISWI chromatin remodeling complex, at least
CC composed of SMARCA5/SNF2H and BAZ2B, which regulates the spacing of
CC histone octamers on the DNA template to facilitate access to DNA
CC (PubMed:28801535). Within the BRF-5 ISWI chromatin remodeling complex
CC interacts with SMARCA5/SNF2H; the interaction is direct
CC (PubMed:28801535). Interacts with acetylated lysine residues on histone
CC H1.4, H2A, H2B, H3 and H4 (in vitro). Interacts with EHMT1 (By
CC similarity). {ECO:0000250|UniProtKB:A2AUY4,
CC ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:28801535}.
CC -!- INTERACTION:
CC Q9UIF8-2; P56545-3: CTBP2; NbExp=3; IntAct=EBI-10321972, EBI-10171902;
CC Q9UIF8-2; P51116: FXR2; NbExp=3; IntAct=EBI-10321972, EBI-740459;
CC Q9UIF8-2; Q96MF2: STAC3; NbExp=3; IntAct=EBI-10321972, EBI-745680;
CC Q9UIF8-2; O43829: ZBTB14; NbExp=3; IntAct=EBI-10321972, EBI-10176632;
CC Q9UIF8-2; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-10321972, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9UIF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIF8-2; Sequence=VSP_037115, VSP_000553;
CC Name=3;
CC IsoId=Q9UIF8-3; Sequence=VSP_000554;
CC Name=4;
CC IsoId=Q9UIF8-4; Sequence=VSP_037114;
CC Name=5;
CC IsoId=Q9UIF8-5; Sequence=VSP_037115, VSP_000554;
CC -!- TISSUE SPECIFICITY: Expressed at varying levels in several tissues,
CC whereas a smaller transcript was expressed specifically in testis.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12576.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH12576.1; Type=Miscellaneous discrepancy; Note=contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA96000.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55231.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB032255; BAA89212.1; -; mRNA.
DR EMBL; AB040909; BAA96000.2; ALT_INIT; mRNA.
DR EMBL; AL080173; CAB45759.1; -; mRNA.
DR EMBL; AL834381; CAD39044.2; -; mRNA.
DR EMBL; CH471058; EAX11404.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11405.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11407.1; -; Genomic_DNA.
DR EMBL; BC012576; AAH12576.1; ALT_SEQ; mRNA.
DR EMBL; AK027612; BAB55231.1; ALT_INIT; mRNA.
DR CCDS; CCDS2209.2; -. [Q9UIF8-1]
DR CCDS; CCDS74594.1; -. [Q9UIF8-5]
DR PIR; T12495; T12495.
DR RefSeq; NP_001276904.1; NM_001289975.1. [Q9UIF8-5]
DR RefSeq; NP_038478.2; NM_013450.3. [Q9UIF8-1]
DR PDB; 2E7O; NMR; -; A=2062-2166.
DR PDB; 3G0L; X-ray; 2.03 A; A=2054-2168.
DR PDB; 3Q2F; X-ray; 2.06 A; A=2054-2168.
DR PDB; 4CUP; X-ray; 1.88 A; A=2054-2168.
DR PDB; 4CUQ; X-ray; 2.11 A; A=2054-2168.
DR PDB; 4CUR; X-ray; 1.84 A; A=2054-2168.
DR PDB; 4CUS; X-ray; 1.78 A; A=2054-2168.
DR PDB; 4CUT; X-ray; 1.84 A; A=2054-2168.
DR PDB; 4CUU; X-ray; 1.80 A; A=2054-2168.
DR PDB; 4IR3; X-ray; 2.00 A; A=2054-2168.
DR PDB; 4IR4; X-ray; 2.05 A; A=2054-2168.
DR PDB; 4IR5; X-ray; 1.70 A; A=2054-2168.
DR PDB; 4IR6; X-ray; 1.80 A; A=2054-2168.
DR PDB; 4NR9; X-ray; 1.98 A; A=2054-2168.
DR PDB; 4NRA; X-ray; 1.85 A; A=2054-2168.
DR PDB; 4NRB; X-ray; 2.08 A; A=2054-2168.
DR PDB; 4NRC; X-ray; 1.86 A; A=2054-2168.
DR PDB; 4QC1; X-ray; 1.99 A; A/B=2062-2166.
DR PDB; 4QC3; X-ray; 1.60 A; A/B=2062-2166.
DR PDB; 4QF3; X-ray; 1.60 A; A/B=1928-1983.
DR PDB; 4RVR; X-ray; 1.98 A; A=2054-2168.
DR PDB; 4XUA; X-ray; 1.75 A; A=2054-2168.
DR PDB; 4XUB; X-ray; 1.98 A; A=2054-2168.
DR PDB; 5CQ3; X-ray; 1.93 A; A=2054-2168.
DR PDB; 5CQ4; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5CQ5; X-ray; 1.96 A; A=2054-2168.
DR PDB; 5CQ6; X-ray; 1.97 A; A=2054-2168.
DR PDB; 5CQ7; X-ray; 1.86 A; A=2054-2166.
DR PDB; 5CQ8; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5CQA; X-ray; 2.13 A; A=2054-2166.
DR PDB; 5CU8; X-ray; 2.05 A; A=2054-2166.
DR PDB; 5CUA; X-ray; 1.89 A; A=2054-2168.
DR PDB; 5CUB; X-ray; 2.10 A; A=2054-2166.
DR PDB; 5CUC; X-ray; 1.85 A; A=2054-2166.
DR PDB; 5CUD; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5CUE; X-ray; 2.08 A; A=2054-2166.
DR PDB; 5CUG; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5DYU; X-ray; 1.65 A; A=2054-2167.
DR PDB; 5DYX; X-ray; 1.85 A; A=2054-2167.
DR PDB; 5E73; X-ray; 1.71 A; A=2054-2167.
DR PDB; 5E74; X-ray; 1.78 A; A=2054-2167.
DR PDB; 5E9I; X-ray; 1.96 A; A=2054-2167.
DR PDB; 5E9K; X-ray; 2.07 A; A=2054-2167.
DR PDB; 5E9L; X-ray; 1.90 A; A=2054-2167.
DR PDB; 5E9M; X-ray; 1.78 A; A=2054-2167.
DR PDB; 5E9Y; X-ray; 1.65 A; A=2054-2167.
DR PDB; 5L8T; X-ray; 1.85 A; A=2054-2167.
DR PDB; 5L8U; X-ray; 1.85 A; A=2054-2167.
DR PDB; 5L96; X-ray; 2.15 A; A=2054-2167.
DR PDB; 5L97; X-ray; 2.05 A; A=2054-2167.
DR PDB; 5L98; X-ray; 2.26 A; A=2054-2167.
DR PDB; 5L99; X-ray; 2.00 A; A=2054-2167.
DR PDB; 5MGE; X-ray; 1.95 A; A=2054-2167.
DR PDB; 5MGF; X-ray; 1.90 A; A=2054-2167.
DR PDB; 5MGG; X-ray; 2.10 A; A=2054-2167.
DR PDB; 5OR9; X-ray; 2.00 A; A=2054-2168.
DR PDB; 5ORB; X-ray; 2.10 A; A=2054-2168.
DR PDB; 5PB7; X-ray; 1.66 A; A=2054-2168.
DR PDB; 5PB8; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PB9; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PBA; X-ray; 1.93 A; A=2054-2168.
DR PDB; 5PBB; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PBC; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PBD; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PBE; X-ray; 1.83 A; A=2054-2168.
DR PDB; 5PBF; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PBG; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PBH; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PBI; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PBJ; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PBK; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PBL; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PBM; X-ray; 1.67 A; A=2054-2168.
DR PDB; 5PBN; X-ray; 1.86 A; A=2054-2168.
DR PDB; 5PBO; X-ray; 1.95 A; A=2054-2168.
DR PDB; 5PBP; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PBQ; X-ray; 1.93 A; A=2054-2168.
DR PDB; 5PBR; X-ray; 1.81 A; A=2054-2168.
DR PDB; 5PBS; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PBT; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PBU; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PBV; X-ray; 1.74 A; A=2054-2168.
DR PDB; 5PBW; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PBX; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PBY; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PBZ; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PC0; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PC1; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PC2; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PC3; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PC4; X-ray; 1.86 A; A=2054-2168.
DR PDB; 5PC5; X-ray; 1.85 A; A=2054-2168.
DR PDB; 5PC6; X-ray; 1.74 A; A=2054-2168.
DR PDB; 5PC7; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PC8; X-ray; 1.85 A; A=2054-2168.
DR PDB; 5PC9; X-ray; 1.76 A; A=2054-2168.
DR PDB; 5PCA; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PCB; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PCC; X-ray; 1.83 A; A=2054-2168.
DR PDB; 5PCD; X-ray; 1.76 A; A=2054-2168.
DR PDB; 5PCE; X-ray; 2.16 A; A=2054-2168.
DR PDB; 5PCF; X-ray; 2.02 A; A=2054-2168.
DR PDB; 5PCG; X-ray; 1.98 A; A=2054-2168.
DR PDB; 5PCH; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PCI; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PCJ; X-ray; 1.97 A; A=2054-2168.
DR PDB; 5PCK; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PCL; X-ray; 2.19 A; A=2054-2168.
DR PDB; 5PCM; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PCN; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PCO; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PCP; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PCQ; X-ray; 2.29 A; A=2054-2168.
DR PDB; 5PCR; X-ray; 1.90 A; A=2054-2168.
DR PDB; 5PCS; X-ray; 1.83 A; A=2054-2168.
DR PDB; 5PCT; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PCU; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PCV; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PCW; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PCX; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PCZ; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PD0; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PD1; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PD2; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PD3; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PD4; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PD5; X-ray; 1.89 A; A=2054-2168.
DR PDB; 5PD6; X-ray; 2.01 A; A=2054-2168.
DR PDB; 5PD7; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PD8; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PD9; X-ray; 1.86 A; A=2054-2168.
DR PDB; 5PDA; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PDB; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PDC; X-ray; 1.74 A; A=2054-2168.
DR PDB; 5PDD; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PDE; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PDF; X-ray; 1.68 A; A=2054-2168.
DR PDB; 5PDG; X-ray; 1.63 A; A=2054-2168.
DR PDB; 5PDH; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PDI; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PDJ; X-ray; 1.84 A; A=2054-2168.
DR PDB; 5PDK; X-ray; 1.74 A; A=2054-2168.
DR PDB; 5PDL; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PDM; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PDN; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PDO; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PDP; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PDQ; X-ray; 2.26 A; A=2054-2168.
DR PDB; 5PDR; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PDS; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PDT; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PDU; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PDV; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PDW; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PDX; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PDY; X-ray; 1.93 A; A=2054-2168.
DR PDB; 5PDZ; X-ray; 1.90 A; A=2054-2168.
DR PDB; 5PE0; X-ray; 1.76 A; A=2054-2168.
DR PDB; 5PE1; X-ray; 1.91 A; A=2054-2168.
DR PDB; 5PE2; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PE3; X-ray; 1.76 A; A=2054-2168.
DR PDB; 5PE4; X-ray; 1.74 A; A=2054-2168.
DR PDB; 5PE5; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PE6; X-ray; 1.67 A; A=2054-2168.
DR PDB; 5PE7; X-ray; 1.81 A; A=2054-2168.
DR PDB; 5PE8; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PE9; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PEA; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PEB; X-ray; 2.11 A; A=2054-2168.
DR PDB; 5PEC; X-ray; 1.85 A; A=2054-2168.
DR PDB; 5PED; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PEE; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PEF; X-ray; 1.73 A; A=2054-2168.
DR PDB; 5PEG; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PEH; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PEI; X-ray; 1.66 A; A=2054-2168.
DR PDB; 5PEJ; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PEK; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PEL; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PEM; X-ray; 1.97 A; A=2054-2168.
DR PDB; 5PEN; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PEO; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PEQ; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PER; X-ray; 2.00 A; A=2054-2168.
DR PDB; 5PES; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PET; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PEU; X-ray; 1.90 A; A=2054-2168.
DR PDB; 5PEV; X-ray; 1.81 A; A=2054-2168.
DR PDB; 5PEW; X-ray; 1.77 A; A=2054-2168.
DR PDB; 5PEX; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PEY; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PEZ; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PF0; X-ray; 1.95 A; A=2054-2168.
DR PDB; 5PF1; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PF2; X-ray; 1.89 A; A=2054-2168.
DR PDB; 5PF3; X-ray; 1.83 A; A=2054-2168.
DR PDB; 5PF4; X-ray; 2.01 A; A=2054-2168.
DR PDB; 5PF5; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PF6; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PF7; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PF8; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PF9; X-ray; 1.91 A; A=2054-2168.
DR PDB; 5PFA; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PFB; X-ray; 1.80 A; A=2054-2168.
DR PDB; 5PFC; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PFD; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PFE; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PFF; X-ray; 1.96 A; A=2054-2168.
DR PDB; 5PFG; X-ray; 1.68 A; A=2054-2168.
DR PDB; 5PFH; X-ray; 1.66 A; A=2054-2168.
DR PDB; 5PFI; X-ray; 1.66 A; A=2054-2168.
DR PDB; 5PFJ; X-ray; 2.07 A; A=2054-2168.
DR PDB; 5PFL; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PFM; X-ray; 1.54 A; A=2054-2168.
DR PDB; 5PFN; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PFO; X-ray; 1.82 A; A=2054-2168.
DR PDB; 5PFP; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PFQ; X-ray; 1.78 A; A=2054-2168.
DR PDB; 5PFR; X-ray; 1.89 A; A=2054-2168.
DR PDB; 5PFS; X-ray; 2.00 A; A=2054-2168.
DR PDB; 5PFT; X-ray; 2.02 A; A=2054-2168.
DR PDB; 5PFU; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PFV; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PFW; X-ray; 1.64 A; A=2054-2168.
DR PDB; 5PFX; X-ray; 1.90 A; A=2054-2168.
DR PDB; 5PFY; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PFZ; X-ray; 1.72 A; A=2054-2168.
DR PDB; 5PG0; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PG1; X-ray; 1.49 A; A=2054-2168.
DR PDB; 5PG2; X-ray; 1.68 A; A=2054-2168.
DR PDB; 5PG3; X-ray; 1.66 A; A=2054-2168.
DR PDB; 5PG4; X-ray; 2.49 A; A=2054-2168.
DR PDB; 5PG5; X-ray; 1.75 A; A=2054-2168.
DR PDB; 5PG6; X-ray; 1.65 A; A=2054-2168.
DR PDB; 5PG7; X-ray; 1.96 A; A=2054-2168.
DR PDB; 5PG8; X-ray; 1.69 A; A=2054-2168.
DR PDB; 5PG9; X-ray; 1.62 A; A=2054-2168.
DR PDB; 5PGA; X-ray; 1.59 A; A=2054-2168.
DR PDB; 5PGB; X-ray; 1.57 A; A=2054-2168.
DR PDB; 5PGC; X-ray; 1.61 A; A=2054-2168.
DR PDB; 5PGD; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PGE; X-ray; 1.70 A; A=2054-2168.
DR PDB; 5PGF; X-ray; 1.82 A; A=2054-2168.
DR PDB; 5PGG; X-ray; 1.68 A; A=2054-2168.
DR PDB; 5PGH; X-ray; 1.93 A; A=2054-2168.
DR PDB; 5PGI; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PGJ; X-ray; 1.58 A; A=2054-2168.
DR PDB; 5PGK; X-ray; 1.83 A; A=2054-2168.
DR PDB; 5PGL; X-ray; 2.23 A; A=2054-2168.
DR PDB; 5PGN; X-ray; 1.79 A; A=2054-2168.
DR PDB; 5PGO; X-ray; 1.88 A; A=2054-2168.
DR PDB; 5PGP; X-ray; 1.76 A; A=2054-2168.
DR PDB; 5PGQ; X-ray; 1.71 A; A=2054-2168.
DR PDB; 5PGR; X-ray; 2.00 A; A=2054-2168.
DR PDB; 5PGS; X-ray; 1.64 A; A=2054-2168.
DR PDB; 5PGT; X-ray; 1.72 A; A=2054-2168.
DR PDB; 6FGT; X-ray; 2.00 A; A=2054-2168.
DR PDB; 6FGU; X-ray; 2.05 A; A=2054-2168.
DR PDB; 6FH6; X-ray; 2.08 A; A=2054-2168.
DR PDB; 6FH7; X-ray; 2.10 A; A=2054-2168.
DR PDB; 6FHQ; X-ray; 1.95 A; A/B=1928-1983.
DR PDB; 6FI1; X-ray; 2.70 A; A/B=1928-1983.
DR PDB; 7WIN; X-ray; 1.95 A; A/B=736-846.
DR PDBsum; 2E7O; -.
DR PDBsum; 3G0L; -.
DR PDBsum; 3Q2F; -.
DR PDBsum; 4CUP; -.
DR PDBsum; 4CUQ; -.
DR PDBsum; 4CUR; -.
DR PDBsum; 4CUS; -.
DR PDBsum; 4CUT; -.
DR PDBsum; 4CUU; -.
DR PDBsum; 4IR3; -.
DR PDBsum; 4IR4; -.
DR PDBsum; 4IR5; -.
DR PDBsum; 4IR6; -.
DR PDBsum; 4NR9; -.
DR PDBsum; 4NRA; -.
DR PDBsum; 4NRB; -.
DR PDBsum; 4NRC; -.
DR PDBsum; 4QC1; -.
DR PDBsum; 4QC3; -.
DR PDBsum; 4QF3; -.
DR PDBsum; 4RVR; -.
DR PDBsum; 4XUA; -.
DR PDBsum; 4XUB; -.
DR PDBsum; 5CQ3; -.
DR PDBsum; 5CQ4; -.
DR PDBsum; 5CQ5; -.
DR PDBsum; 5CQ6; -.
DR PDBsum; 5CQ7; -.
DR PDBsum; 5CQ8; -.
DR PDBsum; 5CQA; -.
DR PDBsum; 5CU8; -.
DR PDBsum; 5CUA; -.
DR PDBsum; 5CUB; -.
DR PDBsum; 5CUC; -.
DR PDBsum; 5CUD; -.
DR PDBsum; 5CUE; -.
DR PDBsum; 5CUG; -.
DR PDBsum; 5DYU; -.
DR PDBsum; 5DYX; -.
DR PDBsum; 5E73; -.
DR PDBsum; 5E74; -.
DR PDBsum; 5E9I; -.
DR PDBsum; 5E9K; -.
DR PDBsum; 5E9L; -.
DR PDBsum; 5E9M; -.
DR PDBsum; 5E9Y; -.
DR PDBsum; 5L8T; -.
DR PDBsum; 5L8U; -.
DR PDBsum; 5L96; -.
DR PDBsum; 5L97; -.
DR PDBsum; 5L98; -.
DR PDBsum; 5L99; -.
DR PDBsum; 5MGE; -.
DR PDBsum; 5MGF; -.
DR PDBsum; 5MGG; -.
DR PDBsum; 5OR9; -.
DR PDBsum; 5ORB; -.
DR PDBsum; 5PB7; -.
DR PDBsum; 5PB8; -.
DR PDBsum; 5PB9; -.
DR PDBsum; 5PBA; -.
DR PDBsum; 5PBB; -.
DR PDBsum; 5PBC; -.
DR PDBsum; 5PBD; -.
DR PDBsum; 5PBE; -.
DR PDBsum; 5PBF; -.
DR PDBsum; 5PBG; -.
DR PDBsum; 5PBH; -.
DR PDBsum; 5PBI; -.
DR PDBsum; 5PBJ; -.
DR PDBsum; 5PBK; -.
DR PDBsum; 5PBL; -.
DR PDBsum; 5PBM; -.
DR PDBsum; 5PBN; -.
DR PDBsum; 5PBO; -.
DR PDBsum; 5PBP; -.
DR PDBsum; 5PBQ; -.
DR PDBsum; 5PBR; -.
DR PDBsum; 5PBS; -.
DR PDBsum; 5PBT; -.
DR PDBsum; 5PBU; -.
DR PDBsum; 5PBV; -.
DR PDBsum; 5PBW; -.
DR PDBsum; 5PBX; -.
DR PDBsum; 5PBY; -.
DR PDBsum; 5PBZ; -.
DR PDBsum; 5PC0; -.
DR PDBsum; 5PC1; -.
DR PDBsum; 5PC2; -.
DR PDBsum; 5PC3; -.
DR PDBsum; 5PC4; -.
DR PDBsum; 5PC5; -.
DR PDBsum; 5PC6; -.
DR PDBsum; 5PC7; -.
DR PDBsum; 5PC8; -.
DR PDBsum; 5PC9; -.
DR PDBsum; 5PCA; -.
DR PDBsum; 5PCB; -.
DR PDBsum; 5PCC; -.
DR PDBsum; 5PCD; -.
DR PDBsum; 5PCE; -.
DR PDBsum; 5PCF; -.
DR PDBsum; 5PCG; -.
DR PDBsum; 5PCH; -.
DR PDBsum; 5PCI; -.
DR PDBsum; 5PCJ; -.
DR PDBsum; 5PCK; -.
DR PDBsum; 5PCL; -.
DR PDBsum; 5PCM; -.
DR PDBsum; 5PCN; -.
DR PDBsum; 5PCO; -.
DR PDBsum; 5PCP; -.
DR PDBsum; 5PCQ; -.
DR PDBsum; 5PCR; -.
DR PDBsum; 5PCS; -.
DR PDBsum; 5PCT; -.
DR PDBsum; 5PCU; -.
DR PDBsum; 5PCV; -.
DR PDBsum; 5PCW; -.
DR PDBsum; 5PCX; -.
DR PDBsum; 5PCZ; -.
DR PDBsum; 5PD0; -.
DR PDBsum; 5PD1; -.
DR PDBsum; 5PD2; -.
DR PDBsum; 5PD3; -.
DR PDBsum; 5PD4; -.
DR PDBsum; 5PD5; -.
DR PDBsum; 5PD6; -.
DR PDBsum; 5PD7; -.
DR PDBsum; 5PD8; -.
DR PDBsum; 5PD9; -.
DR PDBsum; 5PDA; -.
DR PDBsum; 5PDB; -.
DR PDBsum; 5PDC; -.
DR PDBsum; 5PDD; -.
DR PDBsum; 5PDE; -.
DR PDBsum; 5PDF; -.
DR PDBsum; 5PDG; -.
DR PDBsum; 5PDH; -.
DR PDBsum; 5PDI; -.
DR PDBsum; 5PDJ; -.
DR PDBsum; 5PDK; -.
DR PDBsum; 5PDL; -.
DR PDBsum; 5PDM; -.
DR PDBsum; 5PDN; -.
DR PDBsum; 5PDO; -.
DR PDBsum; 5PDP; -.
DR PDBsum; 5PDQ; -.
DR PDBsum; 5PDR; -.
DR PDBsum; 5PDS; -.
DR PDBsum; 5PDT; -.
DR PDBsum; 5PDU; -.
DR PDBsum; 5PDV; -.
DR PDBsum; 5PDW; -.
DR PDBsum; 5PDX; -.
DR PDBsum; 5PDY; -.
DR PDBsum; 5PDZ; -.
DR PDBsum; 5PE0; -.
DR PDBsum; 5PE1; -.
DR PDBsum; 5PE2; -.
DR PDBsum; 5PE3; -.
DR PDBsum; 5PE4; -.
DR PDBsum; 5PE5; -.
DR PDBsum; 5PE6; -.
DR PDBsum; 5PE7; -.
DR PDBsum; 5PE8; -.
DR PDBsum; 5PE9; -.
DR PDBsum; 5PEA; -.
DR PDBsum; 5PEB; -.
DR PDBsum; 5PEC; -.
DR PDBsum; 5PED; -.
DR PDBsum; 5PEE; -.
DR PDBsum; 5PEF; -.
DR PDBsum; 5PEG; -.
DR PDBsum; 5PEH; -.
DR PDBsum; 5PEI; -.
DR PDBsum; 5PEJ; -.
DR PDBsum; 5PEK; -.
DR PDBsum; 5PEL; -.
DR PDBsum; 5PEM; -.
DR PDBsum; 5PEN; -.
DR PDBsum; 5PEO; -.
DR PDBsum; 5PEQ; -.
DR PDBsum; 5PER; -.
DR PDBsum; 5PES; -.
DR PDBsum; 5PET; -.
DR PDBsum; 5PEU; -.
DR PDBsum; 5PEV; -.
DR PDBsum; 5PEW; -.
DR PDBsum; 5PEX; -.
DR PDBsum; 5PEY; -.
DR PDBsum; 5PEZ; -.
DR PDBsum; 5PF0; -.
DR PDBsum; 5PF1; -.
DR PDBsum; 5PF2; -.
DR PDBsum; 5PF3; -.
DR PDBsum; 5PF4; -.
DR PDBsum; 5PF5; -.
DR PDBsum; 5PF6; -.
DR PDBsum; 5PF7; -.
DR PDBsum; 5PF8; -.
DR PDBsum; 5PF9; -.
DR PDBsum; 5PFA; -.
DR PDBsum; 5PFB; -.
DR PDBsum; 5PFC; -.
DR PDBsum; 5PFD; -.
DR PDBsum; 5PFE; -.
DR PDBsum; 5PFF; -.
DR PDBsum; 5PFG; -.
DR PDBsum; 5PFH; -.
DR PDBsum; 5PFI; -.
DR PDBsum; 5PFJ; -.
DR PDBsum; 5PFL; -.
DR PDBsum; 5PFM; -.
DR PDBsum; 5PFN; -.
DR PDBsum; 5PFO; -.
DR PDBsum; 5PFP; -.
DR PDBsum; 5PFQ; -.
DR PDBsum; 5PFR; -.
DR PDBsum; 5PFS; -.
DR PDBsum; 5PFT; -.
DR PDBsum; 5PFU; -.
DR PDBsum; 5PFV; -.
DR PDBsum; 5PFW; -.
DR PDBsum; 5PFX; -.
DR PDBsum; 5PFY; -.
DR PDBsum; 5PFZ; -.
DR PDBsum; 5PG0; -.
DR PDBsum; 5PG1; -.
DR PDBsum; 5PG2; -.
DR PDBsum; 5PG3; -.
DR PDBsum; 5PG4; -.
DR PDBsum; 5PG5; -.
DR PDBsum; 5PG6; -.
DR PDBsum; 5PG7; -.
DR PDBsum; 5PG8; -.
DR PDBsum; 5PG9; -.
DR PDBsum; 5PGA; -.
DR PDBsum; 5PGB; -.
DR PDBsum; 5PGC; -.
DR PDBsum; 5PGD; -.
DR PDBsum; 5PGE; -.
DR PDBsum; 5PGF; -.
DR PDBsum; 5PGG; -.
DR PDBsum; 5PGH; -.
DR PDBsum; 5PGI; -.
DR PDBsum; 5PGJ; -.
DR PDBsum; 5PGK; -.
DR PDBsum; 5PGL; -.
DR PDBsum; 5PGN; -.
DR PDBsum; 5PGO; -.
DR PDBsum; 5PGP; -.
DR PDBsum; 5PGQ; -.
DR PDBsum; 5PGR; -.
DR PDBsum; 5PGS; -.
DR PDBsum; 5PGT; -.
DR PDBsum; 6FGT; -.
DR PDBsum; 6FGU; -.
DR PDBsum; 6FH6; -.
DR PDBsum; 6FH7; -.
DR PDBsum; 6FHQ; -.
DR PDBsum; 6FI1; -.
DR PDBsum; 7WIN; -.
DR AlphaFoldDB; Q9UIF8; -.
DR SMR; Q9UIF8; -.
DR BioGRID; 119019; 37.
DR IntAct; Q9UIF8; 25.
DR MINT; Q9UIF8; -.
DR STRING; 9606.ENSP00000376534; -.
DR BindingDB; Q9UIF8; -.
DR ChEMBL; CHEMBL1741220; -.
DR GuidetoPHARMACOLOGY; 2722; -.
DR GlyGen; Q9UIF8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UIF8; -.
DR PhosphoSitePlus; Q9UIF8; -.
DR BioMuta; BAZ2B; -.
DR DMDM; 229462995; -.
DR EPD; Q9UIF8; -.
DR jPOST; Q9UIF8; -.
DR MassIVE; Q9UIF8; -.
DR MaxQB; Q9UIF8; -.
DR PaxDb; Q9UIF8; -.
DR PeptideAtlas; Q9UIF8; -.
DR PRIDE; Q9UIF8; -.
DR ProteomicsDB; 84506; -. [Q9UIF8-1]
DR ProteomicsDB; 84507; -. [Q9UIF8-2]
DR ProteomicsDB; 84508; -. [Q9UIF8-3]
DR ProteomicsDB; 84509; -. [Q9UIF8-4]
DR ProteomicsDB; 84510; -. [Q9UIF8-5]
DR ABCD; Q9UIF8; 1 sequenced antibody.
DR Antibodypedia; 19022; 136 antibodies from 27 providers.
DR DNASU; 29994; -.
DR Ensembl; ENST00000392782.5; ENSP00000376533.1; ENSG00000123636.19. [Q9UIF8-5]
DR Ensembl; ENST00000392783.7; ENSP00000376534.2; ENSG00000123636.19. [Q9UIF8-1]
DR GeneID; 29994; -.
DR KEGG; hsa:29994; -.
DR MANE-Select; ENST00000392783.7; ENSP00000376534.2; NM_013450.4; NP_038478.2.
DR UCSC; uc002uao.4; human. [Q9UIF8-1]
DR CTD; 29994; -.
DR DisGeNET; 29994; -.
DR GeneCards; BAZ2B; -.
DR HGNC; HGNC:963; BAZ2B.
DR HPA; ENSG00000123636; Low tissue specificity.
DR MalaCards; BAZ2B; -.
DR MIM; 605683; gene.
DR neXtProt; NX_Q9UIF8; -.
DR OpenTargets; ENSG00000123636; -.
DR PharmGKB; PA25273; -.
DR VEuPathDB; HostDB:ENSG00000123636; -.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000155359; -.
DR HOGENOM; CLU_000899_0_0_1; -.
DR InParanoid; Q9UIF8; -.
DR OMA; IHIGKAP; -.
DR OrthoDB; 200493at2759; -.
DR PhylomeDB; Q9UIF8; -.
DR TreeFam; TF329083; -.
DR PathwayCommons; Q9UIF8; -.
DR SignaLink; Q9UIF8; -.
DR SIGNOR; Q9UIF8; -.
DR BioGRID-ORCS; 29994; 18 hits in 1094 CRISPR screens.
DR ChiTaRS; BAZ2B; human.
DR EvolutionaryTrace; Q9UIF8; -.
DR GenomeRNAi; 29994; -.
DR Pharos; Q9UIF8; Tchem.
DR PRO; PR:Q9UIF8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UIF8; protein.
DR Bgee; ENSG00000123636; Expressed in sural nerve and 201 other tissues.
DR ExpressionAtlas; Q9UIF8; baseline and differential.
DR Genevisible; Q9UIF8; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
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; 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 Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
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; Coiled coil;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2168
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 2B"
FT /id="PRO_0000211174"
FT DOMAIN 739..810
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 1087..1152
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 2077..2147
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1931..1981
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1998..2040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..1061
FT /evidence="ECO:0000255"
FT COILED 1334..1375
FT /evidence="ECO:0000255"
FT COMPBIAS 144..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2014
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 1425
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..196
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10662543"
FT /id="VSP_037114"
FT VAR_SEQ 112..113
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10819331,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037115"
FT VAR_SEQ 633..730
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000553"
FT VAR_SEQ 789..822
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10819331,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_000554"
FT VARIANT 71
FT /note="M -> T (in dbSNP:rs10202670)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_055549"
FT VARIANT 422
FT /note="L -> S (in dbSNP:rs3213790)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_055550"
FT VARIANT 530
FT /note="P -> L (in dbSNP:rs3732287)"
FT /id="VAR_055551"
FT VARIANT 702
FT /note="G -> V (in dbSNP:rs2302924)"
FT /id="VAR_055552"
FT VARIANT 2024
FT /note="S -> N (in dbSNP:rs415793)"
FT /id="VAR_055553"
FT CONFLICT 95
FT /note="L -> G (in Ref. 6; AAH12576)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="S -> F (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="G -> E (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="E -> K (in Ref. 6; AAH12576)"
FT /evidence="ECO:0000305"
FT CONFLICT 986
FT /note="R -> Q (in Ref. 6; AAH12576)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="K -> Q (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 1379
FT /note="Q -> P (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 1391
FT /note="Q -> R (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 1649
FT /note="S -> L (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT CONFLICT 2034
FT /note="K -> Q (in Ref. 1; BAA89212)"
FT /evidence="ECO:0000305"
FT TURN 1935..1937
FT /evidence="ECO:0007829|PDB:4QF3"
FT HELIX 1943..1945
FT /evidence="ECO:0007829|PDB:4QF3"
FT STRAND 1946..1949
FT /evidence="ECO:0007829|PDB:4QF3"
FT TURN 1950..1952
FT /evidence="ECO:0007829|PDB:4QF3"
FT STRAND 1955..1957
FT /evidence="ECO:0007829|PDB:4QF3"
FT TURN 1958..1960
FT /evidence="ECO:0007829|PDB:4QF3"
FT STRAND 1961..1963
FT /evidence="ECO:0007829|PDB:4QF3"
FT HELIX 1976..1982
FT /evidence="ECO:0007829|PDB:4QF3"
FT HELIX 2065..2078
FT /evidence="ECO:0007829|PDB:5PG1"
FT HELIX 2080..2082
FT /evidence="ECO:0007829|PDB:5PE8"
FT HELIX 2083..2085
FT /evidence="ECO:0007829|PDB:5PG1"
FT TURN 2091..2093
FT /evidence="ECO:0007829|PDB:5PG1"
FT STRAND 2094..2096
FT /evidence="ECO:0007829|PDB:2E7O"
FT HELIX 2097..2100
FT /evidence="ECO:0007829|PDB:5PG1"
FT HELIX 2107..2115
FT /evidence="ECO:0007829|PDB:5PG1"
FT HELIX 2122..2139
FT /evidence="ECO:0007829|PDB:5PG1"
FT STRAND 2142..2144
FT /evidence="ECO:0007829|PDB:5PG1"
FT HELIX 2145..2165
FT /evidence="ECO:0007829|PDB:5PG1"
SQ SEQUENCE 2168 AA; 240459 MW; C64EEEE6243CF779 CRC64;
MESGERLPSS AASSTTPTSS STPSVASVVS KGGLSTGVAS LSSTINPCGH LFRTAGDQPF
NLSTVSSAFP MVSHPVFGLH SASSGHSEFG GLGTLGTPTA LAAHPQLASF PGAEWWRTTD
AHTRTGATFF PPLLGIPPLF APPAQNHDSS SFHSRTSGKS NRNGPEKGVN GSINGSNTSS
VIGINTSVLS TTASSSMGQT KSTSSGGGNR KCNQEQSKNQ PLDARVDKIK DKKPRKKAME
SSSNSDSDSG TSSDTSSEGI SSSDSDDLEE DEEEEDQSIE ESEDDDSDSE SEAQHKSNNQ
VLLHGISDPK ADGQKATEKA QEKRIHQPLP LASESQTHSF QSQQKQPQVL SQQLPFIFQS
SQAKEESVNK HTSVIQSTGL VSNVKPLSLV NQAKKETYMK LIVPSPDVLK AGNKNTSEES
SLLTSELRSK REQYKQAFPS QLKKQESSKS LKKVIAALSN PKATSSSPAH PKQTLENNHP
NPFLTNALLG NHQPNGVIQS VIQEAPLALT TKTKMQSKIN ENIAAASSTP FSSPVNLSTS
GRRTPGNQTP VMPSASPILH SQGKEKAVSN NVNPVKTQHH SHPAKSLVEQ FRGTDSDIPS
SKDSEDSNED EEEDDEEEDE EDDEDDESDD SQSESDSNSE SDTEGSEEED DDDKDQDESD
SDTEGEKTSM KLNKTTSSVK SPSMSLTGHS TPRNLHIAKA PGSAPAALCS ESQSPAFLGT
SSSTLTSSPH SGTSKRRRVT DERELRIPLE YGWQRETRIR NFGGRLQGEV AYYAPCGKKL
RQYPEVIKYL SRNGIMDISR DNFSFSAKIR VGDFYEARDG PQGMQWCLLK EEDVIPRIRA
MEGRRGRPPN PDRQRAREES RMRRRKGRPP NVGNAEFLDN ADAKLLRKLQ AQEIARQAAQ
IKLLRKLQKQ EQARVAKEAK KQQAIMAAEE KRKQKEQIKI MKQQEKIKRI QQIRMEKELR
AQQILEAKKK KKEEAANAKL LEAEKRIKEK EMRRQQAVLL KHQERERRRQ HMMLMKAMEA
RKKAEEKERL KQEKRDEKRL NKERKLEQRR LELEMAKELK KPNEDMCLAD QKPLPELPRI
PGLVLSGSTF SDCLMVVQFL RNFGKVLGFD VNIDVPNLSV LQEGLLNIGD SMGEVQDLLV
RLLSAAVCDP GLITGYKAKT ALGEHLLNVG VNRDNVSEIL QIFMEAHCGQ TELTESLKTK
AFQAHTPAQK ASVLAFLINE LACSKSVVSE IDKNIDYMSN LRRDKWVVEG KLRKLRIIHA
KKTGKRDTSG GIDLGEEQHP LGTPTPGRKR RRKGGDSDYD DDDDDDSDDQ GDEDDEDEED
KEDKKGKKTD ICEDEDEGDQ AASVEELEKQ IEKLSKQQSQ YRRKLFDASH SLRSVMFGQD
RYRRRYWILP QCGGIFVEGM ESGEGLEEIA KEREKLKKAE SVQIKEEMFE TSGDSLNCSN
TDHCEQKEDL KEKDNTNLFL QKPGSFSKLS KLLEVAKMPP ESEVMTPKPN AGANGCTLSY
QNSGKHSLGS VQSTATQSNV EKADSNNLFN TGSSGPGKFY SPLPNDQLLK TLTEKNRQWF
SLLPRTPCDD TSLTHADMST ASLVTPQSQP PSKSPSPTPA PLGSSAQNPV GLNPFALSPL
QVKGGVSMMG LQFCGWPTGV VTSNIPFTSS VPSLGSGLGL SEGNGNSFLT SNVASSKSES
PVPQNEKATS AQPAAVEVAK PVDFPSPKPI PEEMQFGWWR IIDPEDLKAL LKVLHLRGIR
EKALQKQIQK HLDYITQACL KNKDVAIIEL NENEENQVTR DIVENWSVEE QAMEMDLSVL
QQVEDLERRV ASASLQVKGW MCPEPASERE DLVYFEHKSF TKLCKEHDGE FTGEDESSAH
ALERKSDNPL DIAVTRLADL ERNIERRIEE DIAPGLRVWR RALSEARSAA QVALCIQQLQ
KSIAWEKSIM KVYCQICRKG DNEELLLLCD GCDKGCHTYC HRPKITTIPD GDWFCPACIA
KASGQTLKIK KLHVKGKKTN ESKKGKKVTL TGDTEDEDSA STSSSLKRGN KDLKKRKMEE
NTSINLSKQE SFTSVKKPKR DDSKDLALCS MILTEMETHE DAWPFLLPVN LKLVPGYKKV
IKKPMDFSTI REKLSSGQYP NLETFALDVR LVFDNCETFN EDDSDIGRAG HNMRKYFEKK
WTDTFKVS
