BAZ2B_MOUSE
ID BAZ2B_MOUSE Reviewed; 2123 AA.
AC A2AUY4; B9EKB5; Q8C0K4; Q8CFP4;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 2B {ECO:0000305};
GN Name=Baz2b {ECO:0000312|MGI:MGI:2442782};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAC27164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-861 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC27164.1};
RC TISSUE=Thymus {ECO:0000312|EMBL:BAC27164.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAI50815.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1943-2123 (ISOFORMS 1/2).
RC TISSUE=Eye {ECO:0000312|EMBL:AAH42646.1}, and
RC Testis {ECO:0000312|EMBL:AAI50815.1};
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 [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH EHMT1.
RX PubMed=32103178; DOI=10.1038/s41586-020-2037-y;
RA Yuan J., Chang S.Y., Yin S.G., Liu Z.Y., Cheng X., Liu X.J., Jiang Q.,
RA Gao G., Lin D.Y., Kang X.L., Ye S.W., Chen Z., Yin J.A., Hao P., Jiang L.,
RA Cai S.Q.;
RT "Two conserved epigenetic regulators prevent healthy ageing.";
RL Nature 579:118-122(2020).
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 (By similarity).
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 (By similarity). The BRF-1 ISWI chromatin remodeling complex
CC has a lower ATP hydrolysis rate than the BRF-5 ISWI chromatin
CC remodeling complex (By similarity). Chromatin reader protein, involved
CC in positively modulating the rate of age-related behavioral
CC deterioration (PubMed:32103178). Represses the expression of
CC mitochondrial function-related genes, perhaps by occupying their
CC promoter regions, working in concert with histone methyltransferase
CC EHMT1 (PubMed:32103178). {ECO:0000250|UniProtKB:Q9UIF8,
CC ECO:0000269|PubMed:32103178}.
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 (By
CC similarity). Within the BRF-1 ISWI chromatin remodeling complex
CC interacts with SMARCA1; the interaction is direct (By similarity).
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 (By
CC similarity). Within the BRF-5 ISWI chromatin remodeling complex
CC interacts with SMARCA5/SNF2H; the interaction is direct (By
CC similarity). Interacts with acetylated lysine residues on histone H1.4,
CC H2A, H2B, H3 and H4 (in vitro) (By similarity). Interacts with EHMT1
CC (PubMed:32103178). {ECO:0000250|UniProtKB:Q9UIF8,
CC ECO:0000269|PubMed:32103178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=A2AUY4-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=A2AUY4-2; Sequence=VSP_060916, VSP_060917, VSP_060918;
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH42646.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK030867; BAC27164.1; -; mRNA.
DR EMBL; AL929211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042646; AAH42646.1; ALT_INIT; mRNA.
DR EMBL; BC150814; AAI50815.1; -; mRNA.
DR CCDS; CCDS16056.1; -. [A2AUY4-1]
DR RefSeq; NP_001001182.2; NM_001001182.3. [A2AUY4-1]
DR RefSeq; XP_017174584.1; XM_017319095.1. [A2AUY4-2]
DR RefSeq; XP_017174585.1; XM_017319096.1. [A2AUY4-2]
DR RefSeq; XP_017174591.1; XM_017319102.1.
DR AlphaFoldDB; A2AUY4; -.
DR SMR; A2AUY4; -.
DR IntAct; A2AUY4; 4.
DR STRING; 10090.ENSMUSP00000108169; -.
DR PhosphoSitePlus; A2AUY4; -.
DR EPD; A2AUY4; -.
DR jPOST; A2AUY4; -.
DR MaxQB; A2AUY4; -.
DR PaxDb; A2AUY4; -.
DR PeptideAtlas; A2AUY4; -.
DR PRIDE; A2AUY4; -.
DR ProteomicsDB; 343345; -.
DR Antibodypedia; 19022; 136 antibodies from 27 providers.
DR DNASU; 407823; -.
DR Ensembl; ENSMUST00000090925; ENSMUSP00000088443; ENSMUSG00000026987. [A2AUY4-1]
DR Ensembl; ENSMUST00000112550; ENSMUSP00000108169; ENSMUSG00000026987. [A2AUY4-1]
DR GeneID; 407823; -.
DR KEGG; mmu:407823; -.
DR UCSC; uc008jtr.1; mouse. [A2AUY4-1]
DR CTD; 29994; -.
DR MGI; MGI:2442782; Baz2b.
DR VEuPathDB; HostDB:ENSMUSG00000026987; -.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000155359; -.
DR HOGENOM; CLU_000899_0_0_1; -.
DR InParanoid; A2AUY4; -.
DR OMA; PRGLNNW; -.
DR OrthoDB; 200493at2759; -.
DR PhylomeDB; A2AUY4; -.
DR TreeFam; TF329083; -.
DR BioGRID-ORCS; 407823; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Baz2b; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AUY4; protein.
DR Bgee; ENSMUSG00000026987; Expressed in retinal neural layer and 255 other tissues.
DR ExpressionAtlas; A2AUY4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Alternative splicing; Bromodomain; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2123
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 2B"
FT /id="PRO_0000452177"
FT DOMAIN 690..765
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 1004..1069
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 2032..2102
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1886..1936
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1254..1281
FT /evidence="ECO:0000255"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1404..1444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1983..1998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 67
FT /note="A -> HLFRAAGDQPFNLSTVPSAFPMLSHPGFGLHSASSGHSEFGGLGTLG
FT TPTALAAHPQLTSFP (in isoform 2)"
FT /id="VSP_060916"
FT VAR_SEQ 920
FT /note="Q -> QELERHRLDM (in isoform 2)"
FT /id="VSP_060917"
FT VAR_SEQ 1808..1842
FT /note="Missing (in isoform 2)"
FT /id="VSP_060918"
FT CONFLICT 107
FT /note="S -> P (in Ref. 3; AAI50815)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="Q -> R (in Ref. 1; BAC27164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2123 AA; 234001 MW; FE9A0B249BD82217 CRC64;
MESGELLPSS PASSTTPTSS SAPSVASAVS KSSLSTGAAS LSSTASPCVL EAGKSKIKVS
PDSVSGAEWW RTTDGHSRAG TPFFPPLLGI PPLFAPPAQN HDSSFHSRTS GKSSRNGPEK
GINGSVNGTS AASVLGVNAS VVATPASSSM GQNQSTSSGG GTLKCHQEQN KSQPVDARAD
RIKDKKPRKK AMESSSNSDS DSGTSSDTSS EGISSSDSDD LEEEEEEDQS VEESEDDDSD
SETEAQHKSN NQVLLHGISD PKTDGQKATE KAQERRTHQP LPPVSESQTH PPFQSQQKQP
QVLSQQLPFI FQSSQAKEES VTKHTSVIQS TGLVSNVKPL SLVNQAKKET YRKLVVPSPD
VLKAGNKNTS EESSSLTSEL RSKREQYKQT FPSQGKKQEM GKSLKKVIAA LSNTKATSSS
PAHPKLPLDN NHPNPFLTNA LLGNHQPNGV IQSVIQEAPL ALTTKTKMQS KINENVSSST
PFSSPVNLST SGRRAPGSQT PALPSASPIL HSSGKEKRVS NDATPLKAHH HPHPAAAAAA
LVEQFRGTDS DVPSSKDSED SNEDEEEDDE EEDEEDDEDD ESDDSQSESD SNSQSDSEGS
EDDEEKDQEE SDSDTEGEKP AVNLTQTSSS AKSPPSSLTA HSAPHLHIGS PPGSAPAALC
SESQPPAFLG TSSSTLTSTP HSGTSKRRRV ADDQELRIPL DYGWQRETRV RNFGGRLPGE
VAYYAPCGKK LRQCPDMVKG MQWCLLKEED VIPRIRAMDG RRGRPPNPDR PRAREESRMK
RRKGRPPNVG SAEFLDNTDA KLLRKLQAQE IARQAAQIKL LRKLQKQEQA RVAKEAKKQQ
AIMAAEEKRK QKEQMKIIKQ QEKIKRIQQI RMEKELRAQQ ILEAKKKKKE EAANAKLLEA
EKRTKEKELR RQQAVLLKHQ ERERRRQHVM LMKAMEARKK AEEKERLKQE KRDEKRLNKE
RKLEQRRLEL EMAKELKKPK EDMCLADQKP LPEWPRIPGL VLSGTTFSDC LMVVQFLRNF
GKVLGFDVNI DVPNLSVLQE GLLNIGDSMG EVQDLLVRLL SAAVCDPGLI TGYKAKTALG
EHLLNVGVNR DNVSEVLQIF MEAHCGQTEL TESLKTKAFQ AHTPAQKASI LAFLVNELAC
SKSVVSEIDK NIEYMSNLRR DKWMVEGKLR KLRIIHAKKT GKRDASGGID LGEEQHPLGT
PTPGRKRRRK GGDSDYDDDD DDDSDDQADE DEEDEEDKDD KKGKKTDICE DEDEGDQTAS
VEELEKQIEK LSKQQSQYRR KLFDASHSLR SMMFGQDRYR RRYWILPQCG GIFVEGMESG
EGLEEIAKEK EKLKKAESLQ IKEEVFETSA ETLNCSIRDH CEQKDDPKEK DNTNLFLQKP
GSFSKLSKLL EVAKMPPESD VMTPPKVNVS TNGGPLSHQN SGKHPLGSVP SATTAQSPVG
KTDASLFSSG SGSCGKFYSP LPNDQLLKTL TEKNRQWFSL LPKTPCDDTS LTHADLSTTL
VTPQSQPPSK SPSPAPAALL GPSSVQSPPG LNPFALSPLQ VKGGVSMMGL QFCGWPAGVL
ASNVPFTSPL PALGSGLGLP EGNGSSSFLT SSVASSKSDS PVPPAERPSS AQPVAVEVAK
PVDFPSPKPI PEEMQFGWWR IIDPEDLKTL LKVLHLRGIR EKALQKQIQK HLDYITQACV
RNKDVAIIEL NENEDNQVTR DLVENWSVEE QAMELDLSIL QQVEDLERRV ASASLQVKGW
MCPEPASERE DLVYFEHKSL TKLFKEHDGE LTGDEENSAH ALARKSDNPL DIAVTRLADL
ERNIERRYLK SPLSTTIQIK LDNVGTVTVP APAPSISGDG DGIEEDIAPG LRVWRRALAE
ARSAAQVALC IQQLQRSIAW EKSIMKVYCQ ICRKGDNEEL LLLCDGCDKG CHTYCHRPKI
TTIPDGDWFC PACISKASGQ SIKIKKIHVK GKKTNDSKKT KKGNVAGDTE DEDSASTSSS
LKRGSKELKK RKMEETTSLN LSKAESTTSI KKPKKDESRD LALCSMILTE METHEDSWPF
LLPVNLKLVP GYKKVIKKPM DFSTIREKLN NGQYPNFETF ALDVRLVFDN CETFNEDDSD
IGRAGHSMRK YFEKKWTDTF KVS
