BAZ2B_CHICK
ID BAZ2B_CHICK Reviewed; 2130 AA.
AC Q9DE13;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 2B;
DE AltName: Full=Extracellular matrix protein F22;
GN Name=BAZ2B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yoon H., Philp N.J.;
RT "Cloning of a new extracellular matrix protein expressed in retina.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). Represses the expression of mitochondrial function-related
CC genes, perhaps by transcriptional regulation (By similarity).
CC {ECO:0000250|UniProtKB:A2AUY4, ECO:0000250|UniProtKB:Q9UIF8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063}.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
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DR EMBL; AF224275; AAG36791.1; -; mRNA.
DR RefSeq; NP_990008.1; NM_204677.1.
DR AlphaFoldDB; Q9DE13; -.
DR SMR; Q9DE13; -.
DR STRING; 9031.ENSGALP00000020513; -.
DR PaxDb; Q9DE13; -.
DR PRIDE; Q9DE13; -.
DR GeneID; 395400; -.
DR KEGG; gga:395400; -.
DR CTD; 29994; -.
DR VEuPathDB; HostDB:geneid_395400; -.
DR eggNOG; KOG1245; Eukaryota.
DR InParanoid; Q9DE13; -.
DR OrthoDB; 200493at2759; -.
DR PhylomeDB; Q9DE13; -.
DR PRO; PR:Q9DE13; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0032039; C:integrator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034472; P:snRNA 3'-end processing; IBA:GO_Central.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; SSF48371; SSF48371; 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 2: Evidence at transcript level;
KW Bromodomain; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2130
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 2B"
FT /id="PRO_0000211175"
FT DOMAIN 687..762
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 1010..1075
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 2039..2109
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1895..1945
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1431..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 797..984
FT /evidence="ECO:0000255"
FT COMPBIAS 92..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..608
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..2005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2130 AA; 236141 MW; 208C48FB0BA68F70 CRC64;
MESGERLTSS SVSSTAAASS PVSSTPSVAS AVSKSGLTTG AASLSSTINT GEWWRTADSH
SRSGAAFFPP LLGPPLLGIS PLFAPPAQNH DSTPFHPRTT GKNNRGSLEK GINGSLNGNS
TTAASAISTS VLSTSIATSA GQVKVVTSGA GGRKYNQEQN KVQLLDTRAD KIKDKKPRKK
AVESSSNSDS DSGSSSDTSS EGISSSDSDD LEEDEEEEED QSAEESEDDE SDSENEAHHE
NKNKVLMHSG VKDMKTDGQK AHEKSQEKRT HQQIPLVSDS QTHSSFQSQQ KQPQVLSQQL
PFIFQSSQAK EESVNKHTSV IQSTGLVPNV KPLSLVHQTK KEAYLKIIVP PPDLLKAGNK
NTSEESIPLI SDVRSKREQY KQTFPAAQLK KQESSKNLKK VIASLSSSKP TSCSPAHQKL
TSLENNHSNP FLTNALLGNH QPNGVIQSVI QEVPLALTTK QKSQTKINES VAIASSTPFS
LPVNLSACGK KTTGNRTLVV PSTSPVLPGS GKDKPVSNNA VNAVKTQHCL PSAKLVVEQF
RGVDSDAPSS KESDDSNDDD DDDEDEDEDD EDDDSDDSQS ESDSNSESDT DGSEDEDDED
DKDQDESDTD TEGEKTPLKL KKTGSSIKSS SIGPVAHSTP LNLQVAKTPS SAPSALCPET
QPAVFLGTTP STLTPSSHCG ISKRRRVTDE RELRVPLEYG WQRETRIRNF GGRLQGEVAY
FAPCGKKLRQ YPEVVKGVQW CLLKEEEVVP CIRAMEGRRG RPPNPDRQHS REESRMRRRK
GRPPNVGSTE FLDSTDAKLL RKLQAQEIAR QAAQIKLLRK LQKQEQARAA KEAKKQQAIM
AAEEKRKQKE QIKIMKQQEK IKRIQQIRME KELRAQQILE AKKKKKEEAA NAKLLEAEKR
IKEKEMRRQQ AVLLKHQELE RHRLDMERER RRQHMMLMKA MEARKKAEEK ERLKQEKRDE
KRLNKERKLE QRRLELEMAK ELKKPNEDMC LADQKALPEL PRIPGLVLSG STFSDCLMIV
QFLRNFGKVL GFDVNTDVPS LSTLQEGLLN IGDSRGEVQD LLVKLVTAAV CDPGLVTGYK
AKTILGEHLL NVGINRDNVS EILQIFMEAH CGQTELTESL KTKAFQAHTP AQKAAVLAFL
VNELACSKSV VSEIDKNIDY MSNLRRDKWM VEGKLRNLRI IHAKKTGKRD ATGGGEVGEE
PHSLETPTPG RKRRRKGGDS DYDDDDDDDS DDQADEDDED EEDKEDKKGK KAEVCEDEDD
GDQTVSVEEL EKQIEKLTKQ QSQYRKKLFE ASHCLRSMMF GQDRYRRRYW ILPQCGGIFV
EGMESGEGLE EIAKEKEKLK KVESIHIKEE VFEISEEKIS CLNTTRCEQK EDLKEKDNTN
LFLQKPGSFS KLSKLLEVAK MPPECDVMPQ KPNGGAANGC TPSYQNTSQN SLCSLQPSVS
QSSSEKSDSS NLFSPTASGT GKFYSSPLIP SDQLLKTLTE KNRQWFSLLP RVPCDDMSVT
HVDTPATTSL TPQSHPPSKS PSPVPSPLLG STSAQSPMGL SPFAMPPLQQ MKPGLPVMGL
QFCGWPTGVL TSNVQFSSPL PTLGSGLGLS EGNGNSFLTS SVPTSKSESP ALQTEKVAFA
TCTAVEVAKP VDHPNPKPIP EEMQYGWWRI TDPEDLKSLH KVLHLRGIRE KALQKQIQKH
MDYITLACIK NKDVAIIDIN ENEDNQVTRD VVENWSVEEQ AMEVDLAILQ QVEDLERRVA
SASLQVKGWL CPEPASERED LVYHEHKSII RLHKKHDGDS AGGGEGSTSS LERKNDNPLD
IAVTRLADLE RNIERRYLKS PLSTTIQIKL DNVGTVTVPA PAPSISGDGD GTEEDIAPGL
RVWRKALSEA RSAAQVALCI QQLQKSIAWE KSIMKVYCQI CRKGDNEELL LLCDGCDKGC
HTYCHRPKIT TIPDGDWFCP ACIAKASGQT LKLKKLQIKG KKSNEQKRGR KLPGDTEDED
SATTSTSLKR GKTEPKKRKM DESVSVSQGK QENFTAIKKP KRDDSKDLAI CSMILSELET
HEDAWPFLLP VNLKLVPGYK KVIKKPMDFS TIRDKLTSGQ YPNVEAFSLD VRLVFDNCET
FNEDDSDIGR AGHNMRKYFE KKWTEIFKLS
