ID G3RKQ7_GORGO Unreviewed; 2110 AA.
AC G3RKQ7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2B {ECO:0000313|Ensembl:ENSGGOP00000016335.3};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSGGOP00000016335.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000016335.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000016335.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000016335.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000016335.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR EMBL; CABD030016600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030016602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000016799.3; ENSGGOP00000016335.3; ENSGGOG00000016720.3.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000155359; -.
DR HOGENOM; CLU_000899_0_0_1; -.
DR TreeFam; TF329083; -.
DR Proteomes; UP000001519; Chromosome 2B.
DR Bgee; ENSGGOG00000016720; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15630; PHD_BAZ2B; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR45915:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
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; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 738..809
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1029..1094
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1873..1923
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2019..2089
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
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 408..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1526..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1262
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2110 AA; 233348 MW; 2B0C7018398EC8A2 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
SSLTSELRSK REQYKQAFPS QLKKQESSKS LKKVIAALSN PKATSSSPAH PKQTLENNHP
NPFLTNALLG NHQPNGVIQS VIQEAPLALT TKTKMQSKIN ENIAAASSTP FSSPVNLSTS
GRRTPGNQTP VMPSASPILH SQGKEKAVSN NVNPVKTQHH SHPAKSLVEQ FRGTDSDIPS
SKDSEDSNED EEEDEEEDEE DDEDDESDDS QSESDSNSES DTEGSEEEDD DDKDQDESDS
DTEGEKTSMK LNKTTSSVKS PSMSLTGHST PRNLHIAKAP GSAPAALCSE SQSPAFLGTS
SSTLTSSPHS GTSKRRRVTD ERELRIPLEY GWQRETRIRN FGGRLQGEVA YYAPCGKKLR
QYPEVIKYLS RNGIMDISRD NFSFSAKIRV GDFYEARDGP QGMQWCLLKE EDVIPRIRAM
EGRRGRPPNP DRQRAREESR MRRRKGRPPN VGNAEFLDNA DAKLLRKLQA QEIARQAAQI
KLLRKLQKQE QARVAKEAKK QQAIMAAEEK RKQKEQIKIM KQQVCERERR RQHMMLMKAM
EARKKAEEKE RLKQEKRDEK RLNKERKLEQ RRLELEMAKE LKKPNEDMCL ADQKPLPELP
RIPGLVLSGS TFSDCLMVVQ FLRNFGKVLG FDVNIDVPNL SVLQEGLLNI GDSMGEVQDL
LVRLLSAAVC DPGLITGYKA KTALGEHLLN VGVNRDNVSE ILQIFMEAHC GQTELTESLK
TKAFQAHTPA QKASVLAFLI NELACSKSVV SEIDKNIDYM SNLRRDKWVV EGKLRKLRII
HAKKTGKRDT SGGIDLGEEQ HPLGTPTPGR KRRRKGGDSD YDDDDDDDSD DQGDEDDEDE
EDKEDKKGKK TDICEDEDEG DQAASVEELE KQIEKLSKQQ SQYRKKLFDA SHSLRSVMFG
QDRYRRRYWI LPQCGGIFVE GMESGEGLEE IAKEREKLKK AESVQIKEEM FETSGDSLNC
SNTDHCEQKE DLKEKDNTNL FLQKPGSFSK LSKLLEVAKM PPESEVMTPK PNAGANGCTL
SYQNSGKHSL GSVQSTATQS NVEKADSNNL FNTGSSGPGK FYSPLPNDQL LKTLTEKNRQ
WFSLLPRTPC DDTSLTHADM SIASLVTPQS QPPSKSPSPT PAPLGSSAQN PVGLNPFALS
PLQVKGGVSM MGLQFCGWPT GVVTSNIPFT SSVPSLGSGL GLSEGNGNSF LTSNVASSKS
ESPVSQNEKA TSAQPAAVEV AKPVDFPSPK PIPEEMQFGW WRIIDPEDLK ALLKVLHLRG
IREKALQKQI QKHLDYITQA CLKNKDVAII ELNENEENQV TRDIVENWSV EEQAMEMDLS
VLQQVEDLER RVASASLQVK GWMCPEPASE REDLVYFEHK SFTKLCKEHD GEFTGEDESS
AHALERKSDN PLDIAVTRLA DLERNIERRI EEDIAPGLRV WRRALSEARS AAQVALCIQQ
LQKSIAWEKS IMKVYCQICR KGDNEELLLL CDGCDKGCHT YCHRPKITTI PDGDWFCPAC
IAKASGQTLK IKKLHVKGKK TNESKKGKKV TLTGDTEDED SASTSSSLKR GNKDLKKRKM
EENTSINLSK QESFTSVKKP KRDDSKDLAL CSMILTEMET HEDAWPFLLP VNLKLVPGYK
KVIKKPMDFS TIREKLSSGQ YPNLETFALD VRLVFDNCET FNEDDSDIGR AGHNMRKYFE
KKWTDTFKVS
//
