ID A0A2I2YP45_GORGO Unreviewed; 2131 AA.
AC A0A2I2YP45;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2B {ECO:0000313|Ensembl:ENSGGOP00000036655.1};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSGGOP00000036655.1};
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:ENSGGOP00000036655.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000036655.1, 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:ENSGGOP00000036655.1, 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:ENSGGOP00000036655.1}
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 RefSeq; XP_018878134.1; XM_019022589.1.
DR Ensembl; ENSGGOT00000063440.1; ENSGGOP00000036655.1; ENSGGOG00000016720.3.
DR GeneTree; ENSGT00940000155359; -.
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 736..811
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1050..1115
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1894..1944
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2040..2110
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 138..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..286
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..657
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1283
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2131 AA; 236256 MW; EB2B76CA5241A8BB CRC64;
MESGERLPSS AASSTTPTSS STPSVASVVS KGGLSTGVAS LSSTINPCGH LFRTAGDQPF
NLSTVSSAFP MVSHPVFGLH SASSGHSEFG GLGTLGTPTA LAAHPQLASF PEWWRTTDAH
TRTGATFFPP LLGIPPLFAP PAQNHDSSSF HSRTSGKSNR NGPEKGVNGS INGSNTSSVI
GINTSVLSTT ASSSMGQTKS TSSGGGNRKC NQEQSKNQPL DARVDKIKDK KPRKKAMESS
SNSDSDSGTS SDTSSEGISS SDSDDLEEDE EEEDQSIEES EDDDSDSESE AQHKSNNQVL
LHGISDPKAD GQKATEKAQE KRIHQPLPLA SESQTHSFQS QQKQPQVLSQ QLPFIFQSSQ
AKEESVNKHT SVIQSTGLVS NVKPLSLVNQ AKKETYMKLI VPSPDVLKAG NKNTSEESSS
LTSELRSKRE QYKQAFPSQL KKQESSKSLK KVIAALSNPK ATSSSPAHPK QTLENNHPNP
FLTNALLGNH QPNGVIQSVI QEAPLALTTK TKMQSKINEN IAAASSTPFS SPVNLSTSGR
RTPGNQTPVM PSASPILHSQ GKEKAVSNNV NPVKTQHHSH PAKSLVEQFR GTDSDIPSSK
DSEDSNEDEE EDEEEDEEDD EDDESDDSQS ESDSNSESDT EGSEEEDDDD KDQDESDSDT
EGEKTSMKLN KTTSSVKSPS MSLTGHSTPR NLHIAKAPGS APAALCSESQ SPAFLGTSSS
TLTSSPHSGT SKRRRVTDER ELRIPLEYGW QRETRIRNFG GRLQGEVAYY APCGKKLRQY
PEVIKGMQWC LLKEEDVIPR IRAMEGRRGR PPNPDRQRAR EESRMRRRKG RPPNVGNAEF
LDNADAKLLR KLQAQEIARQ AAQIKLLRKL QKQEQARVAK EAKKQQAIMA AEEKRKQKEQ
IKIMKQQEKI KRIQQIRMEK ELRAQQILEA KKKKKEEAAN AKLLEAEKRI KEKEMRRQQA
VLLKHQERER RRQHMMLMKA MEARKKAEEK ERLKQEKRDE KRLNKERKLE QRRLELEMAK
ELKKPNEDMC LADQKPLPEL PRIPGLVLSG STFSDCLMVV QFLRNFGKVL GFDVNIDVPN
LSVLQEGLLN IGDSMGEVQD LLVRLLSAAV CDPGLITGYK AKTALGEHLL NVGVNRDNVS
EILQIFMEAH CGQTELTESL KTKAFQAHTP AQKASVLAFL INELACSKSV VSEIDKNIDY
MSNLRRDKWV VEGKLRKLRI IHAKKTGKRD TSGGIDLGEE QHPLGTPTPG RKRRRKGGDS
DYDDDDDDDS DDQGDEDDED EEDKEDKKGK KTDICEDEDE GDQAASVEEL EKQIEKLSKQ
QSQYRKKLFD ASHSLRSVMF GQDRYRRRYW ILPQCGGIFV EGMESGEGLE EIAKEREKLK
KAESVQIKEE MFETSGDSLN CSNTDHCEQK EDLKEKDNTN LFLQKPGSFS KLSKLLEVAK
MPPESEVMTP KPNAGANGCT LSYQNSGKHS LGSVQSTATQ SNVEKADSNN LFNTGSSGPG
KFYSPLPNDQ LLKTLTEKNR QWFSLLPRTP CDDTSLTHAD MSIASLVTPQ SQPPSKSPSP
TPAPLGSSAQ NPVGLNPFAL SPLQVKGGVS MMGLQFCGWP TGVVTSNIPF TSSVPSLGSG
LGLSEGNGNS FLTSNVASSK SESPVSQNEK ATSAQPAAVE VAKPVDFPSP KPIPEEMQFG
WWRIIDPEDL KALLKVLHLR GIREKALQKQ IQKHLDYITQ ACLKNKDVAI IELNENEENQ
VTRDIVENWS VEEQAMEMDL SVLQQVEDLE RRVASASLQV KGWMCPEPAS EREDLVYFEH
KSFTKLCKEH DGEFTGEDES SAHALERKSD NPLDIAVTRL ADLERNIERR IEEDIAPGLR
VWRRALSEAR SAAQVALCIQ QLQKSIAWEK SIMKVYCQIC RKGDNEELLL LCDGCDKGCH
TYCHRPKITT IPDGDWFCPA CIAKASGQTL KIKKLHVKGK KTNESKKGKK VTLTGDTEDE
DSASTSSSLK RGNKDLKKRK MEENTSINLS KQESFTSVKK PKRDDSKDLA LCSMILTEME
THEDAWPFLL PVNLKLVPGY KKVIKKPMDF STIREKLSSG QYPNLETFAL DVRLVFDNCE
TFNEDDSDIG RAGHNMRKYF EKKWTDTFKV S
//
