ID A0A2K5NQZ0_CERAT Unreviewed; 1887 AA.
AC A0A2K5NQZ0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2A {ECO:0000313|Ensembl:ENSCATP00000039902.1};
GN Name=BAZ2A {ECO:0000313|Ensembl:ENSCATP00000039902.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000039902.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000039902.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR Ensembl; ENSCATT00000064216.1; ENSCATP00000039902.1; ENSCATG00000042491.1.
DR GeneTree; ENSGT00940000159490; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000042491; Expressed in thymus and 12 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; cd15629; PHD_BAZ2A; 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; IPR017956; AT_hook_DNA-bd_motif.
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; IPR028940; PHD_BAZ2A.
DR InterPro; IPR028942; WHIM1_dom.
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:SF5; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A; 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; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 4.
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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
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 546..617
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 826..891
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1658..1708
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1792..1862
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1265..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1887 AA; 209201 MW; 98E9E1A990FD7320 CRC64;
MLKMEANDHF NFTGLPPAPA ASGLKPSPSS GEGLYTNGSP MNFPQQGKSL NGDVNVNGLS
TVSHTTTSGI LNSAPHSSST SHLHHPSVAY DCLWNYSQYP SANSGSNLKD PPLLSQFSGG
QYPLNGILGG SRQPSSPSHN TNLRAGSQEF WANGTQSPMG LNFDSQELYD SFPDQNFEVM
PNGPPSFFTS PQTSPMLGSS IQTFAPSQEV GSDIHPDEAA EKEMTSVVAE NRTGLVGSLE
LEEEQPELKM CGYNGSVPSV ESLHQEVSVL VPDPTVSCLD DPSHLPDQLE DTPILSEDSL
EPFNSLAPEP VSGGLYGIDD TELMGAEDKL PLEDSPVISA LDCPSLNNAT AFSLLADDSQ
TSASIFASPT SPPVLGESVL QDNSFDLNNG SDAEQEEMET QSSDFPPSLT QPAPDQSSTI
QLHPATSPAV SPTTSPAVSL VVSPAASPEI SPEVCPAAST VVSPAVLVVS PASSAVLPAV
SSEVPLTASV TSPKASPVTS PAAAFPTASP ASKDASSFLE TTADLEEITG EELTTSSSGD
VMRRRIATPE EVRLPLQHGW RREVRIKKGS HRWQGETWYY GPCGKRMKQF PEVIKYLSRN
VVHSVRREHF SFSPRMPVGD FFEERDTPEG LQWVQLSAEE IPSRIQAITG KRGRPRNTEK
TKTKEVPKVK RGRGRPPKVK ITELLDKTDN RLLKKLEAQE TSNEEDKAKI GKSKKKMRQK
VQRGECQTTI QGQAEKEKGK TKQEKLKEKV KREKKEKVKM KEKEEVAKAK PACKADKTLA
TQRRLEERQR QQMILEEMKK PTEDMCLTDH QPLPDFSRVP GLTLPSGAFS DCLTIVEFLH
SFGKVLGFDP AKDVPSLGVL QEGLLCQGDS LGEVQDLLVR LLKAALHDPG LPSYCQSLKI
LGEKVSEIPL TRDNVSEILR CFLMAYGVEP ALCDRLRTQP FQAQSPQQKA AVLAFLVHEL
NGSTLIINEI DKTLESMSSY RKNKWIVEGR LRRLKTVLAK RTGRSEVEME GPEECLGRRR
SSRIMEETSG MEEEEEEEST AAVHGRRGRR DGEVDATASS IPELERQIEK LSKRQLFFRK
KLLHSSQMLR AVSLGQDRYR RRYWVLPYLA GIFVEGTEGN LVPEDVIKKE TDSLKVAAHT
SLNPVLFSMK MELAGSNTTA SSPARARGRP RKTKPGSMQP RHLKSPVRGQ DSEQPQAQLQ
PEAQLHAPAQ PQPQLQLQLQ SHPQSHKGFL EQEGSPLSLG QSQHDLSQSA FLSWLSQTQS
HSSLLSSSVL TPDSSPGKLD PAPSQPLEEP EPDEAESSPD PQALWFNISA QMPCNAAPTP
PPAVSEDQPT PSPQQLASSK PINRPSAANP CSPVQFSSTP LAGLAPKRRA GDPGEMPQSP
TGLGQPKRRG RPPSKFFKQM EQRYLTQLTA QPVPPEMCSG WWWIRDPETL DAMLKALHPR
GIREKALHKH LNKHRDFLQE VCLRPSADPI FEPRQLPVFQ EGMMSWSPKE KTYETDLAVL
QWVEDLEQRV IMSDLQIRGW TCPSPDSTRE DLAYCEHLSS SQEDITWRGR GREGLAPQRK
TTNPLDLAVM RLAALEQNVE RRYLREPLWP THEVVLEKAL LSTPNGAPEG TTTEISYEIT
PRIRVWRQTL ERCRSAAQVC LCLGQLERSI AWEKSVNKVT CLVCRKGDND EFLLLCDGCD
RGCHIYCHRP KMEAVPEGDW FCTVCLAQQV EGEFTQKPGF PKRGQKRKSA YSLNFSEGDG
RRRRVLLRGR ESPAAGPRYS EEGQSPSKRR RLSMRNHHSD LTFCEIILME MESHDAAWPF
LEPVNPRLVS GYRRIIKNPM DFSTMRERLL RGGYTSSEEF AADALLVFDN CQTFNEDDSE
VGKAGHIMRR FFESRWEEFY QGKQANL
//
