ID A0A2R9CKS7_PANPA Unreviewed; 2108 AA.
AC A0A2R9CKS7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bromodomain adjacent to zinc finger domain 2B {ECO:0000313|Ensembl:ENSPPAP00000042574.1};
GN Name=BAZ2B {ECO:0000313|Ensembl:ENSPPAP00000042574.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000042574.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000042574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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; AJFE02072007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02072008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02072009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000065504.1; ENSPPAP00000042574.1; ENSPPAG00000043827.1.
DR GeneTree; ENSGT00940000155359; -.
DR Proteomes; UP000240080; Unplaced.
DR Bgee; ENSPPAG00000043827; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000240080};
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 739..810
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1030..1095
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1871..1921
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2017..2087
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..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1522..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1938..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 926..993
FT /evidence="ECO:0000256|SAM:Coils"
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..660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2108 AA; 233285 MW; 044C6A7864442283 CRC64;
MESGERLPSS AASSTTPTSS STPSVASVVS KGGLSTGVAS LSSTINPCGH LFRTAGDQPF
NLSTVSSAFP MVSHPVFGLH AASSGHSEFG 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 EEEDDEEEDE EDDEDDESDD SQSESDSNSE SDTEGSEEED DDDKDQDESD
SDTEGEKTSM KLNKTTSSVK SPSMSLTGHS TPRNLHIAKA PGSAPAALCS ESQSPAFLGT
SSSTLTSSPH SGTSKRRRVT DERELRIPLE YGWQRETRIR NFGGRLQGEV AYYAPCGKKL
RQYPEVIKYL SRNGIMDISR DNFSFSAKIR VGDFYEARDG PQGMQWCLLK EEDVIPRIRA
MEGRRGRPPN PDRQRAREES RMRRRKGRPP NVGNAEFLDN ADAKLLRKLQ AQEIARQAAQ
IKLLRKLQKQ EQARVAKEAK KQQAIMAAEE KRKQKEQIKI MKQQEKIKRI QQIRMEKELR
AQQILEVEEK 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 KTDICEDEIN DTVFSYLEKQ IEKLSKQQSQ YRRKLFDASH SLRSVMFGQD
RYRRRYWILP QCGGIFVEGM ESGEGLEEIA KEREKLKKAE SVQIKEEMFE TSGDSLNCSN
TDHCEQKEDL KEKDNTNLFL QKPGSFSKLS KLLEVAKMPP ESEVMTPKPN AGANGCTLSY
QNSGKHSLGS VQSTATQSNV EKADSNNLFN TGSSGPGKFY SPLPNDQLLK TLTEKNRQWF
SLLPRTPCDD TSLTHADMST ASLVTPQSQP PSKSPSPTPA PLGSSAQNPV GLNPFVLSPL
QVKGGVSMMG LQFCGWPTGV VTSNIPFTSS VPSLGSGLGL SEGNGNSFLT SNVASTKSES
PVPQNEKATS AQPAAVEVAK PVDFPSPKPI PEEMQFGWWR IIDPEDLKAL LKVLHLRGIR
EKALQKQIQK HLDYITQACL KNKDVAIIEL NENEENQVTR DIVENWSVEE QAMEMDLSVL
QQVEDLERRV ASASLQVKGW MCPEPASERE DLVYFEHKSF TKLCKEHDGE FTGEDESSAH
ALERKSDNPL DIAVTRLADL ERNIERRIEE DIAPGLRVWR RALSEARSAA QVALCIQQLQ
KSIAWEKSIM KVYCQICRKG DNEELLLLCD GCDKGCHTYC HRPKITTIPD GDWFCPACIA
KASGQTLKIK KLHVKGKKTN ESKKGKKVTL TGDTEDEDSA STSSSLKRGN KDLKKRKMEE
NTSINLSKQE SFTSVKKPKR DDSKDLALCS MILTEMETHE DAWPFLLPVN LKLVPGYKKV
IKKPMDFSTI REKLSGGQYP NLETFALDVR LVFDNCETFN EDDSDIGRAG HNMRKYFEKK
WTDTFKVS
//
