ID A0A2K5UQM2_MACFA Unreviewed; 1189 AA.
AC A0A2K5UQM2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Bromodomain containing 1 {ECO:0000313|Ensembl:ENSMFAP00000014735.1};
GN Name=BRD1 {ECO:0000313|Ensembl:ENSMFAP00000014735.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000014735.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000014735.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000014735.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_015312522.1; XM_015457036.1.
DR AlphaFoldDB; A0A2K5UQM2; -.
DR STRING; 9541.ENSMFAP00000014735; -.
DR Ensembl; ENSMFAT00000065238.2; ENSMFAP00000014735.1; ENSMFAG00000030538.2.
DR VEuPathDB; HostDB:ENSMFAG00000030538; -.
DR GeneTree; ENSGT00940000157236; -.
DR OMA; GMWISTD; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000233100; Chromosome 10.
DR Bgee; ENSMFAG00000030538; Expressed in cerebellum and 13 other cell types or tissues.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043997; F:histone H4K12 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043995; F:histone H4K5 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043996; F:histone H4K8 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0140566; F:histone reader activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15702; ePHD_BRPF2; 1.
DR CDD; cd15677; PHD_BRPF2; 1.
DR CDD; cd20157; PWWP_BRPF2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR042004; BRPF2_ePHD.
DR InterPro; IPR042009; BRPF2_PHD.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR13793:SF17; BROMODOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF00855; PWWP; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 214..264
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 268..389
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 579..649
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1060..1143
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 515..558
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 801..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 133210 MW; 9084C6268F25B598 CRC64;
MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSAHGT PASASALPEP
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIIN EKRKGDCVPA
VSQSMFEFLM DRFEKESHCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL
YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKDSSVKTV
RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW
LLKRLSRNGA PLLRRLQSSL QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE
LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL
DHIKQPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR AAVRLRDQGG
VVLRQARREV DSIGLEEASG MHLAERPAVA PRRPFSWEDV DRLLDPANRA HLGLEEQLRE
LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPPPVGPGSE GCDEDGASLG
LEAGEEGDNS PPKLEPSDAL PLPSNSETNS EPPTLKPVEL NPEQSKLFKR VTFDNESHSA
CTQSALVSGR PPEPTRASSG DVPAAAASAV AEPASDVNRR TSVLFCKSKS VSPPKSAKNT
ETQPTSPQLG TKTFLSVVLP RLETLLQPRK RSRSTCGDSE VEEESPGKRL DAGLTNGFGG
TRSEQEPGGG LGRKATPRRR CASESSISSS NSPLCDSSFS VPKCGRGKPA LVRRHTLEDR
SELISCIENG NYAKAARIAA EVGQNSMWIS TDAAASVLEP LKVVWAKCSG YPSYPALIID
PKMPRVPGHH NGVTIPAPPL DVLKIGEHMQ TKSDEKLFLV LFFDNKRSWQ WLPKSKMVPL
GIDETIDKLK MMEGRNSSIR KAVRIAFDRA MNHLSRVHGE PTSDLSDID
//