ID A0A0D9RE58_CHLSB Unreviewed; 1044 AA.
AC A0A0D9RE58;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Bromodomain and PHD finger containing 1 {ECO:0000313|Ensembl:ENSCSAP00000006897.1};
GN Name=BRPF1 {ECO:0000313|Ensembl:ENSCSAP00000006897.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000006897.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000006897.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000006897.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AQIB01138399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9RE58; -.
DR STRING; 60711.ENSCSAP00000006897; -.
DR Ensembl; ENSCSAT00000008759.1; ENSCSAP00000006897.1; ENSCSAG00000010677.1.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157794; -.
DR OMA; THTFVHI; -.
DR Proteomes; UP000029965; Chromosome 22.
DR Bgee; ENSCSAG00000010677; Expressed in caudate nucleus and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0010698; F:acetyltransferase activator 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:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd20156; PWWP_BRPF1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR049583; BRPF1_PWWP.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13793:SF85; PEREGRIN; 1.
DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF10513; EPL1; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 21..52
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 476..546
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 915..998
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 43..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 118664 MW; AA8BC39102FA4516 CRC64;
MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDNP PPPQQTPLRK
HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS
EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHHNVSA STTPKLPEVV
YRELEQDTPD APPRPTSYYR YIEKSAEELD EEVEYDMDEE DYIWLDIMNE RRKTEGVSPI
PQEIFEYLMD RLEKESYFES HNKGDPNALV DEDAVCCICN DGSARRLPAL SHSEGEEDED
EEEDEGKGWS SEKVKKAKAK SRIKMKKARK ILAEKRAAAP VVSVPCIPPH RLSKITNRLT
IQRKSQFMQR LHSYWTLKRQ SRNGVPLLRR LQTHLQSQRN CDQVGRDSED KNWALKEQLK
SWQRLRHDLE RARLLVELIR KREKLKRETI KVQQIAMEMQ LTPFLILLRK TLEQLQEKDT
GNIFSEPVPL SEVPDYLDHI KKPMDFFTMK QNLEAYRYLN FDDFEEDFNL IVSNCLKYNA
KDTIFYRAAV RLREQGGAVL RQARRQAEKM GIDFETGMHI PHSLTGDEAT HHTEDAEEER
LVLLENQKHL PVEEQLKLLL ERLDEVNASK QSVGRSRRAK MIKKEMTALR RKLAHQRETA
RDGPERHGPS SRGSLTPHPA ACDKDGQTDS AAEESSSQET SKGLGPNMSS TPAHEVGRRT
SVLFSKKNPK TAGPPKRPGR PPKNRESQMT PSHGGSPVGP PQLPIMSSLR QRKRGRSPRP
SSSSDSDSDK STEDPPMDLP ANGFSGGNQP VKKSFLVYRN DCSLPRSSSD SESSSSSSSS
AASDRTSTTP SKQGRGKPSF SRGTFPEDSS EDTSGTENEA YSVGTGRGVG HSMVRKSLGR
GAGWLSEDED SPLDALDLVW AKCRGYPSYP ALIIDPKMPR EGMFHHGVPI PVPPLEVLKL
GEQMTQEARE HLYLVLFFDN KRTWQWLPRT KLVPLGVNQD LDKEKMLEGR KSNIRKSVQI
AYHRALQHRS KVQGEQSSET SDSD
//
