ID U3KEJ4_FICAL Unreviewed; 1210 AA.
AC U3KEJ4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Bromodomain and PHD finger containing 1 {ECO:0000313|Ensembl:ENSFALP00000013448.1};
GN Name=BRPF1 {ECO:0000313|Ensembl:ENSFALP00000013448.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013448.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000013448.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000013448.1}
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_005053221.1; XM_005053164.1.
DR AlphaFoldDB; U3KEJ4; -.
DR STRING; 59894.ENSFALP00000013448; -.
DR Ensembl; ENSFALT00000013504.2; ENSFALP00000013448.1; ENSFALG00000012865.2.
DR GeneID; 101810487; -.
DR KEGG; fab:101810487; -.
DR CTD; 7862; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157794; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR OMA; TRHKMRE; -.
DR OrthoDB; 163389at2759; -.
DR Proteomes; UP000016665; Chromosome 12.
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:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15701; ePHD_BRPF1; 1.
DR CDD; cd15676; PHD_BRPF1; 1.
DR CDD; cd20156; PWWP_BRPF1; 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; IPR042008; BRPF1_PHD.
DR InterPro; IPR049583; BRPF1_PWWP.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR042061; Peregrin_ePHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
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:SF85; PEREGRIN; 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 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|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
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 272..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 326..447
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 642..712
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1081..1164
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 46..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1060
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 819..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 137420 MW; 5FED0D4A9C515E10 CRC64;
MGVDFDVKTF CHNLRATKPP YECPVGTCRK IYKSYSGIEY HLYHYDHDNP PLPQHTPLRK
HKKKGRQARA ANKQSPSPSE TSQSPGREVM TYAQAQRMVE VDLHGRVHRI SIFDNLDVVS
EDEDIPEEVP ENGSNKESAE TQSVPPKSGK HKNKEKRKDS NHHHHNASAS ATPKLPEVVY
RELEQDTPDA PPRPTSYYRY IEKSAEELDE EVEYDMDEED YIWLDIMNER RKNEGVSPIP
QEIFEYLMDR LEKESYFESH NKGDPNALVD EDAVCCICND GECQNSNVIL FCDMCNLAVH
QECYGVPYIP EGQWLCRRCL QSPSRAVDCA LCPNKGGAFK QTDDGRWAHV VCALWIPEVC
FANTVFLEPI DSIEHIPPAR WKLTCYICKQ RGSGACIQCH KANCYTAFHV TCAQQAGLYM
KMEPVRETGA NGTSFSVRKT AYCDIHTPPG SVRRLPALSH SEGEEEDEEE EEEGKGWSSE
KVKKAKAKSR IKMKKARKIL AEKRAAAPVV SVPCIPPHRL SKITNRLTIQ RKSQFMQRLH
SYWTLKRQSR NGVPLLRRLQ THLQSQRNCD QRDTEDKNWA LKEQLKSWQR LRHDLERARL
LVELIRKREK LKRETIKVQQ VALEMQLTPF LILLRKTLEQ LQEKDTGNIF SEPVPLSEVP
DYLDHIKKPM DFQTMKQNLE AYRYLNFDDF EEDFNLIINN CLKYNAKDTI FYRAAIRLRE
QGGAVLRQAR RQAEKMGIDF ETGMHFPHCV TVEEAQIQDI EDEDVRLLLS ENQKHLPLEE
QLKILLERLD EVNAGKQSIG RSRRAKMIKK EITVLRRKLA HPRDLGRDGL ERHGSSARGV
LQSHNPCEKD LQTDSAAEES SSQETGKGLG PNSSSTPAHE VGRRTSVLFS KKNPKTAGPP
KRPGRPPKNR DSQITPGHGS SPIGPPQLPI MGSSQRQRKR GRSPRPSSTS DSDSDKSTED
ATMDLPANGF SSGNQPVKKS FLVYRNDCNL PRSSSDSESS SSSSSSAASD RTSTTPSKQG
RGKPSFSRVN FPEDSSEETS GTENESYSVG TGRGVGHGMV RKGMGRGAGW LSEDEDSSLD
ALDLVWAKCR GYPSYPALII DPKMPREGMF HHGVPIPVPP LEVLKLGEQM TQEAREHLYL
VLFFDNKRTW QWLPRTKLVP LGVNQDLDKE KMLEGRKSNI RKSVQIAYHR AMQHRNKVQG
EQSSDSSESD
//
