ID G1RCQ4_NOMLE Unreviewed; 1205 AA.
AC G1RCQ4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Bromodomain and PHD finger containing 3 {ECO:0000313|Ensembl:ENSNLEP00000011003.1};
GN Name=BRPF3 {ECO:0000313|Ensembl:ENSNLEP00000011003.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000011003.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000011003.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000011003.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; ADFV01115259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01115260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01115261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003278916.1; XM_003278868.3.
DR AlphaFoldDB; G1RCQ4; -.
DR STRING; 61853.ENSNLEP00000011003; -.
DR Ensembl; ENSNLET00000011540.2; ENSNLEP00000011003.1; ENSNLEG00000008999.2.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000155056; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; G1RCQ4; -.
DR OMA; XRSLLMP; -.
DR OrthoDB; 163389at2759; -.
DR TreeFam; TF316118; -.
DR Proteomes; UP000001073; Chromosome 1a.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
DR CDD; cd05512; Bromo_brd1_like; 1.
DR CDD; cd15703; ePHD_BRPF3; 1.
DR CDD; cd15572; PHD_BRPF; 1.
DR CDD; cd20158; PWWP_BRPF3; 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; IPR042005; BRPF3_ePHD.
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:SF19; BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 3; 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:UP000001073};
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 212..262
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 266..387
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 606..676
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1076..1159
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..592
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 75..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..432
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 135724 MW; 8F8E2685011749A4 CRC64;
MRKPRRKSRQ NAEGRRSPSP YSLKCSPTRE TLTYAQAQRI VEVDIDGRLH RISIYDPLKI
ITEDELTAQD ITECNSNKEN SEQPQFPGKS KKPSSKGKKK ESCSKHASGT SFHLPQPSFR
MVDSGIQPEA PPLPAAYYRY IEKPPEDLDA EVEYDMDEED LAWLDMVNEK RRVDGHSLVS
ADTFELLLDR LEKESYLESR SSGAQQSLID EDAFCCVCLD DECHNSNVIL FCDICNLAVH
QECYGVPYIP EGQWLCRCCL QSPSRPVDCV LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC
FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM
KIEPMRETSL NGTIFTVRKT AYCEAHSPPG AATARRKGDS PRSISETGDE EGLKEGDGEE
EEEEEVEEEE QEGQGGVSGP LKGVPKKNKM SLKQKIKKEP EEAGQDTPST LPMLAVPQIP
SYRLNKICSG LSFQRKNQFM QRLHNYWLLK RQARNGVPLI RRLHSHLQSQ RNAEQREEDE
KTSAVKEELK YWQKLRHDLE RARLLIELIR KREKLKREQV KVQQAAMELE LMPFNVLLRT
TLDLLQEKDP AHIFAEPVNL SEVPDYLEFI SKPMDFSTMR RKLESHLYRT LEEFEEDFNL
IVTNCMKYNA KDTIFHRAAV RLRDLGGAIL RHARRQAENI GYDPERGTHL PESPKLEDFY
RFSWEDVDNI LIPENRAHLS PEVQLKELLE KLDLVSAMRS SGARTRRVRL LRREINALRQ
KLAQPPPPQP PSLNKTVSNG ELPAGPQGDA AVLEQALQEE PEDDGDRDDS KLPPPPTLEP
TGPAPSLSEQ ESPPEPPTLK PINDSKPPSR FLKPRKVEED ELLEKSPLQL GSEPLQRLLS
DNGINRLSLM APDTPAGTPL SGVGRRTSVL FKKAKNGVKL QRSPDRVLEN GEDHGVAGSP
ASPASIEEER HSRKRPRSRS CSESEGERSP QQEEETGITN GFGKHTESGS DSECSLGLSG
GLAFEACSGL TPPKRSRGKP ALSRVPFLEG VNGDSDYNGS GRSLLLPFED RGDLEPLELV
WAKCRGYPSY PALIIDPKMP REGLLHNGVP IPVPPLDVLK LGEQKQAEAG EKLFLVLFFD
NKRTWQWLPR DKVLPLGVED TVDKLKMLEG RKTSIRKSVQ VAYDRAMIHL SRVRGPHSFV
TSSYL
//
