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Database: UniProt
Entry: A0A2K5XQR7_MANLE
LinkDB: A0A2K5XQR7_MANLE
Original site: A0A2K5XQR7_MANLE 
ID   A0A2K5XQR7_MANLE        Unreviewed;       871 AA.
AC   A0A2K5XQR7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Bromodomain and PHD finger containing 3 {ECO:0000313|Ensembl:ENSMLEP00000005651.1};
GN   Name=BRPF3 {ECO:0000313|Ensembl:ENSMLEP00000005651.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000005651.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000005651.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A2K5XQR7; -.
DR   Ensembl; ENSMLET00000026951.1; ENSMLEP00000005651.1; ENSMLEG00000024307.1.
DR   GeneTree; ENSGT00940000155056; -.
DR   OMA; XRSLLMP; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000233140};
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          742..825
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..469
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"
SQ   SEQUENCE   871 AA;  99770 MW;  5E8CCDE050A38D2C CRC64;
     MRKPRRKSRQ NAEGRRSPSP YSLKCSPTRE TLTYAQAQRI VEVDIDGRLH RISIYDPLKI
     ITEDELTAQD ITECNSNKEN SEQPQFPGKS KKPSSKGKKK ESCSKHASGT SFHLPQPSFR
     MVDSGIQPEA PPLPAAYYRY IEKPPEDLDA EVEYDMDEED LAWLDMVNEK RRVDGHSLVS
     ADTFELLVDR LEKESYLESR SSGAQQSLID EDAFCCVCLD DECHNSNVIL FCDICNLAVH
     QECYGVPYIP EGQWLCRCCL QSPSRPVDCV LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC
     FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM
     KIEPMRETSL NGTIFTVRKT AYCEAHSPPS TATARRKGDS PRSISETGDE EGLKEGDGEE
     EEEEEVEEEE QEGQGGVSGP LKGVPKKNKM SLKQKIKKEP EEAGQDTSST LPLVTVPQIP
     SYRLNKICSG LSFQRKNQFM QRLHNYWLLK RQARNGVPLI RRLHSHLQSQ RNAEQREQDE
     KTSAVKEELK YWQKLRHDLE RARLLIELIR KREKLKREQV KVQQAAMELE LMPFNVLLRT
     TLDLLQEKDP AHIFAEPVNL SEVPDYLEFI SKPMDFSTMR RKLESHLYRT LEEFEEDFNL
     IVTNCMKYNA KDTIFHRAAV RLRDLGGAIL RHARRQAENI GYDPERGTHL PESPKLEDFY
     RFSWEDGRSL LLPFEDRGDL EPLELVWAKC RGYPSYPALI IDPKMPREGL LHNGVPIPVP
     PLDVLKLGEQ KQAEAGEKLF LVLFFDNKRT WQWLPRDKVL PLGVEDTVDK LKMLEGRKTS
     IRKSVQVAYD RAMIHLSRVR GPHSFVTSSY L
//
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