BRPF3_HUMAN
ID BRPF3_HUMAN Reviewed; 1205 AA.
AC Q9ULD4; A6ND56; A6NJE2; B7ZLN5; E7EX85; Q17RB6; Q5R3K8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Bromodomain and PHD finger-containing protein 3 {ECO:0000303|PubMed:26620551};
GN Name=BRPF3 {ECO:0000303|PubMed:26620551, ECO:0000312|HGNC:HGNC:14256};
GN Synonyms=KIAA1286 {ECO:0000303|PubMed:10574462};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE MOZ/MORF COMPLEX.
RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
RA Lane W.S., Tan S., Yang X.-J., Cote J.;
RT "ING tumor suppressor proteins are critical regulators of chromatin
RT acetylation required for genome expression and perpetuation.";
RL Mol. Cell 21:51-64(2006).
RN [6]
RP IDENTIFICATION IN THE MOZ/MORF COMPLEX.
RX PubMed=18794358; DOI=10.1128/mcb.01297-08;
RA Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C.,
RA Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J.,
RA Yang X.-J.;
RT "Molecular architecture of quartet MOZ/MORF histone acetyltransferase
RT complexes.";
RL Mol. Cell. Biol. 28:6828-6843(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962 AND SER-965, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-447; LYS-449 AND LYS-671, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-400; SER-403 AND
RP SER-900, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-740 AND SER-900, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX.
RX PubMed=26620551; DOI=10.15252/embj.201591293;
RA Feng Y., Vlassis A., Roques C., Lalonde M.E., Gonzalez-Aguilera C.,
RA Lambert J.P., Lee S.B., Zhao X., Alabert C., Johansen J.V., Paquet E.,
RA Yang X.J., Gingras A.C., Cote J., Groth A.;
RT "BRPF3-HBO1 regulates replication origin activation and histone H3K14
RT acetylation.";
RL EMBO J. 35:176-192(2016).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KAT7.
RX PubMed=26677226; DOI=10.1074/jbc.m115.703041;
RA Yan K., You L., Degerny C., Ghorbani M., Liu X., Chen L., Li L., Miao D.,
RA Yang X.J.;
RT "The chromatin regulator BRPF3 preferentially activates the HBO1
RT acetyltransferase but is dispensable for mouse development and survival.";
RL J. Biol. Chem. 291:2647-2663(2016).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1056-1195.
RX PubMed=21720545; DOI=10.1371/journal.pone.0018919;
RA Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L.,
RA Qiu W., Wang Y., Min J.;
RT "Structural and histone binding ability characterizations of human PWWP
RT domains.";
RL PLoS ONE 6:E18919-E18919(2011).
CC -!- FUNCTION: Scaffold subunit of various histone acetyltransferase (HAT)
CC complexes, such as the MOZ/MORF and HBO1 complexes, which have a
CC histone H3 acetyltransferase activity (PubMed:16387653,
CC PubMed:26620551, PubMed:26677226). Plays a role in DNA replication
CC initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-
CC 14' acetylation (H3K14ac), thereby facilitating the activation of
CC replication origins (PubMed:26620551). Component of the MOZ/MORF
CC complex which has a histone H3 acetyltransferase activity
CC (PubMed:16387653). {ECO:0000269|PubMed:16387653,
CC ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:26677226}.
CC -!- SUBUNIT: Component of some HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING4 or ING5, and BRPF3 (PubMed:26620551). Component of the MOZ/MORF
CC complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of
CC BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358).
CC Interacts with KAT7/HBO1; the interaction is direct (PubMed:26677226).
CC {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:18794358,
CC ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:26677226}.
CC -!- INTERACTION:
CC Q9ULD4; P16333: NCK1; NbExp=3; IntAct=EBI-1753470, EBI-389883;
CC Q9ULD4; Q16236: NFE2L2; NbExp=3; IntAct=EBI-1753470, EBI-2007911;
CC Q9ULD4-2; P61158: ACTR3; NbExp=3; IntAct=EBI-23662416, EBI-351428;
CC Q9ULD4-2; P07550: ADRB2; NbExp=3; IntAct=EBI-23662416, EBI-491169;
CC Q9ULD4-2; P28329-3: CHAT; NbExp=3; IntAct=EBI-23662416, EBI-25837549;
CC Q9ULD4-2; P22607: FGFR3; NbExp=3; IntAct=EBI-23662416, EBI-348399;
CC Q9ULD4-2; Q14957: GRIN2C; NbExp=3; IntAct=EBI-23662416, EBI-8285963;
CC Q9ULD4-2; P06396: GSN; NbExp=3; IntAct=EBI-23662416, EBI-351506;
CC Q9ULD4-2; P01112: HRAS; NbExp=3; IntAct=EBI-23662416, EBI-350145;
CC Q9ULD4-2; P11021: HSPA5; NbExp=3; IntAct=EBI-23662416, EBI-354921;
CC Q9ULD4-2; P02545: LMNA; NbExp=3; IntAct=EBI-23662416, EBI-351935;
CC Q9ULD4-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-23662416, EBI-5235340;
CC Q9ULD4-2; P17987: TCP1; NbExp=3; IntAct=EBI-23662416, EBI-356553;
CC Q9ULD4-2; Q99816: TSG101; NbExp=3; IntAct=EBI-23662416, EBI-346882;
CC Q9ULD4-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-23662416, EBI-741480;
CC Q9ULD4-2; Q9Y649; NbExp=3; IntAct=EBI-23662416, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26677226}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ULD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULD4-2; Sequence=VSP_055549;
CC Name=3;
CC IsoId=Q9ULD4-3; Sequence=VSP_055549, VSP_055550;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB033112; BAA86600.1; ALT_INIT; mRNA.
DR EMBL; Z84485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03878.1; -; Genomic_DNA.
DR EMBL; BC117387; AAI17388.1; -; mRNA.
DR EMBL; BC143917; AAI43918.1; -; mRNA.
DR EMBL; BC143918; AAI43919.1; -; mRNA.
DR CCDS; CCDS34437.1; -. [Q9ULD4-1]
DR RefSeq; NP_056510.2; NM_015695.2. [Q9ULD4-1]
DR RefSeq; XP_005249067.1; XM_005249010.2. [Q9ULD4-1]
DR RefSeq; XP_005249068.1; XM_005249011.3. [Q9ULD4-1]
DR RefSeq; XP_011512791.1; XM_011514489.1. [Q9ULD4-1]
DR PDB; 3PFS; X-ray; 1.90 A; A/B=1056-1195.
DR PDBsum; 3PFS; -.
DR AlphaFoldDB; Q9ULD4; -.
DR SMR; Q9ULD4; -.
DR BioGRID; 118036; 163.
DR ComplexPortal; CPX-736; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-740; MORF3 histone acetyltransferase complex.
DR CORUM; Q9ULD4; -.
DR IntAct; Q9ULD4; 32.
DR MINT; Q9ULD4; -.
DR STRING; 9606.ENSP00000350267; -.
DR BindingDB; Q9ULD4; -.
DR ChEMBL; CHEMBL3108644; -.
DR GuidetoPHARMACOLOGY; 2731; -.
DR iPTMnet; Q9ULD4; -.
DR PhosphoSitePlus; Q9ULD4; -.
DR BioMuta; BRPF3; -.
DR DMDM; 71153496; -.
DR EPD; Q9ULD4; -.
DR jPOST; Q9ULD4; -.
DR MassIVE; Q9ULD4; -.
DR MaxQB; Q9ULD4; -.
DR PaxDb; Q9ULD4; -.
DR PeptideAtlas; Q9ULD4; -.
DR PRIDE; Q9ULD4; -.
DR ProteomicsDB; 61143; -.
DR ProteomicsDB; 7229; -.
DR ProteomicsDB; 84995; -. [Q9ULD4-1]
DR ABCD; Q9ULD4; 1 sequenced antibody.
DR Antibodypedia; 15345; 81 antibodies from 18 providers.
DR DNASU; 27154; -.
DR Ensembl; ENST00000339717.11; ENSP00000345419.7; ENSG00000096070.19. [Q9ULD4-2]
DR Ensembl; ENST00000357641.10; ENSP00000350267.6; ENSG00000096070.19. [Q9ULD4-1]
DR Ensembl; ENST00000534694.5; ENSP00000434501.1; ENSG00000096070.19. [Q9ULD4-3]
DR GeneID; 27154; -.
DR KEGG; hsa:27154; -.
DR MANE-Select; ENST00000357641.10; ENSP00000350267.6; NM_015695.3; NP_056510.2.
DR UCSC; uc003olv.5; human. [Q9ULD4-1]
DR CTD; 27154; -.
DR GeneCards; BRPF3; -.
DR HGNC; HGNC:14256; BRPF3.
DR HPA; ENSG00000096070; Low tissue specificity.
DR neXtProt; NX_Q9ULD4; -.
DR OpenTargets; ENSG00000096070; -.
DR PharmGKB; PA25425; -.
DR VEuPathDB; HostDB:ENSG00000096070; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000155056; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; Q9ULD4; -.
DR OMA; KNHCPNS; -.
DR OrthoDB; 566217at2759; -.
DR PhylomeDB; Q9ULD4; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; Q9ULD4; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR SignaLink; Q9ULD4; -.
DR BioGRID-ORCS; 27154; 19 hits in 1089 CRISPR screens.
DR ChiTaRS; BRPF3; human.
DR GenomeRNAi; 27154; -.
DR Pharos; Q9ULD4; Tchem.
DR PRO; PR:Q9ULD4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9ULD4; protein.
DR Bgee; ENSG00000096070; Expressed in ganglionic eminence and 138 other tissues.
DR ExpressionAtlas; Q9ULD4; baseline and differential.
DR Genevisible; Q9ULD4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0050793; P:regulation of developmental process; IC:ComplexPortal.
DR GO; GO:1903706; P:regulation of hemopoiesis; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05839; BR140_related; 1.
DR CDD; cd15703; ePHD_BRPF3; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR035502; BR140-rel_PWWD.
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 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; SM00249; PHD; 2.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Bromodomain;
KW Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1205
FT /note="Bromodomain and PHD finger-containing protein 3"
FT /id="PRO_0000211188"
FT DOMAIN 606..676
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1076..1159
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 212..262
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 266..299
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 323..387
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
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 387..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 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"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 447
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 671
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 727..996
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055549"
FT VAR_SEQ 997..1060
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055550"
FT VARIANT 177
FT /note="S -> G (in dbSNP:rs45504893)"
FT /id="VAR_061042"
FT VARIANT 278
FT /note="A -> G (in dbSNP:rs17658935)"
FT /id="VAR_048431"
FT CONFLICT 1075
FT /note="E -> K (in Ref. 1; BAA86600)"
FT /evidence="ECO:0000305"
FT STRAND 1079..1083
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1089..1095
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1104..1106
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1109..1111
FT /evidence="ECO:0007829|PDB:3PFS"
FT HELIX 1116..1129
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1133..1138
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1145..1149
FT /evidence="ECO:0007829|PDB:3PFS"
FT HELIX 1150..1152
FT /evidence="ECO:0007829|PDB:3PFS"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:3PFS"
FT HELIX 1160..1167
FT /evidence="ECO:0007829|PDB:3PFS"
FT TURN 1168..1172
FT /evidence="ECO:0007829|PDB:3PFS"
FT HELIX 1175..1193
FT /evidence="ECO:0007829|PDB:3PFS"
SQ SEQUENCE 1205 AA; 135745 MW; F51DCAB253ED35C7 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 QSPSRPVDCI LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC
FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM
KIEPMRETSL NGTIFTVRKT AYCEAHSPPG AATARRKGDS PRSISETGDE EGLKEGDGEE
EEEEEVEEEE QEAQGGVSGS LKGVPKKSKM SLKQKIKKEP EEAGQDTPST LPMLAVPQIP
SYRLNKICSG LSFQRKNQFM QRLHNYWLLK RQARNGVPLI RRLHSHLQSQ RNAEQREQDE
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 GNEPLQRLLS
DNGINRLSLM APDTPAGTPL SGVGRRTSVL FKKAKNGVKL QRSPDRVLEN GEDHGVAGSP
ASPASIEEER HSRKRPRSRS CSESEGERSP QQEEETGMTN GFGKHTESGS DSECSLGLSG
GLAFEACSGL TPPKRSRGKP ALSRVPFLEG VNGDSDYNGS GRSLLLPFED RGDLEPLELV
WAKCRGYPSY PALIIDPKMP REGLLHNGVP IPVPPLDVLK LGEQKQAEAG EKLFLVLFFD
NKRTWQWLPR DKVLPLGVED TVDKLKMLEG RKTSIRKSVQ VAYDRAMIHL SRVRGPHSFV
TSSYL
