BRPF1_MOUSE
ID BRPF1_MOUSE Reviewed; 1212 AA.
AC B2RRD7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Peregrin {ECO:0000305};
DE AltName: Full=Bromodomain and PHD finger-containing protein 1 {ECO:0000312|MGI:MGI:1926033};
GN Name=Brpf1 {ECO:0000312|MGI:MGI:1926033};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-459; SER-461;
RP THR-856; SER-858; SER-915; SER-920 AND SER-924, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-579, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24646517; DOI=10.4161/epi.28530;
RA You L., Chen L., Penney J., Miao D., Yang X.J.;
RT "Expression atlas of the multivalent epigenetic regulator Brpf1 and its
RT requirement for survival of mouse embryos.";
RL Epigenetics 9:860-872(2014).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=25773539; DOI=10.1074/jbc.m115.643189;
RA You L., Yan K., Zou J., Zhao H., Bertos N.R., Park M., Wang E., Yang X.J.;
RT "The chromatin regulator Brpf1 regulates embryo development and cell
RT proliferation.";
RL J. Biol. Chem. 290:11349-11364(2015).
RN [8]
RP FUNCTION.
RX PubMed=27939640; DOI=10.1016/j.ajhg.2016.11.011;
RG DDD Study;
RG CAUSES Study;
RA Yan K., Rousseau J., Littlejohn R.O., Kiss C., Lehman A., Rosenfeld J.A.,
RA Stumpel C.T., Stegmann A.P., Robak L., Scaglia F., Nguyen T.T., Fu H.,
RA Ajeawung N.F., Camurri M.V., Li L., Gardham A., Panis B., Almannai M.,
RA Sacoto M.J., Baskin B., Ruivenkamp C., Xia F., Bi W., Cho M.T.,
RA Potjer T.P., Santen G.W., Parker M.J., Canham N., McKinnon M., Potocki L.,
RA MacKenzie J.J., Roeder E.R., Campeau P.M., Yang X.J.;
RT "Mutations in the chromatin regulator gene BRPF1 cause syndromic
RT intellectual disability and deficient histone acetylation.";
RL Am. J. Hum. Genet. 100:91-104(2017).
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 (By similarity). Plays a key role
CC in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3
CC 'Lys-14' acetylation (H3K14ac) (By similarity). Some HAT complexes
CC preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation
CC (PubMed:27939640). Positively regulates the transcription of RUNX1 and
CC RUNX2 (By similarity). {ECO:0000250|UniProtKB:P55201,
CC ECO:0000269|PubMed:27939640}.
CC -!- SUBUNIT: Component of some HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING5, and BRPF1. Component of the MOZ/MORF complex composed at least of
CC ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
CC Interacts (via PHD-type zinc finger domains) with unmethylated histone
CC H3 at 'Lys-4' (H3K4me0). Interacts with trimethylated 'Lys-36' of
CC histone H3 (H3K36me3). Interacts with ING5; interaction directs BRPF1
CC to H4K4me3-enriched chromatin at the 5' of active genes. Interacts with
CC KAT7. {ECO:0000250|UniProtKB:P55201}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55201}.
CC Chromosome {ECO:0000250|UniProtKB:P55201}. Cytoplasm
CC {ECO:0000250|UniProtKB:P55201}. Note=Localization to the nucleus
CC depends on KAT6A, ING5 and MEAF6. Localizes to transcription start
CC sites. {ECO:0000250|UniProtKB:P55201}.
CC -!- TISSUE SPECIFICITY: Expressed at low level in most tissues, with high
CC expression in the testis and specific regions of the brain.
CC {ECO:0000269|PubMed:24646517}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the placenta, yolk sac, limb buds,
CC brain, spinal cord, retina, nose, bone and brown fat at the prenatal
CC stages. {ECO:0000269|PubMed:24646517}.
CC -!- PTM: Acetylated by KAT6A. {ECO:0000250|UniProtKB:P55201}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality around embryonic day 9.5
CC caused by arrested vasculogenesis in the yolk sac and embryo proper
CC (PubMed:24646517, PubMed:25773539). Embryos also display abnormal
CC neural tube closure (PubMed:25773539). {ECO:0000269|PubMed:24646517,
CC ECO:0000269|PubMed:25773539}.
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DR EMBL; AC155287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466523; EDK99448.1; -; Genomic_DNA.
DR EMBL; BC138361; AAI38362.1; -; mRNA.
DR CCDS; CCDS71810.1; -.
DR RefSeq; NP_001269056.1; NM_001282127.1.
DR RefSeq; XP_006506851.1; XM_006506788.3.
DR AlphaFoldDB; B2RRD7; -.
DR SMR; B2RRD7; -.
DR IntAct; B2RRD7; 2.
DR STRING; 10090.ENSMUSP00000108744; -.
DR iPTMnet; B2RRD7; -.
DR PhosphoSitePlus; B2RRD7; -.
DR jPOST; B2RRD7; -.
DR MaxQB; B2RRD7; -.
DR PeptideAtlas; B2RRD7; -.
DR PRIDE; B2RRD7; -.
DR ProteomicsDB; 273706; -.
DR Antibodypedia; 933; 54 antibodies from 16 providers.
DR DNASU; 78783; -.
DR Ensembl; ENSMUST00000113122; ENSMUSP00000108747; ENSMUSG00000001632.
DR GeneID; 78783; -.
DR KEGG; mmu:78783; -.
DR UCSC; uc009dfb.1; mouse.
DR CTD; 7862; -.
DR MGI; MGI:1926033; Brpf1.
DR VEuPathDB; HostDB:ENSMUSG00000001632; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000157794; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR OrthoDB; 566217at2759; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 78783; 14 hits in 79 CRISPR screens.
DR ChiTaRS; Brpf1; mouse.
DR PRO; PR:B2RRD7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; B2RRD7; protein.
DR Bgee; ENSMUSG00000001632; Expressed in humerus cartilage element and 259 other tissues.
DR ExpressionAtlas; B2RRD7; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0010698; F:acetyltransferase activator activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; IMP:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043972; P:histone H3-K23 acetylation; IMP:UniProtKB.
DR GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0048145; P:regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR CDD; cd05839; BR140_related; 1.
DR CDD; cd15701; ePHD_BRPF1; 1.
DR CDD; cd15676; PHD_BRPF1; 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; IPR042008; BRPF1_PHD.
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 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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Bromodomain; Chromatin regulator; Chromosome;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1212
FT /note="Peregrin"
FT /id="PRO_0000439813"
FT DOMAIN 644..714
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1083..1166
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 21..47
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..322
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 326..359
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 383..447
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 43..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..221
FT /note="Interaction with KAT6A and KAT6B"
FT /evidence="ECO:0000250|UniProtKB:P55201"
FT REGION 118..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..819
FT /note="Interaction with MEAF6 and ING5"
FT /evidence="ECO:0000250|UniProtKB:P55201"
FT REGION 542..1077
FT /note="Required for RUNX1 and RUNX2 transcriptional
FT activation"
FT /evidence="ECO:0000250|UniProtKB:P55201"
FT REGION 817..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 817..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55201"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 856
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1074
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55201"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55201"
SQ SEQUENCE 1212 AA; 137310 MW; 2FC14ECF8FF5DECE CRC64;
MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDSP PPPQQTPLRK
HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS
EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHSAPAS AAPKLPEVVY
RELEQDTPDA PPRPTSYYRY IEKSAEELDE EVEYDMDEED YIWLDIMNER RKTEGVSPIP
QEIFEYLMDR LEKESYFESH NKGDPNALVD EDAVCCICND GECQNSNVIL FCDMCNLAVH
QECYGVPYIP EGQWLCRRCL QSPSRAVDCA LCPNKGGAFK QTDDGRWAHV VCALWIPEVC
FANTVFLEPI DSIEHIPPAR WKLTCYICKQ RGSGACIQCH KANCYTAFHV TCAQQAGLYM
KMEPVRETGA NGTSFSVRKT AYCDIHTPPG SARRLPALSH SEGEEEEDEE EDEGKSWSSE
KVKKAKAKSR IKMKKARKIL AEKRAAAPVV SVPCIPPHRL SKITNRLTIQ RKSQFMQRLH
SYWTLKRQSR NGVPLLRRLQ THLQSQRNCE QVGRDSDDKN WALKEQLKSW QRLRHDLERA
RLLVELIRKR EKLKRETIKI QQIAMEMQLT PFLILLRKTL EQLQEKDTGN IFSEPVPLSE
VPDYLDHIKK PMDFFTMKQN LEAYRYLNFD DFEEDFNLIV SNCLKYNAKD TIFYRAAVRL
REQGGAVLRQ ARRQAEKMGI DFETGMHIPH NLAGDEVSHH TEDVEEERLV LLENQKHLPV
EEQLKLLLER LDEVNASKQS VGRSRRAKMI KKEMTALRRK LAHQRETGRD GPERHGPSGR
GNLTPHPAAC DKDGQTDSAA EESSSQETSK GLGPNMSSTP AHEVGRRTSV LFSKKNPKTA
GPPKRPGRPP KNRESQMTPS HGGSPVGPPQ LPIMGSLRQR KRGRSPRPSS SSDSDSDKST
EDPPMDLPAN GFSSGNQPVK KSFLVYRNDC NLPRSSSDSE SSSSSSSSAA SDRTSTTPSK
QGRGKPSFSR GTFPEDSSED TSGTENEAYS VGTGRGVGHS MVRKSLGRGA GWLSEDEDSP
LDALDLVWAK CRGYPSYPAL IIDPKMPREG MFHHGVPIPV PPLEVLKLGE QMTQEAREHL
YLVLFFDNKR TWQWLPRTKL VPLGVNQDLD KEKMLEGRKS NIRKSVQIAY HRALQHRSKV
QGEQSSETSD SD
