BRPF3_MOUSE
ID BRPF3_MOUSE Reviewed; 1204 AA.
AC B2KF05; A0A3B2WAQ0; Q3TRM7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Bromodomain and PHD finger-containing protein 3 {ECO:0000303|PubMed:26677226};
GN Name=Brpf3 {ECO:0000303|PubMed:26677226, ECO:0000312|MGI:MGI:2146836};
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI57916.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-1204 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE37001.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAE37001.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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] {ECO:0007744|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
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. 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. Component of the MOZ/MORF complex which has a
CC histone H3 acetyltransferase activity. {ECO:0000250|UniProtKB:Q9ULD4}.
CC -!- SUBUNIT: Component of some HBO1 complexes composed of KAT7/HBO1, MEAF6,
CC ING4 or ING5, and BRPF3. Component of the MOZ/MORF complex composed at
CC least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and
CC BRPF3. Interacts with KAT7/HBO1; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q9ULD4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULD4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B2KF05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B2KF05-2; Sequence=VSP_060569, VSP_060570;
CC -!- TISSUE SPECIFICITY: Highly expressed in the adult testis and brain.
CC {ECO:0000269|PubMed:26677226}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in embryos at 12.5 dpc.
CC {ECO:0000269|PubMed:26677226}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:26677226}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE37001.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC140278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC157915; AAI57916.1; -; mRNA.
DR EMBL; AK162638; BAE37001.1; ALT_INIT; mRNA.
DR CCDS; CCDS37532.1; -. [B2KF05-1]
DR RefSeq; NP_001074784.1; NM_001081315.1. [B2KF05-1]
DR RefSeq; XP_006524389.1; XM_006524326.3. [B2KF05-1]
DR RefSeq; XP_006524391.1; XM_006524328.3. [B2KF05-2]
DR RefSeq; XP_017172972.1; XM_017317483.1.
DR AlphaFoldDB; B2KF05; -.
DR SMR; B2KF05; -.
DR ComplexPortal; CPX-802; MOZ3 histone acetyltransferase complex.
DR ComplexPortal; CPX-804; MORF3 histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000004985; -.
DR iPTMnet; B2KF05; -.
DR PhosphoSitePlus; B2KF05; -.
DR EPD; B2KF05; -.
DR MaxQB; B2KF05; -.
DR PaxDb; B2KF05; -.
DR PeptideAtlas; B2KF05; -.
DR PRIDE; B2KF05; -.
DR ProteomicsDB; 342883; -. [B2KF05-1]
DR Antibodypedia; 15345; 81 antibodies from 18 providers.
DR DNASU; 268936; -.
DR Ensembl; ENSMUST00000004985; ENSMUSP00000004985; ENSMUSG00000063952. [B2KF05-1]
DR Ensembl; ENSMUST00000233701; ENSMUSP00000156455; ENSMUSG00000063952. [B2KF05-2]
DR GeneID; 268936; -.
DR KEGG; mmu:268936; -.
DR UCSC; uc008brp.1; mouse. [B2KF05-1]
DR UCSC; uc008brs.1; mouse.
DR CTD; 27154; -.
DR MGI; MGI:2146836; Brpf3.
DR VEuPathDB; HostDB:ENSMUSG00000063952; -.
DR eggNOG; KOG0955; Eukaryota.
DR GeneTree; ENSGT00940000155056; -.
DR HOGENOM; CLU_003589_1_0_1; -.
DR InParanoid; B2KF05; -.
DR OMA; KNHCPNS; -.
DR OrthoDB; 566217at2759; -.
DR PhylomeDB; B2KF05; -.
DR TreeFam; TF316118; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 268936; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Brpf3; mouse.
DR PRO; PR:B2KF05; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; B2KF05; protein.
DR Bgee; ENSMUSG00000063952; Expressed in animal zygote and 262 other tissues.
DR ExpressionAtlas; B2KF05; baseline and differential.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
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; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
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 Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..1204
FT /note="Bromodomain and PHD finger-containing protein 3"
FT /id="PRO_0000449611"
FT DOMAIN 605..675
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1075..1158
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 76..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 447
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 670
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD4"
FT VAR_SEQ 1060..1105
FT /note="GRSLLMPFEDHGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLH -> DH
FT RSQDAPGGPPAQRCPHPCPSTGRAEAGRAEAGRGWREALSCPLL (in isoform
FT 2)"
FT /id="VSP_060569"
FT VAR_SEQ 1106..1204
FT /note="Missing (in isoform 2)"
FT /id="VSP_060570"
SQ SEQUENCE 1204 AA; 135294 MW; 6AB172FEC7071D9B CRC64;
MRKPRRKSRQ NAEGRRSPSP YSLKCSPTRE TLTYAQAQRI VEVDIDGRLH RISIYDPLKI
ITEDELTAQD ITECNSNKEN SEQPQFPAKS KKPSSKGKRK ESCSKHASGT SFHLPQPSFR
VVDTGSQPEA PPLPAAYYRY IEKPPEDLDA EVEYDMDEED IAWLDMVNEK RRADGHSSVS
ADTFELLVDR LEKESYLESR SSGAQQSLID EDAFCCVCLD DECHNSNVIL FCDICNLAVH
QECYGVPYIP EGQWLCRCCL QSPSRPVDCV LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC
FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM
KIEPMRETSL NGTTFTVRKT AYCEAHSPSV AVARRKGDSP RSLSEVGDED GPKEGGGEEE
QEEAEEEGQE GQGGVGSPLK GVSKKGKMSL KQKIKKEPEE AGREAPSITL PMVTVPQIPS
YRLNKICSGL SFQRKTQFMQ RLHNYWLLKR QARNGVPLIR RLHSHLQSQR NAEQREQDEK
TSAVKEELKY WQKLRHDLER ARLLIELIRK REKLKREQVK VQQAAMELEL MPFTVLLRTT
LDLLQEKDSA HIFAEPVSLS EVPDYLEFIS KPMDFSTMRR KLESHLYHTL EEFEEDFNLI
VTNCMKYNAK DTIFHRAAVR LRDLGGAILR HARRQAENIG YDPERGTHLP ESPRLEDFYR
FSWEDVDNIL IPENRAHLSP EAQLKELLEK LDLVSTMRSS GARTRRVRML RREINALRQK
LAQPPPPQLL SLNKTVPNGE LPAGSRGDTA VLEQAQQEEP EEEGDRDDSK LPAPPTLEPT
GPAPSLSEQE SPPDPPTLKP ISDSKPSSRF LKSRKVEDEE LLEKSALQLG SEPLQCLLSD
NGIDRLSLTN PDSHPDTPLG TVGRRTSVLF KKAKNGVKLQ RGPDGTLENG EDHGPEDDPA
SPASTEDEHY SRKRPRSRSC SDSEGERSPQ QEEETGVTNG FGKHTESGSD SECSLGLSGG
LAFEAGSGLT PPKRSRGKPA LSRVPFLEGV NGDSDHSGSG RSLLMPFEDH GDLEPLELVW
AKCRGYPSYP ALIIDPKMPR EGLLHNGVPI PVPPLDVLKL GEQKQAEAGE RLFLVLFFDN
KRTWQWLPRD KVLPLGVEDT VDKLKMLEGR KTSIRKSVQV AYDRAMIHLS RVRGSHAFVT
SSYL
