Reviewed, UniProtKB/Swiss-Prot Q9ULD4 (BRPF3_HUMAN)

Names and origin

Protein names

Recommended name:
    Bromodomain and PHD finger-containing protein 3

Gene names

Name:	BRPF3
Synonyms:	KIAA1286

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1205 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Ref.4
Subunit structure	Component of the MOZ/MORF complex composed at least of ING5, MYST3/MOZ, MYST4/MORF, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.
Sequence similarities	Contains 1 bromo domain. Contains 1 PHD-type zinc finger. Contains 1 PWWP domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Bromodomain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histone H3 acetylation Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	MOZ/MORF histone acetyltransferase complex Ref.4 Ref.6 Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome extracellular region Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-1753470,EBI-375543
FYN	P06241	1	EBI-1753470,EBI-515315
GRB2	P62993	1	EBI-1753470,EBI-401755
NCK1	P16333	1	EBI-1753470,EBI-389883
PIK3R1	P27986	1	EBI-1753470,EBI-79464

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1205	1205	Bromodomain and PHD finger-containing protein 3		PRO_0000211188
Regions
	Domain	606 – 676	71	Bromo
	Domain	1076 – 1159	84	PWWP
	Zinc finger	212 – 262	51	PHD-type
	Compositional bias	406 – 432	27	Glu-rich
Amino acid modifications
	Modified residue	105	1	N6-acetyllysine Ref.8
	Modified residue	447	1	N6-acetyllysine Ref.8
	Modified residue	449	1	N6-acetyllysine Ref.8
	Modified residue	546	1	N6-acetyllysine Ref.8
	Modified residue	554	1	N6-acetyllysine Ref.8
	Modified residue	671	1	N6-acetyllysine Ref.8
	Modified residue	720	1	Phosphotyrosine Ref.5
	Modified residue	962	1	Phosphoserine Ref.7
	Modified residue	965	1	Phosphoserine Ref.7
Natural variations
	Natural variant	177	1	S → G: dbSNP rs45504893.		VAR_061042
	Natural variant	278	1	A → G: dbSNP rs17658935.		VAR_048431
Experimental info
	Sequence conflict	1075	1	E → K in BAA86600. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9ULD4-1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: F51DCAB253ED35C7	FASTA	1,205	135,745
	10 20 30 40 50 60 MRKPRRKSRQ NAEGRRSPSP YSLKCSPTRE TLTYAQAQRI VEVDIDGRLH RISIYDPLKI 70 80 90 100 110 120 ITEDELTAQD ITECNSNKEN SEQPQFPGKS KKPSSKGKKK ESCSKHASGT SFHLPQPSFR 130 140 150 160 170 180 MVDSGIQPEA PPLPAAYYRY IEKPPEDLDA EVEYDMDEED LAWLDMVNEK RRVDGHSLVS 190 200 210 220 230 240 ADTFELLVDR LEKESYLESR SSGAQQSLID EDAFCCVCLD DECHNSNVIL FCDICNLAVH 250 260 270 280 290 300 QECYGVPYIP EGQWLCRCCL QSPSRPVDCI LCPNKGGAFK QTSDGHWAHV VCAIWIPEVC 310 320 330 340 350 360 FANTVFLEPI EGIDNIPPAR WKLTCYICKQ KGLGAAIQCH KVNCYTAFHV TCAQRAGLFM 370 380 390 400 410 420 KIEPMRETSL NGTIFTVRKT AYCEAHSPPG AATARRKGDS PRSISETGDE EGLKEGDGEE 430 440 450 460 470 480 EEEEEVEEEE QEAQGGVSGS LKGVPKKSKM SLKQKIKKEP EEAGQDTPST LPMLAVPQIP 490 500 510 520 530 540 SYRLNKICSG LSFQRKNQFM QRLHNYWLLK RQARNGVPLI RRLHSHLQSQ RNAEQREQDE 550 560 570 580 590 600 KTSAVKEELK YWQKLRHDLE RARLLIELIR KREKLKREQV KVQQAAMELE LMPFNVLLRT 610 620 630 640 650 660 TLDLLQEKDP AHIFAEPVNL SEVPDYLEFI SKPMDFSTMR RKLESHLYRT LEEFEEDFNL 670 680 690 700 710 720 IVTNCMKYNA KDTIFHRAAV RLRDLGGAIL RHARRQAENI GYDPERGTHL PESPKLEDFY 730 740 750 760 770 780 RFSWEDVDNI LIPENRAHLS PEVQLKELLE KLDLVSAMRS SGARTRRVRL LRREINALRQ 790 800 810 820 830 840 KLAQPPPPQP PSLNKTVSNG ELPAGPQGDA AVLEQALQEE PEDDGDRDDS KLPPPPTLEP 850 860 870 880 890 900 TGPAPSLSEQ ESPPEPPTLK PINDSKPPSR FLKPRKVEED ELLEKSPLQL GNEPLQRLLS 910 920 930 940 950 960 DNGINRLSLM APDTPAGTPL SGVGRRTSVL FKKAKNGVKL QRSPDRVLEN GEDHGVAGSP 970 980 990 1000 1010 1020 ASPASIEEER HSRKRPRSRS CSESEGERSP QQEEETGMTN GFGKHTESGS DSECSLGLSG 1030 1040 1050 1060 1070 1080 GLAFEACSGL TPPKRSRGKP ALSRVPFLEG VNGDSDYNGS GRSLLLPFED RGDLEPLELV 1090 1100 1110 1120 1130 1140 WAKCRGYPSY PALIIDPKMP REGLLHNGVP IPVPPLDVLK LGEQKQAEAG EKLFLVLFFD 1150 1160 1170 1180 1190 1200 NKRTWQWLPR DKVLPLGVED TVDKLKMLEG RKTSIRKSVQ VAYDRAMIHL SRVRGPHSFV TSSYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O. DNA Res. 6:337-345(1999) [PubMed: 10574462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[2]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation." Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J. Mol. Cell 21:51-64(2006) [PubMed: 16387653] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-720, MASS SPECTROMETRY. Tissue: Epithelium.
[6]	"Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes." Ullah M., Pelletier N., Xiao L., Zhao S.P., Wang K., Degerny C., Tahmasebi S., Cayrou C., Doyon Y., Goh S.-L., Champagne N., Cote J., Yang X.-J. Mol. Cell. Biol. 28:6828-6843(2008) [PubMed: 18794358] [Abstract] Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[7]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962 AND SER-965, MASS SPECTROMETRY. Tissue: T-cell.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105; LYS-447; LYS-449; LYS-546; LYS-554 AND LYS-671, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB033112 mRNA. Translation: BAA86600.1. Different initiation. Z84485 Genomic DNA. Translation: CAI21669.1. CH471081 Genomic DNA. Translation: EAX03878.1.
IPI	IPI00008054.
RefSeq	NP_056510.2.
UniGene	Hs.520096
3D structure databases
SMR	Q9ULD4. Positions 199-266, 594-707, 1070-1185.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULD4. 5 interactions.
STRING	Q9ULD4.
PTM databases
PhosphoSite	Q9ULD4.
Proteomic databases
PRIDE	Q9ULD4.
Genome annotation databases
Ensembl	ENST00000357641; ENSP00000350267; ENSG00000096070; Homo sapiens. [Genome view]
GeneID	27154.
KEGG	hsa:27154.
UCSC	uc003olv.2. human.
Organism-specific databases
CTD	27154.
GeneCards	GC06P036272.
HGNC	HGNC:14256. BRPF3.
HPA	HPA022787.
PharmGKB	PA25425.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09034.
HOGENOM	HBG717256.
HOVERGEN	Q9ULD4.
InParanoid	Q9ULD4.
OMA	AEVEYDM.
OrthoDB	EOG980MGM.
PhylomeDB	Q9ULD4.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9ULD4.
Bgee	Q9ULD4.
CleanEx	HS_BRPF3.
Genevestigator	Q9ULD4.
GermOnline	ENSG00000096070. Homo sapiens.
Family and domain databases
InterPro	IPR001487. Bromodomain. IPR018359. Bromodomain_CS. IPR019542. Enhancer_of_polycomb-like. IPR000313. PWWP. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. [Graphical view]
Gene3D	G3DSA:1.20.920.10. Bromodomain. 1 hit.
Pfam	PF00439. Bromodomain. 1 hit. PF10513. EPL1. 1 hit. PF00855. PWWP. 1 hit. [Graphical view]
PRINTS	PR00503. BROMODOMAIN.
SMART	SM00297. BROMO. 1 hit. SM00249. PHD. 2 hits. SM00293. PWWP. 1 hit. [Graphical view]
PROSITE	PS00633. BROMODOMAIN_1. 1 hit. PS50014. BROMODOMAIN_2. 1 hit. PS50812. PWWP. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	49923.

Entry information

Entry name

BRPF3_HUMAN

Accession

Primary (citable) accession number: Q9ULD4
Secondary accession number(s): A6NJE2, Q5R3K8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	July 19, 2005
Last modified:	January 19, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.