Q9ULD4 (BRPF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain and PHD finger-containing protein 3

Gene names

Name:	BRPF3
Synonyms:	KIAA1286

Organism

Homo sapiens (Human)

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, KAT6A, KAT6B, 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.
Sequence caution	The sequence BAA86600.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Bromodomain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	histone H3 acetylation Inferred from direct assay Ref.4. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular component	MOZ/MORF histone acetyltransferase complex Inferred from direct assay Ref.4Ref.6. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	3	EBI-1753470,EBI-389883

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.
Corresponds to variant rs45504893 [ dbSNP | Ensembl ].

VAR_061042

Natural variant

278

1

A → G.
Corresponds to variant rs17658935 [ dbSNP | Ensembl ].

VAR_048431

Experimental info

Sequence conflict

1075

1

E → K in BAA86600. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1205

Helix Strand Turn

Details...

Beta strand

1079 – 1083

5

Beta strand

1089 – 1095

7

Helix

1116 – 1120

5

Helix

1124 – 1128

5

Beta strand

1133 – 1138

6

Beta strand

1145 – 1149

5

Helix

1150 – 1152

3

Beta strand

1153 – 1155

3

Helix

1160 – 1167

8

Helix

1176 – 1193

18

Sequences

	Sequence		Length	Mass (Da)
	Q9ULD4 [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: Cervix carcinoma.
[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: Leukemic 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. NM_015695.2.

UniGene

Hs.520096.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PFS	X-ray	1.90	A/B	1056-1195	[»]

ProteinModelPortal

Q9ULD4.

SMR

Q9ULD4. Positions 206-266, 594-707, 1061-1194.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9ULD4. 7 interactions.

MINT

MINT-7241520.

STRING

Q9ULD4.

PTM databases

PhosphoSite

Q9ULD4.

Polymorphism databases

DMDM

71153496.

Proteomic databases

PRIDE

Q9ULD4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357641; ENSP00000350267; ENSG00000096070.

GeneID

27154.

KEGG

hsa:27154.

UCSC

uc003olv.2. human.

Organism-specific databases

CTD

27154.

GeneCards

GC06P036211.

H-InvDB

HIX0200828.

HGNC

HGNC:14256. BRPF3.

HPA

HPA022787.

neXtProt

NX_Q9ULD4.

PharmGKB

PA25425.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09034.

GeneTree

ENSGT00600000084089.

HOGENOM

HBG717256.

HOVERGEN

HBG004895.

InParanoid

Q9ULD4.

OMA

RDTPSTV.

OrthoDB

EOG45B1DQ.

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_polycomb-like_N.
IPR000313. PWWP.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K11350.

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]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 1 hit.

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

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 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.