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Protein

Bromodomain and PHD finger-containing protein 3

Gene

BRPF3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri212 – 26251PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • histone H3 acetylation Source: UniProtKB
  • platelet degranulation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain and PHD finger-containing protein 3
Gene namesi
Name:BRPF3
Synonyms:KIAA1286
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:14256. BRPF3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular region Source: Reactome
  • MOZ/MORF histone acetyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25425.

Chemistry

ChEMBLiCHEMBL3108644.
GuidetoPHARMACOLOGYi2731.

Polymorphism and mutation databases

BioMutaiBRPF3.
DMDMi71153496.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12051205Bromodomain and PHD finger-containing protein 3PRO_0000211188Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphoserineCombined sources
Modified residuei400 – 4001PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei447 – 4471N6-acetyllysineCombined sources
Modified residuei449 – 4491N6-acetyllysineCombined sources
Modified residuei671 – 6711N6-acetyllysineCombined sources
Modified residuei900 – 9001PhosphoserineCombined sources
Modified residuei962 – 9621PhosphoserineCombined sources
Modified residuei965 – 9651PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9ULD4.
MaxQBiQ9ULD4.
PaxDbiQ9ULD4.
PRIDEiQ9ULD4.

PTM databases

iPTMnetiQ9ULD4.
PhosphoSiteiQ9ULD4.

Expressioni

Gene expression databases

BgeeiQ9ULD4.
CleanExiHS_BRPF3.
ExpressionAtlasiQ9ULD4. baseline and differential.
GenevisibleiQ9ULD4. HS.

Organism-specific databases

HPAiHPA022787.

Interactioni

Subunit structurei

Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163333EBI-1753470,EBI-389883

Protein-protein interaction databases

BioGridi118036. 6 interactions.
IntActiQ9ULD4. 10 interactions.
MINTiMINT-7241520.
STRINGi9606.ENSP00000350267.

Chemistry

BindingDBiQ9ULD4.

Structurei

Secondary structure

1
1205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1079 – 10835Combined sources
Beta strandi1089 – 10957Combined sources
Beta strandi1104 – 11063Combined sources
Beta strandi1109 – 11113Combined sources
Helixi1116 – 112914Combined sources
Beta strandi1133 – 11386Combined sources
Beta strandi1145 – 11495Combined sources
Helixi1150 – 11523Combined sources
Beta strandi1153 – 11553Combined sources
Helixi1160 – 11678Combined sources
Turni1168 – 11725Combined sources
Helixi1175 – 119319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFSX-ray1.90A/B1056-1195[»]
ProteinModelPortaliQ9ULD4.
SMRiQ9ULD4. Positions 206-266, 315-391, 590-698, 1061-1194.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini606 – 67671BromoPROSITE-ProRule annotationAdd
BLAST
Domaini1076 – 115984PWWPPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi406 – 43227Glu-richAdd
BLAST

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 PWWP domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri212 – 26251PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

eggNOGiKOG0955. Eukaryota.
COG5076. LUCA.
COG5141. LUCA.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000000705.
HOVERGENiHBG004895.
InParanoidiQ9ULD4.
KOiK11350.
OMAiLDADVEY.
OrthoDBiEOG7FBRM7.
PhylomeDBiQ9ULD4.
TreeFamiTF316118.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR019542. Enhancer_polycomb-like_N.
IPR000313. PWWP_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF10513. EPL1. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULD4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

TSSYL
Length:1,205
Mass (Da):135,745
Last modified:July 19, 2005 - v2
Checksum:iF51DCAB253ED35C7
GO
Isoform 2 (identifier: Q9ULD4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     727-996: Missing.

Note: No experimental confirmation available.
Show »
Length:935
Mass (Da):106,187
Checksum:i1BCEE6338BAE1ABB
GO
Isoform 3 (identifier: Q9ULD4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     727-996: Missing.
     997-1060: Missing.

Note: No experimental confirmation available.
Show »
Length:871
Mass (Da):99,713
Checksum:iED046A8987D83B7E
GO

Sequence cautioni

The sequence BAA86600.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1075 – 10751E → K in BAA86600 (PubMed:10574462).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771S → G.
Corresponds to variant rs45504893 [ dbSNP | Ensembl ].
VAR_061042
Natural varianti278 – 2781A → G.
Corresponds to variant rs17658935 [ dbSNP | Ensembl ].
VAR_048431

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei727 – 996270Missing in isoform 2 and isoform 3. 1 PublicationVSP_055549Add
BLAST
Alternative sequencei997 – 106064Missing in isoform 3. 1 PublicationVSP_055550Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033112 mRNA. Translation: BAA86600.1. Different initiation.
Z84485 Genomic DNA. Translation: CAI21669.1.
CH471081 Genomic DNA. Translation: EAX03878.1.
BC117387 mRNA. Translation: AAI17388.1.
BC143917 mRNA. Translation: AAI43918.1.
BC143918 mRNA. Translation: AAI43919.1.
CCDSiCCDS34437.1. [Q9ULD4-1]
RefSeqiNP_056510.2. NM_015695.2. [Q9ULD4-1]
XP_005249067.1. XM_005249010.1. [Q9ULD4-1]
XP_005249068.1. XM_005249011.2. [Q9ULD4-1]
XP_011512791.1. XM_011514489.1. [Q9ULD4-1]
UniGeneiHs.520096.

Genome annotation databases

EnsembliENST00000339717; ENSP00000345419; ENSG00000096070. [Q9ULD4-2]
ENST00000357641; ENSP00000350267; ENSG00000096070. [Q9ULD4-1]
ENST00000534694; ENSP00000434501; ENSG00000096070. [Q9ULD4-3]
GeneIDi27154.
KEGGihsa:27154.
UCSCiuc003olv.5. human. [Q9ULD4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB033112 mRNA. Translation: BAA86600.1. Different initiation.
Z84485 Genomic DNA. Translation: CAI21669.1.
CH471081 Genomic DNA. Translation: EAX03878.1.
BC117387 mRNA. Translation: AAI17388.1.
BC143917 mRNA. Translation: AAI43918.1.
BC143918 mRNA. Translation: AAI43919.1.
CCDSiCCDS34437.1. [Q9ULD4-1]
RefSeqiNP_056510.2. NM_015695.2. [Q9ULD4-1]
XP_005249067.1. XM_005249010.1. [Q9ULD4-1]
XP_005249068.1. XM_005249011.2. [Q9ULD4-1]
XP_011512791.1. XM_011514489.1. [Q9ULD4-1]
UniGeneiHs.520096.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFSX-ray1.90A/B1056-1195[»]
ProteinModelPortaliQ9ULD4.
SMRiQ9ULD4. Positions 206-266, 315-391, 590-698, 1061-1194.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118036. 6 interactions.
IntActiQ9ULD4. 10 interactions.
MINTiMINT-7241520.
STRINGi9606.ENSP00000350267.

Chemistry

BindingDBiQ9ULD4.
ChEMBLiCHEMBL3108644.
GuidetoPHARMACOLOGYi2731.

PTM databases

iPTMnetiQ9ULD4.
PhosphoSiteiQ9ULD4.

Polymorphism and mutation databases

BioMutaiBRPF3.
DMDMi71153496.

Proteomic databases

EPDiQ9ULD4.
MaxQBiQ9ULD4.
PaxDbiQ9ULD4.
PRIDEiQ9ULD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339717; ENSP00000345419; ENSG00000096070. [Q9ULD4-2]
ENST00000357641; ENSP00000350267; ENSG00000096070. [Q9ULD4-1]
ENST00000534694; ENSP00000434501; ENSG00000096070. [Q9ULD4-3]
GeneIDi27154.
KEGGihsa:27154.
UCSCiuc003olv.5. human. [Q9ULD4-1]

Organism-specific databases

CTDi27154.
GeneCardsiBRPF3.
H-InvDBHIX0005816.
HIX0200828.
HGNCiHGNC:14256. BRPF3.
HPAiHPA022787.
neXtProtiNX_Q9ULD4.
PharmGKBiPA25425.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0955. Eukaryota.
COG5076. LUCA.
COG5141. LUCA.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000000705.
HOVERGENiHBG004895.
InParanoidiQ9ULD4.
KOiK11350.
OMAiLDADVEY.
OrthoDBiEOG7FBRM7.
PhylomeDBiQ9ULD4.
TreeFamiTF316118.

Enzyme and pathway databases

ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

ChiTaRSiBRPF3. human.
GenomeRNAii27154.
PROiQ9ULD4.

Gene expression databases

BgeeiQ9ULD4.
CleanExiHS_BRPF3.
ExpressionAtlasiQ9ULD4. baseline and differential.
GenevisibleiQ9ULD4. HS.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR019542. Enhancer_polycomb-like_N.
IPR000313. PWWP_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF10513. EPL1. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS00633. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
  6. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962 AND SER-965, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-447; LYS-449 AND LYS-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-400; SER-403 AND SER-900, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural and histone binding ability characterizations of human PWWP domains."
    Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L., Qiu W., Wang Y., Min J.
    PLoS ONE 6:E18919-E18919(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1056-1195.

Entry informationi

Entry nameiBRPF3_HUMAN
AccessioniPrimary (citable) accession number: Q9ULD4
Secondary accession number(s): A6ND56
, A6NJE2, B7ZLN5, E7EX85, Q17RB6, Q5R3K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 19, 2005
Last modified: June 8, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.