Reviewed, UniProtKB/Swiss-Prot O95696 (BRD1_HUMAN)

Names and origin

Protein names

Recommended name:
    Bromodomain-containing protein 1
Alternative name(s):
    BR140-like protein

Gene names

Name:	BRD1
Synonyms:	BRL, BRPF2

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	1058 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. Ref.5
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.
Subcellular location	Nucleus.
Tissue specificity	Highly expressed in testis.
Sequence similarities	Contains 1 bromo domain. Contains 1 PHD-type zinc finger. Contains 1 PWWP domain.

Ontologies

Keywords
Cellular component	Nucleus
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.5 Inferred from direct assay. Source: UniProtKB
Cellular component	MOZ/MORF histone acetyltransferase complex Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1058	1058	Bromodomain-containing protein 1		PRO_0000211177
Regions
	Domain	579 – 649	71	Bromo
	Domain	929 – 1012	84	PWWP
	Zinc finger	214 – 264	51	PHD-type
Amino acid modifications
	Modified residue	25	1	Phosphoserine Ref.4
	Modified residue	128	1	Phosphoserine Ref.6
	Modified residue	368	1	N6-acetyllysine Ref.11
	Modified residue	418	1	N6-acetyllysine Ref.11
	Modified residue	516	1	N6-acetyllysine Ref.11
	Modified residue	519	1	N6-acetyllysine Ref.11
	Modified residue	523	1	N6-acetyllysine Ref.11
	Modified residue	903	1	N6-acetyllysine Ref.11
	Modified residue	1051	1	Phosphothreonine
	Modified residue	1052	1	Phosphoserine Ref.8
	Modified residue	1055	1	Phosphoserine Ref.8
Natural variations
	Natural variant	38	1	R → G: dbSNP rs11549978.		VAR_048424
	Natural variant	321	1	A → S: dbSNP rs12157714.		VAR_048425
	Natural variant	730	1	A → T: dbSNP rs35331092.		VAR_048426

Sequences

	Sequence		Length	Mass (Da)
	O95696-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6E7B07E8A030E104	FASTA	1,058	119,520
	10 20 30 40 50 60 MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII 70 80 90 100 110 120 LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSAHGT PASASALPEP 130 140 150 160 170 180 KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA 190 200 210 220 230 240 VSQSMFEFLM DRFEKESHCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA 250 260 270 280 290 300 VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 310 320 330 340 350 360 VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL 370 380 390 400 410 420 YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV 430 440 450 460 470 480 RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW 490 500 510 520 530 540 LLKRLSRNGA PLLRRLQSSL QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE 550 560 570 580 590 600 LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL 610 620 630 640 650 660 DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR AAVRLRDQGG 670 680 690 700 710 720 VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV DRLLDPANRA HLGLEEQLRE 730 740 750 760 770 780 LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPLPTGPGLE GFEEDGAALG 790 800 810 820 830 840 PEAGEEVLPR LETLLQPRKR SRSTCGDSEV EEESPGKRLD AGLTNGFGGA RSEQEPGGGL 850 860 870 880 890 900 GRKATPRRRC ASESSISSSN SPLCDSSFNA PKCGRGKPAL VRRHTLEDRS ELISCIENGN 910 920 930 940 950 960 YAKAARIAAE VGQSSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP KMPRVPGHHN 970 980 990 1000 1010 1020 GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW LPKSKMVPLG IDETIDKLKM 1030 1040 1050 MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP TSDLSDID

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cloning, mapping and expression of a novel gene, BRL, related to the AF10 leukaemia gene." McCullagh P., Chaplin T., Meerabux J., Grenzelias D., Lillington D., Poulsom R., Gregorini A., Saha V., Young B.D. Oncogene 18:7442-7452(1999) [PubMed: 10602503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16387653] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[6]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, MASS SPECTROMETRY.
[7]	"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.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052 AND SER-1055, MASS SPECTROMETRY.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; THR-1051 AND SER-1055, MASS SPECTROMETRY.
[10]	"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-128 AND SER-1055, MASS SPECTROMETRY. Tissue: T-cell.
[11]	"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-368; LYS-418; LYS-516; LYS-519; LYS-523 AND LYS-903, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF005067 mRNA. Translation: AAF34320.1. CR456408 mRNA. Translation: CAG30294.1. Z98885 Genomic DNA. Translation: CAB11574.1.
IPI	IPI00032214.
RefSeq	NP_055392.1.
UniGene	Hs.127950
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O95696. 2 interactions.
STRING	O95696.
PTM databases
PhosphoSite	O95696.
2-D gel databases
OGP	O95696.
Proteomic databases
PRIDE	O95696.
Genome annotation databases
Ensembl	ENST00000216267; ENSP00000216267; ENSG00000100425; Homo sapiens. [Genome view] ENST00000404034; ENSP00000384076; ENSG00000100425; Homo sapiens. [Genome view]
GeneID	23774.
KEGG	hsa:23774.
UCSC	uc003biv.1. human.
Organism-specific databases
CTD	23774.
GeneCards	GC22M048552.
H-InvDB	HIX0005816. HIX0016601.
HGNC	HGNC:1102. BRD1.
HPA	HPA000807. HPA001063.
MIM	604589. gene.
PharmGKB	PA25413.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O95696.
Gene expression databases
ArrayExpress	O95696.
Bgee	O95696.
CleanEx	HS_BRD1.
Genevestigator	O95696.
GermOnline	ENSG00000100425. 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. PF00628. PHD. 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	46753.
PMAP-CutDB	O95696.
SOURCE	Search...

Entry information

Entry name

BRD1_HUMAN

Accession

Primary (citable) accession number: O95696

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 1999
Last modified:	November 24, 2009
This is version 73 of the entry and version 1 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.