O95696 (BRD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bromodomain-containing protein 1

Alternative name(s):
BR140-like protein
Bromodomain and PHD finger-containing protein 2

Gene names

Name:	BRD1
Synonyms:	BRL, BRPF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1058 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.7 Ref.14
Subunit structure	Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts (via PHD-type zinc finger domain) with unmodified histone H3. Interacts (via PWWP domain) with dimethylated and trimethylated 'Lys-79' on histone H3. Ref.7 Ref.8 Ref.14 Ref.15
Subcellular location	Nucleus Ref.14.
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	Alternative splicing 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.7. Source: UniProtKB
Cellular_component	MOZ/MORF histone acetyltransferase complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	histone binding Inferred from direct assay Ref.14. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95696-1)

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.

Isoform 2 (identifier: O95696-2)

The sequence of this isoform differs from the canonical sequence as follows:
     786-786: E → EGDKSPPKLE...QLGTKTFLSV

Note: Contains a phosphoserine at position 906.

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

128

1

Phosphoserine Ref.13

Modified residue

368

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

1052

1

Phosphoserine Ref.12 Ref.13

Modified residue

1055

1

Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13

Natural variations

Alternative sequence

786

1

E → EGDKSPPKLEPSDALPLPSN SETNSEPPTLKPVELNPEQS KLFKRVTFDNESHSACTQSA LVSGRPPEPTRASSGDVPAA AASAVAEPASDVNRRTSVLF CKSKSVSPPKSAKNTETQPT SPQLGTKTFLSV in isoform 2.

VSP_040262

Natural variant

38

1

R → G.
Corresponds to variant rs11549978 [ dbSNP | Ensembl ].

VAR_048424

Natural variant

321

1

A → S.
Corresponds to variant rs12157714 [ dbSNP | Ensembl ].

VAR_048425

Natural variant

730

1

A → T.
Corresponds to variant rs35331092 [ dbSNP | Ensembl ].

VAR_048426

Secondary structure

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1058

Helix Strand Turn

Details...

Beta strand

218 – 220

3

Beta strand

222 – 225

4

Beta strand

227 – 229

3

Beta strand

231 – 233

3

Beta strand

235 – 237

3

Beta strand

240 – 242

3

Helix

243 – 246

4

Helix

259 – 266

8

Turn

328 – 331

4

Beta strand

338 – 340

3

Turn

344 – 346

3

Beta strand

349 – 351

3

Helix

352 – 358

7

Beta strand

362 – 369

8

Turn

371 – 373

3

Beta strand

376 – 383

8

Helix

386 – 388

3

Beta strand

389 – 392

4

Helix

566 – 580

15

Beta strand

586 – 589

4

Turn

593 – 595

3

Helix

599 – 602

4

Helix

609 – 617

9

Helix

624 – 641

18

Helix

647 – 676

30

Beta strand

932 – 935

4

Beta strand

943 – 947

5

Helix

969 – 980

12

Beta strand

986 – 991

6

Beta strand

998 – 1002

5

Helix

1003 – 1005

3

Beta strand

1006 – 1011

6

Helix

1013 – 1020

8

Helix

1026 – 1045

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 770DB2F610CB5052	FASTA	1,189	133,243
	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 PEAGEEGDKS PPKLEPSDAL PLPSNSETNS EPPTLKPVEL NPEQSKLFKR VTFDNESHSA 850 860 870 880 890 900 CTQSALVSGR PPEPTRASSG DVPAAAASAV AEPASDVNRR TSVLFCKSKS VSPPKSAKNT 910 920 930 940 950 960 ETQPTSPQLG TKTFLSVVLP RLETLLQPRK RSRSTCGDSE VEEESPGKRL DAGLTNGFGG 970 980 990 1000 1010 1020 ARSEQEPGGG LGRKATPRRR CASESSISSS NSPLCDSSFN APKCGRGKPA LVRRHTLEDR 1030 1040 1050 1060 1070 1080 SELISCIENG NYAKAARIAA EVGQSSMWIS TDAAASVLEP LKVVWAKCSG YPSYPALIID 1090 1100 1110 1120 1130 1140 PKMPRVPGHH NGVTIPAPPL DVLKIGEHMQ TKSDEKLFLV LFFDNKRSWQ WLPKSKMVPL 1150 1160 1170 1180 GIDETIDKLK MMEGRNSSIR KAVRIAFDRA MNHLSRVHGE PTSDLSDID

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"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.
[8]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, MASS SPECTROMETRY. Tissue: Leukemic 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.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-368; LYS-516; LYS-519; LYS-523 AND LYS-903, MASS SPECTROMETRY.
[12]	"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-1052 AND SER-1055, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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-128; SER-1052 AND SER-1055, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 (ISOFORM 2), MASS SPECTROMETRY.
[14]	"Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF)." Qin S., Jin L., Zhang J., Liu L., Ji P., Wu M., Wu J., Shi Y. J. Biol. Chem. 286:36944-36955(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 208-269, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UNMODIFIED HISTONE H3.
[15]	"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 (2.1 ANGSTROMS) OF 925-1049, INTERACTION WITH METHYLATED HISTONE H3.
[16]	"Histone recognition and large-scale structural analysis of the human bromodomain family." Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S. Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 556-688.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF005067 mRNA. Translation: AAF34320.1.
CR456408 mRNA. Translation: CAG30294.1.
AK292428 mRNA. Translation: BAF85117.1.
Z98885 Genomic DNA. Translation: CAB11574.1.
Z98885 Genomic DNA. Translation: CAO72061.1.
CH471138 Genomic DNA. Translation: EAW73473.1.

IPI

IPI00032214.
IPI00384471.

RefSeq

NP_055392.1. NM_014577.1.

UniGene

Hs.127950.
Hs.679408.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KU3	NMR	-	A	208-269	[»]
2L43	NMR	-	A	208-269	[»]
2LQ6	NMR	-	A	317-392	[»]
3LYI	X-ray	2.10	A/B	925-1049	[»]
3RCW	X-ray	2.21	A/B/C/D/E/F/G/H	556-688	[»]

ProteinModelPortal

O95696.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95696. 2 interactions.

MINT

MINT-1186761.

STRING

9606.ENSP00000216267.

PTM databases

PhosphoSite

O95696.

2D gel databases

OGP

O95696.

Proteomic databases

PaxDb

O95696.

PRIDE

O95696.

Protocols and materials databases

DNASU

23774.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216267; ENSP00000216267; ENSG00000100425.
ENST00000404034; ENSP00000384076; ENSG00000100425.
ENST00000404760; ENSP00000385858; ENSG00000100425.

GeneID

23774.

KEGG

hsa:23774.

UCSC

uc003biu.4. human.
uc003biv.3. human.

Organism-specific databases

CTD

23774.

GeneCards

GC22M050166.

HGNC

HGNC:1102. BRD1.

HPA

HPA000807.
HPA001063.

MIM

604589. gene.

neXtProt

NX_O95696.

PharmGKB

PA25413.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5141.

HOGENOM

HOG000000705.

HOVERGEN

HBG004895.

KO

K11349.

OMA

KVGEHMQ.

OrthoDB

EOG44QT08.

Gene expression databases

ArrayExpress

O95696.

Bgee

O95696.

CleanEx

HS_BRD1.

Genevestigator

O95696.

GermOnline

ENSG00000100425. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.30.40.10. 1 hit.

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]

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

EvolutionaryTrace

O95696.

GenomeRNAi

23774.

NextBio

46753.

PMAP-CutDB

O95696.

SOURCE

Search...

Entry information

Entry name

BRD1_HUMAN

Accession

Primary (citable) accession number: O95696
Secondary accession number(s): A6ZJA4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 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.