Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O95696

- BRD1_HUMAN

UniProt

O95696 - BRD1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bromodomain-containing protein 1

Gene

BRD1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri214 – 26451PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3 acetylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 1
Alternative name(s):
BR140-like protein
Bromodomain and PHD finger-containing protein 2
Gene namesi
Name:BRD1
Synonyms:BRL, BRPF2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:1102. BRD1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10581058Bromodomain-containing protein 1PRO_0000211177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine1 Publication
Modified residuei368 – 3681N6-acetyllysine1 Publication
Modified residuei516 – 5161N6-acetyllysine1 Publication
Modified residuei519 – 5191N6-acetyllysine1 Publication
Modified residuei903 – 9031N6-acetyllysine1 Publication
Modified residuei1052 – 10521Phosphoserine2 Publications
Modified residuei1055 – 10551Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95696.
PaxDbiO95696.
PRIDEiO95696.

2D gel databases

OGPiO95696.

PTM databases

PhosphoSiteiO95696.

Miscellaneous databases

PMAP-CutDBO95696.

Expressioni

Tissue specificityi

Highly expressed in testis.

Gene expression databases

BgeeiO95696.
CleanExiHS_BRD1.
ExpressionAtlasiO95696. baseline and differential.
GenevestigatoriO95696.

Organism-specific databases

HPAiHPA000807.
HPA001063.

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. Interacts (via PHD-type zinc finger domain) with unmodified histone H3. Interacts (via PWWP domain) with dimethylated and trimethylated 'Lys-79' on histone H3.4 Publications

Protein-protein interaction databases

BioGridi117273. 12 interactions.
IntActiO95696. 3 interactions.
MINTiMINT-1186761.
STRINGi9606.ENSP00000216267.

Structurei

Secondary structure

1
1058
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni205 – 2084Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi240 – 2423Combined sources
Helixi243 – 2464Combined sources
Helixi259 – 2668Combined sources
Turni328 – 3314Combined sources
Beta strandi338 – 3403Combined sources
Turni344 – 3463Combined sources
Beta strandi349 – 3513Combined sources
Helixi352 – 3587Combined sources
Beta strandi362 – 3698Combined sources
Turni371 – 3733Combined sources
Beta strandi376 – 3838Combined sources
Helixi386 – 3883Combined sources
Beta strandi389 – 3924Combined sources
Helixi566 – 58015Combined sources
Beta strandi586 – 5894Combined sources
Turni593 – 5953Combined sources
Helixi599 – 6024Combined sources
Helixi609 – 6179Combined sources
Helixi624 – 64118Combined sources
Helixi647 – 67630Combined sources
Beta strandi932 – 9354Combined sources
Beta strandi943 – 9475Combined sources
Helixi969 – 98012Combined sources
Beta strandi986 – 9916Combined sources
Beta strandi998 – 10025Combined sources
Helixi1003 – 10053Combined sources
Beta strandi1006 – 10116Combined sources
Helixi1013 – 10208Combined sources
Helixi1026 – 104520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KU3NMR-A208-269[»]
2L43NMR-A205-269[»]
2LQ6NMR-A317-392[»]
3LYIX-ray2.10A/B925-1049[»]
3RCWX-ray2.21A/B/C/D/E/F/G/H556-688[»]
ProteinModelPortaliO95696.
SMRiO95696. Positions 208-269, 317-394, 563-680, 928-1047.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95696.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini579 – 64971BromoPROSITE-ProRule annotationAdd
BLAST
Domaini929 – 101284PWWPPROSITE-ProRule annotationAdd
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 fingeri214 – 26451PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

eggNOGiCOG5141.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000000705.
HOVERGENiHBG004895.
InParanoidiO95696.
KOiK11349.
OMAiSERPPVC.
OrthoDBiEOG7FBRM7.
PhylomeDBiO95696.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

TSDLSDID
Length:1,058
Mass (Da):119,520
Last modified:May 1, 1999 - v1
Checksum:i6E7B07E8A030E104
GO
Isoform 2 (identifier: O95696-2) [UniParc]FASTAAdd to Basket

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

Note: Contains a phosphoserine at position 906.

Show »
Length:1,189
Mass (Da):133,243
Checksum:i770DB2F610CB5052
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381R → G.
Corresponds to variant rs11549978 [ dbSNP | Ensembl ].
VAR_048424
Natural varianti321 – 3211A → S.
Corresponds to variant rs12157714 [ dbSNP | Ensembl ].
VAR_048425
Natural varianti730 – 7301A → T.
Corresponds to variant rs35331092 [ dbSNP | Ensembl ].
VAR_048426

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei786 – 7861E → EGDKSPPKLEPSDALPLPSN SETNSEPPTLKPVELNPEQS KLFKRVTFDNESHSACTQSA LVSGRPPEPTRASSGDVPAA AASAVAEPASDVNRRTSVLF CKSKSVSPPKSAKNTETQPT SPQLGTKTFLSV in isoform 2. 1 PublicationVSP_040262

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14080.1. [O95696-1]
RefSeqiNP_055392.1. NM_014577.1. [O95696-1]
XP_005261528.1. XM_005261471.1. [O95696-2]
XP_006724273.1. XM_006724210.1. [O95696-2]
XP_006724274.1. XM_006724211.1. [O95696-2]
XP_006724276.1. XM_006724213.1. [O95696-1]
UniGeneiHs.127950.

Genome annotation databases

EnsembliENST00000216267; ENSP00000216267; ENSG00000100425. [O95696-1]
ENST00000404034; ENSP00000384076; ENSG00000100425. [O95696-1]
ENST00000404760; ENSP00000385858; ENSG00000100425. [O95696-2]
ENST00000457780; ENSP00000410042; ENSG00000100425. [O95696-2]
GeneIDi23774.
KEGGihsa:23774.
UCSCiuc003biu.4. human. [O95696-2]
uc003biv.3. human. [O95696-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS14080.1. [O95696-1 ]
RefSeqi NP_055392.1. NM_014577.1. [O95696-1 ]
XP_005261528.1. XM_005261471.1. [O95696-2 ]
XP_006724273.1. XM_006724210.1. [O95696-2 ]
XP_006724274.1. XM_006724211.1. [O95696-2 ]
XP_006724276.1. XM_006724213.1. [O95696-1 ]
UniGenei Hs.127950.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KU3 NMR - A 208-269 [» ]
2L43 NMR - A 205-269 [» ]
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 [» ]
ProteinModelPortali O95696.
SMRi O95696. Positions 208-269, 317-394, 563-680, 928-1047.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117273. 12 interactions.
IntActi O95696. 3 interactions.
MINTi MINT-1186761.
STRINGi 9606.ENSP00000216267.

Chemistry

ChEMBLi CHEMBL2176774.

PTM databases

PhosphoSitei O95696.

2D gel databases

OGPi O95696.

Proteomic databases

MaxQBi O95696.
PaxDbi O95696.
PRIDEi O95696.

Protocols and materials databases

DNASUi 23774.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216267 ; ENSP00000216267 ; ENSG00000100425 . [O95696-1 ]
ENST00000404034 ; ENSP00000384076 ; ENSG00000100425 . [O95696-1 ]
ENST00000404760 ; ENSP00000385858 ; ENSG00000100425 . [O95696-2 ]
ENST00000457780 ; ENSP00000410042 ; ENSG00000100425 . [O95696-2 ]
GeneIDi 23774.
KEGGi hsa:23774.
UCSCi uc003biu.4. human. [O95696-2 ]
uc003biv.3. human. [O95696-1 ]

Organism-specific databases

CTDi 23774.
GeneCardsi GC22M050166.
HGNCi HGNC:1102. BRD1.
HPAi HPA000807.
HPA001063.
MIMi 604589. gene.
neXtProti NX_O95696.
PharmGKBi PA25413.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5141.
GeneTreei ENSGT00740000114866.
HOGENOMi HOG000000705.
HOVERGENi HBG004895.
InParanoidi O95696.
KOi K11349.
OMAi SERPPVC.
OrthoDBi EOG7FBRM7.
PhylomeDBi O95696.
TreeFami TF316118.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi BRD1. human.
EvolutionaryTracei O95696.
GenomeRNAii 23774.
NextBioi 46753.
PMAP-CutDB O95696.
PROi O95696.
SOURCEi Search...

Gene expression databases

Bgeei O95696.
CleanExi HS_BRD1.
ExpressionAtlasi O95696. baseline and differential.
Genevestigatori O95696.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR001487. 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 ]
Pfami PF00439. Bromodomain. 1 hit.
PF10513. EPL1. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
SM00249. PHD. 2 hits.
SM00293. PWWP. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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 AND LYS-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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. Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 556-688.

Entry informationi

Entry nameiBRD1_HUMAN
AccessioniPrimary (citable) accession number: O95696
Secondary accession number(s): A6ZJA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 121 of the entry and version 1 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 22
    Human chromosome 22: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3