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O95696

- BRD1_HUMAN

UniProt

O95696 - BRD1_HUMAN

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Protein

Bromodomain-containing protein 1

Gene
BRD1, BRL, BRPF2
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-typeAdd
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

ArrayExpressiO95696.
BgeeiO95696.
CleanExiHS_BRD1.
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 – 2084
Beta strandi218 – 2203
Beta strandi222 – 2254
Beta strandi227 – 2293
Beta strandi231 – 2333
Beta strandi235 – 2373
Beta strandi240 – 2423
Helixi243 – 2464
Helixi259 – 2668
Turni328 – 3314
Beta strandi338 – 3403
Turni344 – 3463
Beta strandi349 – 3513
Helixi352 – 3587
Beta strandi362 – 3698
Turni371 – 3733
Beta strandi376 – 3838
Helixi386 – 3883
Beta strandi389 – 3924
Helixi566 – 58015
Beta strandi586 – 5894
Turni593 – 5953
Helixi599 – 6024
Helixi609 – 6179
Helixi624 – 64118
Helixi647 – 67630
Beta strandi932 – 9354
Beta strandi943 – 9475
Helixi969 – 98012
Beta strandi986 – 9916
Beta strandi998 – 10025
Helixi1003 – 10053
Beta strandi1006 – 10116
Helixi1013 – 10208
Helixi1026 – 104520

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiO95696.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini579 – 64971BromoAdd
BLAST
Domaini929 – 101284PWWPAdd
BLAST

Sequence similaritiesi

Contains 1 bromo domain.
Contains 1 PWWP domain.

Keywords - Domaini

Bromodomain, Zinc-finger

Phylogenomic databases

eggNOGiCOG5141.
HOGENOMiHOG000000705.
HOVERGENiHBG004895.
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

MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR     50
ISIFDPLEII LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK 100
NEALPSAHGT PASASALPEP KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL 150
DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA VSQSMFEFLM DRFEKESHCE 200
NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA VHQECYGVPY 250
IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 300
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF 350
HVTCAQKAGL YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI 400
YGDVEMKNGV CRKESSVKTV RSTSKVRKKA KKAKKALAEP CAVLPTVCAP 450
YIPPQRLNRI ANQVAIQRKK QFVERAHSYW LLKRLSRNGA PLLRRLQSSL 500
QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE LLRKREKLKR 550
EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL 600
DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR 650
AAVRLRDQGG VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV 700
DRLLDPANRA HLGLEEQLRE LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL 750
LRNKLSQQHS QPLPTGPGLE GFEEDGAALG PEAGEEVLPR LETLLQPRKR 800
SRSTCGDSEV EEESPGKRLD AGLTNGFGGA RSEQEPGGGL GRKATPRRRC 850
ASESSISSSN SPLCDSSFNA PKCGRGKPAL VRRHTLEDRS ELISCIENGN 900
YAKAARIAAE VGQSSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP 950
KMPRVPGHHN GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW 1000
LPKSKMVPLG IDETIDKLKM MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP 1050
TSDLSDID 1058
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. VSP_040262

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 ]
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.
HOGENOMi HOG000000705.
HOVERGENi HBG004895.
KOi K11349.
OMAi SERPPVC.
OrthoDBi EOG7FBRM7.
PhylomeDBi O95696.
TreeFami TF316118.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

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

Gene expression databases

ArrayExpressi O95696.
Bgeei O95696.
CleanExi HS_BRD1.
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: September 3, 2014
This is version 118 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

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