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Q9H0E9

- BRD8_HUMAN

UniProt

Q9H0E9 - BRD8_HUMAN

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Protein
Bromodomain-containing protein 8
Gene
BRD8, SMAP, SMAP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.3 Publications

GO - Molecular functioni

  1. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  2. thyroid hormone receptor activity Source: ProtInc

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. chromatin organization Source: Reactome
  3. histone H2A acetylation Source: UniProtKB
  4. histone H4 acetylation Source: UniProtKB
  5. intracellular receptor signaling pathway Source: GOC
  6. regulation of growth Source: UniProtKB-KW
  7. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  8. regulation of transcription, DNA-templated Source: UniProtKB
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 8
Alternative name(s):
Skeletal muscle abundant protein
Skeletal muscle abundant protein 2
Thyroid hormone receptor coactivating protein of 120 kDa
Short name:
TrCP120
p120
Gene namesi
Name:BRD8
Synonyms:SMAP, SMAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:19874. BRD8.

Subcellular locationi

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: UniProtKB
  2. Swr1 complex Source: UniProtKB
  3. mitochondrion Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134923194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12351235Bromodomain-containing protein 8
PRO_0000211185Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851N6-acetyllysine By similarity
Modified residuei387 – 3871Phosphoserine1 Publication
Modified residuei481 – 4811N6-acetyllysine1 Publication
Modified residuei621 – 6211Phosphoserine1 Publication
Modified residuei637 – 6371Phosphoserine1 Publication
Modified residuei641 – 6411Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0E9.
PaxDbiQ9H0E9.
PRIDEiQ9H0E9.

Miscellaneous databases

PMAP-CutDBQ9H0E9.

Expressioni

Tissue specificityi

Expressed in adipose tissue, brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.1 Publication

Gene expression databases

ArrayExpressiQ9H0E9.
BgeeiQ9H0E9.
CleanExiHS_BRD8.
HS_SMAP2.
GenevestigatoriQ9H0E9.

Organism-specific databases

HPAiHPA001841.

Interactioni

Subunit structurei

Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. BRD8 isoform 2 interacts with RXRA/NR2B1 and THRB/ERBA2 By similarity. Component of a SWR1-like complex.5 Publications

Protein-protein interaction databases

BioGridi116108. 18 interactions.
IntActiQ9H0E9. 13 interactions.
MINTiMINT-3065717.
STRINGi9606.ENSP00000254900.

Structurei

3D structure databases

ProteinModelPortaliQ9H0E9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini724 – 79471Bromo 1
Add
BLAST
Domaini1120 – 119071Bromo 2
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili97 – 17175 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Contains 2 bromo domains.

Keywords - Domaini

Bromodomain, Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5076.
HOGENOMiHOG000074125.
HOVERGENiHBG050732.
InParanoidiQ9H0E9.
KOiK11321.
PhylomeDBiQ9H0E9.
TreeFamiTF106422.

Family and domain databases

Gene3Di1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 2 hits.
PROSITEiPS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H0E9-1) [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

MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA     50
EPGRPPDWFS QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL 100
TAERVEELKK VIKETQERYR RLKRDAELIQ AGHMDSRLDE LCNDIATKKK 150
LEEEEAEVKR KATDAAYQAR QAVKTPPRRL PTVMVRSPID SASPGGDYPL 200
GDLTPTTMEE ATSGVNESEM AVASGHLNST GVLLEVGGVL PMIHGGEIQQ 250
TPNTVAASPA ASGAPTLSRL LEAGPTQFTT PLASFTTVAS EPPVKLVPPP 300
VESVSQATIV MMPALPAPSS APAVSTTESV APVSQPDNCV PMEAVGDPHT 350
VTVSMDSSEI SMIINSIKEE CFRSGVAEAP VGSKAPSIDG KEELDLAEKM 400
DIAVSYTGEE LDFETVGDII AIIEDKVDDH PEVLDVAAVE AALSFCEEND 450
DPQSLPGPWE HPIQQERDKP VPLPAPEMTV KQERLDFEET ENKGIHELVD 500
IREPSAEIKV EPAEPEPVIS GAEIVAGVVP ATSMEPPELR SQDLDEELGS 550
TAAGEIVEAD VAIGKGDETP LTNVKTEASP ESMLSPSHGS NPIEDPLEAE 600
TQHKFEMSDS LKEESGTIFG SQIKDAPGED EEEDGVSEAA SLEEPKEEDQ 650
GEGYLSEMDN EPPVSESDDG FSIHNATLQS HTLADSIPSS PASSQFSVCS 700
EDQEAIQAQK IWKKAIMLVW RAAANHRYAN VFLQPVTDDI APGYHSIVQR 750
PMDLSTIKKN IENGLIRSTA EFQRDIMLMF QNAVMYNSSD HDVYHMAVEM 800
QRDVLEQIQQ FLATQLIMQT SESGISAKSL RGRDSTRKQD ASEKDSVPMG 850
SPAFLLSLFM GHEWVWLDSE QDHPNDSELS NDCRSLFSSW DSSLDLDVGN 900
WRETEDPEAE ELEESSPERE PSELLVGDGG SEESQEAARK ASHQNLLHFL 950
SEVAYLMEPL CISSNESSEG CCPPSGTRQE GREIKASEGE RELCRETEEL 1000
SAKGDPLVAE KPLGENGKPE VASAPSVICT VQGLLTESEE GEAQQESKGE 1050
DQGEVYVSEM EDQPPSGECD DAFNIKETPL VDTLFSHATS SKLTDLSQDD 1100
PVQDHLLFKK TLLPVWKMIA SHRFSSPFLK PVSERQAPGY KDVVKRPMDL 1150
TSLKRNLSKG RIRTMAQFLR DLMLMFQNAV MYNDSDHHVY HMAVEMRQEV 1200
LEQIQVLNIW LDKRKGSSSL EGEPANPVDD GKPVF 1235
Length:1,235
Mass (Da):135,336
Last modified:November 30, 2010 - v2
Checksum:i3738078C77FC17D1
GO
Isoform 2 (identifier: Q9H0E9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
     860-878: MGHEWVWLDSEQDHPNDSE → DGGTRGRRCAIEADMKMKK
     879-1235: Missing.

Note: Contains a phosphothreonine at position 264. Contains a phosphoserine at position 268. Contains a phosphoserine at position 284. Contains a phosphoserine at position 924.

Show »
Length:951
Mass (Da):102,839
Checksum:i80C0A7A6ACB4E8ED
GO
Isoform 3 (identifier: Q9H0E9-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-147: MATGTGKHKL...LDELCNDIAT → MSFAMTL
     215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
     263-301: Missing.
     845-859: Missing.
     860-878: MGHEWVWLDSEQDHPNDSE → DGGTRGRRCAIEADMKMKK
     879-1235: Missing.

Note: Contains a phosphothreonine at position 124. Contains a phosphoserine at position 128. Contains a phosphoserine at position 144.

Show »
Length:757
Mass (Da):81,354
Checksum:iC1D728727505F85D
GO
Isoform 4 (identifier: Q9H0E9-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
     263-332: Missing.
     846-846: S → G
     847-975: Missing.
     979-992: QEGREIKASEGERE → GRRCAIEADMKMKK
     993-1235: Missing.

Note: Contains a phosphothreonine at position 264. Contains a phosphoserine at position 268. Contains a phosphoserine at position 284.

Show »
Length:866
Mass (Da):94,297
Checksum:i3400AEB14E9412FC
GO

Sequence cautioni

The sequence AAB87858.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH08039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH08076.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAA63925.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti490 – 4901T → M.1 Publication
Corresponds to variant rs11750814 [ dbSNP | Ensembl ].
VAR_030695
Natural varianti896 – 8961L → P.
Corresponds to variant rs6883021 [ dbSNP | Ensembl ].
VAR_048428
Natural varianti1198 – 11981Q → R.6 Publications
Corresponds to variant rs412051 [ dbSNP | Ensembl ].
VAR_048429

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 147147MATGT…NDIAT → MSFAMTL in isoform 3.
VSP_012879Add
BLAST
Alternative sequencei215 – 2151V → VTPGTLPSTPVTSFPGIPDT LPPGSAPLEAPMTPVTDDSP QKKMLGQKATPPPSPLLSEL LKKGSLLPTSPRLV in isoform 2, isoform 3 and isoform 4.
VSP_012880
Alternative sequencei263 – 33270Missing in isoform 4.
VSP_023187Add
BLAST
Alternative sequencei263 – 30139Missing in isoform 3.
VSP_012881Add
BLAST
Alternative sequencei845 – 85915Missing in isoform 3.
VSP_012882Add
BLAST
Alternative sequencei846 – 8461S → G in isoform 4.
VSP_023188
Alternative sequencei847 – 975129Missing in isoform 4.
VSP_023189Add
BLAST
Alternative sequencei860 – 87819MGHEW…PNDSE → DGGTRGRRCAIEADMKMKK in isoform 2 and isoform 3.
VSP_012883Add
BLAST
Alternative sequencei879 – 1235357Missing in isoform 2 and isoform 3.
VSP_012884Add
BLAST
Alternative sequencei979 – 99214QEGRE…EGERE → GRRCAIEADMKMKK in isoform 4.
VSP_023190Add
BLAST
Alternative sequencei993 – 1235243Missing in isoform 4.
VSP_023191Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti306 – 3061Q → H in AAB87858. 1 Publication
Sequence conflicti557 – 5571V → L in CAA60949. 1 Publication
Sequence conflicti557 – 5571V → L in CAA63925. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X87613 mRNA. Translation: CAA60949.1.
AL136823 mRNA. Translation: CAB66757.1.
AB209079 mRNA. Translation: BAD92316.1.
AC109442 Genomic DNA. No translation available.
AC113382 Genomic DNA. No translation available.
BC008039 mRNA. Translation: AAH08039.1. Different initiation.
BC008076 mRNA. Translation: AAH08076.1. Different initiation.
AF016270 mRNA. Translation: AAB87858.1. Different initiation.
X94234 mRNA. Translation: CAA63925.1. Different initiation.
CCDSiCCDS34241.1. [Q9H0E9-2]
CCDS4198.1. [Q9H0E9-1]
CCDS54907.1. [Q9H0E9-4]
PIRiS58225.
S68142.
RefSeqiNP_001157798.1. NM_001164326.1. [Q9H0E9-4]
NP_006687.3. NM_006696.3. [Q9H0E9-2]
NP_631938.1. NM_139199.1.
UniGeneiHs.519337.

Genome annotation databases

EnsembliENST00000230901; ENSP00000230901; ENSG00000112983. [Q9H0E9-2]
ENST00000254900; ENSP00000254900; ENSG00000112983. [Q9H0E9-1]
ENST00000411594; ENSP00000394330; ENSG00000112983. [Q9H0E9-4]
GeneIDi10902.
KEGGihsa:10902.
UCSCiuc003lcf.1. human. [Q9H0E9-1]
uc003lcg.3. human. [Q9H0E9-2]
uc003lci.3. human. [Q9H0E9-4]
uc021yea.1. human. [Q9H0E9-3]

Polymorphism databases

DMDMi313104080.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X87613 mRNA. Translation: CAA60949.1 .
AL136823 mRNA. Translation: CAB66757.1 .
AB209079 mRNA. Translation: BAD92316.1 .
AC109442 Genomic DNA. No translation available.
AC113382 Genomic DNA. No translation available.
BC008039 mRNA. Translation: AAH08039.1 . Different initiation.
BC008076 mRNA. Translation: AAH08076.1 . Different initiation.
AF016270 mRNA. Translation: AAB87858.1 . Different initiation.
X94234 mRNA. Translation: CAA63925.1 . Different initiation.
CCDSi CCDS34241.1. [Q9H0E9-2 ]
CCDS4198.1. [Q9H0E9-1 ]
CCDS54907.1. [Q9H0E9-4 ]
PIRi S58225.
S68142.
RefSeqi NP_001157798.1. NM_001164326.1. [Q9H0E9-4 ]
NP_006687.3. NM_006696.3. [Q9H0E9-2 ]
NP_631938.1. NM_139199.1.
UniGenei Hs.519337.

3D structure databases

ProteinModelPortali Q9H0E9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116108. 18 interactions.
IntActi Q9H0E9. 13 interactions.
MINTi MINT-3065717.
STRINGi 9606.ENSP00000254900.

Polymorphism databases

DMDMi 313104080.

Proteomic databases

MaxQBi Q9H0E9.
PaxDbi Q9H0E9.
PRIDEi Q9H0E9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230901 ; ENSP00000230901 ; ENSG00000112983 . [Q9H0E9-2 ]
ENST00000254900 ; ENSP00000254900 ; ENSG00000112983 . [Q9H0E9-1 ]
ENST00000411594 ; ENSP00000394330 ; ENSG00000112983 . [Q9H0E9-4 ]
GeneIDi 10902.
KEGGi hsa:10902.
UCSCi uc003lcf.1. human. [Q9H0E9-1 ]
uc003lcg.3. human. [Q9H0E9-2 ]
uc003lci.3. human. [Q9H0E9-4 ]
uc021yea.1. human. [Q9H0E9-3 ]

Organism-specific databases

CTDi 10902.
GeneCardsi GC05M137475.
HGNCi HGNC:19874. BRD8.
HPAi HPA001841.
MIMi 602848. gene.
neXtProti NX_Q9H0E9.
PharmGKBi PA134923194.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5076.
HOGENOMi HOG000074125.
HOVERGENi HBG050732.
InParanoidi Q9H0E9.
KOi K11321.
PhylomeDBi Q9H0E9.
TreeFami TF106422.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi BRD8. human.
GeneWikii BRD8.
GenomeRNAii 10902.
NextBioi 41403.
PMAP-CutDB Q9H0E9.
PROi Q9H0E9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H0E9.
Bgeei Q9H0E9.
CleanExi HS_BRD8.
HS_SMAP2.
Genevestigatori Q9H0E9.

Family and domain databases

Gene3Di 1.20.920.10. 2 hits.
InterProi IPR001487. Bromodomain.
[Graphical view ]
Pfami PF00439. Bromodomain. 2 hits.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 2 hits.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 2 hits.
PROSITEi PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a human cDNA encoding a putative transcription factor containing a bromodomain."
    Nielsen M.S., Petersen C.M., Gliemann J., Madsen P.
    Biochim. Biophys. Acta 1306:14-16(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANT ARG-1198.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-1198.
    Tissue: Testis.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS MET-490 AND ARG-1198.
    Tissue: Brain.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 2-1235 (ISOFORM 2), VARIANT ARG-1198.
    Tissue: Muscle.
  6. "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein."
    Monden T., Wondisford F.E., Hollenberg A.N.
    J. Biol. Chem. 272:29834-29841(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-1235 (ISOFORM 2), INTERACTION WITH THRB, VARIANT ARG-1198.
    Tissue: Brain.
  7. Nielsen M.S.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-1235 (ISOFORM 4), VARIANT ARG-1198.
    Tissue: Skin.
  8. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-44; 63-79; 83-98; 125-137; 138-148; 150-159; 270-295; 385-399; 485-493; 541-565; 576-604 AND 625-646, IDENTIFICATION IN NUA4 COMPLEX (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
  9. "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers."
    Monden T., Kishi M., Hosoya T., Satoh T., Wondisford F.E., Hollenberg A.N., Yamada M., Mori M.
    Mol. Endocrinol. 13:1695-1703(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RXRA.
  10. "The highly conserved and multifunctional NuA4 HAT complex."
    Doyon Y., Cote J.
    Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON NUA4 COMPLEX.
  11. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX (ISOFORMS 1 AND 2), IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637 AND SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-268 AND SER-284 (ISOFORMS 2 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124; SER-128 AND SER-144 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 THR-264 AND SER-268 (ISOFORMS 2 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND SER-128 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-621 AND SER-641, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.

Entry informationi

Entry nameiBRD8_HUMAN
AccessioniPrimary (citable) accession number: Q9H0E9
Secondary accession number(s): O43178
, Q15355, Q58AB0, Q59GN0, Q969M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 119 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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