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Q9H0E9 (BRD8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BRD8
Synonyms:SMAP, SMAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11 Ref.19

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.11 Ref.19

Subcellular location

Nucleus.

Tissue specificity

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

Sequence similarities

Contains 2 bromo domains.

Caution

It is uncertain whether Met-1 or Met-32 is the initiator.

Sequence caution

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.

Ontologies

Keywords
   Biological processGrowth regulation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainBromodomain
Coiled coil
Repeat
   Molecular functionChromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement Ref.6. Source: ProtInc

chromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

intracellular receptor signaling pathway

Traceable author statement Ref.6. Source: GOC

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.6. Source: ProtInc

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

signal transduction

Traceable author statement Ref.6. Source: ProtInc

   Cellular_componentNuA4 histone acetyltransferase complex

Inferred from direct assay Ref.11. Source: UniProtKB

Swr1 complex

Inferred from direct assay Ref.19. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionsequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

thyroid hormone receptor activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H0E9-1)

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: Q9H0E9-2)

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.
Isoform 3 (identifier: Q9H0E9-3)

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.
Isoform 4 (identifier: Q9H0E9-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235Bromodomain-containing protein 8
PRO_0000211185

Regions

Domain724 – 79471Bromo 1
Domain1120 – 119071Bromo 2
Coiled coil97 – 17175 Potential

Amino acid modifications

Modified residue851N6-acetyllysine By similarity
Modified residue3871Phosphoserine Ref.13
Modified residue4811N6-acetyllysine Ref.17
Modified residue6211Phosphoserine Ref.18
Modified residue6371Phosphoserine Ref.12
Modified residue6411Phosphoserine Ref.12 Ref.18

Natural variations

Alternative sequence1 – 147147MATGT…NDIAT → MSFAMTL in isoform 3.
VSP_012879
Alternative sequence2151V → VTPGTLPSTPVTSFPGIPDT LPPGSAPLEAPMTPVTDDSP QKKMLGQKATPPPSPLLSEL LKKGSLLPTSPRLV in isoform 2, isoform 3 and isoform 4.
VSP_012880
Alternative sequence263 – 33270Missing in isoform 4.
VSP_023187
Alternative sequence263 – 30139Missing in isoform 3.
VSP_012881
Alternative sequence845 – 85915Missing in isoform 3.
VSP_012882
Alternative sequence8461S → G in isoform 4.
VSP_023188
Alternative sequence847 – 975129Missing in isoform 4.
VSP_023189
Alternative sequence860 – 87819MGHEW…PNDSE → DGGTRGRRCAIEADMKMKK in isoform 2 and isoform 3.
VSP_012883
Alternative sequence879 – 1235357Missing in isoform 2 and isoform 3.
VSP_012884
Alternative sequence979 – 99214QEGRE…EGERE → GRRCAIEADMKMKK in isoform 4.
VSP_023190
Alternative sequence993 – 1235243Missing in isoform 4.
VSP_023191
Natural variant4901T → M. Ref.3
Corresponds to variant rs11750814 [ dbSNP | Ensembl ].
VAR_030695
Natural variant8961L → P.
Corresponds to variant rs6883021 [ dbSNP | Ensembl ].
VAR_048428
Natural variant11981Q → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs412051 [ dbSNP | Ensembl ].
VAR_048429

Experimental info

Sequence conflict3061Q → H in AAB87858. Ref.6
Sequence conflict5571V → L in CAA60949. Ref.1
Sequence conflict5571V → L in CAA63925. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 3738078C77FC17D1

FASTA1,235135,336
        10         20         30         40         50         60 
MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA EPGRPPDWFS 

        70         80         90        100        110        120 
QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL TAERVEELKK VIKETQERYR 

       130        140        150        160        170        180 
RLKRDAELIQ AGHMDSRLDE LCNDIATKKK LEEEEAEVKR KATDAAYQAR QAVKTPPRRL 

       190        200        210        220        230        240 
PTVMVRSPID SASPGGDYPL GDLTPTTMEE ATSGVNESEM AVASGHLNST GVLLEVGGVL 

       250        260        270        280        290        300 
PMIHGGEIQQ TPNTVAASPA ASGAPTLSRL LEAGPTQFTT PLASFTTVAS EPPVKLVPPP 

       310        320        330        340        350        360 
VESVSQATIV MMPALPAPSS APAVSTTESV APVSQPDNCV PMEAVGDPHT VTVSMDSSEI 

       370        380        390        400        410        420 
SMIINSIKEE CFRSGVAEAP VGSKAPSIDG KEELDLAEKM DIAVSYTGEE LDFETVGDII 

       430        440        450        460        470        480 
AIIEDKVDDH PEVLDVAAVE AALSFCEEND DPQSLPGPWE HPIQQERDKP VPLPAPEMTV 

       490        500        510        520        530        540 
KQERLDFEET ENKGIHELVD IREPSAEIKV EPAEPEPVIS GAEIVAGVVP ATSMEPPELR 

       550        560        570        580        590        600 
SQDLDEELGS TAAGEIVEAD VAIGKGDETP LTNVKTEASP ESMLSPSHGS NPIEDPLEAE 

       610        620        630        640        650        660 
TQHKFEMSDS LKEESGTIFG SQIKDAPGED EEEDGVSEAA SLEEPKEEDQ GEGYLSEMDN 

       670        680        690        700        710        720 
EPPVSESDDG FSIHNATLQS HTLADSIPSS PASSQFSVCS EDQEAIQAQK IWKKAIMLVW 

       730        740        750        760        770        780 
RAAANHRYAN VFLQPVTDDI APGYHSIVQR PMDLSTIKKN IENGLIRSTA EFQRDIMLMF 

       790        800        810        820        830        840 
QNAVMYNSSD HDVYHMAVEM QRDVLEQIQQ FLATQLIMQT SESGISAKSL RGRDSTRKQD 

       850        860        870        880        890        900 
ASEKDSVPMG SPAFLLSLFM GHEWVWLDSE QDHPNDSELS NDCRSLFSSW DSSLDLDVGN 

       910        920        930        940        950        960 
WRETEDPEAE ELEESSPERE PSELLVGDGG SEESQEAARK ASHQNLLHFL SEVAYLMEPL 

       970        980        990       1000       1010       1020 
CISSNESSEG CCPPSGTRQE GREIKASEGE RELCRETEEL SAKGDPLVAE KPLGENGKPE 

      1030       1040       1050       1060       1070       1080 
VASAPSVICT VQGLLTESEE GEAQQESKGE DQGEVYVSEM EDQPPSGECD DAFNIKETPL 

      1090       1100       1110       1120       1130       1140 
VDTLFSHATS SKLTDLSQDD PVQDHLLFKK TLLPVWKMIA SHRFSSPFLK PVSERQAPGY 

      1150       1160       1170       1180       1190       1200 
KDVVKRPMDL TSLKRNLSKG RIRTMAQFLR DLMLMFQNAV MYNDSDHHVY HMAVEMRQEV 

      1210       1220       1230 
LEQIQVLNIW LDKRKGSSSL EGEPANPVDD GKPVF 

« Hide

Isoform 2 [UniParc].

Checksum: 80C0A7A6ACB4E8ED
Show »

FASTA951102,839
Isoform 3 [UniParc].

Checksum: C1D728727505F85D
Show »

FASTA75781,354
Isoform 4 [UniParc].

Checksum: 3400AEB14E9412FC
Show »

FASTA86694,297

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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 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]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS58225.
S68142.
RefSeqNP_001157798.1. NM_001164326.1.
NP_006687.3. NM_006696.3.
NP_631938.1. NM_139199.1.
UniGeneHs.519337.

3D structure databases

ProteinModelPortalQ9H0E9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116108. 17 interactions.
IntActQ9H0E9. 13 interactions.
MINTMINT-3065717.
STRING9606.ENSP00000254900.

Polymorphism databases

DMDM313104080.

Proteomic databases

PaxDbQ9H0E9.
PRIDEQ9H0E9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230901; ENSP00000230901; ENSG00000112983. [Q9H0E9-2]
ENST00000254900; ENSP00000254900; ENSG00000112983. [Q9H0E9-1]
ENST00000411594; ENSP00000394330; ENSG00000112983. [Q9H0E9-4]
GeneID10902.
KEGGhsa:10902.
UCSCuc003lcf.1. human. [Q9H0E9-1]
uc003lcg.3. human. [Q9H0E9-2]
uc003lci.3. human. [Q9H0E9-4]
uc021yea.1. human. [Q9H0E9-3]

Organism-specific databases

CTD10902.
GeneCardsGC05M137475.
HGNCHGNC:19874. BRD8.
HPAHPA001841.
MIM602848. gene.
neXtProtNX_Q9H0E9.
PharmGKBPA134923194.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000074125.
HOVERGENHBG050732.
InParanoidQ9H0E9.
KOK11321.
PhylomeDBQ9H0E9.
TreeFamTF106422.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9H0E9.
BgeeQ9H0E9.
CleanExHS_BRD8.
HS_SMAP2.
GenevestigatorQ9H0E9.

Family and domain databases

Gene3D1.20.920.10. 2 hits.
InterProIPR001487. Bromodomain.
[Graphical view]
PfamPF00439. Bromodomain. 2 hits.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMSSF47370. SSF47370. 2 hits.
PROSITEPS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBRD8. human.
GeneWikiBRD8.
GenomeRNAi10902.
NextBio41403.
PMAP-CutDBQ9H0E9.
PROQ9H0E9.
SOURCESearch...

Entry information

Entry nameBRD8_HUMAN
AccessionPrimary (citable) accession number: Q9H0E9
Secondary accession number(s): O43178 expand/collapse secondary AC list , Q15355, Q58AB0, Q59GN0, Q969M9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM