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O75528 (TADA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional adapter 3
Alternative name(s):
ADA3 homolog
Short name=hADA3
STAF54
Transcriptional adapter 3-like
Short name=ADA3-like protein
Gene names
Name:TADA3
Synonyms:ADA3, TADA3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. Also known as a coactivator for p53/TP53-dependent transcriptional activation. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Ref.9 Ref.12

Subunit structure

The PCAF complex is composed of a number of TBP-associated factors (TAFS), such as TAF5, TAF5L, TAF6, TAF6L, TAF9, TAF10 and TAF12, PCAF, and also PCAF-associated factors (PAFs), such as TADA2L/ADA2, TADA3L/ADA3 and SPT3. Interacts directly with TADA2L and PCAF and also with the high-risk HPV oncoprotein E6. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Component of the TFTC-HAT complex. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Nucleus Ref.1 Ref.7.

Tissue specificity

Ubiquitously expressed.

Sequence similarities

Belongs to the NGG1 family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin organization

Traceable author statement. Source: Reactome

histone H3 acetylation

Inferred from direct assay Ref.7. Source: UniProtKB

intracellular estrogen receptor signaling pathway

Traceable author statement PubMed 20413580. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20413580. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 20413580. Source: UniProtKB

regulation of histone deacetylation

Inferred from electronic annotation. Source: Ensembl

regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

regulation of tubulin deacetylation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

STAGA complex

Inferred from direct assay Ref.7. Source: UniProtKB

intracellular

Inferred from direct assay. Source: LIFEdb

mitotic spindle

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

transcription factor TFTC complex

Inferred from direct assay PubMed 10373431. Source: UniProtKB

   Molecular_functionligand-dependent nuclear receptor binding

Inferred from physical interaction PubMed 20413580. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

protein domain specific binding

Inferred from physical interaction PubMed 20413580. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Inferred from direct assay Ref.7PubMed 20413580. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIAS4Q8N2W92EBI-473249,EBI-473160
USP5P459742EBI-473249,EBI-741277

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75528-1)

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: O75528-2)

The sequence of this isoform differs from the canonical sequence as follows:
     370-432: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Transcriptional adapter 3
PRO_0000072416

Regions

Coiled coil40 – 6930 Potential
Coiled coil367 – 40741 Potential

Amino acid modifications

Modified residue4181N6-acetyllysine Ref.13

Natural variations

Alternative sequence370 – 43263Missing in isoform 2.
VSP_009739

Experimental info

Sequence conflict1681E → G in AK000228. Ref.3

Sequences

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

Last modified November 1, 1998. Version 1.
Checksum: C86153CFA83F9226

FASTA43248,902
        10         20         30         40         50         60 
MSELKDCPLQ FHDFKSVDHL KVCPRYTAVL ARSEDDGIGI EELDTLQLEL ETLLSSASRR 

        70         80         90        100        110        120 
LRVLEAETQI LTDWQDKKGD RRFLKLGRDH ELGAPPKHGK PKKQKLEGKA GHGPGPGPGR 

       130        140        150        160        170        180 
PKSKNLQPKI QEYEFTDDPI DVPRIPKNDA PNRFWASVEP YCADITSEEV RTLEELLKPP 

       190        200        210        220        230        240 
EDEAEHYKIP PLGKHYSQRW AQEDLLEEQK DGARAAAVAD KKKGLMGPLT ELDTKDVDAL 

       250        260        270        280        290        300 
LKKSEAQHEQ PEDGCPFGAL TQRLLQALVE ENIISPMEDS PIPDMSGKES GADGASTSPR 

       310        320        330        340        350        360 
NQNKPFSVPH TKSLESRIKE ELIAQGLLES EDRPAEDSED EVLAELRKRQ AELKALSAHN 

       370        380        390        400        410        420 
RTKKHDLLRL AKEEVSRQEL RQRVRMADNE VMDAFRKIMA ARQKKRTPTK KEKDQAWKTL 

       430 
KERESILKLL DG 

« Hide

Isoform 2 [UniParc].

Checksum: 782715A6300779A4
Show »

FASTA36941,393

References

« Hide 'large scale' references
[1]"Histone-like TAFs within the PCAF histone acetylase complex."
Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J., Howard B.H., Qin J., Nakatani Y.
Cell 94:35-44(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PCAF; TAF5L; TAF6L; TAF9; TAF10 AND TAF12.
[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 2).
Tissue: Testis.
[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. expand/collapse author list , 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 1).
Tissue: Colon mucosa.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Muscle and Pancreas.
[7]"Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Human papillomavirus oncoprotein E6 inactivates the transcriptional coactivator human ADA3."
Kumar A., Zhao Y., Meng G., Zeng M., Srinivasan S., Delmolino L.M., Gao Q., Dimri G., Weber G.F., Wazer D.E., Band H., Band V.
Mol. Cell. Biol. 22:5801-5812(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53 AND THE HIGH-RISK HPV ONCOPROTEIN E6.
[9]"hADA3 is required for p53 activity."
Wang T., Kobayashi T., Takimoto R., Denes A.E., Snyder E.L., el-Deiry W.S., Brachmann R.K.
EMBO J. 20:6404-6413(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TP53.
[10]"The TAFs in the HAT."
Struhl K., Moqtaderi Z.
Cell 94:1-4(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, PCAF COMPLEX COMPOSITION.
[11]"Novel subunits of the TATA binding protein free TAFII-containing transcription complex identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry following one-dimensional gel electrophoresis."
Cavusoglu N., Brand M., Tora L., van Dorsselaer A.
Proteomics 3:217-223(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX.
[12]"The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
[13]"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-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF069733 mRNA. Translation: AAC39903.1.
AL117487 mRNA. Translation: CAB55957.1.
AK000228 mRNA. No translation available.
CR533543 mRNA. Translation: CAG38574.1.
CH471055 Genomic DNA. Translation: EAW63994.1.
BC009240 mRNA. Translation: AAH09240.1.
BC013433 mRNA. Translation: AAH13433.1.
PIRT17267.
RefSeqNP_001265199.1. NM_001278270.1.
NP_006345.1. NM_006354.3.
NP_597814.1. NM_133480.2.
UniGeneHs.386390.

3D structure databases

ProteinModelPortalO75528.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115737. 40 interactions.
IntActO75528. 19 interactions.
MINTMINT-221730.
STRING9606.ENSP00000307684.

PTM databases

PhosphoSiteO75528.

Proteomic databases

PaxDbO75528.
PRIDEO75528.

Protocols and materials databases

DNASU10474.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301964; ENSP00000307684; ENSG00000171148. [O75528-1]
ENST00000343450; ENSP00000343649; ENSG00000171148. [O75528-2]
ENST00000440161; ENSP00000393471; ENSG00000171148. [O75528-1]
GeneID10474.
KEGGhsa:10474.
UCSCuc003bsw.2. human. [O75528-1]

Organism-specific databases

CTD10474.
GeneCardsGC03M009797.
HGNCHGNC:19422. TADA3.
HPAHPA042250.
MIM602945. gene.
neXtProtNX_O75528.
PharmGKBPA165698494.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265778.
HOGENOMHOG000007362.
HOVERGENHBG055283.
InParanoidO75528.
KOK11315.
OMAQDKKGDK.
OrthoDBEOG79PJP8.
PhylomeDBO75528.
TreeFamTF323397.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressO75528.
BgeeO75528.
CleanExHS_TADA3L.
GenevestigatorO75528.

Family and domain databases

InterProIPR019340. Histone_AcTrfase_su3.
[Graphical view]
PfamPF10198. Ada3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTADA3. human.
GeneWikiTADA3L.
GenomeRNAi10474.
NextBio39724.
PROO75528.
SOURCESearch...

Entry information

Entry nameTADA3_HUMAN
AccessionPrimary (citable) accession number: O75528
Secondary accession number(s): Q6FI83, Q9UFS2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 114 of the entry and version 1 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM