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Q8CHV6 (TAD2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional adapter 2-alpha
Alternative name(s):
Transcriptional adapter 2-like
Short name=ADA2-like protein
Gene names
Name:Tada2a
Synonyms:Tada2l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Required for the function of some acidic activation domains, which activate transcription from a distant site By similarity. Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling By similarity. Ref.4

Subunit structure

Interacts with GCN5 and NR3C1. Associated with the P/CAF protein in the PCAF complex. Component of the PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 By similarity.

Subcellular location

Nucleus. Chromosome Ref.4.

Sequence similarities

Contains 1 SANT domain.

Contains 1 SWIRM domain.

Sequence caution

The sequence AAH25448.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC38925.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H3 acetylation

Inferred from electronic annotation. Source: Ensembl

mitosis

Inferred from mutant phenotype PubMed 20562830. Source: MGI

regulation of histone deacetylation

Inferred from genetic interaction PubMed 20562830. Source: MGI

regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 20562830. Source: MGI

regulation of protein stability

Inferred from mutant phenotype PubMed 20562830. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of tubulin deacetylation

Inferred from genetic interaction PubMed 20562830. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 20562830PubMed 20508642. Source: MGI

PCAF complex

Inferred from electronic annotation. Source: Ensembl

chromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitotic spindle

Inferred from direct assay PubMed 20562830. Source: MGI

nucleus

Inferred from direct assay PubMed 20562830. Source: MGI

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: InterPro

histone acetyltransferase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Transcriptional adapter 2-alpha
PRO_0000240669

Regions

Domain70 – 12253SANT
Domain356 – 44388SWIRM
DNA binding426 – 43510
Compositional bias17 – 4529Cys-rich

Experimental info

Mutagenesis4261K → A: Reduces DNA binding. Ref.4
Mutagenesis4281R → A: Loss of nuclear localization. Reduces DNA binding. Ref.4
Mutagenesis4291K → A: Reduces DNA binding. Ref.4
Sequence conflict2161K → E in BAE34272. Ref.1

Secondary structure

............... 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CHV6 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: A14E88654CDC34D3

FASTA44351,339
        10         20         30         40         50         60 
MDRLGSFSND PSDKPPCRGC SSYLTEPYIK CAECGPPPFF LCLQCFTRGF EYKKHQSDHT 

        70         80         90        100        110        120 
YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN QMCTKTKEEC EKHYMKHFIN 

       130        140        150        160        170        180 
NPLFASTLLN LKQAEAAKAA DTAIPFHSAD DPPRPAFDSL LSRDMAGYMP ARADFIEEFD 

       190        200        210        220        230        240 
NYAEWDLRDI DFVEDDSDIL HALKMAVVDI YHSRLKERQR RKKIIRDHGL VNLRKFRLME 

       250        260        270        280        290        300 
RRYPKEVQDL YETMRRFARI VGPVEHDKFI ESHALEFELR REIKRLQEYR TAGITNFCSA 

       310        320        330        340        350        360 
RTYDHLKKTR EEERLKRTML SEVLQYIQDS SACQQWLRRQ ADIDSGLSPS VLMASNSGRR 

       370        380        390        400        410        420 
SAPPLNLTGL PGTEKLNEKE KELCQVVRLV PGAYLEYKSA LLNECHKQGG LRLAQARALI 

       430        440 
KIDVNKTRKI YDFLIREGYI TKA 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Inner ear.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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].
Strain: Czech II.
Tissue: Mammary gland and Mammary tumor.
[4]"Structure and chromosomal DNA binding of the SWIRM domain."
Qian C., Zhang Q., Li S., Zeng L., Walsh M.J., Zhou M.-M.
Nat. Struct. Mol. Biol. 12:1078-1085(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 355-443, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-426; ARG-428 AND LYS-429.
[5]"Structural and functional differences of SWIRM domain subtypes."
Yoneyama M., Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M., Seki E., Matsuda T., Watanabe S., Tomo Y., Nishimura Y., Harada T., Terada T., Shirouzu M., Hayashizaki Y., Ohara O., Tanaka A., Kigawa T., Yokoyama S.
J. Mol. Biol. 369:222-238(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 343-443.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK083467 mRNA. Translation: BAC38925.1. Different initiation.
AK157938 mRNA. Translation: BAE34272.1.
AL596447, AL645615 Genomic DNA. Translation: CAI25269.1.
AL645615, AL596447 Genomic DNA. Translation: CAI25507.1.
BC025448 mRNA. Translation: AAH25448.1. Different initiation.
BC038821 mRNA. Translation: AAH38821.1.
RefSeqNP_766150.1. NM_172562.3.
UniGeneMm.45159.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQENMR-A355-443[»]
2AQFNMR-A355-443[»]
2CUJNMR-A343-443[»]
ProteinModelPortalQ8CHV6.
SMRQ8CHV6. Positions 13-66, 72-118, 349-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CHV6. 33 interactions.
MINTMINT-4606424.
STRING10090.ENSMUSP00000103735.

PTM databases

PhosphoSiteQ8CHV6.

Proteomic databases

PaxDbQ8CHV6.
PRIDEQ8CHV6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018795; ENSMUSP00000018795; ENSMUSG00000018651.
GeneID217031.
KEGGmmu:217031.
UCSCuc007kqf.1. mouse.

Organism-specific databases

CTD6871.
MGIMGI:2144471. Tada2a.

Phylogenomic databases

eggNOGCOG5114.
GeneTreeENSGT00530000063657.
HOGENOMHOG000068147.
HOVERGENHBG057413.
InParanoidQ8CHV6.
KOK11314.
OMALEFDHEA.
OrthoDBEOG7RFTK1.
PhylomeDBQ8CHV6.
TreeFamTF313975.

Gene expression databases

ArrayExpressQ8CHV6.
BgeeQ8CHV6.
GenevestigatorQ8CHV6.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
PIRSFPIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTADA2A. mouse.
EvolutionaryTraceQ8CHV6.
NextBio375522.
PROQ8CHV6.
SOURCESearch...

Entry information

Entry nameTAD2A_MOUSE
AccessionPrimary (citable) accession number: Q8CHV6
Secondary accession number(s): Q3TZD7, Q8BNK0, Q8R3H5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot