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Q8CHV6

- TAD2A_MOUSE

UniProt

Q8CHV6 - TAD2A_MOUSE

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Protein

Transcriptional adapter 2-alpha

Gene

Tada2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi426 – 43510

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mitotic nuclear division Source: MGI
  2. regulation of histone deacetylation Source: MGI
  3. regulation of protein phosphorylation Source: MGI
  4. regulation of protein stability Source: MGI
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. regulation of tubulin deacetylation Source: MGI
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional adapter 2-alpha
Alternative name(s):
Transcriptional adapter 2-like
Short name:
ADA2-like protein
Gene namesi
Name:Tada2a
Synonyms:Tada2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2144471. Tada2a.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosome 1 Publication

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  2. chromosome Source: UniProtKB-KW
  3. mitotic spindle Source: MGI
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi426 – 4261K → A: Reduces DNA binding. 1 Publication
Mutagenesisi428 – 4281R → A: Loss of nuclear localization. Reduces DNA binding. 1 Publication
Mutagenesisi429 – 4291K → A: Reduces DNA binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Transcriptional adapter 2-alphaPRO_0000240669Add
BLAST

Proteomic databases

PaxDbiQ8CHV6.
PRIDEiQ8CHV6.

PTM databases

PhosphoSiteiQ8CHV6.

Expressioni

Gene expression databases

BgeeiQ8CHV6.
ExpressionAtlasiQ8CHV6. baseline and differential.
GenevestigatoriQ8CHV6.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ8CHV6. 33 interactions.
MINTiMINT-4606424.
STRINGi10090.ENSMUSP00000103735.

Structurei

Secondary structure

1
443
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi365 – 3728Combined sources
Turni373 – 3753Combined sources
Helixi378 – 3869Combined sources
Helixi391 – 40818Combined sources
Helixi413 – 4175Combined sources
Beta strandi420 – 4245Combined sources
Helixi425 – 43612Combined sources
Beta strandi438 – 4403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AQENMR-A355-443[»]
2AQFNMR-A355-443[»]
2CUJNMR-A343-443[»]
ProteinModelPortaliQ8CHV6.
SMRiQ8CHV6. Positions 72-118, 349-443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CHV6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 12253SANTPROSITE-ProRule annotationAdd
BLAST
Domaini356 – 44388SWIRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 4529Cys-richAdd
BLAST

Sequence similaritiesi

Contains 1 SANT domain.PROSITE-ProRule annotation
Contains 1 SWIRM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5114.
GeneTreeiENSGT00530000063657.
HOGENOMiHOG000068147.
HOVERGENiHBG057413.
InParanoidiQ8CHV6.
KOiK11314.
OMAiFIESHAW.
OrthoDBiEOG7RFTK1.
PhylomeDBiQ8CHV6.
TreeFamiTF313975.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
PIRSFiPIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CHV6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRLGSFSND PSDKPPCRGC SSYLTEPYIK CAECGPPPFF LCLQCFTRGF
60 70 80 90 100
EYKKHQSDHT YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN
110 120 130 140 150
QMCTKTKEEC EKHYMKHFIN NPLFASTLLN LKQAEAAKAA DTAIPFHSAD
160 170 180 190 200
DPPRPAFDSL LSRDMAGYMP ARADFIEEFD NYAEWDLRDI DFVEDDSDIL
210 220 230 240 250
HALKMAVVDI YHSRLKERQR RKKIIRDHGL VNLRKFRLME RRYPKEVQDL
260 270 280 290 300
YETMRRFARI VGPVEHDKFI ESHALEFELR REIKRLQEYR TAGITNFCSA
310 320 330 340 350
RTYDHLKKTR EEERLKRTML SEVLQYIQDS SACQQWLRRQ ADIDSGLSPS
360 370 380 390 400
VLMASNSGRR SAPPLNLTGL PGTEKLNEKE KELCQVVRLV PGAYLEYKSA
410 420 430 440
LLNECHKQGG LRLAQARALI KIDVNKTRKI YDFLIREGYI TKA
Length:443
Mass (Da):51,339
Last modified:March 1, 2003 - v1
Checksum:iA14E88654CDC34D3
GO

Sequence cautioni

The sequence AAH25448.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38925.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161K → E in BAE34272. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25183.1.
RefSeqiNP_766150.1. NM_172562.3.
UniGeneiMm.45159.

Genome annotation databases

EnsembliENSMUST00000018795; ENSMUSP00000018795; ENSMUSG00000018651.
GeneIDi217031.
KEGGimmu:217031.
UCSCiuc007kqf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS25183.1.
RefSeqi NP_766150.1. NM_172562.3.
UniGenei Mm.45159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AQE NMR - A 355-443 [» ]
2AQF NMR - A 355-443 [» ]
2CUJ NMR - A 343-443 [» ]
ProteinModelPortali Q8CHV6.
SMRi Q8CHV6. Positions 72-118, 349-443.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CHV6. 33 interactions.
MINTi MINT-4606424.
STRINGi 10090.ENSMUSP00000103735.

PTM databases

PhosphoSitei Q8CHV6.

Proteomic databases

PaxDbi Q8CHV6.
PRIDEi Q8CHV6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018795 ; ENSMUSP00000018795 ; ENSMUSG00000018651 .
GeneIDi 217031.
KEGGi mmu:217031.
UCSCi uc007kqf.1. mouse.

Organism-specific databases

CTDi 6871.
MGIi MGI:2144471. Tada2a.

Phylogenomic databases

eggNOGi COG5114.
GeneTreei ENSGT00530000063657.
HOGENOMi HOG000068147.
HOVERGENi HBG057413.
InParanoidi Q8CHV6.
KOi K11314.
OMAi FIESHAW.
OrthoDBi EOG7RFTK1.
PhylomeDBi Q8CHV6.
TreeFami TF313975.

Enzyme and pathway databases

Reactomei REACT_226917. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi Tada2a. mouse.
EvolutionaryTracei Q8CHV6.
NextBioi 375522.
PROi Q8CHV6.
SOURCEi Search...

Gene expression databases

Bgeei Q8CHV6.
ExpressionAtlasi Q8CHV6. baseline and differential.
Genevestigatori Q8CHV6.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR016827. Transcriptional_adaptor_2.
[Graphical view ]
Pfami PF00249. Myb_DNA-binding. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view ]
PIRSFi PIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTi SM00717. SANT. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 2 hits.
PROSITEi PS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: STRUCTURE BY NMR OF 343-443.

Entry informationi

Entry nameiTAD2A_MOUSE
AccessioniPrimary (citable) accession number: Q8CHV6
Secondary accession number(s): Q3TZD7, Q8BNK0, Q8R3H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3