TAD2A_MOUSE
ID TAD2A_MOUSE Reviewed; 443 AA.
AC Q8CHV6; Q3TZD7; Q8BNK0; Q8R3H5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Transcriptional adapter 2-alpha;
DE AltName: Full=Transcriptional adapter 2-like;
DE Short=ADA2-like protein;
GN Name=Tada2a; Synonyms=Tada2l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP STRUCTURE BY NMR OF 355-443, FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-426; ARG-428 AND LYS-429.
RX PubMed=16299514; DOI=10.1038/nsmb1022;
RA Qian C., Zhang Q., Li S., Zeng L., Walsh M.J., Zhou M.-M.;
RT "Structure and chromosomal DNA binding of the SWIRM domain.";
RL Nat. Struct. Mol. Biol. 12:1078-1085(2005).
RN [5]
RP STRUCTURE BY NMR OF 343-443.
RX PubMed=17428495; DOI=10.1016/j.jmb.2007.03.027;
RA Yoneyama M., Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T.,
RA Aoki M., Seki E., Matsuda T., Watanabe S., Tomo Y., Nishimura Y.,
RA Harada T., Terada T., Shirouzu M., Hayashizaki Y., Ohara O., Tanaka A.,
RA Kigawa T., Yokoyama S.;
RT "Structural and functional differences of SWIRM domain subtypes.";
RL J. Mol. Biol. 369:222-238(2007).
CC -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4 (By similarity).
CC Required for the function of some acidic activation domains, which
CC activate transcription from a distant site (By similarity). Binds
CC double-stranded DNA (PubMed:16299514). Binds dinucleosomes, probably at
CC the linker region between neighboring nucleosomes (PubMed:16299514).
CC Plays a role in chromatin remodeling (By similarity). May promote
CC TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and
CC transcriptional activity (By similarity). May also promote XRCC6
CC acetylation thus facilitating cell apoptosis in response to DNA damage
CC (By similarity). {ECO:0000250|UniProtKB:O75478,
CC ECO:0000269|PubMed:16299514}.
CC -!- SUBUNIT: Interacts with GCN5. Interacts with NR3C1. Associated with the
CC P/CAF protein in the PCAF complex. Component of the PCAF complex, at
CC least composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta,
CC TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and
CC TRRAP. Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC Interacts with CCDC134. {ECO:0000250|UniProtKB:O75478}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:16299514}. Chromosome {ECO:0000269|PubMed:16299514}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25448.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK083467; BAC38925.1; ALT_INIT; mRNA.
DR EMBL; AK157938; BAE34272.1; -; mRNA.
DR EMBL; AL596447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025448; AAH25448.1; ALT_INIT; mRNA.
DR EMBL; BC038821; AAH38821.1; -; mRNA.
DR CCDS; CCDS25183.1; -.
DR RefSeq; NP_766150.1; NM_172562.3.
DR PDB; 2AQE; NMR; -; A=355-443.
DR PDB; 2AQF; NMR; -; A=355-443.
DR PDB; 2CUJ; NMR; -; A=343-443.
DR PDBsum; 2AQE; -.
DR PDBsum; 2AQF; -.
DR PDBsum; 2CUJ; -.
DR AlphaFoldDB; Q8CHV6; -.
DR BMRB; Q8CHV6; -.
DR SMR; Q8CHV6; -.
DR BioGRID; 229835; 8.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q8CHV6; 33.
DR MINT; Q8CHV6; -.
DR STRING; 10090.ENSMUSP00000018795; -.
DR iPTMnet; Q8CHV6; -.
DR PhosphoSitePlus; Q8CHV6; -.
DR EPD; Q8CHV6; -.
DR MaxQB; Q8CHV6; -.
DR PaxDb; Q8CHV6; -.
DR PRIDE; Q8CHV6; -.
DR ProteomicsDB; 259342; -.
DR Antibodypedia; 72747; 189 antibodies from 22 providers.
DR DNASU; 217031; -.
DR Ensembl; ENSMUST00000018795; ENSMUSP00000018795; ENSMUSG00000018651.
DR GeneID; 217031; -.
DR KEGG; mmu:217031; -.
DR UCSC; uc007kqf.1; mouse.
DR CTD; 6871; -.
DR MGI; MGI:2144471; Tada2a.
DR VEuPathDB; HostDB:ENSMUSG00000018651; -.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000156751; -.
DR HOGENOM; CLU_018273_2_1_1; -.
DR InParanoid; Q8CHV6; -.
DR OMA; EFETEYF; -.
DR OrthoDB; 812864at2759; -.
DR PhylomeDB; Q8CHV6; -.
DR TreeFam; TF313975; -.
DR BioGRID-ORCS; 217031; 17 hits in 75 CRISPR screens.
DR ChiTaRS; Tada2a; mouse.
DR EvolutionaryTrace; Q8CHV6; -.
DR PRO; PR:Q8CHV6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CHV6; protein.
DR Bgee; ENSMUSG00000018651; Expressed in metanephric proximal tubule and 242 other tissues.
DR ExpressionAtlas; Q8CHV6; baseline and differential.
DR Genevisible; Q8CHV6; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000124; C:SAGA complex; ISO:MGI.
DR GO; GO:0070461; C:SAGA-type complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IGI:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IGI:MGI.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Transcriptional adapter 2-alpha"
FT /id="PRO_0000240669"
FT DOMAIN 70..122
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 356..443
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT ZN_FING 12..69
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT DNA_BIND 426..435
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75478"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75478"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75478"
FT MUTAGEN 426
FT /note="K->A: Reduces DNA binding."
FT /evidence="ECO:0000269|PubMed:16299514"
FT MUTAGEN 428
FT /note="R->A: Loss of nuclear localization. Reduces DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:16299514"
FT MUTAGEN 429
FT /note="K->A: Reduces DNA binding."
FT /evidence="ECO:0000269|PubMed:16299514"
FT CONFLICT 216
FT /note="K -> E (in Ref. 1; BAE34272)"
FT /evidence="ECO:0000305"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:2AQE"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:2AQE"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:2AQE"
FT HELIX 391..408
FT /evidence="ECO:0007829|PDB:2AQE"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:2AQE"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:2AQE"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:2AQE"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:2AQF"
SQ SEQUENCE 443 AA; 51339 MW; A14E88654CDC34D3 CRC64;
MDRLGSFSND PSDKPPCRGC SSYLTEPYIK CAECGPPPFF LCLQCFTRGF EYKKHQSDHT
YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN QMCTKTKEEC EKHYMKHFIN
NPLFASTLLN LKQAEAAKAA DTAIPFHSAD DPPRPAFDSL LSRDMAGYMP ARADFIEEFD
NYAEWDLRDI DFVEDDSDIL HALKMAVVDI YHSRLKERQR RKKIIRDHGL VNLRKFRLME
RRYPKEVQDL YETMRRFARI VGPVEHDKFI ESHALEFELR REIKRLQEYR TAGITNFCSA
RTYDHLKKTR EEERLKRTML SEVLQYIQDS SACQQWLRRQ ADIDSGLSPS VLMASNSGRR
SAPPLNLTGL PGTEKLNEKE KELCQVVRLV PGAYLEYKSA LLNECHKQGG LRLAQARALI
KIDVNKTRKI YDFLIREGYI TKA
