TAD2A_BOVIN
ID TAD2A_BOVIN Reviewed; 443 AA.
AC Q3SZP8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4. Required for the
CC function of some acidic activation domains, which activate
CC transcription from a distant site. Binds double-stranded DNA. Binds
CC dinucleosomes, probably at the linker region between neighboring
CC nucleosomes. Plays a role in chromatin remodeling. May promote TP53/p53
CC 'Lys-321' acetylation, leading to reduced TP53 stability and
CC transcriptional activity. May also promote XRCC6 acetylation thus
CC facilitating cell apoptosis in response to DNA damage.
CC {ECO:0000250|UniProtKB:O75478, ECO:0000250|UniProtKB:Q8CHV6}.
CC -!- SUBUNIT: Interacts with GCN5 and NR3C1. Associated with the P/CAF
CC protein in the PCAF complex. Component of the PCAF complex, at least
CC composed of TADA2L/ADA2, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-
CC alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Component
CC of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A,
CC TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. Interacts
CC with CCDC134. {ECO:0000250|UniProtKB:O75478}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC Chromosome {ECO:0000250|UniProtKB:Q8CHV6}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC102758; AAI02759.1; -; mRNA.
DR RefSeq; NP_001029416.1; NM_001034244.1.
DR RefSeq; XP_005220048.1; XM_005219991.3.
DR AlphaFoldDB; Q3SZP8; -.
DR BMRB; Q3SZP8; -.
DR SMR; Q3SZP8; -.
DR STRING; 9913.ENSBTAP00000019537; -.
DR PaxDb; Q3SZP8; -.
DR PRIDE; Q3SZP8; -.
DR Ensembl; ENSBTAT00000019537; ENSBTAP00000019537; ENSBTAG00000014677.
DR GeneID; 505401; -.
DR KEGG; bta:505401; -.
DR CTD; 6871; -.
DR VEuPathDB; HostDB:ENSBTAG00000014677; -.
DR VGNC; VGNC:35565; TADA2A.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000156751; -.
DR HOGENOM; CLU_018273_2_1_1; -.
DR InParanoid; Q3SZP8; -.
DR OMA; EFETEYF; -.
DR OrthoDB; 812864at2759; -.
DR TreeFam; TF313975; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000014677; Expressed in oocyte and 104 other tissues.
DR ExpressionAtlas; Q3SZP8; baseline and differential.
DR GO; GO:0140672; C:ATAC complex; IEA:Ensembl.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0051302; P:regulation of cell division; IEA:Ensembl.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0031063; P:regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW 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_0000240668"
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 /evidence="ECO:0000250"
FT REGION 347..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 443 AA; 51469 MW; 07C5F1AB43636FA0 CRC64;
MDRLGSFSSD PSDKPPCRGC SSYLMEPYIK CAECGPPPFF LCLQCFTRGF EYKKHQSDHT
YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN QMCTKTKEEC EKHYMKHFIN
NPLFASTLLN LKQAEEAKTA DTAIPFHSAD DPPRPTFDSL LSRDMAGYMP ARADFIEEFD
NYAEWDLRDI DFVEDDSDIL HALKMAVVDI YHSRLKERQR RKKIIRDHGL INLRKFQLME
RRYPKEVQDL YETMRRFARI VGPVEHDKFI ESHALEFELR REIKRLQEYR TAGITNFCSA
RTYDHLKKTR EEERLKRTML SEVLQYIQDS SACQQWLRRQ ADIDSGLSPS VPMTSNSGRR
SAPPLNLTGL PGTEKLNEKE KELCQMVRLV PGAYLEYKSA LLNECNKQGG LRLAQARALI
KIDVNKTRKI YDFLIREGYI TKA
