位置:首页 > 蛋白库 > TAD2A_RAT
TAD2A_RAT
ID   TAD2A_RAT               Reviewed;         443 AA.
AC   Q6AYE3; A1EC76;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 138.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Dahl salt-sensitive, and Lewis;
RX   PubMed=17218081; DOI=10.1016/j.ygeno.2006.12.005;
RA   Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P.,
RA   Radecki T., Joe B.;
RT   "Fine-mapping and comprehensive transcript analysis reveals nonsynonymous
RT   variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome
RT   10.";
RL   Genomics 89:343-353(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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).
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; EF121983; ABL63422.1; -; mRNA.
DR   EMBL; EF121984; ABL63423.1; -; mRNA.
DR   EMBL; BC079084; AAH79084.1; -; mRNA.
DR   RefSeq; NP_001012141.1; NM_001012141.1.
DR   AlphaFoldDB; Q6AYE3; -.
DR   BMRB; Q6AYE3; -.
DR   SMR; Q6AYE3; -.
DR   STRING; 10116.ENSRNOP00000003699; -.
DR   iPTMnet; Q6AYE3; -.
DR   PhosphoSitePlus; Q6AYE3; -.
DR   PaxDb; Q6AYE3; -.
DR   GeneID; 360581; -.
DR   KEGG; rno:360581; -.
DR   CTD; 6871; -.
DR   RGD; 1309959; Tada2a.
DR   VEuPathDB; HostDB:ENSRNOG00000002757; -.
DR   eggNOG; KOG0457; Eukaryota.
DR   HOGENOM; CLU_018273_2_1_1; -.
DR   InParanoid; Q6AYE3; -.
DR   OMA; EFETEYF; -.
DR   OrthoDB; 812864at2759; -.
DR   PhylomeDB; Q6AYE3; -.
DR   TreeFam; TF313975; -.
DR   PRO; PR:Q6AYE3; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002757; Expressed in pancreas and 20 other tissues.
DR   ExpressionAtlas; Q6AYE3; baseline and differential.
DR   Genevisible; Q6AYE3; RN.
DR   GO; GO:0140672; C:ATAC complex; ISO:RGD.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0000124; C:SAGA complex; ISO:RGD.
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:0043966; P:histone H3 acetylation; ISO:RGD.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; ISO:RGD.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR   GO; GO:0051302; P:regulation of cell division; ISO:RGD.
DR   GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
DR   GO; GO:0031063; P:regulation of histone deacetylation; ISO:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD.
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_0000240670"
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   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;  51399 MW;  E89255BB908880DE CRC64;
     MDRLGSFSND PSDKPPCRGC SSYLMEPYIK CAECGPPPFF LCLQCFTRGF EYKKHQSDHT
     YEIMTSDFPV LDPSWTAQEE MALLEAVMDC GFGNWQDVAN QMCTKTKEEC EKHYMKHFIN
     NPLFASTLLN LKQAEAAKTA 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024