TAD2B_DANRE
ID TAD2B_DANRE Reviewed; 486 AA.
AC Q503N9; B5DDS4; Q7SXK2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transcriptional adapter 2-beta;
GN Name=tada2b; ORFNames=zgc:110397;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional coactivator. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55562.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC055562; AAH55562.1; ALT_INIT; mRNA.
DR EMBL; BC095241; AAH95241.1; -; mRNA.
DR EMBL; BC165604; AAI65604.1; -; mRNA.
DR RefSeq; NP_001019614.1; NM_001024443.1.
DR AlphaFoldDB; Q503N9; -.
DR SMR; Q503N9; -.
DR STRING; 7955.ENSDARP00000012853; -.
DR PaxDb; Q503N9; -.
DR PRIDE; Q503N9; -.
DR GeneID; 554156; -.
DR KEGG; dre:554156; -.
DR CTD; 93624; -.
DR ZFIN; ZDB-GENE-050522-557; tada2b.
DR eggNOG; KOG0457; Eukaryota.
DR InParanoid; Q503N9; -.
DR OrthoDB; 812864at2759; -.
DR PhylomeDB; Q503N9; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR PRO; PR:Q503N9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..486
FT /note="Transcriptional adapter 2-beta"
FT /id="PRO_0000313713"
FT DOMAIN 65..118
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 4..59
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 237..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 35
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT CONFLICT 290
FT /note="G -> E (in Ref. 1; AAH55562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53719 MW; 73A6201C4444F5C4 CRC64;
MADLGKKYCV NCLADVTNLR IRCAECQDIE LCPECFSAGA EIGNHRRWHG YQQVDGGRFS
LWGPEAEGGW TSREEQSLLD AIEQYGFGNW EDMAAHVGAS RTPQEVMDHY VSMYIHGNLG
KACIPDSIPN RVTDHTCPSG GPLSPSLTTP LPPLDITVVE QQQLGYMPLR DDYEIEYDQE
AEKLISGLSV NYDDEDIEIE MKRAHVDMYV RKLRERQRRK NIARDYNLVP AFLGRDKKDK
ERERAGGTVG VGGPGGAVGS GSGATVVPAG PLGSSTAATP KRKITKEEKG QRTKLRALCQ
FMPQREFEEF FDNMHKERML RAKVRELQRY RRNGITRLDE SAEYEAARHK REKRKENKSI
AGSKRGSSGG GGGTAGLGGG VGAGGGLGGG GGVSTIKEEG KDSEFSAIEN LSGFELLSDR
EKVLCNSMNL SPMRYLTVKT IIIKDHLQKR QGIPSKSRLP SYLDKVLKKR ILNFLSESGW
ISRDAS
