TAD2B_DROME
ID TAD2B_DROME Reviewed; 555 AA.
AC Q8I8V0; Q9VHV0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Transcriptional adapter 2B;
DE AltName: Full=dADA2b;
GN Name=Ada2b {ECO:0000312|FlyBase:FBgn0037555};
GN Synonyms=Ada2S {ECO:0000303|PubMed:12697829}; ORFNames=CG9638;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN52141.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, ASSOCIATION WITH
RP SAGA-TYPE COMPLEX, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12697829; DOI=10.1128/mcb.23.9.3305-3319.2003;
RA Kusch T., Guelman S., Abmayr S.M., Workman J.L.;
RT "Two Drosophila Ada2 homologues function in different multiprotein
RT complexes.";
RL Mol. Cell. Biol. 23:3305-3319(2003).
RN [2] {ECO:0000312|EMBL:AAZ52519.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAZ52519.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAL13775.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13775.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GCN5 AND ADA3, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12482983; DOI=10.1128/mcb.23.1.306-321.2003;
RA Muratoglu S., Georgieva S., Papai G., Scheer E., Enunlu I., Komonyi O.,
RA Cserpan I., Lebedeva L., Nabirochkina E., Udvardy A., Tora L., Boros I.;
RT "Two different Drosophila ADA2 homologues are present in distinct GCN5
RT histone acetyltransferase-containing complexes.";
RL Mol. Cell. Biol. 23:306-321(2003).
CC -!- FUNCTION: Required for the function of some acidic activation domains,
CC which activate transcription from a distant site. Binds double-stranded
CC DNA. Binds dinucleosomes, probably at the linker region between
CC neighboring nucleosomes. Plays a role in chromatin remodeling.
CC {ECO:0000250|UniProtKB:O75478, ECO:0000269|PubMed:12482983,
CC ECO:0000269|PubMed:12697829}.
CC -!- SUBUNIT: Interacts with Gcn5 and Ada3 as part of a GCN5-containing ADA
CC multiprotein complex (PubMed:12482983). Associated with a SAGA-type
CC complex that also contains Taf5, e(y)1/Taf9, Taf10, Spt3 and Taf1
CC (PubMed:12697829). {ECO:0000269|PubMed:12482983,
CC ECO:0000269|PubMed:12697829}.
CC -!- INTERACTION:
CC Q8I8V0; O76216: Gcn5; NbExp=7; IntAct=EBI-109247, EBI-867710;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:12482983, ECO:0000269|PubMed:12697829}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000269|PubMed:12697829};
CC IsoId=Q8I8V0-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=Q8I8V0-2; Sequence=VSP_052370, VSP_052371;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:12482983,
CC ECO:0000269|PubMed:12697829}.
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DR EMBL; AY142213; AAN52141.1; -; mRNA.
DR EMBL; AE014297; AAF54199.1; -; Genomic_DNA.
DR EMBL; AE014297; AAZ52519.1; -; Genomic_DNA.
DR EMBL; AY058546; AAL13775.1; -; mRNA.
DR RefSeq; NP_001027151.1; NM_001031980.2. [Q8I8V0-1]
DR RefSeq; NP_001262367.1; NM_001275438.1. [Q8I8V0-2]
DR RefSeq; NP_649773.1; NM_141516.3. [Q8I8V0-2]
DR AlphaFoldDB; Q8I8V0; -.
DR SMR; Q8I8V0; -.
DR BioGRID; 66149; 118.
DR IntAct; Q8I8V0; 19.
DR MINT; Q8I8V0; -.
DR STRING; 7227.FBpp0099776; -.
DR PaxDb; Q8I8V0; -.
DR EnsemblMetazoa; FBtr0081807; FBpp0081303; FBgn0037555. [Q8I8V0-2]
DR EnsemblMetazoa; FBtr0100368; FBpp0099776; FBgn0037555. [Q8I8V0-1]
DR EnsemblMetazoa; FBtr0334315; FBpp0306430; FBgn0037555. [Q8I8V0-2]
DR GeneID; 40966; -.
DR KEGG; dme:Dmel_CG9638; -.
DR CTD; 559295; -.
DR FlyBase; FBgn0037555; Ada2b.
DR VEuPathDB; VectorBase:FBgn0037555; -.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000157318; -.
DR HOGENOM; CLU_018273_4_1_1; -.
DR InParanoid; Q8I8V0; -.
DR OMA; NGCIRQC; -.
DR PhylomeDB; Q8I8V0; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR SignaLink; Q8I8V0; -.
DR BioGRID-ORCS; 40966; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 40966; -.
DR PRO; PR:Q8I8V0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037555; Expressed in cleaving embryo and 27 other tissues.
DR ExpressionAtlas; Q8I8V0; baseline and differential.
DR Genevisible; Q8I8V0; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
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:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IMP:FlyBase.
DR GO; GO:2000331; P:regulation of terminal button organization; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0035222; P:wing disc pattern formation; IGI:FlyBase.
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 Pfam; PF00569; ZZ; 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 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..555
FT /note="Transcriptional adapter 2B"
FT /id="PRO_0000283734"
FT DOMAIN 69..121
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 8..63
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 318..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT VAR_SEQ 331..418
FT /note="DHTHTSNGSHRPPSSSLHSPQPNLRKVEMSSGGEASSNSIAPRNTLHIADPT
FT CSGALLPSKNYLDSCRGSSAATMLQTTGMVMGVTVD -> LHCIINAPNNERSNGSIRQ
FT CLTTGPHAYLQWKSSAAKLFLALPTTESQKGRNVKRRRGKFKFNRTKKHAPHRRPDLLR
FT RIIAQQKLLG (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052370"
FT VAR_SEQ 419..555
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052371"
SQ SEQUENCE 555 AA; 62031 MW; 89079A24FF11F381 CRC64;
MTTIADLFTK YNCTNCQDDI QGIRVHCAEC ENFDLCLQCF AAGAEIGAHQ NNHSYQFMDT
GTSILSVFRG KGAWTAREEI RLLDAIEQYG FGNWEDISKH IETKSAEDAK EEYVNKFVNG
TIGRATWTPA QSQRPRLIDH TGDDDAGPLG TNALSTLPPL EINSDEAMQL GYMPNRDSFE
REYDPTAEQL ISNISLSSED TEVDVMLKLA HVDIYTRRLR ERARRKRMVR DYQLVSNFFR
NRNYAQQQGL TKEQREFRDR FRVYAQFYTC NEYERLLGSL EREKELRIRQ SELYRYRYNG
LTKIAECTHF EQHAATATHR STGPYGHGKT DHTHTSNGSH RPPSSSLHSP QPNLRKVEMS
SGGEASSNSI APRNTLHIAD PTCSGALLPS KNYLDSCRGS SAATMLQTTG MVMGVTVDSG
ATTGVTSTAT TMANLPTNSA KGSQQHLQPL QQHPQLLQSG NQHKMQNEAA GGGSDQVPSM
SLKLRTQLEE LKHLPQPPGS ELLSHNELDL CKKHNITPTT YLSVKTVCLS GAPSLGSPME
TSLRKFFIKC GWLSH
