Reviewed, UniProtKB/Swiss-Prot Q8I8V0 (TAD2B_DROME)

Names and origin

Protein names

Recommended name:
    Transcriptional adapter 2B
Alternative name(s):
    dADA2b

Gene names

Name:	Ada2b
Synonyms:	Ada2S
ORF Names:	CG9638

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	555 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the function of some acidic activation domains, which activate transcription from a distant site. Binds double-stranded DNA. Binds dinucleosomes, probably at the linker region between neighboring nucleosomes. Plays a role in chromatin remodeling. Ref.1 Ref.5 UniProtKB O75478
Subunit structure	Interacts with Pcaf/GCN5 and dik/ADA3 as part of a GCN5-containing ADA multiprotein complex. Associated with a SAGA-type complex that also contains Taf5, e(y)1/Taf9, Taf10, Spt3 and Taf1. Ref.1 Ref.5
Subcellular location	Nucleus.
Developmental stage	Expressed both maternally and zygotically throughout development. Ref.1 Ref.5
Sequence similarities	Contains 1 SANT domain. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	axon target recognition Inferred from mutant phenotype. Source: FlyBase chromatin remodeling Ref.5 Inferred from direct assay. Source: UniProtKB positive regulation of histone acetylation Inferred from mutant phenotype. Source: FlyBase regulation of transcription Ref.1 Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	SAGA complex Ref.1 Inferred from physical interaction. Source: FlyBase polytene chromosome Ref.1 Ref.5 Inferred from direct assay. Source: FlyBase
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q8INH9	1	EBI-109247,EBI-112777
	Q9VKN9	1	EBI-109247,EBI-146251
	Q9VTX1	1	EBI-109247,EBI-82861
	Q9VWA8	1	EBI-109247,EBI-187948
CSN1a	Q9VJR9	1	EBI-109247,EBI-163377
dik	Q9VWZ1	2	EBI-109247,EBI-144686

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform B Ref.1 (identifier: Q8I8V0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A Ref.2 (identifier: Q8I8V0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     331-418: DHTHTSNGSH...TGMVMGVTVD → LHCIINAPNN...RIIAQQKLLG
     419-555: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 555	555	Transcriptional adapter 2B		PRO_0000283734
Regions
	Domain	69 – 121	53	SANT
	Zinc finger	7 – 53	47	ZZ-type
Natural variations
	Alternative sequence	331 – 418	88	DHTHT…GVTVD → LHCIINAPNNERSNGSIRQC LTTGPHAYLQWKSSAAKLFL ALPTTESQKGRNVKRRRGKF KFNRTKKHAPHRRPDLLRRI IAQQKLLG in isoform A. Ref.2		VSP_052370
	Alternative sequence	419 – 555	137	Missing in isoform A. Ref.2		VSP_052371

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 89079A24FF11F381	FASTA	555	62,031
	10 20 30 40 50 60 MTTIADLFTK YNCTNCQDDI QGIRVHCAEC ENFDLCLQCF AAGAEIGAHQ NNHSYQFMDT 70 80 90 100 110 120 GTSILSVFRG KGAWTAREEI RLLDAIEQYG FGNWEDISKH IETKSAEDAK EEYVNKFVNG 130 140 150 160 170 180 TIGRATWTPA QSQRPRLIDH TGDDDAGPLG TNALSTLPPL EINSDEAMQL GYMPNRDSFE 190 200 210 220 230 240 REYDPTAEQL ISNISLSSED TEVDVMLKLA HVDIYTRRLR ERARRKRMVR DYQLVSNFFR 250 260 270 280 290 300 NRNYAQQQGL TKEQREFRDR FRVYAQFYTC NEYERLLGSL EREKELRIRQ SELYRYRYNG 310 320 330 340 350 360 LTKIAECTHF EQHAATATHR STGPYGHGKT DHTHTSNGSH RPPSSSLHSP QPNLRKVEMS 370 380 390 400 410 420 SGGEASSNSI APRNTLHIAD PTCSGALLPS KNYLDSCRGS SAATMLQTTG MVMGVTVDSG 430 440 450 460 470 480 ATTGVTSTAT TMANLPTNSA KGSQQHLQPL QQHPQLLQSG NQHKMQNEAA GGGSDQVPSM 490 500 510 520 530 540 SLKLRTQLEE LKHLPQPPGS ELLSHNELDL CKKHNITPTT YLSVKTVCLS GAPSLGSPME 550 TSLRKFFIKC GWLSH
	Isoform A. Checksum: 346A5B36222638B6	FASTA	418	48,316
	10 20 30 40 50 60 MTTIADLFTK YNCTNCQDDI QGIRVHCAEC ENFDLCLQCF AAGAEIGAHQ NNHSYQFMDT 70 80 90 100 110 120 GTSILSVFRG KGAWTAREEI RLLDAIEQYG FGNWEDISKH IETKSAEDAK EEYVNKFVNG 130 140 150 160 170 180 TIGRATWTPA QSQRPRLIDH TGDDDAGPLG TNALSTLPPL EINSDEAMQL GYMPNRDSFE 190 200 210 220 230 240 REYDPTAEQL ISNISLSSED TEVDVMLKLA HVDIYTRRLR ERARRKRMVR DYQLVSNFFR 250 260 270 280 290 300 NRNYAQQQGL TKEQREFRDR FRVYAQFYTC NEYERLLGSL EREKELRIRQ SELYRYRYNG 310 320 330 340 350 360 LTKIAECTHF EQHAATATHR STGPYGHGKT LHCIINAPNN ERSNGSIRQC LTTGPHAYLQ 370 380 390 400 410 WKSSAAKLFL ALPTTESQKG RNVKRRRGKF KFNRTKKHAP HRRPDLLRRI IAQQKLLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two Drosophila Ada2 homologues function in different multiprotein complexes." Kusch T., Guelman S., Abmayr S.M., Workman J.L. Mol. Cell. Biol. 23:3305-3319(2003) [PubMed: 12697829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, ASSOCIATION WITH SAGA-TYPE COMPLEX, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: Berkeley. Tissue: Embryo.
[5]	"Two different Drosophila ADA2 homologues are present in distinct GCN5 histone acetyltransferase-containing complexes." Muratoglu S., Georgieva S., Papai G., Scheer E., Enunlu I., Komonyi O., Cserpan I., Lebedeva L., Nabirochkina E., Udvardy A., Tora L., Boros I. Mol. Cell. Biol. 23:306-321(2003) [PubMed: 12482983] [Abstract] Cited for: FUNCTION, INTERACTION WITH PCAF AND DIK, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY142213 mRNA. Translation: AAN52141.1. AE014297 Genomic DNA. Translation: AAF54199.1. AE014297 Genomic DNA. Translation: AAZ52519.1. AY058546 mRNA. Translation: AAL13775.1.
RefSeq	NP_001027151.1. NP_649773.1.
UniGene	Dm.20776
3D structure databases
HSSP	HSSP built from PDB template 1X41 based on UniProtKB O75478.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8I8V0. 34 interactions.
STRING	Q8I8V0.
Proteomic databases
PRIDE	Q8I8V0.
Genome annotation databases
Ensembl	FBtr0081807; FBpp0081303; FBgn0037555; Drosophila melanogaster. [Genome view] FBtr0100368; FBpp0099776; FBgn0037555; Drosophila melanogaster. [Genome view]
GeneID	40966.
KEGG	dme:Dmel_CG9638.
Organism-specific databases
CTD	40966.
FlyBase	FBgn0037555. Ada2b.
Phylogenomic databases
OrthoDB	EOG9FFD81
Gene expression databases
Bgee	Q8I8V0.
Family and domain databases
InterPro	IPR009057. Homeodomain-like. IPR012287. Homeodomain-rel. IPR014778. Myb_DNA-bd. IPR001005. SANT_DNA-bd. IPR017884. SANT_eukarya. IPR016827. Transcriptional_adaptor_2. IPR000433. Znf_ZZ. [Graphical view]
Gene3D	G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
Pfam	PF00249. Myb_DNA-binding. 1 hit. PF00569. ZZ. 1 hit. [Graphical view]
PIRSF	PIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMART	SM00717. SANT. 1 hit. SM00291. ZnF_ZZ. 1 hit. [Graphical view]
PROSITE	PS51293. SANT. 1 hit. PS01357. ZF_ZZ_1. 1 hit. PS50135. ZF_ZZ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	821505.

Entry information

Entry name

TAD2B_DROME

Accession

Primary (citable) accession number: Q8I8V0
Secondary accession number(s): Q9VHV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	March 1, 2003
Last modified:	November 24, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project