Transcription factor GAGA - Drosophila melanogaster (Fruit fly)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Transcription factor GAGA

Alternative name(s):
Adh transcription factor 2
GAGA factor
Short name=GAF
Neural conserved at 70F
Trithorax-like protein

Gene names

Name:	Trl
Synonyms:	Adf-2, GAGA, Nc70F, TFGAGA
ORF Names:	CG33261

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	581 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator that functions by regulating chromatin structure. Overcomes the repressive effects of chromatin by promoting the open chromatin conformation in promoter gene regions, thereby allowing access to other transcription factors. Binds to DNA Polycomb response elements (PREs) at the bithorax complex and to the proximal region of the engrailed promoter, and positively regulates transcription of many genes including homeotic ones. Binds to the DNA sequence (GA)n, with optimal binding to the pentamer 5'-GAGAG-3'. Binds DNA as an oligomer. May also act as a transcriptional repressor, maintaining the repressed state of genes including lolal, and down-regulating its own transcription. Required for dosage compensation in males and may be involved in oogenesis. Also has a role in nuclear division. Ref.1 Ref.2 Ref.11 Ref.15 Ref.17 Ref.18 Ref.21 Ref.22
Subunit structure	Interacts with Bin1, lolal, corto, ttk and ph-p. Interacts with FACT subunits Ssrp and dre4/SPT16. Interacts with E(bx). Ref.2 Ref.10 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Nucleus Ref.1 Ref.2.
Tissue specificity	Expressed in the central nervous system throughout development. Ref.9
Developmental stage	Expressed ubiquitously during embryogenesis with higher levels found from 9-12 hours after egg laying. Low levels are found in larvae and adults. Ref.2
Domain	The N-terminal BTB domain mediates protein oligomerization. The C-terminal glutamine-rich region is required for transcriptional activation activity. Ref.12 Ref.14
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Contains 1 BTB (POZ) domain. Contains 1 C2H2-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Cell division Differentiation Mitosis Oogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Chromatin regulator Developmental protein Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW chromatin assembly Inferred from direct assay Ref.2. Source: UniProtKB chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW dosage compensation Inferred from mutant phenotype Ref.22. Source: FlyBase imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 16648592 PubMed 21635778. Source: FlyBase mitosis Inferred from electronic annotation. Source: UniProtKB-KW nuclear division Inferred from mutant phenotype Ref.11. Source: FlyBase oogenesis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of chromatin silencing Inferred from direct assay PubMed 14630938. Source: FlyBase positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 18367161. Source: FlyBase protein oligomerization Inferred from direct assay Ref.12. Source: UniProtKB syncytial blastoderm mitotic cell cycle Inferred from mutant phenotype Ref.11. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centromeric heterochromatin Inferred from direct assay PubMed 11024164. Source: FlyBase euchromatin Inferred from direct assay Ref.2. Source: UniProtKB nucleus Inferred from direct assay Ref.1 Ref.2. Source: UniProtKB polytene chromosome Inferred from direct assay Ref.2. Source: UniProtKB
Molecular_function	chromatin binding Inferred from direct assay PubMed 18367161. Source: FlyBase sequence-specific DNA binding Inferred from direct assay PubMed 14630938. Source: FlyBase sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype PubMed 11024164. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
Bin1	Q9VEX9	4	EBI-665803,EBI-129424
corto	P41046	2	EBI-300317,EBI-300379
lolal	Q7KRI2	6	EBI-300317,EBI-84493

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q08605-1) Also known as: F; GAGA-581; 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 B (identifier: Q08605-2) Also known as: C; D; E; H; GAGA-519a; GAGA-519b; The sequence of this isoform differs from the canonical sequence as follows: 378-581: TTSGKKSSSG...QQQQQTQQTL → SKSGNDTTLD...IPQQQQPQPQ

Isoform G (identifier: Q08605-3) Also known as: GAGA-566; The sequence of this isoform differs from the canonical sequence as follows: 65-107: Missing.

Isoform I (identifier: Q08605-4) The sequence of this isoform differs from the canonical sequence as follows: 547-581: VNMTDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL → GNNKNILVKKVFILKGGNNT

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 581

581

Transcription factor GAGA

PRO_0000047071

Regions

Domain

34 – 99

66

BTB

Zinc finger

343 – 366

24

C2H2-type; degenerate

Region

201 – 397

197

Interaction with E(bx)

Compositional bias

404 – 579

176

Gln-rich

Amino acid modifications

Modified residue

237

1

Phosphothreonine Ref.23

Natural variations

Alternative sequence

65 – 107

43

Missing in isoform G.

VSP_015536

Alternative sequence

378 – 581

204

TTSGK…TQQTL → SKSGNDTTLDSSMEMNTTAE GDNTVGSDGAGGAGSAGGQS SGTTPTRVISNAPQAAGAPA ILAQGVLPQQQQQQQLQQQH QQHLTATLAGGGQAYIKHEG GGGGGTGQQQQQQAAQQQGM QNVIHIVGDQVFIPQQQQPQ PQ in isoform B.

VSP_015537

Alternative sequence

547 – 581

35

VNMTD…TQQTL → GNNKNILVKKVFILKGGNNT in isoform I.

VSP_015538

Experimental info

Sequence conflict

23 – 24

2

AI → DL in AAB81113. Ref.2

Sequence conflict

278

1

V → L in AAA16072. Ref.1

Sequence conflict

441

1

Q → QQ in AAF49709. Ref.4

Sequence conflict

549

1

M → I in AAF49709. Ref.4

Isoform B:

Sequence conflict

437

1

A → G in AAB81113. Ref.2

Sequence conflict

437

1

A → G in AAB81117. Ref.2

Secondary structure

1

.

581

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform A (F) (GAGA-581) [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 04826A1B630E3320 Show »	FASTA	581	62,489
10 20 30 40 50 60 MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL 70 80 90 100 110 120 DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ 130 140 150 160 170 180 TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT 190 200 210 220 230 240 NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS 250 260 270 280 290 300 SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETIVTM DPNNMIPVTS ANAATGEITP 310 320 330 340 350 360 AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR 370 380 390 400 410 420 HLELRHFAKP GVKKEKKTTS GKKSSSGSSG SGSGALSSSG SVPQVQTVQS LHTLQGVQVK 430 440 450 460 470 480 KDPDAQQQQQ QQQQQQQQQQ QAMTVSGATG GQVQQQVQQV QQQVQQQQQQ QQQQQQQLQH 490 500 510 520 530 540 HQIIDSSGNI TTATTSAQAA AAAQQQAAGQ QQQLVAQSDG SESGAPLSIA QVQTLQGHQI 550 560 570 580 IGNLNQVNMT DFQQQQPQQQ QQQQQQQQQQ QQQQQQTQQT L « Hide
Isoform B (C) (D) (E) (H) (GAGA-519a) (GAGA-519b) [UniParc]. Checksum: 46EE082ACE1A0663 Show »	FASTA	519	54,816
10 20 30 40 50 60 MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL 70 80 90 100 110 120 DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ 130 140 150 160 170 180 TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT 190 200 210 220 230 240 NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS 250 260 270 280 290 300 SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETIVTM DPNNMIPVTS ANAATGEITP 310 320 330 340 350 360 AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR 370 380 390 400 410 420 HLELRHFAKP GVKKEKKSKS GNDTTLDSSM EMNTTAEGDN TVGSDGAGGA GSAGGQSSGT 430 440 450 460 470 480 TPTRVISNAP QAAGAPAILA QGVLPQQQQQ QQLQQQHQQH LTATLAGGGQ AYIKHEGGGG 490 500 510 GGTGQQQQQQ AAQQQGMQNV IHIVGDQVFI PQQQQPQPQ « Hide
Isoform G (GAGA-566) [UniParc]. Checksum: 38AAE5F71EB91C35 Show »	FASTA	538	57,817
10 20 30 40 50 60 MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL 70 80 90 100 110 120 DLLKAAQCLN IQGLAPQTVT KDDYTTHSIQ LQHMIPQHHD QDQLIATIAT APQQTVHAQV 130 140 150 160 170 180 VEDIHHQGQI LQATTQTNAA GQQQTIVTTD AAKHDQAVIQ AFLPARKRKP RVKKMSPTAP 190 200 210 220 230 240 KISKVEGMDT IMGTPTSSHG SGSVQQVLGE NGAEGQLLSS TPIIKSEGQK VETIVTMDPN 250 260 270 280 290 300 NMIPVTSANA ATGEITPAQG ATGSSGGNTS GVLSTPKAKR AKHPPGTEKP RSRSQSEQPA 310 320 330 340 350 360 TCPICYAVIR QSRNLRRHLE LRHFAKPGVK KEKKTTSGKK SSSGSSGSGS GALSSSGSVP 370 380 390 400 410 420 QVQTVQSLHT LQGVQVKKDP DAQQQQQQQQ QQQQQQQQAM TVSGATGGQV QQQVQQVQQQ 430 440 450 460 470 480 VQQQQQQQQQ QQQQLQHHQI IDSSGNITTA TTSAQAAAAA QQQAAGQQQQ LVAQSDGSES 490 500 510 520 530 GAPLSIAQVQ TLQGHQIIGN LNQVNMTDFQ QQQPQQQQQQ QQQQQQQQQQ QQQTQQTL « Hide
Isoform I [UniParc]. Checksum: 70D0FEBA7035CE0F Show »	FASTA	566	60,319
10 20 30 40 50 60 MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLL 70 80 90 100 110 120 DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQ 130 140 150 160 170 180 TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT IATAPQQTVH AQVVEDIHHQ GQILQATTQT 190 200 210 220 230 240 NAAGQQQTIV TTDAAKHDQA VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS 250 260 270 280 290 300 SHGSGSVQQV LGENGAEGQL LSSTPIIKSE GQKVETIVTM DPNNMIPVTS ANAATGEITP 310 320 330 340 350 360 AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA VIRQSRNLRR 370 380 390 400 410 420 HLELRHFAKP GVKKEKKTTS GKKSSSGSSG SGSGALSSSG SVPQVQTVQS LHTLQGVQVK 430 440 450 460 470 480 KDPDAQQQQQ QQQQQQQQQQ QAMTVSGATG GQVQQQVQQV QQQVQQQQQQ QQQQQQQLQH 490 500 510 520 530 540 HQIIDSSGNI TTATTSAQAA AAAQQQAAGQ QQQLVAQSDG SESGAPLSIA QVQTLQGHQI 550 560 IGNLNQGNNK NILVKKVFIL KGGNNT « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNAs encoding the Drosophila GAGA transcription factor." Soeller W.C., Oh C.E., Kornberg T.B. Mol. Cell. Biol. 13:7961-7970(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), PROTEIN SEQUENCE OF 393-405 AND 498-518 (ISOFORM B), FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION. Strain: Oregon-R. Tissue: Embryo.
[2]	"Multiple isoforms of GAGA factor, a critical component of chromatin structure." Benyajati C., Mueller L., Xu N., Pappano M., Gao J., Mosammaparast M., Conklin D., Granok H., Craig C., Elgin S.C.R. Nucleic Acids Res. 25:3345-3353(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, HETERODIMERIZATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[3]	"Molecular genetic analysis of Thrithorax-like gene encoded transcriptional factor GAGA in Drosophila melanogaster." Katokhin A.V., Pindiurin A.V., Fedorova E.V., Baricheva E.M. Genetika 37:467-474(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[4]	"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. Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"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. Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Embryo.
[7]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. Celniker S.E. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). Strain: Berkeley. Tissue: Testis.
[8]	"New forms mRNA of the Trl gene." Karagodin D.A., Baricheva E.M. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-197 (ISOFORM G), NUCLEOTIDE SEQUENCE [MRNA] OF 363-581 (ISOFORM I).
[9]	"The evolutionarily conserved gene Nc70F, expressed in nerve tissue of Drosophila melanogaster, encodes a protein homologous to the mouse delta transcription factor." Perelygina L.M., Baricheva E.M., Sebeleva T.E., Kokoza V.A. Genetika 29:1597-1607(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-581 (ISOFORM B), TISSUE SPECIFICITY. Tissue: Prepupa.
[10]	"Dual functions of largest NURF subunit NURF301 in nucleosome sliding and transcription factor interactions." Xiao H., Sandaltzopoulos R., Wang H.-M., Hamiche A., Ranallo R., Lee K.-M., Fu D., Wu C. Mol. Cell 8:531-543(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 197-209; 274-288 AND 475-494 (ISOFORM B), INTERACTION WITH E(BX).
[11]	"The GAGA factor is required in the early Drosophila embryo not only for transcriptional regulation but also for nuclear division." Bhat K.M., Farkas G., Karch F., Gyurkovics H., Gausz J., Schedl P. Development 122:1113-1124(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"The N-terminal POZ domain of GAGA mediates the formation of oligomers that bind DNA with high affinity and specificity." Espinas M.L., Jimenez-Garcia E., Vaquero A., Canudas S., Bernues J., Azorin F. J. Biol. Chem. 274:16461-16469(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, PROTEIN OLIGOMERIZATION, CHARACTERIZATION OF PTB DOMAIN.
[13]	"The GAGA factor of Drosophila interacts with SAP18, a Sin3-associated polypeptide." Espinas M.L., Canudas S., Fanti L., Pimpinelli S., Casanova J., Azorin F. EMBO Rep. 1:253-259(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BIN1.
[14]	"Functional mapping of the GAGA factor assigns its transcriptional activity to the C-terminal glutamine-rich domain." Vaquero A., Espinas M.L., Azorin F., Bernues J. J. Biol. Chem. 275:19461-19468(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF GLN-RICH DOMAIN.
[15]	"GAGA factor down-regulates its own promoter." Kosoy A., Pagans S., Espinas M.L., Azorin F., Bernues J. J. Biol. Chem. 277:42280-42288(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"The Drosophila transcription factor tramtrack (TTK) interacts with Trithorax-like (GAGA) and represses GAGA-mediated activation." Pagans S., Ortiz-Lombardia M., Espinas M.L., Bernues J., Azorin F. Nucleic Acids Res. 30:4406-4413(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTK.
[17]	"Drosophila FACT contributes to Hox gene expression through physical and functional interactions with GAGA factor." Shimojima T., Okada M., Nakayama T., Ueda H., Okawa K., Iwamatsu A., Handa H., Hirose S. Genes Dev. 17:1605-1616(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP AND DRE4.
[18]	"Trl-GAGA directly interacts with lola like and both are part of the repressive complex of Polycomb group of genes." Mishra K., Chopra V.S., Srinivasan A., Mishra R.K. Mech. Dev. 120:681-689(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LOLAL AND PHP.
[19]	"The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor." Salvaing J., Lopez A., Boivin A., Deutsch J.S., Peronnet F. Nucleic Acids Res. 31:2873-2882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CORTO.
[20]	"Genomewide analysis of Drosophila GAGA factor target genes reveals context-dependent DNA binding." van Steensel B., Delrow J., Bussemaker H.J. Proc. Natl. Acad. Sci. U.S.A. 100:2580-2585(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING SPECIFICITY.
[21]	"Function of the Trithorax-like gene during Drosophila development." Bejarano F., Busturia A. Dev. Biol. 268:327-341(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"The Drosophila GAGA factor is required for dosage compensation in males and for the formation of the male-specific-lethal complex chromatin entry site at 12DE." Greenberg A.J., Yanowitz J.L., Schedl P. Genetics 166:279-289(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, MASS SPECTROMETRY. Tissue: Embryo.
[24]	"The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode." Omichinski J.G., Pedone P.V., Felsenfeld G., Gronenborn A.M., Clore G.M. Nat. Struct. Biol. 4:122-132(1997) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 310-372.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L22205 mRNA. Translation: AAA16072.1.
U16728 mRNA. Translation: AAB81112.1.
U18386 mRNA. Translation: AAB81113.1.
U68563 mRNA. Translation: AAB81117.1.
AJ225042 Genomic DNA. Translation: CAA12383.1.
AJ225042 Genomic DNA. Translation: CAB86986.1.
AE014296 Genomic DNA. Translation: AAF49709.1.
AE014296 Genomic DNA. Translation: AAF49710.1.
AY069651 mRNA. Translation: AAL39796.1.
BT003649 mRNA. Translation: AAO39653.1.
AJ441087 mRNA. Translation: CAD29581.1.
AJ459425 mRNA. Translation: CAD30828.1.
X59784 mRNA. Translation: CAA42446.1.

PIR

A54590.

RefSeq

NP_001034014.1. NM_001038925.3.
NP_996077.1. NM_206355.4.
NP_996078.1. NM_206356.3.
NP_996079.1. NM_206357.3.
NP_996080.1. NM_206358.3.
NP_996081.1. NM_206359.4.
NP_996082.1. NM_206360.1.

UniGene

Dm.7610.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YUI	NMR	-	A	319-372	[»]
1YUJ	NMR	-	A	319-372	[»]

DisProt

DP00328.

ProteinModelPortal

Q08605.

SMR

Q08605. Positions 15-118, 319-372.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08605. 9 interactions.

MINT

MINT-266758.

Proteomic databases

PaxDb

Q08605.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2768981.

KEGG

dme:Dmel_CG33261.

Organism-specific databases

FlyBase

FBgn0013263. Trl.

Phylogenomic databases

eggNOG

NOG44966.

InParanoid

Q08605.

OMA

NANQANG.

OrthoDB

EOG47D7XR.

Enzyme and pathway databases

SignaLink

Q08605.

Gene expression databases

Bgee

Q08605.

GermOnline

CG33261. Drosophila melanogaster.

Family and domain databases

Gene3D

3.30.160.60. 1 hit.
3.30.710.10. 1 hit.

InterPro

IPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR013069. BTB_POZ.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR015318. Znf_GAGA-bd_fac.
[Graphical view]

Pfam

PF00651. BTB. 1 hit.
PF09237. GAGA. 1 hit.
[Graphical view]

SMART

SM00225. BTB. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

SUPFAM

SSF54695. BTB/POZ_fold. 1 hit.

PROSITE

PS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Trl. drosophila.

GenomeRNAi

2768981.

NextBio

848930.

Entry information

Entry name

GAGA_DROME

Accession

Primary (citable) accession number: Q08605
Secondary accession number(s): O18349

Q9VUH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 13, 2005
Last modified:	May 29, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents