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Protein

Transcription factor GAGA

Gene

Trl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri343 – 36624C2H2-type; degenerateAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: FlyBase
  • DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • POZ domain binding Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: FlyBase
  • sequence-specific DNA binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • chromatin assembly Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • chromatin organization Source: FlyBase
  • dosage compensation Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: FlyBase
  • nuclear division Source: FlyBase
  • oogenesis Source: FlyBase
  • positive regulation of chromatin silencing Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • protein oligomerization Source: UniProtKB
  • regulation of transcription, DNA-templated Source: FlyBase
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • spermatogenesis Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Cell cycle, Cell division, Differentiation, Mitosis, Oogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ08605.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Trl
Synonyms:Adf-2, GAGA, Nc70F, TFGAGA
ORF Names:CG33261
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0013263. Trl.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: FlyBase
  • euchromatin Source: UniProtKB
  • nucleus Source: UniProtKB
  • pericentric heterochromatin Source: FlyBase
  • polytene chromosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 581581Transcription factor GAGAPRO_0000047071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei237 – 2371Phosphothreonine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PeptideAtlasiQ08605.
PRIDEiQ08605.

PTM databases

iPTMnetiQ08605.

Expressioni

Tissue specificityi

Expressed in the central nervous system throughout development.1 Publication

Developmental stagei

Expressed ubiquitously during embryogenesis with higher levels found from 9-12 hours after egg laying. Low levels are found in larvae and adults.1 Publication

Gene expression databases

BgeeiQ08605.
ExpressionAtlasiQ08605. differential.
GenevisibleiQ08605. DM.

Interactioni

Subunit structurei

Interacts with Bin1, lolal, corto, ttk and ph-p. Interacts with FACT subunits Ssrp and dre4/SPT16. Interacts with E(bx).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Bin1Q9VEX94EBI-665803,EBI-129424
cortoP410462EBI-300317,EBI-300379
lolalQ7KRI26EBI-300317,EBI-84493

GO - Molecular functioni

  • POZ domain binding Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi77830. 21 interactions.
IntActiQ08605. 9 interactions.
MINTiMINT-266758.

Structurei

Secondary structure

1
581
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi334 – 3374Combined sources
Turni346 – 3483Combined sources
Beta strandi351 – 3544Combined sources
Helixi355 – 36511Combined sources
Turni366 – 3683Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YUINMR-A319-372[»]
1YUJNMR-A319-372[»]
DisProtiDP00328.
ProteinModelPortaliQ08605.
SMRiQ08605. Positions 20-124, 319-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 9966BTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 397197Interaction with E(bx)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi404 – 579176Gln-richAdd
BLAST

Domaini

The N-terminal BTB domain mediates protein oligomerization. The C-terminal glutamine-rich region is required for transcriptional activation activity.

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 1 C2H2-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri343 – 36624C2H2-type; degenerateAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiQ08605.
OMAiTIDFVCA.
OrthoDBiEOG7HTHH0.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR015318. Znf_GAGA-bd_fac.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF09237. GAGA. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q08605-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI
60 70 80 90 100
VLCAASPFLL DLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA
110 120 130 140 150
QLPSLLQAAQ CLNIQGLAPQ TVTKDDYTTH SIQLQHMIPQ HHDQDQLIAT
160 170 180 190 200
IATAPQQTVH AQVVEDIHHQ GQILQATTQT NAAGQQQTIV TTDAAKHDQA
210 220 230 240 250
VIQAFLPARK RKPRVKKMSP TAPKISKVEG MDTIMGTPTS SHGSGSVQQV
260 270 280 290 300
LGENGAEGQL LSSTPIIKSE GQKVETIVTM DPNNMIPVTS ANAATGEITP
310 320 330 340 350
AQGATGSSGG NTSGVLSTPK AKRAKHPPGT EKPRSRSQSE QPATCPICYA
360 370 380 390 400
VIRQSRNLRR HLELRHFAKP GVKKEKKTTS GKKSSSGSSG SGSGALSSSG
410 420 430 440 450
SVPQVQTVQS LHTLQGVQVK KDPDAQQQQQ QQQQQQQQQQ QAMTVSGATG
460 470 480 490 500
GQVQQQVQQV QQQVQQQQQQ QQQQQQQLQH HQIIDSSGNI TTATTSAQAA
510 520 530 540 550
AAAQQQAAGQ QQQLVAQSDG SESGAPLSIA QVQTLQGHQI IGNLNQVNMT
560 570 580
DFQQQQPQQQ QQQQQQQQQQ QQQQQQTQQT L
Length:581
Mass (Da):62,489
Last modified:September 13, 2005 - v2
Checksum:i04826A1B630E3320
GO
Isoform B (identifier: Q08605-2) [UniParc]FASTAAdd to basket

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

Show »
Length:519
Mass (Da):54,816
Checksum:i46EE082ACE1A0663
GO
Isoform G (identifier: Q08605-3) [UniParc]FASTAAdd to basket

Also known as: GAGA-566

The sequence of this isoform differs from the canonical sequence as follows:
     65-107: Missing.

Show »
Length:538
Mass (Da):57,817
Checksum:i38AAE5F71EB91C35
GO
Isoform I (identifier: Q08605-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     547-581: VNMTDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL → GNNKNILVKKVFILKGGNNT

Show »
Length:566
Mass (Da):60,319
Checksum:i70D0FEBA7035CE0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 242AI → DL in AAB81113 (PubMed:9241251).Curated
Sequence conflicti278 – 2781V → L in AAA16072 (PubMed:7504178).Curated
Sequence conflicti441 – 4411Q → QQ in AAF49709 (PubMed:10731132).Curated
Sequence conflicti549 – 5491M → I in AAF49709 (PubMed:10731132).Curated
Isoform B (identifier: Q08605-2)
Sequence conflicti437 – 4371A → G in AAB81113 (PubMed:9241251).Curated
Sequence conflicti437 – 4371A → G in AAB81117 (PubMed:9241251).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 10743Missing in isoform G. 1 PublicationVSP_015536Add
BLAST
Alternative sequencei378 – 581204TTSGK…TQQTL → SKSGNDTTLDSSMEMNTTAE GDNTVGSDGAGGAGSAGGQS SGTTPTRVISNAPQAAGAPA ILAQGVLPQQQQQQQLQQQH QQHLTATLAGGGQAYIKHEG GGGGGTGQQQQQQAAQQQGM QNVIHIVGDQVFIPQQQQPQ PQ in isoform B. 4 PublicationsVSP_015537Add
BLAST
Alternative sequencei547 – 58135VNMTD…TQQTL → GNNKNILVKKVFILKGGNNT in isoform I. 1 PublicationVSP_015538Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA54590.
RefSeqiNP_001034014.1. NM_001038925.3. [Q08605-2]
NP_996077.1. NM_206355.4. [Q08605-2]
NP_996078.1. NM_206356.3. [Q08605-2]
NP_996079.1. NM_206357.3. [Q08605-2]
NP_996080.1. NM_206358.4.
NP_996081.1. NM_206359.4. [Q08605-2]
NP_996082.1. NM_206360.1.
UniGeneiDm.7610.

Genome annotation databases

GeneIDi2768981.
KEGGidme:Dmel_CG33261.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA54590.
RefSeqiNP_001034014.1. NM_001038925.3. [Q08605-2]
NP_996077.1. NM_206355.4. [Q08605-2]
NP_996078.1. NM_206356.3. [Q08605-2]
NP_996079.1. NM_206357.3. [Q08605-2]
NP_996080.1. NM_206358.4.
NP_996081.1. NM_206359.4. [Q08605-2]
NP_996082.1. NM_206360.1.
UniGeneiDm.7610.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YUINMR-A319-372[»]
1YUJNMR-A319-372[»]
DisProtiDP00328.
ProteinModelPortaliQ08605.
SMRiQ08605. Positions 20-124, 319-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi77830. 21 interactions.
IntActiQ08605. 9 interactions.
MINTiMINT-266758.

PTM databases

iPTMnetiQ08605.

Proteomic databases

PeptideAtlasiQ08605.
PRIDEiQ08605.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2768981.
KEGGidme:Dmel_CG33261.

Organism-specific databases

FlyBaseiFBgn0013263. Trl.

Phylogenomic databases

InParanoidiQ08605.
OMAiTIDFVCA.
OrthoDBiEOG7HTHH0.

Enzyme and pathway databases

SignaLinkiQ08605.

Miscellaneous databases

ChiTaRSiTrl. fly.
GenomeRNAii2768981.
PROiQ08605.

Gene expression databases

BgeeiQ08605.
ExpressionAtlasiQ08605. differential.
GenevisibleiQ08605. DM.

Family and domain databases

Gene3Di3.30.160.60. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
IPR015318. Znf_GAGA-bd_fac.
[Graphical view]
PfamiPF00651. BTB. 1 hit.
PF09237. GAGA. 1 hit.
[Graphical view]
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Embryo.
  7. 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. 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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiGAGA_DROME
AccessioniPrimary (citable) accession number: Q08605
Secondary accession number(s): O18349
, O18350, O18526, Q08083, Q7JN57, Q8MYL3, Q8T387, Q9V3X7, Q9VUH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 13, 2005
Last modified: July 6, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.