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Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (NF-E1 DNA-binding protein) (NF-E1a)

 GATA1_CHICK             Reviewed;         304 AA.
P17678;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
28-FEB-2018, entry version 129.
RecName: Full=Erythroid transcription factor;
AltName: Full=Eryf1;
AltName: Full=GATA-binding factor 1;
Short=GATA-1;
AltName: Full=NF-E1 DNA-binding protein;
Short=NF-E1a;
Name=GATA1; Synonyms=ERYF1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2776214; DOI=10.1016/0092-8674(89)90940-9;
Evans T., Felsenfeld G.;
"The erythroid-specific transcription factor Eryf1: a new finger
protein.";
Cell 58:877-885(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2249770; DOI=10.1101/gad.4.10.1650;
Yamamoto M., Ko L.J., Leonard M.W., Beug H., Orkin S.H., Engel J.D.;
"Activity and tissue-specific expression of the transcription factor
NF-E1 multigene family.";
Genes Dev. 4:1650-1662(1990).
[3]
INTERACTION WITH EP300, ACETYLATION AT LYS-151; LYS-152; LYS-158;
LYS-214; LYS-218 AND LYS-220, AND MUTAGENESIS OF 151-LYS-LYS-152 AND
LYS-158.
PubMed=9859997; DOI=10.1038/25166;
Boyes J., Byfield P., Nakatani Y., Ogryzko V.;
"Regulation of activity of the transcription factor GATA-1 by
acetylation.";
Nature 396:594-598(1998).
[4]
STRUCTURE BY NMR OF 158-223.
PubMed=8332909; DOI=10.1126/science.8332909;
Omichinski J.G., Clore G.M., Schaad O., Felsenfeld G., Trainor C.,
Appella E., Stahl S.J., Gronenborn A.M.;
"NMR structure of a specific DNA complex of Zn-containing DNA binding
domain of GATA-1.";
Science 261:438-446(1993).
[5]
STRUCTURE BY NMR OF 158-223.
PubMed=9303001; DOI=10.1038/nsb0997-732;
Tjandra N., Omichinski J.G., Gronenborn A.M., Clore G.M., Bax A.;
"Use of dipolar 1H-15N and 1H-13C couplings in the structure
determination of magnetically oriented macromolecules in solution.";
Nat. Struct. Biol. 4:732-738(1997).
-!- FUNCTION: Transcriptional activator or repressor which probably
serves as a general switch factor for erythroid development. It
binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3'
within regulatory regions of globin genes and of other genes
expressed in erythroid cells.
-!- SUBUNIT: Interacts with EP300; the interaction enhances
transcriptional activity as a direct result of acetylation.
{ECO:0000269|PubMed:9859997}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Erythrocytes.
-!- DOMAIN: The two fingers are functionally distinct and cooperate to
achieve specific, stable DNA binding. The first finger is
necessary only for full specificity and stability of binding,
whereas the second one is required for binding (By similarity).
{ECO:0000250}.
-!- PTM: Acetylated on Lys-158, Lys-214, Lys-218 and Lys-220 by EP300.
Acetylation increases DNA binding and stimulates transcriptional
activity. {ECO:0000269|PubMed:9859997}.
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EMBL; M26209; AAA49055.1; -; mRNA.
PIR; A32993; A32993.
RefSeq; NP_990795.1; NM_205464.1.
UniGene; Gga.827; -.
PDB; 1GAT; NMR; -; A=158-217.
PDB; 1GAU; NMR; -; A=158-217.
PDB; 2GAT; NMR; -; A=158-223.
PDB; 3GAT; NMR; -; A=158-223.
PDBsum; 1GAT; -.
PDBsum; 1GAU; -.
PDBsum; 2GAT; -.
PDBsum; 3GAT; -.
ProteinModelPortal; P17678; -.
SMR; P17678; -.
BioGrid; 676699; 3.
iPTMnet; P17678; -.
PRIDE; P17678; -.
GeneID; 107050548; -.
KEGG; gga:396450; -.
CTD; 2623; -.
InParanoid; P17678; -.
KO; K09182; -.
EvolutionaryTrace; P17678; -.
PRO; PR:P17678; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IBA:GO_Central.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
Gene3D; 3.30.50.10; -; 2.
InterPro; IPR000679; Znf_GATA.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00320; GATA; 2.
PRINTS; PR00619; GATAZNFINGER.
SMART; SM00401; ZnF_GATA; 2.
PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome; DNA-binding;
Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 304 Erythroid transcription factor.
/FTId=PRO_0000083400.
ZN_FING 110 134 GATA-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00094}.
ZN_FING 164 188 GATA-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00094}.
MOD_RES 151 151 N6-acetyllysine; by EP300.
{ECO:0000305|PubMed:9859997}.
MOD_RES 152 152 N6-acetyllysine; by EP300.
{ECO:0000305|PubMed:9859997}.
MOD_RES 158 158 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:9859997}.
MOD_RES 214 214 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:9859997}.
MOD_RES 218 218 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:9859997}.
MOD_RES 220 220 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:9859997}.
MUTAGEN 151 152 KK->RR: Reduces acetylation and
activation by EP300.
{ECO:0000269|PubMed:9859997}.
MUTAGEN 158 158 K->R: Reduces acetylation and activation
by EP300. {ECO:0000269|PubMed:9859997}.
TURN 165 167 {ECO:0000244|PDB:1GAT}.
STRAND 173 178 {ECO:0000244|PDB:1GAT}.
TURN 179 181 {ECO:0000244|PDB:1GAT}.
STRAND 182 185 {ECO:0000244|PDB:1GAT}.
HELIX 186 195 {ECO:0000244|PDB:1GAT}.
HELIX 201 203 {ECO:0000244|PDB:1GAT}.
SEQUENCE 304 AA; 31417 MW; 64C9D6FDB58CE83F CRC64;
MEFVALGGPD AGSPTPFPDE AGAFLGLGGG ERTEAGGLLA SYPPSGRVSL VPWADTGTLG
TPQWVPPATQ MEPPHYLELL QPPRGSPPHP SSGPLLPLSS GPPPCEAREC VNCGATATPL
WRRDGTGHYL CNACGLYHRL NGQNRPLIRP KKRLLVSKRA GTVCSNCQTS TTTLWRRSPM
GDPVCNACGL YYKLHQVNRP LTMRKDGIQT RNRKVSSKGK KRRPPGGGNP SATAGGGAPM
GGGGDPSMPP PPPPPAAAPP QSDALYALGP VVLSGHFLPF GNSGGFFGGG AGGYTAPPGL
SPQI


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