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Protein

Erythroid transcription factor

Gene

GATA1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri110 – 13425GATA-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri164 – 18825GATA-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Erythroid transcription factor
Alternative name(s):
Eryf1
GATA-binding factor 1
Short name:
GATA-1
NF-E1 DNA-binding protein
Short name:
NF-E1a
Gene namesi
Name:GATA1
Synonyms:ERYF1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1522KK → RR: Reduces acetylation and activation by EP300. 1 Publication
Mutagenesisi158 – 1581K → R: Reduces acetylation and activation by EP300. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 304304Erythroid transcription factorPRO_0000083400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei151 – 1511N6-acetyllysine; by EP300Curated
Modified residuei152 – 1521N6-acetyllysine; by EP300Curated
Modified residuei158 – 1581N6-acetyllysine; by EP3001 Publication
Modified residuei214 – 2141N6-acetyllysine; by EP3001 Publication
Modified residuei218 – 2181N6-acetyllysine; by EP3001 Publication
Modified residuei220 – 2201N6-acetyllysine; by EP3001 Publication

Post-translational modificationi

Acetylated on Lys-158, Lys-214, Lys-218 and Lys-220 by EP300. Acetylation increases DNA binding and stimulates transcriptional activity.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP17678.

PTM databases

iPTMnetiP17678.

Expressioni

Tissue specificityi

Erythrocytes.

Interactioni

Subunit structurei

Interacts with EP300; the interaction enhances transcriptional activity as a direct result of acetylation.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi676699. 3 interactions.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni165 – 1673Combined sources
Beta strandi173 – 1786Combined sources
Turni179 – 1813Combined sources
Beta strandi182 – 1854Combined sources
Helixi186 – 19510Combined sources
Helixi201 – 2033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GATNMR-A158-217[»]
1GAUNMR-A158-217[»]
2GATNMR-A158-223[»]
3GATNMR-A158-223[»]
ProteinModelPortaliP17678.
SMRiP17678. Positions 106-149, 158-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17678.

Family & Domainsi

Domaini

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).By similarity

Sequence similaritiesi

Contains 2 GATA-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri110 – 13425GATA-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri164 – 18825GATA-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

InParanoidiP17678.
KOiK09182.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF187. PTHR10071:SF187. 1 hit.
PfamiPF00320. GATA. 2 hits.
[Graphical view]
PRINTSiPR00619. GATAZNFINGER.
SMARTiSM00401. ZnF_GATA. 2 hits.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17678-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFVALGGPD AGSPTPFPDE AGAFLGLGGG ERTEAGGLLA SYPPSGRVSL
60 70 80 90 100
VPWADTGTLG TPQWVPPATQ MEPPHYLELL QPPRGSPPHP SSGPLLPLSS
110 120 130 140 150
GPPPCEAREC VNCGATATPL WRRDGTGHYL CNACGLYHRL NGQNRPLIRP
160 170 180 190 200
KKRLLVSKRA GTVCSNCQTS TTTLWRRSPM GDPVCNACGL YYKLHQVNRP
210 220 230 240 250
LTMRKDGIQT RNRKVSSKGK KRRPPGGGNP SATAGGGAPM GGGGDPSMPP
260 270 280 290 300
PPPPPAAAPP QSDALYALGP VVLSGHFLPF GNSGGFFGGG AGGYTAPPGL

SPQI
Length:304
Mass (Da):31,417
Last modified:August 1, 1990 - v1
Checksum:i64C9D6FDB58CE83F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26209 mRNA. Translation: AAA49055.1.
PIRiA32993.
RefSeqiNP_990795.1. NM_205464.1.
UniGeneiGga.827.

Genome annotation databases

GeneIDi396450.
KEGGigga:396450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26209 mRNA. Translation: AAA49055.1.
PIRiA32993.
RefSeqiNP_990795.1. NM_205464.1.
UniGeneiGga.827.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GATNMR-A158-217[»]
1GAUNMR-A158-217[»]
2GATNMR-A158-223[»]
3GATNMR-A158-223[»]
ProteinModelPortaliP17678.
SMRiP17678. Positions 106-149, 158-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676699. 3 interactions.

PTM databases

iPTMnetiP17678.

Proteomic databases

PRIDEiP17678.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396450.
KEGGigga:396450.

Organism-specific databases

CTDi2623.

Phylogenomic databases

InParanoidiP17678.
KOiK09182.

Miscellaneous databases

EvolutionaryTraceiP17678.
PROiP17678.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF187. PTHR10071:SF187. 1 hit.
PfamiPF00320. GATA. 2 hits.
[Graphical view]
PRINTSiPR00619. GATAZNFINGER.
SMARTiSM00401. ZnF_GATA. 2 hits.
[Graphical view]
PROSITEiPS00344. GATA_ZN_FINGER_1. 2 hits.
PS50114. GATA_ZN_FINGER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The erythroid-specific transcription factor Eryf1: a new finger protein."
    Evans T., Felsenfeld G.
    Cell 58:877-885(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Activity and tissue-specific expression of the transcription factor NF-E1 multigene family."
    Yamamoto M., Ko L.J., Leonard M.W., Beug H., Orkin S.H., Engel J.D.
    Genes Dev. 4:1650-1662(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Regulation of activity of the transcription factor GATA-1 by acetylation."
    Boyes J., Byfield P., Nakatani Y., Ogryzko V.
    Nature 396:594-598(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-158; LYS-214; LYS-218 AND LYS-220, MUTAGENESIS OF 151-LYS-LYS-152 AND LYS-158.
  4. "NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1."
    Omichinski J.G., Clore G.M., Schaad O., Felsenfeld G., Trainor C., Appella E., Stahl S.J., Gronenborn A.M.
    Science 261:438-446(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 158-223.
  5. "Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution."
    Tjandra N., Omichinski J.G., Gronenborn A.M., Clore G.M., Bax A.
    Nat. Struct. Biol. 4:732-738(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 158-223.

Entry informationi

Entry nameiGATA1_CHICK
AccessioniPrimary (citable) accession number: P17678
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.