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Protein

Erythroid transcription factor

Gene

Gata1

Organism
Mus musculus (Mouse)
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. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity).By similarity5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri204 – 228GATA-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri258 – 282GATA-type 2PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

  • animal organ morphogenesis Source: GO_Central
  • basophil differentiation Source: Ensembl
  • cell-cell signaling Source: MGI
  • cell development Source: MGI
  • cell fate commitment Source: GO_Central
  • cellular response to thyroid hormone stimulus Source: MGI
  • dendritic cell differentiation Source: MGI
  • digestive tract development Source: GO_Central
  • embryonic hemopoiesis Source: MGI
  • eosinophil fate commitment Source: MGI
  • erythrocyte development Source: MGI
  • erythrocyte differentiation Source: BHF-UCL
  • heart development Source: GO_Central
  • homeostasis of number of cells within a tissue Source: MGI
  • in utero embryonic development Source: MGI
  • male gonad development Source: MGI
  • megakaryocyte differentiation Source: MGI
  • myeloid cell differentiation Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of bone mineralization Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of transcription regulatory region DNA binding Source: MGI
  • platelet aggregation Source: BHF-UCL
  • platelet formation Source: MGI
  • positive regulation of erythrocyte differentiation Source: MGI
  • positive regulation of osteoblast proliferation Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of definitive erythrocyte differentiation Source: BHF-UCL
  • regulation of glycoprotein biosynthetic process Source: BHF-UCL
  • regulation of primitive erythrocyte differentiation Source: MGI
  • transcriptional activation by promoter-enhancer looping Source: BHF-UCL
  • transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Erythroid transcription factor
Alternative name(s):
Eryf1
GATA-binding factor 1
Short name:
GATA-1
Short name:
GF-1
NF-E1 DNA-binding protein
Gene namesi
Name:Gata1
Synonyms:Gf-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:95661. Gata1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi49S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi72S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi137K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. 1 Publication1
Mutagenesisi142S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi178S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi187S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi203E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication1
Mutagenesisi204C → R: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication1
Mutagenesisi205V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication1
Mutagenesisi205V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication1
Mutagenesisi207C → G, R or W: Disrupts interaction with ZFPM1. 2 Publications1
Mutagenesisi207C → P: Stability of binding to DNA reduced. 2 Publications1
Mutagenesisi208G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication1
Mutagenesisi218D → G or V: No effect on interaction with ZFPM1. 1 Publication1
Mutagenesisi222H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication1
Mutagenesisi224L → P: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication1
Mutagenesisi225C → R, S or Y: Disrupts interaction with ZFPM1. 1 Publication1
Mutagenesisi228C → R or S: Disrupts interaction with ZFPM1. 1 Publication1
Mutagenesisi230L → F: Stability of binding to DNA reduced. 1 Publication1
Mutagenesisi233K → E: No effect on interaction with ZFPM1. 1 Publication1
Mutagenesisi245 – 246KK → AA: No effect on DNA binding. Reduces acetylation. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 312-A--A-316. Abrogates ability to induce erythroid differentiation; when associated with 312-A--A-316. Reduces binding to CREBBP; when associated with 312-A--A-316. Disrupts stable association with chromatin; when associated with 312-A--A-316. 2 Publications2
Mutagenesisi245 – 246KK → RR: No effect on DNA binding. 2 Publications2
Mutagenesisi261C → P: Abolishes DNA-binding. 1 Publication1
Mutagenesisi284L → F: Binds to DNA with reduced affinity. 1 Publication1
Mutagenesisi310S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication1
Mutagenesisi312 – 316KGKKK → AGAAA: No effect on DNA binding. Reduces acetylation. Reduces binding to CREBBP. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 245-A-A-246. Abrogates ability to induce erythroid differentiation; when associated with 245-A-A-246. Reduces binding to CREBBP; when associated with 245-A-A-246. Disrupts stable association with chromatin; when associated with 245-A-A-246. 2 Publications5
Mutagenesisi312 – 316KGKKK → RGRRR: No effect on DNA binding. 2 Publications5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000833981 – 413Erythroid transcription factorAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26Phosphoserine1 Publication1
Modified residuei49Phosphoserine1 Publication1
Modified residuei72Phosphoserine1 Publication1
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei142Phosphoserine1 Publication1
Modified residuei178Phosphoserine1 Publication1
Modified residuei187Phosphoserine1 Publication1
Modified residuei233N6-acetyllysine; by EP300By similarity1
Modified residuei245N6-acetyllysine; by EP300By similarity1
Modified residuei246N6-acetyllysine; by CREBBP1 Publication1
Modified residuei246N6-acetyllysine; by EP300By similarity1
Modified residuei252N6-acetyllysine; by CREBBP1 Publication1
Modified residuei308N6-acetyllysine1 Publication1
Modified residuei310Phosphoserine1 Publication1
Modified residuei312N6-acetyllysine; by CREBBP2 Publications1
Modified residuei314N6-acetyllysine1 Publication1
Modified residuei315N6-acetyllysine1 Publication1

Post-translational modificationi

Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity).By similarity
Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation with SUMO1 has no effect on transcriptional activity.2 Publications
Acetylated on Lys-233, Lys-245 Lys-246 by EP300 (By similarity). Acetylated on Lys-246, Lys-252 and Lys-312 by CREBBP in vitro. Acetylation does not affect DNA-binding in vitro but is essential to induce erythroid differentiation and for binding chromatin in vivo.By similarity2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP17679.
PRIDEiP17679.

PTM databases

iPTMnetiP17679.
PhosphoSitePlusiP17679.

Expressioni

Tissue specificityi

Erythrocytes. Expressed (at protein level) in liver.2 Publications

Developmental stagei

Detected at 11.5-day fetal livers (at protein level). Isoform 2 detected earlier at 8.5-day embryo.1 Publication

Gene expression databases

BgeeiENSMUSG00000031162.
CleanExiMM_GATA1.
ExpressionAtlasiP17679. baseline and differential.
GenevisibleiP17679. MM.

Interactioni

Subunit structurei

May form homodimers or heterodimers with other isoforms. Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity). Interacts with GFI1B. Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner. Interacts with LMCD1. Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo. Interacts with BRD3. Interacts with MED1, CCAR1 and CALCOCO1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Lmo2P258015EBI-3903251,EBI-3903256

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: MGI
  • p53 binding Source: MGI
  • RNA polymerase II transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi199838. 23 interactors.
DIPiDIP-40883N.
IntActiP17679. 5 interactors.
MINTiMINT-94735.
STRINGi10090.ENSMUSP00000033502.

Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni205 – 207Combined sources3
Helixi226 – 235Combined sources10
Turni259 – 261Combined sources3
Helixi280 – 289Combined sources10
Helixi295 – 297Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GNFNMR-A200-243[»]
1Y0JNMR-A200-243[»]
2L5ENMR-B308-320[»]
2L6YNMR-A200-238[»]
2L6ZNMR-A200-238[»]
3VD6X-ray1.98C200-318[»]
3VEKX-ray2.63C/F200-318[»]
ProteinModelPortaliP17679.
SMRiP17679.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17679.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 330Interaction with MED1 and CCAR11 PublicationAdd BLAST131
Regioni203 – 222Required for interaction with ZFPM1By similarityAdd BLAST20
Regioni249 – 315Interaction with CALCOCO11 PublicationAdd BLAST67

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.

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri204 – 228GATA-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri258 – 282GATA-type 2PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1601. Eukaryota.
COG5641. LUCA.
GeneTreeiENSGT00760000119221.
HOGENOMiHOG000047701.
HOVERGENiHBG051705.
InParanoidiP17679.
KOiK09182.
OMAiPSTAHLY.
OrthoDBiEOG091G0AUR.
PhylomeDBiP17679.
TreeFamiTF315391.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF190. PTHR10071:SF190. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P17679-1) [UniParc]FASTAAdd to basket

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
MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP
60 70 80 90 100
NAATAAASAL AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK
110 120 130 140 150
TALYPASTVC PSHEDAPSQA LEDQEGKSNN TFLDTLKTER LSPDLLTLGT
160 170 180 190 200
ALPASLPVTG SAYGGADFPS PFFSPTGSPL SSAAYSSPKF HGSLPLAPCE
210 220 230 240 250
ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRMIV
260 270 280 290 300
SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD
310 320 330 340 350
GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA
360 370 380 390 400
SGLALGTAGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP
410
TTSSTSVIAP LSS
Length:413
Mass (Da):42,674
Last modified:August 1, 1990 - v1
Checksum:iBB627A92700D557A
GO
Isoform 2 (identifier: P17679-2) [UniParc]FASTAAdd to basket
Also known as: GATA-1s

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Note: Produced by alternative initiation at Met-84 of isoform 1. Less effective than isoform 1 in its ability to transactivate target genes.
Show »
Length:330
Mass (Da):34,188
Checksum:i8BF1F251EB8E47A1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29D → G in AAH52653 (PubMed:15489334).Curated1
Sequence conflicti129N → S in AAH52653 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0414521 – 83Missing in isoform 2. CuratedAdd BLAST83

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15763 mRNA. Translation: CAA33769.1.
AK146915 mRNA. Translation: BAE27527.1.
AL670169 Genomic DNA. Translation: CAM17247.1.
CH466638 Genomic DNA. Translation: EDL33938.1.
X57530 Genomic DNA. Translation: CAA40751.1.
BC052653 mRNA. Translation: AAH52653.1.
CCDSiCCDS29981.1. [P17679-1]
PIRiS04655.
RefSeqiNP_032115.1. NM_008089.2. [P17679-1]
XP_011245750.1. XM_011247448.2. [P17679-1]
UniGeneiMm.335973.

Genome annotation databases

EnsembliENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162. [P17679-1]
GeneIDi14460.
KEGGimmu:14460.
UCSCiuc009snl.2. mouse. [P17679-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15763 mRNA. Translation: CAA33769.1.
AK146915 mRNA. Translation: BAE27527.1.
AL670169 Genomic DNA. Translation: CAM17247.1.
CH466638 Genomic DNA. Translation: EDL33938.1.
X57530 Genomic DNA. Translation: CAA40751.1.
BC052653 mRNA. Translation: AAH52653.1.
CCDSiCCDS29981.1. [P17679-1]
PIRiS04655.
RefSeqiNP_032115.1. NM_008089.2. [P17679-1]
XP_011245750.1. XM_011247448.2. [P17679-1]
UniGeneiMm.335973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GNFNMR-A200-243[»]
1Y0JNMR-A200-243[»]
2L5ENMR-B308-320[»]
2L6YNMR-A200-238[»]
2L6ZNMR-A200-238[»]
3VD6X-ray1.98C200-318[»]
3VEKX-ray2.63C/F200-318[»]
ProteinModelPortaliP17679.
SMRiP17679.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199838. 23 interactors.
DIPiDIP-40883N.
IntActiP17679. 5 interactors.
MINTiMINT-94735.
STRINGi10090.ENSMUSP00000033502.

PTM databases

iPTMnetiP17679.
PhosphoSitePlusiP17679.

Proteomic databases

PaxDbiP17679.
PRIDEiP17679.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162. [P17679-1]
GeneIDi14460.
KEGGimmu:14460.
UCSCiuc009snl.2. mouse. [P17679-1]

Organism-specific databases

CTDi2623.
MGIiMGI:95661. Gata1.

Phylogenomic databases

eggNOGiKOG1601. Eukaryota.
COG5641. LUCA.
GeneTreeiENSGT00760000119221.
HOGENOMiHOG000047701.
HOVERGENiHBG051705.
InParanoidiP17679.
KOiK09182.
OMAiPSTAHLY.
OrthoDBiEOG091G0AUR.
PhylomeDBiP17679.
TreeFamiTF315391.

Enzyme and pathway databases

ReactomeiR-MMU-983231. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTraceiP17679.
PROiP17679.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031162.
CleanExiMM_GATA1.
ExpressionAtlasiP17679. baseline and differential.
GenevisibleiP17679. MM.

Family and domain databases

Gene3Di3.30.50.10. 2 hits.
InterProiIPR029524. GATA-1.
IPR000679. Znf_GATA.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR10071:SF190. PTHR10071:SF190. 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...

Entry informationi

Entry nameiGATA1_MOUSE
AccessioniPrimary (citable) accession number: P17679
Secondary accession number(s): Q3UIH9, Q7TMX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 164 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.