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Protein

Erythroid transcription factor

Gene

Gata1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri204 – 228GATA-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri258 – 282GATA-type 2PROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Gata1
Synonyms:Gf-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95661 Gata1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000833981 – 413Erythroid transcription factorAdd BLAST413

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei26Phosphoserine1 Publication1
Modified residuei49Phosphoserine1 Publication1
Modified residuei72Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P17679

PRoteomics IDEntifications database

More...
PRIDEi
P17679

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P17679

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P17679

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000031162 Expressed in 118 organ(s), highest expression level in fetal liver hematopoietic progenitor cell

CleanEx database of gene expression profiles

More...
CleanExi
MM_GATA1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P17679 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P17679 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with EP300 (By similarity). Interacts with CEBPE (By similarity).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199838, 23 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P17679

Database of interacting proteins

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DIPi
DIP-40883N

Protein interaction database and analysis system

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IntActi
P17679, 9 interactors

Molecular INTeraction database

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MINTi
P17679

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000033502

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1413
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P17679

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P17679

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P17679

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni200 – 330Interaction with MED1 and CCAR11 PublicationAdd BLAST131
Regioni203 – 222Required for interaction with ZFPM1By similarityAdd BLAST20
Regioni249 – 315Interaction with CALCOCO11 PublicationAdd BLAST67

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1601 Eukaryota
COG5641 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161156

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000047701

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051705

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P17679

KEGG Orthology (KO)

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KOi
K09182

Identification of Orthologs from Complete Genome Data

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OMAi
YSKTGLY

Database of Orthologous Groups

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OrthoDBi
EOG091G0AUR

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P17679

TreeFam database of animal gene trees

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TreeFami
TF315391

Family and domain databases

Conserved Domains Database

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CDDi
cd00202 ZnF_GATA, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.50.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029524 GATA-1
IPR039355 Transcription_factor_GATA
IPR000679 Znf_GATA
IPR013088 Znf_NHR/GATA

The PANTHER Classification System

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PANTHERi
PTHR10071 PTHR10071, 1 hit
PTHR10071:SF190 PTHR10071:SF190, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00320 GATA, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00619 GATAZNFINGER

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00401 ZnF_GATA, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00344 GATA_ZN_FINGER_1, 2 hits
PS50114 GATA_ZN_FINGER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AUB4B1AUB4_MOUSE
Erythroid transcription factor
Gata1
124Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B1AUB3B1AUB3_MOUSE
Erythroid transcription factor
Gata1
109Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti29D → G in AAH52653 (PubMed:15489334).Curated1
Sequence conflicti129N → S in AAH52653 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0414521 – 83Missing in isoform 2. CuratedAdd BLAST83

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS29981.1 [P17679-1]

Protein sequence database of the Protein Information Resource

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PIRi
S04655

NCBI Reference Sequences

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RefSeqi
NP_032115.1, NM_008089.2 [P17679-1]
XP_011245750.1, XM_011247448.2 [P17679-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.335973

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162 [P17679-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
14460

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14460

UCSC genome browser

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UCSCi
uc009snl.2 mouse [P17679-1]

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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
CORUMiP17679
DIPiDIP-40883N
IntActiP17679, 9 interactors
MINTiP17679
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

Comparative Toxicogenomics Database

More...
CTDi
2623
MGIiMGI:95661 Gata1

Phylogenomic databases

eggNOGiKOG1601 Eukaryota
COG5641 LUCA
GeneTreeiENSGT00940000161156
HOGENOMiHOG000047701
HOVERGENiHBG051705
InParanoidiP17679
KOiK09182
OMAiYSKTGLY
OrthoDBiEOG091G0AUR
PhylomeDBiP17679
TreeFamiTF315391

Enzyme and pathway databases

ReactomeiR-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

EvolutionaryTraceiP17679

Protein Ontology

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PROi
PR:P17679

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000031162 Expressed in 118 organ(s), highest expression level in fetal liver hematopoietic progenitor cell
CleanExiMM_GATA1
ExpressionAtlasiP17679 baseline and differential
GenevisibleiP17679 MM

Family and domain databases

CDDicd00202 ZnF_GATA, 2 hits
Gene3Di3.30.50.10, 2 hits
InterProiView protein in InterPro
IPR029524 GATA-1
IPR039355 Transcription_factor_GATA
IPR000679 Znf_GATA
IPR013088 Znf_NHR/GATA
PANTHERiPTHR10071 PTHR10071, 1 hit
PTHR10071:SF190 PTHR10071:SF190, 1 hit
PfamiView protein in Pfam
PF00320 GATA, 2 hits
PRINTSiPR00619 GATAZNFINGER
SMARTiView protein in SMART
SM00401 ZnF_GATA, 2 hits
PROSITEiView protein in PROSITE
PS00344 GATA_ZN_FINGER_1, 2 hits
PS50114 GATA_ZN_FINGER_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGATA1_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17679
Secondary accession number(s): Q3UIH9, Q7TMX8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: December 5, 2018
This is version 180 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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