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Protein

Autoimmune regulator

Gene

AIRE

Organism
Homo sapiens (Human)
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

Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) (PubMed:26084028). Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla (PubMed:26084028). Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program. Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression. Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes. In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection. In secondary lymphoid organs, induces functional inactivation of CD4+ T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli (By similarity).By similarity2 Publications3 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 fingeri296 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri434 – 475PHD-type 2PROSITE-ProRule annotationAdd BLAST42

<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
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

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SIGNORi
O43918

<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:
Autoimmune regulator
Alternative name(s):
Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein
Short name:
APECED 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:AIRE
Synonyms:APECED
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000160224.16

Human Gene Nomenclature Database

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HGNCi
HGNC:360 AIRE

Online Mendelian Inheritance in Man (OMIM)

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MIMi
607358 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O43918

<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

Cytoplasm, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Autoimmune polyendocrine syndrome 1, with or without reversible metaphyseal dysplasia (APS1)20 Publications
The disease is caused by mutations affecting the gene represented in this entry. Most of the mutations alter the nucleus-cytoplasm distribution of AIRE and disturb its association with nuclear dots and cytoplasmic filaments. Most of the mutations also decrease transactivation of the protein. The HSR domain is responsible for the homomultimerization activity of AIRE. All the missense mutations of the HSR and the SAND domains decrease this activity, but those in other domains do not. The AIRE protein is present in soluble high-molecular-weight complexes. Mutations in the HSR domain and deletion of PHD zinc fingers disturb the formation of these complexes (PubMed:14974083). Heterozygous mutations within the PHD1 domain have dominant-negatif effects and cause organ-specific autoimmune diseases (PubMed:26084028). Patients harbor extremely high-affinity, neutralizing autoantibodies, particularly against specific cytokines such as type I interferons which could protect them from some types of autoimmune diseases, like type I diabetes (PubMed:27426947).3 Publications
Disease descriptionA rare disease characterized by the combination of chronic mucocutaneous candidiasis, hypoparathyroidism and Addison disease. Symptoms of mucocutaneous candidiasis manifest first, followed by hypotension or fatigue occurring as a result of Addison disease. APS1 is associated with other autoimmune disorders including diabetes mellitus, vitiligo, alopecia, hepatitis, pernicious anemia and primary hypothyroidism.
See also OMIM:240300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02648015R → C in APS1. 1 PublicationCorresponds to variant dbSNP:rs179363875EnsemblClinVar.1
Natural variantiVAR_01371315R → L in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity. 3 PublicationsCorresponds to variant dbSNP:rs179363876EnsemblClinVar.1
Natural variantiVAR_01371416T → M in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity. 4 PublicationsCorresponds to variant dbSNP:rs179363877EnsemblClinVar.1
Natural variantiVAR_02648121A → V in APS1; no effect on homooligomerization; no effect on subcellular localization; no effect on the transcriptional transactivation activity. 2 PublicationsCorresponds to variant dbSNP:rs179363886EnsemblClinVar.1
Natural variantiVAR_02648222 – 23Missing in APS1; prevents homodimerization. 1 Publication2
Natural variantiVAR_00500428L → P in APS1; abolishes association with cytoplasmic tubular structures and homodimerization; loss of doted nuclear localization; nuclear smear. 5 PublicationsCorresponds to variant dbSNP:rs179363878EnsemblClinVar.1
Natural variantiVAR_01371529L → P in APS1. 2 PublicationsCorresponds to variant dbSNP:rs179363879EnsemblClinVar.1
Natural variantiVAR_02648377F → S in APS1; loss of homooligomerization. 1 PublicationCorresponds to variant dbSNP:rs179363887EnsemblClinVar.1
Natural variantiVAR_01371678W → R in APS1; loss of homooligomerization. 5 PublicationsCorresponds to variant dbSNP:rs179363880EnsemblClinVar.1
Natural variantiVAR_01371780V → L in APS1. 3 PublicationsCorresponds to variant dbSNP:rs179363881EnsemblClinVar.1
Natural variantiVAR_00500583K → E in APS1. 3 PublicationsCorresponds to variant dbSNP:rs121434255EnsemblClinVar.1
Natural variantiVAR_01371885Y → C in APS1. 3 PublicationsCorresponds to variant dbSNP:rs179363882EnsemblClinVar.1
Natural variantiVAR_01371990Y → C in APS1; decreases doted nuclear localization. 3 PublicationsCorresponds to variant dbSNP:rs179363883EnsemblClinVar.1
Natural variantiVAR_01372093L → R in APS1. 2 PublicationsCorresponds to variant dbSNP:rs179363884EnsemblClinVar.1
Natural variantiVAR_014422228G → W in APS1; changes the subcellular localization and in addition disrupts the transactivating capacity of the wild-type AIRE; acts with a dominant negative effect by binding to the wild-type AIRE thus preventing the protein from forming the complexes needed for transactivation. 3 PublicationsCorresponds to variant dbSNP:rs121434257EnsemblClinVar.1
Natural variantiVAR_026484252P → L in APS1. 1 PublicationCorresponds to variant dbSNP:rs34397615EnsemblClinVar.1
Natural variantiVAR_013721301V → M in APS1; no effect on protein structure or on interaction with histone H3; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 5 PublicationsCorresponds to variant dbSNP:rs150634562EnsemblClinVar.1
Natural variantiVAR_013723311C → Y in APS1; impairs zinc binding and folding of the PHD-type 1 zinc finger; dominant-negatif effect on the regulation of target gene transcription; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 7 PublicationsCorresponds to variant dbSNP:rs386833674EnsemblClinVar.1
Natural variantiVAR_026485326P → L in APS1; no significant effect on structure, but may alter protein interactions; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 3 PublicationsCorresponds to variant dbSNP:rs179363885EnsemblClinVar.1
Natural variantiVAR_013724326P → Q in APS1; alters folding of the PHD-type 1 zinc finger. 5 PublicationsCorresponds to variant dbSNP:rs179363885EnsemblClinVar.1
Natural variantiVAR_026486539P → L in APS1. 1 PublicationCorresponds to variant dbSNP:rs179363889EnsemblClinVar.1

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>Mutagenesisi28 – 29LL → PP: Loss of doted nuclear location, forms nuclear smears. Loss of transactivation activity on target genes transcription. 1 Publication2
Mutagenesisi97L → P: Loss of transactivation activity on target gene transcription; no dominant-negatif effect on target gene transcription. Loss of doted nuclear localization. 1 Publication1
Mutagenesisi295N → A: Abolishes interaction with histone H3. 1 Publication1
Mutagenesisi297D → A: Strongly reduces interaction with unmethylated histone H3 and abolishes interaction with histone H3 trimethylated at 'Lys-4'. No effect on doted nuclear localization. Dominant-negatif effect on target gene transcription. 2 Publications1
Mutagenesisi298E → A: Reduces interaction with histone H3. 1 Publication1
Mutagenesisi302C → P: Reduces transcriptional activation. 1 Publication1
Mutagenesisi303R → P: Alters protein folding and abolishes interaction with histone H3. No effect on doted nuclear localization. Dominant-negatif effect on target gene transcription. 2 Publications1
Mutagenesisi304D → A: Strongly reduces interaction with histone H3. 1 Publication1
Mutagenesisi307E → A: Reduces interaction with histone H3. 1 Publication1
Mutagenesisi312D → A: Abolishes interaction with histone H3. 1 Publication1
Mutagenesisi312D → N: No effect on doted nuclear localization. Dominant-negatif effect on target gene transcription. 1 Publication1
Mutagenesisi437C → P: Reduces transcription activation. 1 Publication1
Mutagenesisi446C → G: Dominant-negatif effect on regulation of target gene transcription. 1 Publication1
Mutagenesisi471R → C: No effect on regulation of target gene transcription. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
326

MalaCards human disease database

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MalaCardsi
AIRE
MIMi109100 phenotype
240300 phenotype

Open Targets

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OpenTargetsi
ENSG00000160224

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
3453 Autoimmune polyendocrinopathy type 1
189466 Familial isolated hypoparathyroidism due to impaired PTH secretion

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24654

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
AIRE

<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_00000645131 – 545Autoimmune regulatorAdd BLAST545

<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

Phosphorylated. Phosphorylation could trigger oligomerization.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O43918

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

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PaxDbi
O43918

PeptideAtlas

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PeptideAtlasi
O43918

PRoteomics IDEntifications database

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PRIDEi
O43918

ProteomicsDB human proteome resource

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ProteomicsDBi
49233
49234 [O43918-2]
49235 [O43918-3]
49236 [O43918-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43918

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

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PhosphoSitePlusi
O43918

<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

Widely expressed. Expressed at higher level in thymus (medullary epithelial cells and monocyte-dendritic cells), pancreas, adrenal cortex and testis. Expressed at lower level in the spleen, fetal liver and lymph nodes. In secondary lymphoid organs, expressed in a discrete population of bone marrow-derived toleregenic antigen presenting cells (APCs) called extrathymic AIRE expressing cells (eTAC)(at protein level) (PubMed:23993652). Isoform 2 and isoform 3 seem to be less frequently expressed than isoform 1, if at all.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000160224 Expressed in 88 organ(s), highest expression level in amniotic fluid

CleanEx database of gene expression profiles

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CleanExi
HS_AIRE

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43918 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA038267

<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

Homodimer and homotetramer. Interacts with CREBBP. Interacts preferentially with histone H3 that is not methylated at 'Lys-4'. Binds with lower affinity to histone H3 that is monomethylated at 'Lys-4'. Trimethylation of histone H3 at 'Lys-4' or phosphorylation at 'Thr-3' abolish the interaction. Binds with lower affinity to histone H3 that is acetylated at 'Lys-4', or that is acetylated at 'Lys-9' or trimethylated at 'Lys-9'. Binds histone H3 that is dimethylated at 'Arg-2' with very low affinity.5 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)

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BioGridi
106823, 93 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O43918

Database of interacting proteins

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DIPi
DIP-47504N

Protein interaction database and analysis system

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IntActi
O43918, 32 interactors

Molecular INTeraction database

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MINTi
O43918

STRING: functional protein association networks

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STRINGi
9606.ENSP00000291582

<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

1545
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
O43918

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

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SMRi
O43918

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

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EvolutionaryTracei
O43918

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 105HSRPROSITE-ProRule annotationAdd BLAST105
Domaini181 – 280SANDPROSITE-ProRule annotationAdd BLAST100

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>Regioni295 – 298Interaction with histone H3 not methylated at 'Lys-4'4
Regioni304 – 312Interaction with histone H3 not methylated at 'Lys-4'9
Regioni331 – 335Interaction with histone H3 not methylated at 'Lys-4'5

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi7 – 11LXXLL motif 15
Motifi63 – 67LXXLL motif 25
Motifi414 – 418LXXLL motif 35
Motifi516 – 520LXXLL motif 45

<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 L-X-X-L-L repeats may be implicated in binding to nuclear receptors.
The HSR domain is required for localization on tubular structures (N-terminal part) and for homodimerization.
Interacts via the first PHD domain with the N-terminus of histone H3 that is not methylated at 'Lys-4'. Disruption of the first PHD domain has been shown to lead to reduced transcriptional activity and to localization of the protein mainly in the cytoplasm in small granules. While the PHD zinc fingers are necessary for the transactivation capacity of the protein, other regions also modulate this function.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri296 – 343PHD-type 1PROSITE-ProRule annotationAdd BLAST48
Zinc fingeri434 – 475PHD-type 2PROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IRE7 Eukaryota
ENOG410XQQA LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161104

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000033872

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG014961

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43918

KEGG Orthology (KO)

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KOi
K10603

Identification of Orthologs from Complete Genome Data

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OMAi
LLSEHTF

Database of Orthologous Groups

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OrthoDBi
EOG091G055U

Database for complete collections of gene phylogenies

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PhylomeDBi
O43918

TreeFam database of animal gene trees

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TreeFami
TF336193

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.390.10, 1 hit
3.30.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008087 AIRE
IPR004865 HSR_dom
IPR010919 SAND-like_dom_sf
IPR000770 SAND_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

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Pfami
View protein in Pfam
PF03172 HSR, 1 hit
PF00628 PHD, 1 hit
PF01342 SAND, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01711 AIREGULATOR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00249 PHD, 2 hits
SM00258 SAND, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57903 SSF57903, 2 hits
SSF63763 SSF63763, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51414 HSR, 1 hit
PS50864 SAND, 1 hit
PS01359 ZF_PHD_1, 2 hits
PS50016 ZF_PHD_2, 1 hit

<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 (4)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 4 <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 splicing. AlignAdd to basket
Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: O43918-1) [UniParc]FASTAAdd to basket
Also known as: AIRE-1

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
MATDAALRRL LRLHRTEIAV AVDSAFPLLH ALADHDVVPE DKFQETLHLK
60 70 80 90 100
EKEGCPQAFH ALLSWLLTQD STAILDFWRV LFKDYNLERY GRLQPILDSF
110 120 130 140 150
PKDVDLSQPR KGRKPPAVPK ALVPPPRLPT KRKASEEARA AAPAALTPRG
160 170 180 190 200
TASPGSQLKA KPPKKPESSA EQQRLPLGNG IQTMSASVQR AVAMSSGDVP
210 220 230 240 250
GARGAVEGIL IQQVFESGGS KKCIQVGGEF YTPSKFEDSG SGKNKARSSS
260 270 280 290 300
GPKPLVRAKG AQGAAPGGGE ARLGQQGSVP APLALPSDPQ LHQKNEDECA
310 320 330 340 350
VCRDGGELIC CDGCPRAFHL ACLSPPLREI PSGTWRCSSC LQATVQEVQP
360 370 380 390 400
RAEEPRPQEP PVETPLPPGL RSAGEEVRGP PGEPLAGMDT TLVYKHLPAP
410 420 430 440 450
PSAAPLPGLD SSALHPLLCV GPEGQQNLAP GARCGVCGDG TDVLRCTHCA
460 470 480 490 500
AAFHWRCHFP AGTSRPGTGL RCRSCSGDVT PAPVEGVLAP SPARLAPGPA
510 520 530 540
KDDTASHEPA LHRDDLESLL SEHTFDGILQ WAIQSMARPA APFPS
Length:545
Mass (Da):57,727
Last modified:June 1, 1998 - 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:i8CF703F8C9411BC5
GO
Isoform 2 (identifier: O43918-2) [UniParc]FASTAAdd to basket
Also known as: AIRE-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-292: MATDAALRRL...LALPSDPQLH → MWLVYSSGAP...VALRRVLHPS

Show »
Length:338
Mass (Da):35,507
Checksum:i7C99ABAD92DDC565
GO
Isoform 3 (identifier: O43918-3) [UniParc]FASTAAdd to basket
Also known as: AIRE-3

The sequence of this isoform differs from the canonical sequence as follows:
     1-292: MATDAALRRL...LALPSDPQLH → MWLVYSSGAP...VALRRVLHPS
     377-545: VRGPPGEPLA...MARPAAPFPS → PRCQGWTPRP...ACAADPAQET

Show »
Length:244
Mass (Da):25,927
Checksum:iBD26FC231E0E5611
GO
Isoform 4 (identifier: O43918-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-292: MATDAALRRL...LALPSDPQLH → MWLVYSSGAP...VALRRVLHPS
     293-293: Q → PVCMGVSCLCQ

Note: No experimental confirmation available.
Show »
Length:348
Mass (Da):36,501
Checksum:i37045012FF585F6E
GO

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 conflicti437 – 467CGDGT…TSRPG → W in CAA08759 (Ref. 3) CuratedAdd BLAST31

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02648015R → C in APS1. 1 PublicationCorresponds to variant dbSNP:rs179363875EnsemblClinVar.1
Natural variantiVAR_01371315R → L in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity. 3 PublicationsCorresponds to variant dbSNP:rs179363876EnsemblClinVar.1
Natural variantiVAR_01371416T → M in APS1; prevents homooligomerization; slightly alters subcellular localization; no effect on the transcriptional transactivation activity. 4 PublicationsCorresponds to variant dbSNP:rs179363877EnsemblClinVar.1
Natural variantiVAR_02648121A → V in APS1; no effect on homooligomerization; no effect on subcellular localization; no effect on the transcriptional transactivation activity. 2 PublicationsCorresponds to variant dbSNP:rs179363886EnsemblClinVar.1
Natural variantiVAR_02648222 – 23Missing in APS1; prevents homodimerization. 1 Publication2
Natural variantiVAR_00500428L → P in APS1; abolishes association with cytoplasmic tubular structures and homodimerization; loss of doted nuclear localization; nuclear smear. 5 PublicationsCorresponds to variant dbSNP:rs179363878EnsemblClinVar.1
Natural variantiVAR_01371529L → P in APS1. 2 PublicationsCorresponds to variant dbSNP:rs179363879EnsemblClinVar.1
Natural variantiVAR_02648377F → S in APS1; loss of homooligomerization. 1 PublicationCorresponds to variant dbSNP:rs179363887EnsemblClinVar.1
Natural variantiVAR_01371678W → R in APS1; loss of homooligomerization. 5 PublicationsCorresponds to variant dbSNP:rs179363880EnsemblClinVar.1
Natural variantiVAR_01371780V → L in APS1. 3 PublicationsCorresponds to variant dbSNP:rs179363881EnsemblClinVar.1
Natural variantiVAR_00500583K → E in APS1. 3 PublicationsCorresponds to variant dbSNP:rs121434255EnsemblClinVar.1
Natural variantiVAR_01371885Y → C in APS1. 3 PublicationsCorresponds to variant dbSNP:rs179363882EnsemblClinVar.1
Natural variantiVAR_01371990Y → C in APS1; decreases doted nuclear localization. 3 PublicationsCorresponds to variant dbSNP:rs179363883EnsemblClinVar.1
Natural variantiVAR_01372093L → R in APS1. 2 PublicationsCorresponds to variant dbSNP:rs179363884EnsemblClinVar.1
Natural variantiVAR_014422228G → W in APS1; changes the subcellular localization and in addition disrupts the transactivating capacity of the wild-type AIRE; acts with a dominant negative effect by binding to the wild-type AIRE thus preventing the protein from forming the complexes needed for transactivation. 3 PublicationsCorresponds to variant dbSNP:rs121434257EnsemblClinVar.1
Natural variantiVAR_026484252P → L in APS1. 1 PublicationCorresponds to variant dbSNP:rs34397615EnsemblClinVar.1
Natural variantiVAR_005006278S → R3 PublicationsCorresponds to variant dbSNP:rs1800520EnsemblClinVar.1
Natural variantiVAR_076940298E → K Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763636007EnsemblClinVar.1
Natural variantiVAR_076941299C → W Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs751066946Ensembl.1
Natural variantiVAR_013721301V → M in APS1; no effect on protein structure or on interaction with histone H3; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 5 PublicationsCorresponds to variant dbSNP:rs150634562EnsemblClinVar.1
Natural variantiVAR_076942302C → Y Found in patients with hypothyroidism and organ- and cytokine-specific autoantibodies; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 1 Publication1
Natural variantiVAR_076943303R → Q Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs139808903Ensembl.1
Natural variantiVAR_076944303R → W Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs778929451Ensembl.1
Natural variantiVAR_013722305G → S Found in a patient with pernicious anemia and neuropathy; unknown pathological significance; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 1 Publication1
Natural variantiVAR_076945306G → R Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs754932526Ensembl.1
Natural variantiVAR_076946309I → M Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs74162062Ensembl.1
Natural variantiVAR_013723311C → Y in APS1; impairs zinc binding and folding of the PHD-type 1 zinc finger; dominant-negatif effect on the regulation of target gene transcription; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 7 PublicationsCorresponds to variant dbSNP:rs386833674EnsemblClinVar.1
Natural variantiVAR_076947316R → Q Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs202027254Ensembl.1
Natural variantiVAR_076948316R → W Unknown pathological significance; found in a patient with pernicious anemia. 1 PublicationCorresponds to variant dbSNP:rs139874934Ensembl.1
Natural variantiVAR_076949319H → P Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776951380Ensembl.1
Natural variantiVAR_026485326P → L in APS1; no significant effect on structure, but may alter protein interactions; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 3 PublicationsCorresponds to variant dbSNP:rs179363885EnsemblClinVar.1
Natural variantiVAR_013724326P → Q in APS1; alters folding of the PHD-type 1 zinc finger. 5 PublicationsCorresponds to variant dbSNP:rs179363885EnsemblClinVar.1
Natural variantiVAR_076950328R → Q Found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; no effect on doted nuclear localization; dominant-negatif effect on regulation of target gene transcription. 1 PublicationCorresponds to variant dbSNP:rs775921321Ensembl.1
Natural variantiVAR_076951328R → W Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs74162063Ensembl.1
Natural variantiVAR_076952332S → R Unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766901260Ensembl.1
Natural variantiVAR_076953484V → A Found in a patient with acrofacial vitiligo and gastric parietal cell autoantibodies; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs769470638Ensembl.1
Natural variantiVAR_026486539P → L in APS1. 1 PublicationCorresponds to variant dbSNP:rs179363889EnsemblClinVar.1

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_0040891 – 292MATDA…DPQLH → MWLVYSSGAPGTQQPARNRV FFPIGMAPGGVCWRPDGWGT GGQGRISGPGSMGAGQRLGS SGTQRCCWGSCFGKEVALRR VLHPS in isoform 2, isoform 3 and isoform 4. 2 PublicationsAdd BLAST292
Alternative sequenceiVSP_043529293Q → PVCMGVSCLCQ in isoform 4. 1 Publication1
Alternative sequenceiVSP_004090377 – 545VRGPP…APFPS → PRCQGWTPRPCTPYCVWVLR VSRTWLLVRVAGCAEMVRTC CGVLTAPLPSTGAATSQPAP PGPGRACAADPAQET in isoform 3. 1 PublicationAdd BLAST169

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB006682 mRNA Translation: BAA23988.1
AB006683 mRNA Translation: BAA23989.1
AB006684 Genomic DNA Translation: BAA23990.1
AB006684 Genomic DNA Translation: BAA23991.1
AB006684 Genomic DNA Translation: BAA23992.1
AB006685 mRNA Translation: BAA23993.1
Z97990 mRNA Translation: CAB10790.1
AJ009610 Genomic DNA Translation: CAA08759.1
AP001754 Genomic DNA Translation: BAA95560.1
AP001060 Genomic DNA No translation available.
CH471079 Genomic DNA Translation: EAX09443.1
BC137268 mRNA Translation: AAI37269.1
BC137270 mRNA Translation: AAI37271.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13706.1 [O43918-1]

NCBI Reference Sequences

More...
RefSeqi
NP_000374.1, NM_000383.3 [O43918-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.129829

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000291582; ENSP00000291582; ENSG00000160224 [O43918-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
326

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:326

UCSC genome browser

More...
UCSCi
uc002zei.4 human [O43918-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

AIREbase

AIRE mutation db

Mendelian genes autoimmune regulator (AIRE)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006682 mRNA Translation: BAA23988.1
AB006683 mRNA Translation: BAA23989.1
AB006684 Genomic DNA Translation: BAA23990.1
AB006684 Genomic DNA Translation: BAA23991.1
AB006684 Genomic DNA Translation: BAA23992.1
AB006685 mRNA Translation: BAA23993.1
Z97990 mRNA Translation: CAB10790.1
AJ009610 Genomic DNA Translation: CAA08759.1
AP001754 Genomic DNA Translation: BAA95560.1
AP001060 Genomic DNA No translation available.
CH471079 Genomic DNA Translation: EAX09443.1
BC137268 mRNA Translation: AAI37269.1
BC137270 mRNA Translation: AAI37271.1
CCDSiCCDS13706.1 [O43918-1]
RefSeqiNP_000374.1, NM_000383.3 [O43918-1]
UniGeneiHs.129829

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XWHNMR-A293-354[»]
2KE1NMR-A293-354[»]
2KFTNMR-A294-347[»]
2LRINMR-C423-485[»]
ProteinModelPortaliO43918
SMRiO43918
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106823, 93 interactors
CORUMiO43918
DIPiDIP-47504N
IntActiO43918, 32 interactors
MINTiO43918
STRINGi9606.ENSP00000291582

PTM databases

iPTMnetiO43918
PhosphoSitePlusiO43918

Polymorphism and mutation databases

BioMutaiAIRE

Proteomic databases

EPDiO43918
PaxDbiO43918
PeptideAtlasiO43918
PRIDEiO43918
ProteomicsDBi49233
49234 [O43918-2]
49235 [O43918-3]
49236 [O43918-4]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291582; ENSP00000291582; ENSG00000160224 [O43918-1]
GeneIDi326
KEGGihsa:326
UCSCiuc002zei.4 human [O43918-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
326
DisGeNETi326
EuPathDBiHostDB:ENSG00000160224.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
AIRE
HGNCiHGNC:360 AIRE
HPAiHPA038267
MalaCardsiAIRE
MIMi109100 phenotype
240300 phenotype
607358 gene
neXtProtiNX_O43918
OpenTargetsiENSG00000160224
Orphaneti3453 Autoimmune polyendocrinopathy type 1
189466 Familial isolated hypoparathyroidism due to impaired PTH secretion
PharmGKBiPA24654

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IRE7 Eukaryota
ENOG410XQQA LUCA
GeneTreeiENSGT00940000161104
HOGENOMiHOG000033872
HOVERGENiHBG014961
InParanoidiO43918
KOiK10603
OMAiLLSEHTF
OrthoDBiEOG091G055U
PhylomeDBiO43918
TreeFamiTF336193

Enzyme and pathway databases

SIGNORiO43918

Miscellaneous databases

EvolutionaryTraceiO43918

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Autoimmune_regulator

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
326

Protein Ontology

More...
PROi
PR:O43918

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000160224 Expressed in 88 organ(s), highest expression level in amniotic fluid
CleanExiHS_AIRE
GenevisibleiO43918 HS

Family and domain databases

Gene3Di3.10.390.10, 1 hit
3.30.40.10, 2 hits
InterProiView protein in InterPro
IPR008087 AIRE
IPR004865 HSR_dom
IPR010919 SAND-like_dom_sf
IPR000770 SAND_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF03172 HSR, 1 hit
PF00628 PHD, 1 hit
PF01342 SAND, 1 hit
PRINTSiPR01711 AIREGULATOR
SMARTiView protein in SMART
SM00249 PHD, 2 hits
SM00258 SAND, 1 hit
SUPFAMiSSF57903 SSF57903, 2 hits
SSF63763 SSF63763, 1 hit
PROSITEiView protein in PROSITE
PS51414 HSR, 1 hit
PS50864 SAND, 1 hit
PS01359 ZF_PHD_1, 2 hits
PS50016 ZF_PHD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiAIRE_HUMAN
<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: O43918
Secondary accession number(s): B2RP50
, O43922, O43932, O75745
<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: July 15, 1998
Last sequence update: June 1, 1998
Last modified: December 5, 2018
This is version 198 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human chromosome 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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