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Autoimmune regulator (Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein homolog) (APECED protein homolog)

 AIRE_MOUSE              Reviewed;         552 AA.
Q9Z0E3; Q9JLW0; Q9JLW1; Q9JLW2; Q9JLW3; Q9JLW4; Q9JLW5; Q9JLW6;
Q9JLW7; Q9JLW8; Q9JLW9; Q9JLX0;
13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 148.
RecName: Full=Autoimmune regulator;
AltName: Full=Autoimmune polyendocrinopathy candidiasis ectodermal dystrophy protein homolog;
Short=APECED protein homolog;
Name=Aire;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1A).
PubMed=10593569; DOI=10.3109/08916939908993859;
Shi J.-D., Wang C.-Y., Marron M.P., Ruan Q.-G., Huang Y.Q.,
Detter J.C., She J.-X.;
"Chromosomal localization and complete genomic sequence of the murine
autoimmune regulator gene (Aire).";
Autoimmunity 31:47-53(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1A).
STRAIN=129/Sv;
PubMed=10049735; DOI=10.1006/bbrc.1999.0223;
Mittaz L., Rossier C., Heino M., Petersen P., Krohn K.J.E., Gos A.,
Morris M.A., Kudoh J., Shimizu N., Antonarakis S.E., Scott H.S.;
"Isolation and characterization of the mouse Aire gene.";
Biochem. Biophys. Res. Commun. 255:483-490(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=10049587; DOI=10.1006/geno.1998.5656;
Wang C.-Y., Shi J.-D., Davoodi-Semiromi A., She J.-X.;
"Cloning of Aire, the mouse homologue of the autoimmune regulator
(AIRE) gene responsible for autoimmune polyglandular syndrome type 1
(ASP1).";
Genomics 55:322-326(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
STRAIN=129;
PubMed=10022980;
Blechschmidt K., Schweiger M., Wertz K., Poulson R.,
Christensen H.-M., Rosenthal A., Lehrach H., Yaspo M.-L.;
"The mouse Aire gene: comparative genomic sequencing, gene
organization, and expression.";
Genome Res. 9:158-166(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 2A; 2B; 2C; 2D;
3A; 3B; 3C AND 3D).
STRAIN=C57BL/6J, NOD, and SJL/J;
PubMed=10550218; DOI=10.1006/jaut.1999.0326;
Ruan Q.-G., Wang C.-Y., Shi J.-D., She J.-X.;
"Expression and alternative splicing of the mouse autoimmune regulator
gene (Aire).";
J. Autoimmun. 13:307-313(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND SUBCELLULAR LOCATION.
TISSUE=Kidney, and Thymus;
PubMed=11156688; DOI=10.1177/002215540104900207;
Halonen M., Pelto-Huikko M., Eskelin P., Peltonen L., Ulmanen I.,
Kolmer M.;
"Subcellular location and expression pattern of autoimmune regulator
(Aire), the mouse orthologue for human gene defective in autoimmune
polyendocrinopathy candidiasis ectodermal dystrophy (APECED).";
J. Histochem. Cytochem. 49:197-208(2001).
[7]
SUBUNIT STRUCTURE, AND PHOSPHORYLATION.
PubMed=11533054; DOI=10.1074/jbc.M104898200;
Kumar P.G., Laloraya M., Wang C.-Y., Ruan Q.-G., Davoodi-Semiromi A.,
Kao K.-J., She J.-X.;
"The autoimmune regulator (AIRE) is a DNA-binding protein.";
J. Biol. Chem. 276:41357-41364(2001).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=19015306; DOI=10.1084/jem.20080046;
Yano M., Kuroda N., Han H., Meguro-Horike M., Nishikawa Y.,
Kiyonari H., Maemura K., Yanagawa Y., Obata K., Takahashi S.,
Ikawa T., Satoh R., Kawamoto H., Mouri Y., Matsumoto M.;
"Aire controls the differentiation program of thymic epithelial cells
in the medulla for the establishment of self-tolerance.";
J. Exp. Med. 205:2827-2838(2008).
[9]
FUNCTION, INTERACTION WITH THE N-TERMINUS OF UNMODIFIED HISTONE H3,
INTERACTION WITH NUCLEOSOMES, DNA-BINDING, AND MUTAGENESIS OF ASP-299;
VAL-303; CYS-312; CYS-313 AND PRO-328.
PubMed=18840680; DOI=10.1073/pnas.0808470105;
Koh A.S., Kuo A.J., Park S.Y., Cheung P., Abramson J., Bua D.,
Carney D., Shoelson S.E., Gozani O., Kingston R.E., Benoist C.,
Mathis D.;
"Aire employs a histone-binding module to mediate immunological
tolerance, linking chromatin regulation with organ-specific
autoimmunity.";
Proc. Natl. Acad. Sci. U.S.A. 105:15878-15883(2008).
[10]
REVIEW OF FUNCTION IN SELF-TOLERANCE.
PubMed=19302042; DOI=10.1146/annurev.immunol.25.022106.141532;
Mathis D., Benoist C.;
"Aire.";
Annu. Rev. Immunol. 27:287-312(2009).
[11]
FUNCTION.
PubMed=19923453; DOI=10.4049/jimmunol.0804133;
Laan M., Kisand K., Kont V., Moell K., Tserel L., Scott H.S.,
Peterson P.;
"Autoimmune regulator deficiency results in decreased expression of
CCR4 and CCR7 ligands and in delayed migration of CD4+ thymocytes.";
J. Immunol. 183:7682-7691(2009).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=21300913; DOI=10.1084/jem.20102327;
Lei Y., Ripen A.M., Ishimaru N., Ohigashi I., Nagasawa T., Jeker L.T.,
Boesl M.R., Hollaender G.A., Hayashi Y., Malefyt R.W., Nitta T.,
Takahama Y.;
"Aire-dependent production of XCL1 mediates medullary accumulation of
thymic dendritic cells and contributes to regulatory T cell
development.";
J. Exp. Med. 208:383-394(2011).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=23993652; DOI=10.1016/j.immuni.2013.08.005;
Gardner J.M., Metzger T.C., McMahon E.J., Au-Yeung B.B., Krawisz A.K.,
Lu W., Price J.D., Johannes K.P., Satpathy A.T., Murphy K.M.,
Tarbell K.V., Weiss A., Anderson M.S.;
"Extrathymic Aire-expressing cells are a distinct bone marrow-derived
population that induce functional inactivation of CD4[?] T cells.";
Immunity 39:560-572(2013).
[14]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=26070482; DOI=10.1016/j.immuni.2015.05.013;
Yamano T., Nedjic J., Hinterberger M., Steinert M., Koser S.,
Pinto S., Gerdes N., Lutgens E., Ishimaru N., Busslinger M., Brors B.,
Kyewski B., Klein L.;
"Thymic B Cells Are Licensed to Present Self Antigens for Central T
Cell Tolerance Induction.";
Immunity 42:1048-1061(2015).
-!- FUNCTION: 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) (Probable).
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 (By
similarity). Also induces self-tolerance through other mechanisms
such as the regulation of the mTEC differentiation program
(PubMed:19015306). Controls the medullary accumulation of thymic
dendritic cells and the development of regulatory T-cell through
the regulation of XCL1 expression (PubMed:21300913). Regulates the
production of CCR4 and CCR7 ligands in medullary thymic epithelial
cells and alters the coordinated maturation and migration of
thymocytes (PubMed:19923453). In thimic B-cells, allows the
presentation of licensing-dependent endogenous self-anitgen for
negative selection (PubMed:26070482). 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
(PubMed:23993652). {ECO:0000250|UniProtKB:O43918,
ECO:0000269|PubMed:19015306, ECO:0000269|PubMed:19923453,
ECO:0000269|PubMed:21300913, ECO:0000269|PubMed:23993652,
ECO:0000269|PubMed:26070482, ECO:0000305|PubMed:19302042}.
-!- SUBUNIT: 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
(By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-80858, EBI-80858;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00185, ECO:0000255|PROSITE-ProRule:PRU00747,
ECO:0000269|PubMed:11156688, ECO:0000269|PubMed:19015306,
ECO:0000269|PubMed:26070482}. Cytoplasm
{ECO:0000269|PubMed:11156688}. Note=Predominantly nuclear but also
cytoplasmic. Found in nuclear body-like structures (dots) and in a
filamentous vimentin-like pattern. {ECO:0000250|UniProtKB:O43918,
ECO:0000269|PubMed:19015306}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Comment=Additional isoforms seem to exist.;
Name=1a;
IsoId=Q9Z0E3-1; Sequence=Displayed;
Name=1b;
IsoId=Q9Z0E3-2; Sequence=VSP_004092;
Name=1c;
IsoId=Q9Z0E3-3; Sequence=VSP_004091;
Name=1d;
IsoId=Q9Z0E3-4; Sequence=VSP_004091, VSP_004092;
Name=2a;
IsoId=Q9Z0E3-5; Sequence=VSP_004093;
Name=2b;
IsoId=Q9Z0E3-6; Sequence=VSP_004092, VSP_004093;
Name=2c;
IsoId=Q9Z0E3-7; Sequence=VSP_004091, VSP_004093;
Name=2d;
IsoId=Q9Z0E3-8; Sequence=VSP_004091, VSP_004092, VSP_004093;
Name=3a;
IsoId=Q9Z0E3-9; Sequence=VSP_004094, VSP_004095;
Note=Probably inactive.;
Name=3b;
IsoId=Q9Z0E3-10; Sequence=VSP_004092, VSP_004094, VSP_004095;
Note=Probably inactive.;
Name=3c;
IsoId=Q9Z0E3-11; Sequence=VSP_004091, VSP_004094, VSP_004095;
Note=Probably inactive.;
Name=3d;
IsoId=Q9Z0E3-12; Sequence=VSP_004091, VSP_004092, VSP_004094,
VSP_004095;
Note=Probably inactive.;
-!- TISSUE SPECIFICITY: Highly expressed in a few cells in the medulla
of the thymus (medullary epithelial cells) (at protein level)
(PubMed:23993652). Expressed in thymic but no peripheral B-cells
(PubMed:26070482). 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). Detected at very low
levels in thymus, lymph node, liver, brain, ovary, lung, testis,
kidney, heart, spleen, bone marrow, skeletal muscle and adrenal
gland. Isoforms 1a to 1d predominate, isoforms 2a to 2d are
intermediate and isoforms 3a to 3d are expressed at extremely low
levels. {ECO:0000269|PubMed:23993652,
ECO:0000269|PubMed:26070482}.
-!- DEVELOPMENTAL STAGE: In the thymus, not expressed at E13.5 but
present at E16.5 and postnatal day 1.
{ECO:0000269|PubMed:19015306}.
-!- DOMAIN: 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 (By similarity).
{ECO:0000250}.
-!- DOMAIN: The L-X-X-L-L repeats may be implicated in binding to
nuclear receptors.
-!- DOMAIN: The N-terminal HSR domain is required for localization on
tubular structures. {ECO:0000250}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:11533054}.
-!- DISRUPTION PHENOTYPE: Deficient mice show an altered thymic
organization with altered morphology and location of mTECs
(PubMed:19015306). They exhibit defective accumulation of thymic
dendritic cells in the medullary region and generation of
naturally ocurring T cells in the thymus (PubMed:21300913).
{ECO:0000269|PubMed:19015306, ECO:0000269|PubMed:21300913}.
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EMBL; AF105002; AAD46421.1; -; Genomic_DNA.
EMBL; AF128772; AAF36481.1; -; mRNA.
EMBL; AF128773; AAF36482.1; -; mRNA.
EMBL; AJ007715; CAA07620.1; -; Genomic_DNA.
EMBL; AF079536; AAD20444.1; -; mRNA.
EMBL; AJ132243; CAB36909.1; -; mRNA.
EMBL; AF128115; AAF36460.1; -; mRNA.
EMBL; AF128116; AAF36461.1; -; mRNA.
EMBL; AF128117; AAF36462.1; -; mRNA.
EMBL; AF128118; AAF36463.1; -; mRNA.
EMBL; AF128119; AAF36464.1; -; mRNA.
EMBL; AF128120; AAF36465.1; -; mRNA.
EMBL; AF128121; AAF36466.1; -; mRNA.
EMBL; AF128122; AAF36467.1; -; mRNA.
EMBL; AF128123; AAF36468.1; -; mRNA.
EMBL; AF128124; AAF36469.1; -; mRNA.
EMBL; AF128125; AAF36470.1; -; mRNA.
EMBL; AJ243821; CAB66141.1; -; mRNA.
CCDS; CCDS23961.1; -. [Q9Z0E3-1]
CCDS; CCDS70051.1; -. [Q9Z0E3-10]
CCDS; CCDS70052.1; -. [Q9Z0E3-6]
CCDS; CCDS70053.1; -. [Q9Z0E3-2]
CCDS; CCDS70054.1; -. [Q9Z0E3-9]
CCDS; CCDS70055.1; -. [Q9Z0E3-5]
CCDS; CCDS70056.1; -. [Q9Z0E3-12]
CCDS; CCDS70057.1; -. [Q9Z0E3-8]
CCDS; CCDS70058.1; -. [Q9Z0E3-4]
CCDS; CCDS70059.1; -. [Q9Z0E3-11]
CCDS; CCDS70060.1; -. [Q9Z0E3-3]
RefSeq; NP_001258478.1; NM_001271549.1. [Q9Z0E3-2]
RefSeq; NP_001258479.1; NM_001271550.1. [Q9Z0E3-3]
RefSeq; NP_001258480.1; NM_001271551.1. [Q9Z0E3-4]
RefSeq; NP_001258481.1; NM_001271552.1. [Q9Z0E3-5]
RefSeq; NP_001258482.1; NM_001271553.1. [Q9Z0E3-6]
RefSeq; NP_001258483.1; NM_001271554.1. [Q9Z0E3-7]
RefSeq; NP_001258484.1; NM_001271555.1. [Q9Z0E3-8]
RefSeq; NP_001258485.1; NM_001271556.1. [Q9Z0E3-9]
RefSeq; NP_001258486.1; NM_001271557.1. [Q9Z0E3-10]
RefSeq; NP_001258487.1; NM_001271558.1. [Q9Z0E3-11]
RefSeq; NP_001258488.1; NM_001271559.1. [Q9Z0E3-12]
RefSeq; NP_033776.1; NM_009646.2. [Q9Z0E3-1]
UniGene; Mm.35300; -.
ProteinModelPortal; Q9Z0E3; -.
DIP; DIP-31030N; -.
IntAct; Q9Z0E3; 90.
STRING; 10090.ENSMUSP00000114904; -.
iPTMnet; Q9Z0E3; -.
PhosphoSitePlus; Q9Z0E3; -.
PaxDb; Q9Z0E3; -.
PRIDE; Q9Z0E3; -.
Ensembl; ENSMUST00000019257; ENSMUSP00000019257; ENSMUSG00000000731. [Q9Z0E3-2]
Ensembl; ENSMUST00000105395; ENSMUSP00000101034; ENSMUSG00000000731. [Q9Z0E3-9]
Ensembl; ENSMUST00000105396; ENSMUSP00000101035; ENSMUSG00000000731. [Q9Z0E3-6]
Ensembl; ENSMUST00000128241; ENSMUSP00000114904; ENSMUSG00000000731. [Q9Z0E3-1]
Ensembl; ENSMUST00000130972; ENSMUSP00000122659; ENSMUSG00000000731. [Q9Z0E3-4]
Ensembl; ENSMUST00000140636; ENSMUSP00000121477; ENSMUSG00000000731. [Q9Z0E3-12]
Ensembl; ENSMUST00000145975; ENSMUSP00000120150; ENSMUSG00000000731. [Q9Z0E3-3]
Ensembl; ENSMUST00000148469; ENSMUSP00000118317; ENSMUSG00000000731. [Q9Z0E3-11]
Ensembl; ENSMUST00000154374; ENSMUSP00000117094; ENSMUSG00000000731. [Q9Z0E3-5]
Ensembl; ENSMUST00000155021; ENSMUSP00000122190; ENSMUSG00000000731. [Q9Z0E3-8]
Ensembl; ENSMUST00000156417; ENSMUSP00000115162; ENSMUSG00000000731. [Q9Z0E3-10]
GeneID; 11634; -.
KEGG; mmu:11634; -.
UCSC; uc007fwr.2; mouse. [Q9Z0E3-1]
UCSC; uc007fws.2; mouse. [Q9Z0E3-4]
UCSC; uc007fwt.2; mouse. [Q9Z0E3-10]
UCSC; uc007fwu.2; mouse. [Q9Z0E3-6]
UCSC; uc007fwv.2; mouse. [Q9Z0E3-12]
UCSC; uc007fww.2; mouse. [Q9Z0E3-8]
UCSC; uc007fwx.2; mouse. [Q9Z0E3-3]
UCSC; uc007fwz.2; mouse. [Q9Z0E3-9]
UCSC; uc007fxa.2; mouse. [Q9Z0E3-11]
UCSC; uc007fxb.2; mouse. [Q9Z0E3-7]
CTD; 326; -.
MGI; MGI:1338803; Aire.
eggNOG; ENOG410IRE7; Eukaryota.
eggNOG; ENOG410XQQA; LUCA.
GeneTree; ENSGT00920000149099; -.
HOVERGEN; HBG014961; -.
InParanoid; Q9Z0E3; -.
KO; K10603; -.
OMA; LLSEHTF; -.
OrthoDB; EOG091G055U; -.
PhylomeDB; Q9Z0E3; -.
TreeFam; TF336193; -.
ChiTaRS; Aire; mouse.
PRO; PR:Q9Z0E3; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000000731; Expressed in 79 organ(s), highest expression level in vestibular labyrinth.
ExpressionAtlas; Q9Z0E3; baseline and differential.
Genevisible; Q9Z0E3; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045182; F:translation regulator activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0002509; P:central tolerance induction to self antigen; ISS:UniProtKB.
GO; GO:0032602; P:chemokine production; IMP:UniProtKB.
GO; GO:0006959; P:humoral immune response; IMP:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IGI:MGI.
GO; GO:0002458; P:peripheral T cell tolerance induction; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:2000410; P:regulation of thymocyte migration; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0097536; P:thymus epithelium morphogenesis; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.10.390.10; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR008087; AIRE.
InterPro; IPR004865; HSR_dom.
InterPro; IPR010919; SAND-like_dom_sf.
InterPro; IPR000770; SAND_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF03172; HSR; 1.
Pfam; PF00628; PHD; 1.
Pfam; PF01342; SAND; 1.
PRINTS; PR01711; AIREGULATOR.
SMART; SM00249; PHD; 2.
SMART; SM00258; SAND; 1.
SUPFAM; SSF57903; SSF57903; 2.
SUPFAM; SSF63763; SSF63763; 1.
PROSITE; PS51414; HSR; 1.
PROSITE; PS50864; SAND; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Zinc; Zinc-finger.
CHAIN 1 552 Autoimmune regulator.
/FTId=PRO_0000064514.
DOMAIN 1 106 HSR. {ECO:0000255|PROSITE-
ProRule:PRU00747}.
DOMAIN 182 282 SAND. {ECO:0000255|PROSITE-
ProRule:PRU00185}.
ZN_FING 298 345 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 434 475 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
MOTIF 8 12 LXXLL motif 1.
MOTIF 64 68 LXXLL motif 2.
MOTIF 114 134 Nuclear localization signal.
{ECO:0000255}.
MOTIF 414 418 LXXLL motif 3.
MOTIF 520 524 LXXLL motif 4.
VAR_SEQ 265 268 Missing (in isoform 1c, isoform 1d,
isoform 2c, isoform 2d, isoform 3c and
isoform 3d).
{ECO:0000303|PubMed:10550218}.
/FTId=VSP_004091.
VAR_SEQ 296 296 Missing (in isoform 1b, isoform 1d,
isoform 2b, isoform 2d, isoform 3b and
isoform 3d).
{ECO:0000303|PubMed:10550218}.
/FTId=VSP_004092.
VAR_SEQ 367 425 Missing (in isoform 2a, isoform 2b,
isoform 2c and isoform 2d).
{ECO:0000303|PubMed:10550218}.
/FTId=VSP_004093.
VAR_SEQ 368 409 ILVGLRSASEKTRGPSRELKASSDAAVTYVNLLAPHPAAPL
L -> DQSPLQILLCRLDSHARHTGRSCTHLWAPSSTWACQ
GRGRLC (in isoform 3a, isoform 3b,
isoform 3c and isoform 3d).
{ECO:0000303|PubMed:10550218}.
/FTId=VSP_004094.
VAR_SEQ 410 552 Missing (in isoform 3a, isoform 3b,
isoform 3c and isoform 3d).
{ECO:0000303|PubMed:10550218}.
/FTId=VSP_004095.
MUTAGEN 299 299 D->A: Abolishes interaction with histone
H3. {ECO:0000269|PubMed:18840680}.
MUTAGEN 303 303 V->M: No effect on interaction with
histone H3.
{ECO:0000269|PubMed:18840680}.
MUTAGEN 312 312 C->W: Abolishes interaction with histone
H3. {ECO:0000269|PubMed:18840680}.
MUTAGEN 313 313 C->Y: Abolishes interaction with histone
H3. {ECO:0000269|PubMed:18840680}.
MUTAGEN 328 328 P->L: Reduces interaction with histone
H3. {ECO:0000269|PubMed:18840680}.
SEQUENCE 552 AA; 59042 MW; BF30F8F66B71239A CRC64;
MAGGDGMLRR LLRLHRTEIA VAIDSAFPLL HALADHDVVP EDKFQETLRL KEKEGCPQAF
HALLSWLLTR DSGAILDFWR ILFKDYNLER YSRLHSILDG FPKDVDLNQS RKGRKPLAGP
KAAVLPPRPP TKRKALEEPR ATPPATLASK SVSSPGSHLK TKPPKKPDGN LESQHLPLGN
GIQTMAASVQ RAVTVASGDV PGTRGAVEGI LIQQVFESGR SKKCIQVGGE FYTPNKFEDP
SGNLKNKARS GSSLKPVVRA KGAQVTIPGR DEQKVGQQCG VPPLPSLPSE PQVNQKNEDE
CAVCHDGGEL ICCDGCPRAF HLACLSPPLQ EIPSGLWRCS CCLQGRVQQN LSQPEVSRPP
ELPAETPILV GLRSASEKTR GPSRELKASS DAAVTYVNLL APHPAAPLLE PSALCPLLSA
GNEGRPGPAP SARCSVCGDG TEVLRCAHCA AAFHWRCHFP TAAARPGTNL RCKSCSADST
PTPGTPGEAV PTSGPRPAPG LAKVGDDSAS HDPVLHRDDL ESLLNEHSFD GILQWAIQSM
SRPLAETPPF SS


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