Arnt
entrez
11863
canonical
uniprot
P53762
canonical
ensembl
ENSMUSG00000015522
resolver
ensp
ENSMUSP00000088313
resolver
ensp
ENSMUSP00000099810
resolver
ensp
ENSMUSP00000102779
resolver
ensp
ENSMUSP00000308501
resolver
ensp
ENSMUSP00000308504
resolver
ensp
ENSMUSP00000308511
resolver
ensp
ENSMUSP00000308523
resolver
enst
ENSMUST00000090804
resolver
enst
ENSMUST00000107161
resolver
genesymbol
Arnt
resolver
uniprot
F6ZFW9
resolver
uniprot
F7D8F0
resolver
uniprot
Q3ULM2
resolver
uniprot
Q60661
resolver
uniprot
Q8CEC2
resolver
uniprot
Q921F3
resolver
uniprot_entry
ARNT_MOUSE
resolver
uniprot_entry
F6ZFW9_MOUSE
resolver
uniprot_entry
F7D8F0_MOUSE
resolver
uniprot_entry
Q3ULM2_MOUSE
resolver
uniprot_entry
Q8CEC2_MOUSE
resolver
uniprot_sec
Q60661
resolver
uniprot_sec
Q921F3
resolver
amino_acid_sequence
MAATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEVEVNTKFLRCDDDQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIPRSQLGPTANLSLEMGTGQLPSRQQQQQHTELDMVPGRDGLASYNHSQVSVQPVASAGSEHSKPLEKSEGLFAQDRDPRFPEIYPSITADQSKGISSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNPAQGSAPTWTSSSRPGFAAQQVPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASSGTAAYPALPNRGSNFPPETGQTTGQFQARTAEGVGVWPQWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE
uniprot
proteins
function
FUNCTION: Transcription factor that functions as an obligate heterodimerization partner for several basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) proteins. Forms heterodimers with the aryl hydrocarbon receptor (AHR) to mediate the transcriptional response to xenobiotics by binding xenobiotic response elements (XREs) or dioxin response elements (DREs) in target gene promoters (PubMed:28602820). Also heterodimerizes with hypoxia-inducible factor alpha subunits (HIF1A, EPAS1, NPAS1 or NPAS3) to form hypoxia-inducible transcription factors that bind hypoxia response elements (HREs) and activate genes involved in cellular and systemic responses to hypoxia, including angiogenesis, erythropoiesis, and metabolic adaptation (PubMed:26245371, PubMed:27782878). Plays a central role in environmental sensing and developmental and physiological regulation of gene expression (By similarity). {ECO:0000250|UniProtKB:P27540, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878, ECO:0000269|PubMed:28602820}.
uniprot
proteins
mass_dalton
86963
uniprot
proteins
mutagenesis
MUTAGEN 94; /note="H->A: Reduces DNA binding."; /evidence="ECO:0000269|PubMed:26245371"; MUTAGEN 98; /note="E->A: Reduces DNA binding."; /evidence="ECO:0000269|PubMed:26245371"; MUTAGEN 102; /note="R->E: Reduces DNA binding. Decreases transcription factor activity."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:28602820"; MUTAGEN 112; /note="L->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 112; /note="L->E: Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 132; /note="L->E: Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 136; /note="V->D: Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 139; /note="M->D: Interferes with transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 164; /note="L->D: Does not affect transcription factor activity."; /evidence="ECO:0000269|PubMed:28602820"; MUTAGEN 167; /note="L->E: Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 168; /note="I->D: Highly reduces transcription activity. Impairs interaction with AHR. Impairs heterodimer formation with EPAS1. Impairs heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 171; /note="A->D: Reduces transcription activity. Markedly reduces interaction with AHR. Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Compromise NPAS4:ARNT heterodimer stability. Compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:24001774, ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 264; /note="I->D: Impairs heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 266; /note="R->A: Markedly decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 305; /note="V->D: Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 307; /note="H->A: Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 366; /note="R->A: Markedly decreases heterodimer formation with EPAS1. Markedly decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with N-448. Impairs heterodimer formation with HIF1A; when associated with N-448. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 448; /note="N->A: Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Impairs heterodimer formation with EPAS1; when associated with A-366. Impairs heterodimer formation with HIF1A; when associated with A-366. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878"; MUTAGEN 456; /note="Y->D: Decreases heterodimer formation with EPAS1. Decreases heterodimer formation with HIF1A. Significantly destabilizes ARNT?s heterodimeric interactions with both NPAS1 and NPAS3. Compromises SIM1:ARNT heterodimer stability. Does not compromise NPAS4:ARNT heterodimer stability. Does not compromise AHR:ARNT heterodimer stability."; /evidence="ECO:0000269|PubMed:26245371, ECO:0000269|PubMed:27782878
uniprot
proteins
pubmed
11025203
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24001774
uniprot
proteins
pubmed
26245371
uniprot
proteins
pubmed
27782878
uniprot
proteins
pubmed
28602820
uniprot
proteins
pubmed
7961746
uniprot
proteins
pubmed
8065341
uniprot
proteins
pubmed
9887096
uniprot
proteins
sequence_length
791
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27540}.
uniprot
proteins