ADAR
entrez
103
canonical
uniprot
P55265
canonical
ensembl
ENSG00000160710
resolver
ensp
ENSP00000357456
resolver
ensp
ENSP00000357459
resolver
ensp
ENSP00000431794
resolver
ensp
ENSP00000497210
resolver
ensp
ENSP00000497555
resolver
ensp
ENSP00000497932
resolver
ensp
ENSP00000506666
resolver
ensp
ENSP00000518929
resolver
ensp
ENSP00000518934
resolver
ensp
ENSP00000591245
resolver
ensp
ENSP00000743791
resolver
enst
ENST00000526905
resolver
genesymbol
ADAR
resolver
genesymbol_syn
ADAR1
resolver
genesymbol_syn
DSRAD
resolver
genesymbol_syn
G1P1
resolver
genesymbol_syn
IFI4
resolver
hgnc
HGNC:225
resolver
uniprot
A0AAQ5BGH8
resolver
uniprot
B1AQQ9
resolver
uniprot
B1AQR0
resolver
uniprot
D3DV76
resolver
uniprot
O15223
resolver
uniprot
O43859
resolver
uniprot
O43860
resolver
uniprot
Q9BYM3
resolver
uniprot
Q9BYM4
resolver
uniprot_entry
A0AAQ5BGH8_HUMAN
resolver
uniprot_entry
DSRAD_HUMAN
resolver
uniprot_sec
B1AQQ9
resolver
uniprot_sec
B1AQR0
resolver
uniprot_sec
D3DV76
resolver
uniprot_sec
O15223
resolver
uniprot_sec
O43859
resolver
uniprot_sec
O43860
resolver
uniprot_sec
Q9BYM3
resolver
uniprot_sec
Q9BYM4
resolver
amino_acid_sequence
MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVSTQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSAQAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIKEKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNASNNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFENGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQTPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISESLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIAMLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFKKGLKDMGYGNWISKPQEEKNFYLCPV
uniprot
proteins
disease_involvement
DISEASE: Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]: An autosomal dominant pigmentary genodermatosis characterized by a mixture of hyperpigmented and hypopigmented macules distributed on the face and the dorsal parts of the hands and feet, that appear in infancy or early childhood. {ECO:0000269|PubMed:12916015, ECO:0000269|PubMed:15146470, ECO:0000269|PubMed:15659327}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood. {ECO:0000269|PubMed:23001123}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.4.37
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:12618436, PubMed:7565688, PubMed:7972084). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication. {ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:15556947, ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16120648, ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874, ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260, ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222, ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}.
uniprot
proteins
mass_dalton
136066
uniprot
proteins
mutagenesis
MUTAGEN 418; /note="K->R: Abolishes sumoylation."; /evidence="ECO:0000269|PubMed:16120648"; MUTAGEN 708..801; /note="Missing: Abolishes nuclear location."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 708..710; /note="MMP->AMA: Decreased nuclear and partially cytoplasmic location."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 712..715; /note="KVRK->AVAA: No effect on nuclear location. No effect on RNA binding."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 716..724; /note="Missing: Disrupts the bi-partite nuclear localization signal and abolishes nuclear location."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 716; /note="I->N: Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with S-719 and N-723."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 718; /note="E->A: No effect on nuclear location; when associated with A-721 and A-724."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 719; /note="L->S: Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and N-723."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 721; /note="R->A: No effect on nuclear location; when associated with A-721 and A-724."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 723; /note="L->N: Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and S-719."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 724; /note="N->A: No effect on nuclear location; when associated with A-718 and A-721."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 725..801; /note="Missing: Disrupts nuclear localization signal. No effect on RNA binding."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 777..778; /note="KK->AA: Strongly impaired RNA binding. No effect on nuclear location."; /evidence="ECO:0000269|PubMed:24753571"; MUTAGEN 801; /note="R->A: Abolishes interaction with TNPO1, TNPO1-mediated nuclear import and nuclear location."; /evidence="ECO:0000269|PubMed:24753571
uniprot
proteins
post_translational_modification
PTM: Sumoylation reduces RNA-editing activity. {ECO:0000269|PubMed:16120648}.
uniprot
proteins
pubmed
10200312
uniprot
proteins
pubmed
10364558
uniprot
proteins
pubmed
10535945
uniprot
proteins
pubmed
12618436
uniprot
proteins
pubmed
12665561
uniprot
proteins
pubmed
12916015
uniprot
proteins
pubmed
15146470
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15556947
uniprot
proteins
pubmed
15659327
uniprot
proteins
pubmed
15858013
uniprot
proteins
pubmed
16055709
uniprot
proteins
pubmed
16120648
uniprot
proteins
pubmed
16237447
uniprot
proteins
pubmed
16475990
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17079286
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18178553
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18362360
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19124606
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19605474
uniprot
proteins
pubmed
19651874
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19710021
uniprot
proteins
pubmed
19908260
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20192758
uniprot
proteins
pubmed
21182352
uniprot
proteins
pubmed
21211811
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21289159
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21490091
uniprot
proteins
pubmed
21769729
uniprot
proteins
pubmed
22022963
uniprot
proteins
pubmed
22113393
uniprot
proteins
pubmed
22278222
uniprot
proteins
pubmed
22988838
uniprot
proteins
pubmed
23001123
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24753571
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
7565688
uniprot
proteins
pubmed
7972084
uniprot
proteins
pubmed
9020165
uniprot
proteins
sequence_length
1226
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:7565688}. Nucleus {ECO:0000269|PubMed:24753571, ECO:0000269|PubMed:7565688}. Note=Shuttles between the cytoplasm and nucleus (PubMed:24753571, PubMed:7565688). Nuclear import is mediated by TNPO1 (PubMed:24753571). {ECO:0000269|PubMed:24753571, ECO:0000269|PubMed:7565688}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:19124606}. Nucleus {ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:7565688}. Nucleus, nucleolus {ECO:0000269|PubMed:12665561}. Note=Predominantly nuclear but can shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear import whereas XPO5 can mediate its nuclear export. {ECO:0000269|PubMed:19124606}.
uniprot
proteins