P55265 · DSRAD_HUMAN
- ProteinDouble-stranded RNA-specific adenosine deaminase
- GeneADAR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1226 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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
Catalytic activity
- adenosine in double-stranded RNA + H+ + H2O = inosine in double-stranded RNA + NH4+
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
ADAR1 regulates circular RNA biogenesis bidirectionally by both editing-dependent and -independent manners.
Names & Taxonomy
Protein names
- Recommended nameDouble-stranded RNA-specific adenosine deaminase
- EC number
- Short namesDRADA
- Alternative names
Gene names
- Community suggested namesADAR1
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP55265
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 5
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Dyschromatosis symmetrica hereditaria (DSH)
- Note
- DescriptionAn 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.
- See alsoMIM:127400
Natural variants in DSH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_017604 | 923 | L>P | in DSH; dbSNP:rs28936680 | |
VAR_021729 | 966 | C>F | in DSH | |
VAR_026669 | 1155 | R>W | in DSH; dbSNP:rs1044845711 | |
VAR_017605 | 1165 | F>S | in DSH; dbSNP:rs28936681 |
Aicardi-Goutieres syndrome 6 (AGS6)
- Note
- DescriptionA 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.
- See alsoMIM:615010
Natural variants in AGS6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069535 | 193 | P>A | in AGS6; dbSNP:rs145588689 | |
VAR_069536 | 870 | A>T | in AGS6; dbSNP:rs398122893 | |
VAR_069537 | 872 | I>T | in AGS6; dbSNP:rs398122897 | |
VAR_069538 | 892 | R>H | in AGS6; dbSNP:rs398122892 | |
VAR_069539 | 999 | K>N | in AGS6; dbSNP:rs398122896 | |
VAR_069540 | 1007 | G>R | in AGS6; dbSNP:rs398122822 | |
VAR_069541 | 1112 | Y>F | in AGS6; dbSNP:rs398122895 | |
VAR_069542 | 1113 | D>H | in AGS6; dbSNP:rs398122894 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048725 | 100 | in dbSNP:rs1466731 | |||
Sequence: R → G | ||||||
Natural variant | VAR_069535 | 193 | in AGS6; dbSNP:rs145588689 | |||
Sequence: P → A | ||||||
Natural variant | VAR_017240 | 384 | in dbSNP:rs2229857 | |||
Sequence: K → R | ||||||
Mutagenesis | 418 | Abolishes sumoylation. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_024407 | 587 | in dbSNP:rs17843865 | |||
Sequence: Y → C | ||||||
Mutagenesis | 708-710 | Decreased nuclear and partially cytoplasmic location. | ||||
Sequence: MMP → AMA | ||||||
Mutagenesis | 708-801 | Abolishes nuclear location. | ||||
Sequence: Missing | ||||||
Mutagenesis | 712-715 | No effect on nuclear location. No effect on RNA binding. | ||||
Sequence: KVRK → AVAA | ||||||
Mutagenesis | 716 | Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with S-719 and N-723. | ||||
Sequence: I → N | ||||||
Mutagenesis | 716-724 | Disrupts the bi-partite nuclear localization signal and abolishes nuclear location. | ||||
Sequence: Missing | ||||||
Mutagenesis | 718 | No effect on nuclear location; when associated with A-721 and A-724. | ||||
Sequence: E → A | ||||||
Mutagenesis | 719 | Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and N-723. | ||||
Sequence: L → S | ||||||
Mutagenesis | 721 | No effect on nuclear location; when associated with A-721 and A-724. | ||||
Sequence: R → A | ||||||
Mutagenesis | 723 | Disrupts the bi-partite nuclear localization signal and abolishes nuclear location; when associated with N-716 and S-719. | ||||
Sequence: L → N | ||||||
Mutagenesis | 724 | No effect on nuclear location; when associated with A-718 and A-721. | ||||
Sequence: N → A | ||||||
Mutagenesis | 725-801 | Disrupts nuclear localization signal. No effect on RNA binding. | ||||
Sequence: Missing | ||||||
Mutagenesis | 777-778 | Strongly impaired RNA binding. No effect on nuclear location. | ||||
Sequence: KK → AA | ||||||
Mutagenesis | 801 | Abolishes interaction with TNPO1, TNPO1-mediated nuclear import and nuclear location. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_035805 | 806 | in a breast cancer sample; somatic mutation; dbSNP:rs144119808 | |||
Sequence: E → V | ||||||
Natural variant | VAR_069536 | 870 | in AGS6; dbSNP:rs398122893 | |||
Sequence: A → T | ||||||
Natural variant | VAR_069537 | 872 | in AGS6; dbSNP:rs398122897 | |||
Sequence: I → T | ||||||
Natural variant | VAR_069538 | 892 | in AGS6; dbSNP:rs398122892 | |||
Sequence: R → H | ||||||
Natural variant | VAR_017604 | 923 | in DSH; dbSNP:rs28936680 | |||
Sequence: L → P | ||||||
Natural variant | VAR_021729 | 966 | in DSH | |||
Sequence: C → F | ||||||
Natural variant | VAR_069539 | 999 | in AGS6; dbSNP:rs398122896 | |||
Sequence: K → N | ||||||
Natural variant | VAR_069540 | 1007 | in AGS6; dbSNP:rs398122822 | |||
Sequence: G → R | ||||||
Natural variant | VAR_069541 | 1112 | in AGS6; dbSNP:rs398122895 | |||
Sequence: Y → F | ||||||
Natural variant | VAR_069542 | 1113 | in AGS6; dbSNP:rs398122894 | |||
Sequence: D → H | ||||||
Natural variant | VAR_026669 | 1155 | in DSH; dbSNP:rs1044845711 | |||
Sequence: R → W | ||||||
Natural variant | VAR_017605 | 1165 | in DSH; dbSNP:rs28936681 | |||
Sequence: F → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,278 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000171774 | 1-1226 | UniProt | Double-stranded RNA-specific adenosine deaminase | |||
Sequence: MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVSTQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSAQAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIKEKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNASNNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFENGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQTPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISESLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIAMLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFKKGLKDMGYGNWISKPQEEKNFYLCPV | |||||||
Modified residue | 26 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 285 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 349 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 384 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 408 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 418 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | |||||||
Cross-link | 418 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate | ||||
Sequence: K | |||||||
Cross-link | 418 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 481 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 483 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 580 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 588 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 593 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 599 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 601 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 603 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 603 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 605 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 608 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 611 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 614 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 629 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 629 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 636 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 808 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 808 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 814 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 814 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 818 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 823 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 823 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 825 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 825 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 875 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1089 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 5 is expressed at higher levels in astrocytomas as compared to normal brain tissue and expression increases strikingly with the severity of the tumor, being higher in the most aggressive tumors.
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Isoform 5 can form heterodimers with ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90 (PubMed:16055709).
Binding to ILF3/NF90 up-regulates ILF3-mediated gene expression. Isoform 1 and isoform 5 (via DRBM 3 domain) interact with TNPO1 (PubMed:19124606, PubMed:24753571).
Isoform 5 (via DRBM domains) interacts with XPO5 (PubMed:19124606).
Isoform 1 and isoform 5 can interact with EIF2AK2/PKR and UPF1 (PubMed:17079286, PubMed:18362360).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P55265 | NS P03496 | 8 | EBI-2462104, EBI-2547442 | |
XENO | P55265 | PRO_0000037965 P14340 | 2 | EBI-2462104, EBI-9825968 | |
XENO | P55265 | PRO_0000045599 Q99IB8 | 3 | EBI-2462104, EBI-6858501 | |
BINARY | P55265 | TARDBP Q13148 | 3 | EBI-2462104, EBI-372899 | |
BINARY | P55265 | UPF1 Q92900 | 3 | EBI-2462104, EBI-373471 | |
BINARY | P55265-1 | DICER1 Q9UPY3 | 4 | EBI-6913056, EBI-395506 | |
BINARY | P55265-1 | TARBP2 Q15633 | 2 | EBI-6913056, EBI-978581 | |
BINARY | P55265-5 | DICER1 Q9UPY3 | 8 | EBI-6913210, EBI-395506 | |
BINARY | P55265-5 | TARBP2 Q15633 | 3 | EBI-6913210, EBI-978581 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 133-199 | Z-binding 1 | ||||
Sequence: LSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAV | ||||||
Region | 133-202 | Interaction with Z-DNA | ||||
Sequence: LSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVSTQ | ||||||
Region | 208-238 | Disordered | ||||
Sequence: SGVVRPDGHSQGAPNSDPSLEPEDRNSTSVS | ||||||
Region | 258-286 | Disordered | ||||
Sequence: GVVRPDSHSQGSPNSDPGLEPEDSNSTSA | ||||||
Domain | 293-357 | Z-binding 2 | ||||
Sequence: FLDMAEIKEKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTD | ||||||
Domain | 503-571 | DRBM 1 | ||||
Sequence: NPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILLE | ||||||
Compositional bias | 574-597 | Basic and acidic residues | ||||
Sequence: KAKDSGKSEESSHYSTEKESEKTA | ||||||
Region | 574-610 | Disordered | ||||
Sequence: KAKDSGKSEESSHYSTEKESEKTAESQTPTPSATSFF | ||||||
Domain | 614-682 | DRBM 2 | ||||
Sequence: SPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALHG | ||||||
Region | 716-725 | N-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal | ||||
Sequence: IGELVRYLNT | ||||||
Domain | 726-794 | DRBM 3 | ||||
Sequence: NPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIG | ||||||
Region | 795-801 | C-terminal extension of DRBM 3 and constituent of a bi-partite nuclear localization signal | ||||
Sequence: ENEKAER | ||||||
Domain | 886-1221 | A to I editase | ||||
Sequence: SLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFKKGLKDMGYGNWISKPQEEKNF |
Domain
RNA binding interferes with nuclear import (PubMed:19124606, PubMed:24753571).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative promoter usage & Alternative splicing.
P55265-1
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.
- Name1
- SynonymsADAR-a, ADAR1L, p150
- NoteProduced by alternative promoter usage.
- Length1,226
- Mass (Da)136,066
- Last updated2010-11-30 v4
- Checksum9CE095D6F9C1BC79
P55265-2
- Name2
- SynonymsADAR-b
- NoteProduced by alternative splicing of isoform 1.
- Differences from canonical
- 807-832: Missing
P55265-3
- Name3
- SynonymsADAR-c
- NoteProduced by alternative splicing of isoform 1.
P55265-4
- Name4
- NoteProduced by alternative splicing of isoform 1.
- Differences from canonical
- 1-5: MNPRQ → MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDP
P55265-5
- Name5
- SynonymsADAR1S, p110
- NoteProduced by alternative promoter usage.
- Differences from canonical
- 1-295: Missing
Computationally mapped potential isoform sequences
There are 19 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAG2U5V6 | A0AAG2U5V6_HUMAN | ADAR | 1187 | ||
A0AAG2TPR9 | A0AAG2TPR9_HUMAN | ADAR | 97 | ||
A0AAG2TPY2 | A0AAG2TPY2_HUMAN | ADAR | 1236 | ||
A0AAG2U823 | A0AAG2U823_HUMAN | ADAR | 1110 | ||
A0AAQ5BGJ0 | A0AAQ5BGJ0_HUMAN | ADAR | 866 | ||
A0AAQ5BGJ1 | A0AAQ5BGJ1_HUMAN | ADAR | 56 | ||
A0AAQ5BGJ3 | A0AAQ5BGJ3_HUMAN | ADAR | 499 | ||
A0AAQ5BGJ4 | A0AAQ5BGJ4_HUMAN | ADAR | 927 | ||
A0AAQ5BGH8 | A0AAQ5BGH8_HUMAN | ADAR | 905 | ||
A0AAQ5BGK3 | A0AAQ5BGK3_HUMAN | ADAR | 814 | ||
A0AAQ5BGL3 | A0AAQ5BGL3_HUMAN | ADAR | 1220 | ||
A0A7P0TA14 | A0A7P0TA14_HUMAN | ADAR | 263 | ||
A0A7P0Z4K3 | A0A7P0Z4K3_HUMAN | ADAR | 1165 | ||
A0A7P0Z4F9 | A0A7P0Z4F9_HUMAN | ADAR | 912 | ||
A0A3B3IRQ9 | A0A3B3IRQ9_HUMAN | ADAR | 1158 | ||
A0A3B3ISU1 | A0A3B3ISU1_HUMAN | ADAR | 1046 | ||
A0A3B3ISX1 | A0A3B3ISX1_HUMAN | ADAR | 788 | ||
A0A3B3ITG9 | A0A3B3ITG9_HUMAN | ADAR | 350 | ||
A2IBT1 | A2IBT1_HUMAN | ADAR | 87 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008872 | 1-5 | in isoform 4 | |||
Sequence: MNPRQ → MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPEEVQDP | ||||||
Alternative sequence | VSP_019235 | 1-295 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 13 | In isoform P55265-4; in Ref. 5; CAE45853 | ||||
Sequence: R → G | ||||||
Sequence conflict | 53 | in Ref. 4; CAA55968 | ||||
Sequence: E → G | ||||||
Sequence conflict | 245 | in Ref. 5; CAE45853 | ||||
Sequence: F → L | ||||||
Sequence conflict | 482 | in Ref. 5; CAE45853 | ||||
Sequence: F → L | ||||||
Compositional bias | 574-597 | Basic and acidic residues | ||||
Sequence: KAKDSGKSEESSHYSTEKESEKTA | ||||||
Alternative sequence | VSP_008873 | 694-712 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_008874 | 807-832 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 873 | in Ref. 5; CAE45853 | ||||
Sequence: I → V | ||||||
Sequence conflict | 1093 | in Ref. 5; CAE45853 | ||||
Sequence: D → G | ||||||
Sequence conflict | 1184 | in Ref. 4; CAA55967/CAA55968/CAA67169/CAA67170 | ||||
Sequence: E → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U10439 EMBL· GenBank· DDBJ | AAB06697.1 EMBL· GenBank· DDBJ | mRNA | ||
U75503 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75489 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75490 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75491 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75492 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75493 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75494 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75495 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75496 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75497 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75498 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75499 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75500 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75501 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75502 EMBL· GenBank· DDBJ | AAB97116.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75503 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75489 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75490 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75491 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75492 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75493 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75494 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75495 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75496 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75497 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75498 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75499 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75500 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75501 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75502 EMBL· GenBank· DDBJ | AAB97117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75503 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75489 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75490 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75491 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75492 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75493 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75494 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75495 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75496 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75497 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75498 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75499 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75500 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75501 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75502 EMBL· GenBank· DDBJ | AAB97118.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18121 EMBL· GenBank· DDBJ | AAC13782.1 EMBL· GenBank· DDBJ | mRNA | ||
X79448 EMBL· GenBank· DDBJ | CAA55967.1 EMBL· GenBank· DDBJ | mRNA | ||
X79449 EMBL· GenBank· DDBJ | CAA55968.1 EMBL· GenBank· DDBJ | mRNA | ||
X98559 EMBL· GenBank· DDBJ | CAA67169.1 EMBL· GenBank· DDBJ | mRNA | ||
X98559 EMBL· GenBank· DDBJ | CAA67170.1 EMBL· GenBank· DDBJ | mRNA | ||
BX538232 EMBL· GenBank· DDBJ | CAD98075.1 EMBL· GenBank· DDBJ | mRNA | ||
BX640741 EMBL· GenBank· DDBJ | CAE45853.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
AL592078 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL606500 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL691488 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471121 EMBL· GenBank· DDBJ | EAW53183.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW53187.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC038227 EMBL· GenBank· DDBJ | AAH38227.1 EMBL· GenBank· DDBJ | mRNA |