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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Double-stranded RNA-specific editase 1

UniprotKB/SwissProt ID: P78563 (P78563)

Gene Name: ADARB1

Organism: Homo sapiens (Human)

Function: Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. 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; 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 GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis Has a lower catalytic activity than isoform 2 Has a higher catalytic activity than isoform 1

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Nucleus, nucleolus. Nucleus. Nucleus, nucleolus. Nucleus. Nucleus, nucleolus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002466 A_deamin
IPR044458 ADAR2_DSRM_1
IPR044459 ADAR2_DSRM_2
IPR014720 dsRBD_dom
IPR008996 IL1/FGF

The S-nitrosylation sites of P78563

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 393 MSDRGLALND C HAEIISRRSL   
2 556 LQGERLLTMS C SDKIARWNVV