Modomics - A Database of RNA Modifications

ID Card:

Full name:	Double-stranded RNA-specific editase B2
GI:	33112436
UniProt:	Q9NS39
Alpha Fold Predicted Structure:	AF-Q9NS39-F1

Protein sequence:

MASVLGSGRGSGGLSSQLKCKSKRRRRRRSKRKDKVSILSTFLAPFKHLSPGITNTEDDDTLSTSSAEVKENRNVGNLAARPPPSGDRARGGAPGAKRKRPLEEGNGGHLCKLQLVWKKLSWSVAPKNALVQLHELRPGLQYRTVSQTGPVHAPVFAVAVEVNGLTFEGTGPTKKKAKMRAAELALRSFVQFPNACQAHLAMGGGPGPGTDFTSDQADFPDTLFQEFEPPAPRPGLAGGRPGDAALLSAAYGRRRLLCRALDLVGPTPATPAAPGERNPVVLLNRLRAGLRYVCLAEPAERRARSFVMAVSVDGRTFEGSGRSKKLARGQAAQAALQELFDIQMPGHAPGRARRTPMPQEFADSISQLVTQKFREVTTDLTPMHARHKALAGIVMTKGLDARQAQVVALSSGTKCISGEHLSDQGLVVNDCHAEVVARRAFLHFLYTQLELHLSKRREDSERSIFVRLKEGGYRLRENILFHLYVSTSPCGDARLHSPYEITTDLHSSKHLVRKFRGHLRTKIESGEGTVPVRGPSAVQTWDGVLLGEQLITMSCTDKIARWNVLGLQGALLSHFVEPVYLQSIVVGSLHHTGHLARVMSHRMEGVGQLPASYRHNRPLLSGVSDAEARQPGKSPPFSMNWVVGSADLEIINATTGRRSCGGPSRLCKHVLSARWARLYGRLSTRTPSPGDTPSMYCEAKLGAHTYQSVKQQLFKAFQKAGLGTWVRKPPEQQQFLLTL

Comments:

ADAR, ADARB1, and ADARB2 are the three highly conserved members of the ADAR mammalian protein family. ADAR and ADARB1 catalyze the hydrolytic deamination of Adenosine (Nishikura 2010 ) that brings to the occurrence of Inosine (I), one of the most prevalent post-transcriptional modification in higher eukaryotes (Walkley & Li 2017 ). ADARB2 has been identified as inactive in vitro . Experiments suggests that ADARB2 may utilize its arginine rich N-terminal motif to target a selective set of substrates. It has been speculated that this motif may recognize and bind to specific stem loop structures of single stranded (ss) RNAs. Noteworthy, in vitro experiments show that ADARB2 effectively suppresses editing of 5HT_CR RNA by ADAR and ADAB1 (Chen et al. 2000 )

Alpha Fold Predicted Structure:

Downloading... [225018/649414]

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Protein sequence:

M A S V L G S G R G S G G L S S Q L K C K S K R R R R R R S K R K D K V S I L S T F L A P F K H L S P G I T N T E D D D T L S T S S A E V K E N R N V G N L A A R P P P S G D R A R G G A P G A K R K R P L E E G N G G H L C K L Q L V W K K L S W S V A P K N A L V Q L H E L R P G L Q Y R T V S Q T G P V H A P V F A V A V E V N G L T F E G T G P T K K K A K M R A A E L A L R S F V Q F P N A C Q A H L A M G G G P G P G T D F T S D Q A D F P D T L F Q E F E P P A P R P G L A G G R P G D A A L L S A A Y G R R R L L C R A L D L V G P T P A T P A A P G E R N P V V L L N R L R A G L R Y V C L A E P A E R R A R S F V M A V S V D G R T F E G S G R S K K L A R G Q A A Q A A L Q E L F D I Q M P G H A P G R A R R T P M P Q E F A D S I S Q L V T Q K F R E V T T D L T P M H A R H K A L A G I V M T K G L D A R Q A Q V V A L S S G T K C I S G E H L S D Q G L V V N D C H A E V V A R R A F L H F L Y T Q L E L H L S K R R E D S E R S I F V R L K E G G Y R L R E N I L F H L Y V S T S P C G D A R L H S P Y E I T T D L H S S K H L V R K F R G H L R T K I E S G E G T V P V R G P S A V Q T W D G V L L G E Q L I T M S C T D K I A R W N V L G L Q G A L L S H F V E P V Y L Q S I V V G S L H H T G H L A R V M S H R M E G V G Q L P A S Y R H N R P L L S G V S D A E A R Q P G K S P P F S M N W V V G S A D L E I I N A T T G R R S C G G P S R L C K H V L S A R W A R L Y G R L S T R T P S P G D T P S M Y C E A K L G A H T Y Q S V K Q Q L F K A F Q K A G L G T W V R K P P E Q Q Q F L L T L

Secondary Structure Alphabet

G: 3-turn helix (3₁₀helix)
H: α-helix
I: 𝝅-helix (5 - turn helix)
T: Hydrogen Bonded Turn
B: β-sheet
S: Bend
C: Coil (residues not present in any of the above conformations)
N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files	AF-Q9NS39-F1.pdb
Alpha Fold Pdbx/mmCIF Files	AF-Q9NS39-F1.cif
DSSP Secondary Structures	Q9NS39.dssp

Diseases connected to this enzyme:

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Description	Reaction	Disease Name
A mutation on the GRIA2 gene (Q607E) prevents the editing at the Q/R site. Specifically, a cytosine to guanidine base change, immediately 5′ to the adenosine that is edited to inosine by ADAR2, impairs the normal editing of ADARB2. The mutant GAG codon is predicted to be recognized by ADARB2 ~90% less than the normal CAG codon, with a consequent reduction of A:I modifications in the second codon position.	A:I	Intellectual disability
The reduction of ADARB2 is correlated with the grade of malignancy of glioblastoma multiforme	A:I	Glioblastoma


A mutation on the GRIA2 gene (Q607E) prevents the editing at the Q/R site. Specifically, a cytosine to guanidine base change, immediately 5′ to the adenosine that is edited to inosine by ADAR2, impairs the normal editing of ADARB2. The mutant GAG codon is predicted to be recognized by ADARB2 ~90% less than the normal CAG codon, with a consequent reduction of A:I modifications in the second codon position.
The reduction of ADARB2 is correlated with the grade of malignancy of glioblastoma multiforme

A mutation on the GRIA2 gene (Q607E) prevents the editing at the Q/R site. Specifically, a cytosine to guanidine base change, immediately 5′ to the adenosine that is edited to inosine by ADAR2, impairs the normal editing of ADARB2. The mutant GAG codon is predicted to be recognized by ADARB2 ~90% less than the normal CAG codon, with a consequent reduction of A:I modifications in the second codon position.

The reduction of ADARB2 is correlated with the grade of malignancy of glioblastoma multiforme

Showing 1 to 2 of 2 entries

Publications:

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Title	Authors	Journal	Details	PubMed Id	DOI
A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains.	C X Chen, D S Cho, Q Wang, F Lai, K C Carter, and K Nishikura	RNA	[details]	10836796	10.1017/s1355838200000170
Functions and Regulation of RNA Editing by ADAR Deaminases	Kazuko Nishikura	Annu Rev Biochem	[details]	20192758	10.1146/annurev-biochem-060208-105251


A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains.
Functions and Regulation of RNA Editing by ADAR Deaminases

Showing 1 to 2 of 2 entries