ADARB1

Protein-coding gene in the species Homo sapiens
ADARB1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1ZY7, 5ED1, 5ED2, 5HP3, 5HP2

Identifiers
AliasesADARB1, ADAR2, DRABA2, DRADA2, RED1, adenosine deaminase, RNA specific B1, adenosine deaminase RNA specific B1, NEDHYMS
External IDsOMIM: 601218; MGI: 891999; HomoloGene: 8280; GeneCards: ADARB1; OMA:ADARB1 - orthologs
EC number3.5.4.37
Gene location (Human)
Chromosome 21 (human)
Chr.Chromosome 21 (human)[1]
Chromosome 21 (human)
Genomic location for ADARB1
Genomic location for ADARB1
Band21q22.3Start45,073,853 bp[1]
End45,226,560 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for ADARB1
Genomic location for ADARB1
Band10 C1|10 39.72 cMStart77,126,560 bp[2]
End77,254,104 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • tibial arteries

  • gastric mucosa

  • right coronary artery

  • cerebellar vermis

  • saphenous vein

  • lateral nuclear group of thalamus

  • Descending thoracic aorta

  • ascending aorta

  • Achilles tendon

  • left coronary artery
Top expressed in
  • medial dorsal nucleus

  • medial geniculate nucleus

  • lateral geniculate nucleus

  • inferior colliculus

  • cerebellar cortex

  • medulla oblongata

  • nucleus of stria terminalis

  • dentate gyrus of hippocampal formation granule cell

  • pontine nuclei

  • visual cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • adenosine deaminase activity
  • protein binding
  • RNA binding
  • double-stranded RNA binding
  • mRNA binding
  • hydrolase activity
  • double-stranded RNA adenosine deaminase activity
  • tRNA-specific adenosine deaminase activity
Cellular component
  • nucleoplasm
  • nucleolus
  • nucleus
  • cytosol
  • cytoplasm
Biological process
  • RNA processing
  • immune system process
  • mRNA processing
  • base conversion or substitution editing
  • regulation of cell cycle
  • negative regulation of cell migration
  • defense response to virus
  • negative regulation of protein kinase activity by regulation of protein phosphorylation
  • positive regulation of viral genome replication
  • innate immune response
  • adenosine to inosine editing
  • negative regulation of cell population proliferation
  • neuromuscular synaptic transmission
  • facial nerve morphogenesis
  • hypoglossal nerve morphogenesis
  • spinal cord ventral commissure morphogenesis
  • multicellular organism growth
  • neuromuscular process controlling posture
  • innervation
  • muscle tissue morphogenesis
  • motor behavior
  • motor neuron apoptotic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

104

110532

Ensembl

ENSG00000197381

ENSMUSG00000020262

UniProt

P78563

Q91ZS8

RefSeq (mRNA)
NM_001033049
NM_001112
NM_001160230
NM_015833
NM_015834

NM_001346687
NM_001346688

NM_001024837
NM_001024838
NM_001024839
NM_001024840
NM_130895

RefSeq (protein)
NP_001103
NP_001153702
NP_001333616
NP_001333617
NP_056648

NP_056649

NP_001020008
NP_570965
NP_001020009

Location (UCSC)Chr 21: 45.07 – 45.23 MbChr 10: 77.13 – 77.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Double-stranded RNA-specific editase 1 is an enzyme that in humans is encoded by the ADARB1 gene.[5][6][7] The enzyme is a member of ADAR family.

Function

This gene encodes the enzyme responsible for pre-mRNA editing of the glutamate receptor subunit B by site-specific deamination of adenosines. Studies in rats found that this enzyme acted on its own pre-mRNA molecules to convert an AA dinucleotide to an AI dinucleotide which resulted in a new splice site. Alternative splicing of this gene results in several transcript variants, some of which have been characterized by the presence or absence of an Alu cassette insert and a short or long C-terminal region.[7]

ADARB1 requires the small molecule inositol hexakisphosphate (IP6) for proper function.[8] ADARB1 is an A-to-I RNA-editing enzyme that mostly acts on protein-coding substrates.[9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197381 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020262 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mittaz L, Scott HS, Rossier C, Seeburg PH, Higuchi M, Antonarakis SE (April 1997). "Cloning of a human RNA editing deaminase (ADARB1) of glutamate receptors that maps to chromosome 21q22.3". Genomics. 41 (2): 210–7. doi:10.1006/geno.1997.4655. PMID 9143496.
  6. ^ Keegan LP, Leroy A, Sproul D, O'Connell MA (Feb 2004). "Adenosine deaminases acting on RNA (ADARs): RNA-editing enzymes". Genome Biology. 5 (2): 209. doi:10.1186/gb-2004-5-2-209. PMC 395743. PMID 14759252.
  7. ^ a b "Entrez Gene: ADARB1 adenosine deaminase, RNA-specific, B1 (RED1 homolog rat)".
  8. ^ Macbeth MR, Schubert HL, Vandemark AP, Lingam AT, Hill CP, Bass BL (September 2005). "Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing". Science. 309 (5740): 1534–9. Bibcode:2005Sci...309.1534M. doi:10.1126/science.1113150. PMC 1850959. PMID 16141067.
  9. ^ Licht K, Jantsch MF (April 2016). "Rapid and dynamic transcriptome regulation by RNA editing and RNA modifications". The Journal of Cell Biology. 213 (1): 15–22. doi:10.1083/jcb.201511041. PMC 4828693. PMID 27044895.

Further reading

  • Valenzuela A, Blanco J, Callebaut C, Jacotot E, Lluis C, Hovanessian AG, Franco R (1997). "HIV-1 Envelope gp120 and Viral Particles Block Adenosine Deaminase Binding to Human CD26". Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology. Vol. 421. pp. 185–92. doi:10.1007/978-1-4757-9613-1_24. ISBN 978-1-4757-9615-5. PMID 9330696.
  • Melcher T, Maas S, Herb A, Sprengel R, Seeburg PH, Higuchi M (February 1996). "A mammalian RNA editing enzyme". Nature. 379 (6564): 460–4. Bibcode:1996Natur.379..460M. doi:10.1038/379460a0. PMID 8559253. S2CID 4326456.
  • O'Connell MA, Gerber A, Keller W (January 1997). "Purification of human double-stranded RNA-specific editase 1 (hRED1) involved in editing of brain glutamate receptor B pre-mRNA". The Journal of Biological Chemistry. 272 (1): 473–8. doi:10.1074/jbc.272.1.473. PMID 8995285.
  • Valenzuela A, Blanco J, Callebaut C, Jacotot E, Lluis C, Hovanessian AG, Franco R (April 1997). "Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles". Journal of Immunology. 158 (8): 3721–9. doi:10.4049/jimmunol.158.8.3721. PMID 9103436.
  • Lai F, Chen CX, Carter KC, Nishikura K (May 1997). "Editing of glutamate receptor B subunit ion channel RNAs by four alternatively spliced DRADA2 double-stranded RNA adenosine deaminases". Molecular and Cellular Biology. 17 (5): 2413–24. doi:10.1128/MCB.17.5.2413. PMC 232090. PMID 9111310.
  • Yang JH, Sklar P, Axel R, Maniatis T (April 1997). "Purification and characterization of a human RNA adenosine deaminase for glutamate receptor B pre-mRNA editing". Proceedings of the National Academy of Sciences of the United States of America. 94 (9): 4354–9. Bibcode:1997PNAS...94.4354Y. doi:10.1073/pnas.94.9.4354. PMC 20726. PMID 9113993.
  • Gerber A, O'Connell MA, Keller W (May 1997). "Two forms of human double-stranded RNA-specific editase 1 (hRED1) generated by the insertion of an Alu cassette". RNA. 3 (5): 453–63. PMC 1369496. PMID 9149227.
  • Villard L, Tassone F, Haymowicz M, Welborn R, Gardiner K (March 1997). "Map location, genomic organization and expression patterns of the human RED1 RNA editase". Somatic Cell and Molecular Genetics. 23 (2): 135–45. doi:10.1007/BF02679972. PMID 9330641. S2CID 45104326.
  • Blanco J, Valenzuela A, Herrera C, Lluís C, Hovanessian AG, Franco R (July 2000). "The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression". FEBS Letters. 477 (1–2): 123–8. doi:10.1016/S0014-5793(00)01751-8. PMID 10899322. S2CID 22229481.
  • Herrera C, Morimoto C, Blanco J, Mallol J, Arenzana F, Lluis C, Franco R (June 2001). "Comodulation of CXCR4 and CD26 in human lymphocytes". The Journal of Biological Chemistry. 276 (22): 19532–9. doi:10.1074/jbc.M004586200. PMID 11278278.
  • Maas S, Patt S, Schrey M, Rich A (December 2001). "Underediting of glutamate receptor GluR-B mRNA in malignant gliomas". Proceedings of the National Academy of Sciences of the United States of America. 98 (25): 14687–92. Bibcode:2001PNAS...9814687M. doi:10.1073/pnas.251531398. PMC 64742. PMID 11717408.
  • Jayan GC, Casey JL (April 2002). "Increased RNA editing and inhibition of hepatitis delta virus replication by high-level expression of ADAR1 and ADAR2". Journal of Virology. 76 (8): 3819–27. doi:10.1128/JVI.76.8.3819-3827.2002. PMC 136091. PMID 11907222.
  • Jaikaran DC, Collins CH, MacMillan AM (October 2002). "Adenosine to inosine editing by ADAR2 requires formation of a ternary complex on the GluR-B R/G site". The Journal of Biological Chemistry. 277 (40): 37624–9. doi:10.1074/jbc.M204126200. PMID 12163487.
  • Jayan GC, Casey JL (December 2002). "Inhibition of hepatitis delta virus RNA editing by short inhibitory RNA-mediated knockdown of ADAR1 but not ADAR2 expression". Journal of Virology. 76 (23): 12399–404. doi:10.1128/JVI.76.23.12399-12404.2002. PMC 136899. PMID 12414985.
  • Slavov D, Gardiner K (October 2002). "Phylogenetic comparison of the pre-mRNA adenosine deaminase ADAR2 genes and transcripts: conservation and diversity in editing site sequence and alternative splicing patterns". Gene. 299 (1–2): 83–94. doi:10.1016/S0378-1119(02)01016-8. PMID 12459255.

External links

  • v
  • t
  • e
  • 1zy7: Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)
    1zy7: Crystal structure of the catalytic domain of an adenosine deaminase that acts on RNA (hADAR2) bound to inositol hexakisphosphate (IHP)
  • 2b7t: Structure of ADAR2 dsRBM1
    2b7t: Structure of ADAR2 dsRBM1
  • 2b7v: Structure of ADAR2 dsRBM2
    2b7v: Structure of ADAR2 dsRBM2
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