RBM8A

Last updated
RBM8A
Protein RBM8A PDB 1p27.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RBM8A , BOV-1A, BOV-1B, BOV-1C, C1DELq21.1, DEL1q21.1, MDS014, RBM8, RBM8B, TAR, Y14, ZNRP, ZRNP1, RNA binding motif protein 8A
External IDs OMIM: 605313 MGI: 1913129 HomoloGene: 3744 GeneCards: RBM8A
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005105

NM_001102407
NM_025875

RefSeq (protein)

NP_005096

NP_001095877
NP_080151

Location (UCSC) Chr 1: 145.92 – 145.93 Mb Chr 3: 96.54 – 96.54 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

RNA-binding protein 8A is a protein that in humans is encoded by the RBM8A gene. [5] [6]

Contents

This gene encodes a protein with a conserved RNA-binding motif. The protein is found predominantly in the nucleus, although it is also present in the cytoplasm. It is preferentially associated with mRNAs produced by splicing, including both nuclear mRNAs and newly exported cytoplasmic mRNAs. It is thought that the protein remains associated with spliced mRNAs as a tag to indicate where introns had been present, thus coupling pre- and post-mRNA splicing events. Previously, it was thought that two genes encode this protein, RBM8A and RBM8B; it is now thought that the RBM8B locus is a pseudogene. Two alternative start codons result in two forms of the protein, and this gene also uses multiple polyadenylation sites. [7]

Interactions

RBM8A has been shown to interact with IPO13, [8] MAGOH [9] [10] and UPF3A. [11]

Related Research Articles

<span class="mw-page-title-main">RNA splicing</span> Process in molecular biology

RNA splicing is a process in molecular biology where a newly-made precursor messenger RNA (pre-mRNA) transcript is transformed into a mature messenger RNA (mRNA). It works by removing all the introns and splicing back together exons. For nuclear-encoded genes, splicing occurs in the nucleus either during or immediately after transcription. For those eukaryotic genes that contain introns, splicing is usually needed to create an mRNA molecule that can be translated into protein. For many eukaryotic introns, splicing occurs in a series of reactions which are catalyzed by the spliceosome, a complex of small nuclear ribonucleoproteins (snRNPs). There exist self-splicing introns, that is, ribozymes that can catalyze their own excision from their parent RNA molecule. The process of transcription, splicing and translation is called gene expression, the central dogma of molecular biology.

<span class="mw-page-title-main">Alternative splicing</span> Process by which a gene can code for multiple proteins

Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. In this process, particular exons of a gene may be included within or excluded from the final, processed messenger RNA (mRNA) produced from that gene. This means the exons are joined in different combinations, leading to different (alternative) mRNA strands. Consequently, the proteins translated from alternatively spliced mRNAs usually contain differences in their amino acid sequence and, often, in their biological functions.

Gideon Dreyfuss is an American biochemist, the Isaac Norris Professor of Biochemistry and Biophysics at the University of Pennsylvania School of Medicine, and an investigator of the Howard Hughes Medical Institute. He was elected to the National Academy of Sciences in 2012.

<span class="mw-page-title-main">Survival of motor neuron</span> Protein in animal cells

Survival of motor neuron or survival motor neuron (SMN) is a protein that in humans is encoded by the SMN1 and SMN2 genes.

<span class="mw-page-title-main">NXF1</span> Protein-coding gene in the species Homo sapiens

Nuclear RNA export factor 1, also known as NXF1 or TAP, is a protein which in humans is encoded by the NXF1 gene.

<span class="mw-page-title-main">SRRM1</span> Protein-coding gene in the species Homo sapiens

Serine/arginine repetitive matrix protein 1 is a protein that in humans is encoded by the SRRM1 gene.

<span class="mw-page-title-main">RNPS1</span> Protein-coding gene in the species Homo sapiens

RNA-binding protein with serine-rich domain 1 is a protein that in humans is encoded by the RNPS1 gene.

<span class="mw-page-title-main">UPF2</span> Protein-coding gene in the species Homo sapiens

Regulator of nonsense transcripts 2 is a protein that in humans is encoded by the UPF2 gene.

<span class="mw-page-title-main">UPF3B</span> Protein-coding gene in the species Homo sapiens

Regulator of nonsense transcripts 3B is a protein that in humans is encoded by the UPF3B gene.

<span class="mw-page-title-main">ALYREF</span> Protein-coding gene in the species Homo sapiens

Aly/REF export factor, also known as THO complex subunit 4 is a protein that in humans is encoded by the ALYREF gene.

<span class="mw-page-title-main">MAGOH</span> Protein-coding gene in the species Homo sapiens

Protein mago nashi homolog is a protein that in humans is encoded by the MAGOH gene.

<span class="mw-page-title-main">RBM4</span> Protein-coding gene in the species Homo sapiens

RNA-binding protein 4 is a protein that in humans is encoded by the RBM4 gene.

<span class="mw-page-title-main">EIF4A3</span> Protein-coding gene in the species Homo sapiens

Eukaryotic initiation factor 4A-III is a protein that in humans is encoded by the EIF4A3 gene.

<span class="mw-page-title-main">UPF3A</span> Protein-coding gene in the species Homo sapiens

Regulator of nonsense transcripts 3A is a protein that in humans is encoded by the UPF3A gene.

<span class="mw-page-title-main">HNRNPR</span> Protein-coding gene in the species Homo sapiens

Heterogeneous nuclear ribonucleoprotein R is a protein that in humans is encoded by the HNRNPR gene.

<span class="mw-page-title-main">RBM9</span> Protein-coding gene in the species Homo sapiens

RNA binding motif protein 9 (RBM9), also known as Rbfox2, is a protein which in humans is encoded by the RBM9 gene.

<span class="mw-page-title-main">PTBP1</span> Protein-coding gene in the species Homo sapiens

Polypyrimidine tract-binding protein 1 is a protein that in humans is encoded by the PTBP1 gene.

mRNA surveillance mechanisms are pathways utilized by organisms to ensure fidelity and quality of messenger RNA (mRNA) molecules. There are a number of surveillance mechanisms present within cells. These mechanisms function at various steps of the mRNA biogenesis pathway to detect and degrade transcripts that have not properly been processed.

<span class="mw-page-title-main">Exon junction complex</span> Protein complex assembled on mRNA

An exon junction complex (EJC) is a protein complex which forms on a pre-messenger RNA strand at the junction of two exons which have been joined together during RNA splicing. The EJC has major influences on translation, surveillance, localization of the spliced mRNA, and m6A methylation. It is first deposited onto mRNA during splicing and is then transported into the cytoplasm. There it plays a major role in post-transcriptional regulation of mRNA. It is believed that exon junction complexes provide a position-specific memory of the splicing event. The EJC consists of a stable heterotetramer core, which serves as a binding platform for other factors necessary for the mRNA pathway. The core of the EJC contains the protein eukaryotic initiation factor 4A-III bound to an adenosine triphosphate (ATP) analog, as well as the additional proteins Magoh and Y14. The binding of these proteins to nuclear speckled domains has been measured recently and it may be regulated by PI3K/AKT/mTOR signaling pathways. In order for the binding of the complex to the mRNA to occur, the eIF4AIII factor is inhibited, stopping the hydrolysis of ATP. This recognizes EJC as an ATP dependent complex. EJC also interacts with a large number of additional proteins; most notably SR proteins. These interactions are suggested to be important for mRNA compaction. The role of EJC in mRNA export is controversial.

The TREX (TRanscription-EXport) complex is a conserved eukaryotic multi-protein complex that couples mRNA transcription and nuclear export. The TREX complex travels across transcribed genes with RNA polymerase II. TREX binds mRNA and recruits transport proteins NXF1 and NXT1, which shuttle the mRNA out of the nucleus. The TREX complex plays an important role in genome stability and neurodegenerative diseases.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000265241 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000038374 - 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. Conklin DC, Rixon MW, Kuestner RE, Maurer MF, Whitmore TE, Millar RP (October 2000). "Cloning and gene expression of a novel human ribonucleoprotein". Biochim Biophys Acta. 1492 (2–3): 465–9. doi:10.1016/s0167-4781(00)00090-7. PMID   11004516.
  6. Salicioni AM, Xi M, Vanderveer LA, Balsara B, Testa JR, Dunbrack RL Jr, Godwin AK (October 2000). "Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif proteins that interact with OVCA1, a candidate tumor suppressor". Genomics. 69 (1): 54–62. doi:10.1006/geno.2000.6315. PMID   11013075.
  7. "Entrez Gene: RBM8A RNA binding motif protein 8A".
  8. Mingot, J M; Kostka S; Kraft R; Hartmann E; Görlich D (July 2001). "Importin 13: a novel mediator of nuclear import and export". EMBO J. England. 20 (14): 3685–94. doi:10.1093/emboj/20.14.3685. ISSN   0261-4189. PMC   125545 . PMID   11447110.
  9. Zhao, X F; Nowak N J; Shows T B; Aplan P D (January 2000). "MAGOH interacts with a novel RNA-binding protein". Genomics. UNITED STATES. 63 (1): 145–8. doi:10.1006/geno.1999.6064. ISSN   0888-7543. PMID   10662555.
  10. Kataoka, N; Diem M D; Kim V N; Yong J; Dreyfuss G (November 2001). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon–exon junction complex". EMBO J. England. 20 (22): 6424–33. doi:10.1093/emboj/20.22.6424. ISSN   0261-4189. PMC   125744 . PMID   11707413.
  11. Kim, V N; Kataoka N; Dreyfuss G (September 2001). "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex". Science . United States. 293 (5536): 1832–6. Bibcode:2001Sci...293.1832K. doi:10.1126/science.1062829. ISSN   0036-8075. PMID   11546873. S2CID   12018200.
  12. Klopocki E, Schulze H, Strauss G, et al. (February 2007). "Complex Inheritance Pattern Resembling Autosomal Recessive Inheritance Involving a Microdeletion in Thrombocytopenia–Absent Radius Syndrome". Am. J. Hum. Genet. 80 (2): 232–40. doi:10.1086/510919. PMC   1785342 . PMID   17236129.

Further reading