SCUBA

RBM8A — RNA binding motif protein 8A

RBM8A belongs to a gene co-expression module in 11 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

RBM8A's module in each cell type

Cell typeModuleShares the module with
CD4⁺ T cellsRNA processing splicing
RNA processing
BUD31, DNAJC8, EDF1, EIF2S1, GTF3C6, HPRT1, ILF2, LAMTOR5 +11 moreView in SCUBA
CD8⁺ T cellsProteostasis Translation
Protein processing & ER
BZW1, CCT5, CCT7, EIF2S2, HNRNPC, HNRNPM, MDH1, PCBP1 +3 moreView in SCUBA
EndothelialStress RNA Processing
RNA processing & translation
ARF4, CACYBP, ELOC, ENY2, EWSR1, GNA14, HNRNPDL, HNRNPF +5 moreView in SCUBA
Gamma-delta T cellsmRNA Splicing Regulation
RNA processing & translation
ARF6, BTG3, CAPN7, CDV3, CELF2, CNBD2, CUL3, CYTIP +18 more
Glial cellsRNA Translation Processing
RNA processing & translation
CYCS, EEF1B2, EEF1D, HNRNPA1, HNRNPH3, LDHA, NAP1L1, NPM1 +5 moreView in SCUBA
Goblet cellsBasal Transcription
Housekeeping
ACTB, ACTG1, CALM2, DYNLL1, ELOC, ENY2, GTF2A2, LSM8 +2 moreView in SCUBA
Innate lymphoid cellsIntegrated Stress Response
Stress
AMD1, ATF4, CYCS, DDX5, DNAJB6, EIF1, GPBP1, HERPUD1 +3 moreView in SCUBA
Lymphatic endothelialRNA Protein Homeostasis
RNA processing & translation
ADRM1, BAG1, COPRS, ILF2, RAB32, RAN, SLC25A5, SNRPB +2 moreView in SCUBA
MacrophagesRNA Processing Housekeeping
Housekeeping
CISD3, CNIH4, DDX52, DPH3, EXOSC6, FABP5, GTF2E2, IKBKE +20 moreView in SCUBA
Mucosal-associated invariant T cellER Stress UPR
Stress
DDIT3, DNAJB9, EIF4A1, GTF2B, HERPUD1, HNRNPA0, IDI1, LDHA +9 more
PericytesRNA Splicing Processing
Housekeeping
ENY2, PCBP1, PCBP2, PLSCR1, RTN4, SLC3A2, SRSF4, WACView in SCUBA

About the gene

SynonymsBOV-1A, BOV-1B, BOV-1C, RBM8, RBM8B, Y14, ZNRP
Chromosome1: 145921556-145927678
Predicted locationIntracellular
Essential geneYes
Protein classDisease related genes, Essential proteins, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Transporters
Molecular functionRNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Translation regulation, Transport

Function

Required for pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Its removal from cytoplasmic mRNAs requires translation initiation from EJC-bearing spliced mRNAs. Associates preferentially with mRNAs produced by splicing. Does not interact with pre-mRNAs, introns, or mRNAs produced from intronless cDNAs. Associates with both nuclear mRNAs and newly exported cytoplasmic mRNAs. The MAGOH-RBM8A heterodimer is a component of the nonsense mediated decay (NMD) pathway. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl- X(S); the function is different from the established EJC assembly.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.