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Q9Y5S9

- RBM8A_HUMAN

UniProt

Q9Y5S9 - RBM8A_HUMAN

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Protein
RNA-binding protein 8A
Gene
RBM8A, RBM8, HSPC114, MDS014
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 WIBG/PYM 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.6 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB
  2. mRNA binding Source: UniProtKB
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. RNA splicing Source: Reactome
  3. gene expression Source: Reactome
  4. mRNA 3'-end processing Source: Reactome
  5. mRNA export from nucleus Source: Reactome
  6. mRNA metabolic process Source: Reactome
  7. mRNA splicing, via spliceosome Source: UniProtKB
  8. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  9. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  10. regulation of translation Source: UniProtKB-KW
  11. termination of RNA polymerase II transcription Source: Reactome
  12. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein 8A
Alternative name(s):
Binder of OVCA1-1
Short name:
BOV-1
RNA-binding motif protein 8A
RNA-binding protein Y14
Ribonucleoprotein RBM8A
Gene namesi
Name:RBM8A
Synonyms:RBM8
ORF Names:HSPC114, MDS014
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9905. RBM8A.

Subcellular locationi

Nucleus. Nucleus speckle. Cytoplasm
Note: Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles.1 Publication

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. exon-exon junction complex Source: UniProtKB
  5. nuclear speck Source: UniProtKB-SubCell
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi82 – 832EE → RR: Impaired nonsense-mediated decay activity.
Mutagenesisi106 – 1083LDR → RDE: Complete loss of nonsense-mediated decay activity. 1 Publication
Mutagenesisi118 – 1181L → R: Complete loss of nonsense-mediated decay activity. 1 Publication
Mutagenesisi149 – 1502CF → KA: Complete loss of nonsense-mediated decay activity.

Organism-specific databases

Orphaneti3320. Thrombocytopenia - absent radius.
PharmGKBiPA34270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 174173RNA-binding protein 8A
PRO_0000081763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei24 – 241Phosphoserine2 Publications
Modified residuei42 – 421Phosphoserine4 Publications
Modified residuei56 – 561Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y5S9.
PaxDbiQ9Y5S9.
PRIDEiQ9Y5S9.

PTM databases

PhosphoSiteiQ9Y5S9.

Miscellaneous databases

PMAP-CutDBQ9Y5S9.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9Y5S9.
CleanExiHS_RBM8A.
GenevestigatoriQ9Y5S9.

Organism-specific databases

HPAiCAB012803.
HPA018403.

Interactioni

Subunit structurei

Heterodimer with RBM8A. Part of the mRNA splicing-dependent exon junction complex (EJC) complex; the core complex contains CASC3, EIF4A3, MAGOH and RBM8A. Interacts with WIBG/PYM; the interaction is direct and dissociates the EJC from spliced mRNAs. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with BAT1, MAGOH, OVCA1, UPF3B, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with IPO13; the interaction mediates the nuclear import of the MAGOH-RBM8A heterodimer. Identified in the spliceosome C complex. Associates with polysomes.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4A3P3891921EBI-447231,EBI-299104
MAGOHP6132622EBI-447231,EBI-299134
SRPK1Q96SB42EBI-447231,EBI-539478
SRPK2P783622EBI-447231,EBI-593303
UPF3AQ9H1J14EBI-447231,EBI-521530
UPF3BQ9BZI79EBI-447231,EBI-372780

Protein-protein interaction databases

BioGridi115265. 63 interactions.
DIPiDIP-33070N.
IntActiQ9Y5S9. 36 interactions.
MINTiMINT-265248.
STRINGi9606.ENSP00000333001.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi72 – 787
Helixi86 – 938
Helixi94 – 963
Beta strandi99 – 1068
Turni108 – 1103
Beta strandi111 – 12212
Helixi124 – 13411
Beta strandi138 – 1436
Beta strandi145 – 1539

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P27X-ray2.00B/D50-155[»]
2HYIX-ray2.30B/H64-154[»]
2J0QX-ray3.20D/G66-174[»]
2J0SX-ray2.21D66-154[»]
2XB2X-ray3.40D/Z66-155[»]
3EX7X-ray2.30B/G51-174[»]
ProteinModelPortaliQ9Y5S9.
SMRiQ9Y5S9. Positions 12-155.

Miscellaneous databases

EvolutionaryTraceiQ9Y5S9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 15179RRM
Add
BLAST

Sequence similaritiesi

Belongs to the RBM8A family.

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000183826.
HOVERGENiHBG055173.
InParanoidiQ9Y5S9.
KOiK12876.
OMAiWILFVTS.
OrthoDBiEOG7C5MB6.
PhylomeDBiQ9Y5S9.
TreeFamiTF314933.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR008111. RNA-bd_8.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
PRINTSiPR01738. RNABINDINGM8.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y5S9-1) [UniParc]FASTAAdd to Basket

Also known as: BOV-1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM    50
REDYDSVEQD GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK 100
NIHLNLDRRT GYLKGYTLVE YETYKEAQAA MEGLNGQDLM GQPISVDWCF 150
VRGPPKGKRR GGRRRSRSPD RRRR 174
Length:174
Mass (Da):19,889
Last modified:November 1, 1999 - v1
Checksum:i70BBD03CDDFEECFE
GO
Isoform 2 (identifier: Q9Y5S9-2) [UniParc]FASTAAdd to Basket

Also known as: BOV-1b

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: Missing.

Show »
Length:173
Mass (Da):19,760
Checksum:i6710C1BD9CFAF92E
GO

Sequence cautioni

The sequence AAG16782.1 differs from that shown. Reason: Chimeric cDNA. A chimeric cDNA originating from chromosomes 1 and 5.
The sequence AAG14951.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAG16782.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei44 – 441Missing in isoform 2.
VSP_005810

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301A → V in CAG46622. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF127761 mRNA. Translation: AAD21089.1.
AF198620 mRNA. Translation: AAF37551.1.
AF231511 mRNA. Translation: AAG16781.1.
AF231512 mRNA. Translation: AAG16782.1. Different initiation.
AF299118 mRNA. Translation: AAG27091.1.
AF403012 Genomic DNA. Translation: AAL26999.1.
AF182415 mRNA. Translation: AAG14951.1. Different initiation.
AF161463 mRNA. Translation: AAF29078.1.
CR541823 mRNA. Translation: CAG46622.1.
CR541805 mRNA. Translation: CAG46604.1.
AK075009 mRNA. Translation: BAG52051.1.
AL160282 Genomic DNA. No translation available.
CH471244 Genomic DNA. Translation: EAW71419.1.
BC017088 mRNA. Translation: AAH17088.1.
CCDSiCCDS916.1. [Q9Y5S9-1]
RefSeqiNP_005096.1. NM_005105.4. [Q9Y5S9-1]
UniGeneiHs.591455.

Genome annotation databases

EnsembliENST00000330165; ENSP00000333001; ENSG00000131795. [Q9Y5S9-1]
ENST00000369307; ENSP00000358313; ENSG00000131795. [Q9Y5S9-2]
GeneIDi9939.
KEGGihsa:9939.
UCSCiuc001ent.2. human. [Q9Y5S9-1]
uc001enu.2. human. [Q9Y5S9-2]

Polymorphism databases

DMDMi10720244.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF127761 mRNA. Translation: AAD21089.1 .
AF198620 mRNA. Translation: AAF37551.1 .
AF231511 mRNA. Translation: AAG16781.1 .
AF231512 mRNA. Translation: AAG16782.1 . Different initiation.
AF299118 mRNA. Translation: AAG27091.1 .
AF403012 Genomic DNA. Translation: AAL26999.1 .
AF182415 mRNA. Translation: AAG14951.1 . Different initiation.
AF161463 mRNA. Translation: AAF29078.1 .
CR541823 mRNA. Translation: CAG46622.1 .
CR541805 mRNA. Translation: CAG46604.1 .
AK075009 mRNA. Translation: BAG52051.1 .
AL160282 Genomic DNA. No translation available.
CH471244 Genomic DNA. Translation: EAW71419.1 .
BC017088 mRNA. Translation: AAH17088.1 .
CCDSi CCDS916.1. [Q9Y5S9-1 ]
RefSeqi NP_005096.1. NM_005105.4. [Q9Y5S9-1 ]
UniGenei Hs.591455.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P27 X-ray 2.00 B/D 50-155 [» ]
2HYI X-ray 2.30 B/H 64-154 [» ]
2J0Q X-ray 3.20 D/G 66-174 [» ]
2J0S X-ray 2.21 D 66-154 [» ]
2XB2 X-ray 3.40 D/Z 66-155 [» ]
3EX7 X-ray 2.30 B/G 51-174 [» ]
ProteinModelPortali Q9Y5S9.
SMRi Q9Y5S9. Positions 12-155.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115265. 63 interactions.
DIPi DIP-33070N.
IntActi Q9Y5S9. 36 interactions.
MINTi MINT-265248.
STRINGi 9606.ENSP00000333001.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei Q9Y5S9.

Polymorphism databases

DMDMi 10720244.

Proteomic databases

MaxQBi Q9Y5S9.
PaxDbi Q9Y5S9.
PRIDEi Q9Y5S9.

Protocols and materials databases

DNASUi 9939.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330165 ; ENSP00000333001 ; ENSG00000131795 . [Q9Y5S9-1 ]
ENST00000369307 ; ENSP00000358313 ; ENSG00000131795 . [Q9Y5S9-2 ]
GeneIDi 9939.
KEGGi hsa:9939.
UCSCi uc001ent.2. human. [Q9Y5S9-1 ]
uc001enu.2. human. [Q9Y5S9-2 ]

Organism-specific databases

CTDi 9939.
GeneCardsi GC01P145507.
GeneReviewsi RBM8A.
HGNCi HGNC:9905. RBM8A.
HPAi CAB012803.
HPA018403.
MIMi 605313. gene.
neXtProti NX_Q9Y5S9.
Orphaneti 3320. Thrombocytopenia - absent radius.
PharmGKBi PA34270.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000183826.
HOVERGENi HBG055173.
InParanoidi Q9Y5S9.
KOi K12876.
OMAi WILFVTS.
OrthoDBi EOG7C5MB6.
PhylomeDBi Q9Y5S9.
TreeFami TF314933.

Enzyme and pathway databases

Reactomei REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSi RBM8A. human.
EvolutionaryTracei Q9Y5S9.
GeneWikii RBM8A.
GenomeRNAii 9939.
NextBioi 37498.
PMAP-CutDB Q9Y5S9.
PROi Q9Y5S9.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5S9.
CleanExi HS_RBM8A.
Genevestigatori Q9Y5S9.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR008111. RNA-bd_8.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
PRINTSi PR01738. RNABINDINGM8.
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  2. "MAGOH interacts with a novel RNA-binding protein."
    Zhao X.F., Nowak N.J., Shows T.B., Aplan P.D.
    Genomics 63:145-148(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH MAGOH.
  3. "Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif proteins that interact with OVCA1, a candidate tumor suppressor."
    Salicioni A.M., Xi M., Vanderveer L.A., Balsara B., Testa J.R., Dunbrack R.L. Jr., Godwin A.K.
    Genomics 69:54-62(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH OVCA1.
    Tissue: Brain.
  4. "Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm."
    Kataoka N., Yong J., Kim V.N., Velazquez F., Perkinson R.A., Wang F., Dreyfuss G.
    Mol. Cell 6:673-682(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
  5. "The genes encoding the type II gonadotropin-releasing hormone receptor and the ribonucleoprotein RBM8A in humans overlap in two genomic loci."
    Faurholm B., Millar R.P., Katz A.A.
    Genomics 78:15-18(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
    Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hematopoietic stem cell.
  7. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  9. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  10. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  13. "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions."
    Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.
    EMBO J. 19:6860-6869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RNPS1; SRRM1 AND ALYREF/THOC4.
  14. "Importin 13: a novel mediator of nuclear import and export."
    Mingot J.-M., Kostka S., Kraft R., Hartmann E., Goerlich D.
    EMBO J. 20:3685-3694(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO13.
  15. "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex."
    Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.
    EMBO J. 20:6424-6433(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
  16. "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex."
    Kim V.N., Kataoka N., Dreyfuss G.
    Science 293:1832-1836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
  17. "Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1."
    Lykke-Andersen J., Shu M.-D., Steitz J.A.
    Science 293:1836-1839(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
  18. "Translation is required to remove Y14 from mRNAs in the cytoplasm."
    Dostie J., Dreyfuss G.
    Curr. Biol. 12:1060-1067(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSLATION, ASSOCIATION WITH POLYSOMES, RNA-BINDING.
  19. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  20. "An evolutionarily conserved role for SRm160 in 3'-end processing that functions independently of exon junction complex formation."
    McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.
    J. Biol. Chem. 278:44153-44160(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAT1; RNPS1; SRRM1 AND ALYREF/THOC4.
  21. Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH RENT3B.
  22. "A novel mode of RBD-protein recognition in the Y14-Mago complex."
    Fribourg S., Gatfield D., Izaurralde E., Conti E.
    Nat. Struct. Biol. 10:433-439(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAGOH.
  23. "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex."
    Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.
    EMBO Rep. 5:304-310(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WIBG.
  24. "A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex."
    Kataoka N., Dreyfuss G.
    J. Biol. Chem. 279:7009-7013(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RNPS1 AND SRRM1.
  25. "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements."
    Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., Kulozik A.E.
    Mol. Cell 20:65-75(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 82-GLU-GLU-83; 106-LEU--ARG-108; LEU-118 AND 149-CYS-PHE-150.
  26. "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity."
    Ballut L., Marchadier B., Baguet A., Tomasetto C., Seraphin B., Le Hir H.
    Nat. Struct. Mol. Biol. 12:861-869(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX.
  27. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
    Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
    RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "PYM binds the cytoplasmic exon-junction complex and ribosomes to enhance translation of spliced mRNAs."
    Diem M.D., Chan C.C., Younis I., Dreyfuss G.
    Nat. Struct. Mol. Biol. 14:1173-1179(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WIBG.
  30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  32. "Exon junction complex enhances translation of spliced mRNAs at multiple steps."
    Lee H.C., Choe J., Chi S.G., Kim Y.K.
    Biochem. Biophys. Res. Commun. 384:334-340(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA TRANSLATION.
  33. "Disassembly of exon junction complexes by PYM."
    Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.
    Cell 137:536-548(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WIBG.
  34. "Assembly and mobility of exon-exon junction complexes in living cells."
    Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P., Wachsmuth M.
    RNA 15:862-876(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  35. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  36. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-42 AND SER-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
    Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
    Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  40. "Structure of the Y14-Magoh core of the exon junction complex."
    Lau C.K., Diem M.D., Dreyfuss G., Van Duyne G.D.
    Curr. Biol. 13:933-941(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-155 IN COMPLEX WITH MAGOH.
  41. "The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA."
    Bono F., Ebert J., Lorentzen E., Conti E.
    Cell 126:713-725(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 66-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND AMP-PNP.
  42. "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA."
    Andersen C.B., Ballut L., Johansen J.S., Chamieh H., Nielsen K.H., Oliveira C.L., Pedersen J.S., Seraphin B., Le Hir H., Andersen G.R.
    Science 313:1968-1972(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 64-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND ADP-NP.
  43. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 51-174 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND TRANSITION STATE ANALOG ADP-ALF3.

Entry informationi

Entry nameiRBM8A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5S9
Secondary accession number(s): B3KQI9
, Q6FHD1, Q6IQ40, Q9GZX8, Q9NZI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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