Q9Y5S9 (RBM8A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBM8A
Synonyms:	RBM8
ORF Names:	HSPC114, MDS014

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	174 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Core components of the EJC, that remains bound to spliced mRNAs throughout all stages of mRNA metabolism, functions to mark the position of the exon-exon junction in the mature mRNA and thereby influences downstream processes of gene expression including mRNA splicing, nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The heterodimer MAGOH-RBM8A interacts with PYM that function to enhance the translation of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Remains associated with mRNAs in the cytoplasm until the mRNAs engage the translation machinery. 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. Complex with MAGOH is a component of the nonsense mediated decay (NMD) pathway. Ref.17 Ref.20 Ref.21 Ref.26 Ref.34
Subunit structure	Heterodimer with MAGOH. Part of the exon junction complex (EJC) core complex that contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-dependent EJC, at least composed of ACIN1, CASC3, DEK, EIF4A3, MAGOH, NCBP1, NCBP2, PNN, NXF1, RBM8A, UPF2, UPF3A, UPF3B, RNPS1, SAP18, SRRM1 and THOC4. Found in a post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1. Interacts with BAT1, MAGOH, OVCA1, UPF3B, RNPS1, SRRM1 and THOC4. Identified in the spliceosome C complex. Interacts with WIBG/PYM; the interaction is direct and leads to dissociate the EJC from spliced mRNAs. Associates with polysomes. Ref.2 Ref.3 Ref.14 Ref.19 Ref.20 Ref.21 Ref.22 Ref.31 Ref.35
Subcellular location	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, THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. Ref.36
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the RBM8A family. Contains 1 RRM (RNA recognition motif) domain.
Sequence caution	The sequence AAG14951.1 differs from that shown. Reason: Erroneous initiation. The sequence AAG16782.1 differs from that shown. Reason: Erroneous initiation. The sequence AAG16782.1 differs from that shown. Reason: Chimeric cDNA. A chimeric cDNA originating from chromosomes 1 and 5.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Translation regulation Transport mRNA processing mRNA splicing mRNA transport
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA export from nucleus Traceable author statement. Source: Reactome nuclear mRNA splicing, via spliceosome Inferred by curator Ref.18. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from mutant phenotype Ref.26. Source: UniProtKB regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW termination of RNA polymerase II transcription Traceable author statement. Source: Reactome
Cellular component	catalytic step 2 spliceosome Inferred from direct assay Ref.18. Source: UniProtKB cytosol Traceable author statement. Source: Reactome exon-exon junction complex Inferred from direct assay Ref.31Ref.35. Source: UniProtKB nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	mRNA binding Non-traceable author statement Ref.4. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.31Ref.35. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4A3	P38919	8	EBI-447231,EBI-299104
MAGOH	P61326	19	EBI-447231,EBI-299134
UPF3A	Q9H1J1	4	EBI-447231,EBI-521530
UPF3B	Q9BZI7	8	EBI-447231,EBI-372780

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y5S9-1)

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.

Isoform 2 (identifier: Q9Y5S9-2)

Also known as: BOV-1b;

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 174

173

RNA-binding protein 8A

PRO_0000081763

Regions

Domain

73 – 151

79

RRM

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.33

Modified residue

42

1

Phosphoserine Ref.25 Ref.29 Ref.30 Ref.32

Modified residue

46

1

Phosphoserine Ref.24

Modified residue

56

1

Phosphoserine Ref.32 Ref.37

Modified residue

166

1

Phosphoserine Ref.29

Modified residue

168

1

Phosphoserine Ref.29

Natural variations

Alternative sequence

44

1

Missing in isoform 2.

VSP_005810

Experimental info

Mutagenesis

82 – 83

2

EE → RR: Impaired nonsense-mediated decay activity.

Mutagenesis

106 – 108

3

LDR → RDE: Complete loss of nonsense-mediated decay activity. Ref.26

Mutagenesis

118

1

L → R: Complete loss of nonsense-mediated decay activity. Ref.26

Mutagenesis

149 – 150

2

CF → KA: Complete loss of nonsense-mediated decay activity.

Sequence conflict

130

1

A → V in CAG46622. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

174

Helix Strand Turn

Details...

Beta strand

72 – 78

7

Helix

86 – 93

8

Helix

94 – 96

3

Beta strand

99 – 106

8

Turn

108 – 110

3

Beta strand

111 – 122

12

Helix

124 – 134

11

Beta strand

138 – 143

6

Beta strand

145 – 153

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BOV-1a) [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 70BBD03CDDFEECFE	FASTA	174	19,889
	10 20 30 40 50 60 MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEEGSRARM REDYDSVEQD 70 80 90 100 110 120 GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE 130 140 150 160 170 YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR
	Isoform 2 (BOV-1b) [UniParc]. Checksum: 6710C1BD9CFAF92E	FASTA	173	19,760
	10 20 30 40 50 60 MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSEGSRARMR EDYDSVEQDG 70 80 90 100 110 120 DEPGPQRSVE GWILFVTGVH EEATEEDIHD KFAEYGEIKN IHLNLDRRTG YLKGYTLVEY 130 140 150 160 170 ETYKEAQAAM EGLNGQDLMG QPISVDWCFV RGPPKGKRRG GRRRSRSPDR RRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and gene expression of a novel human ribonucleoprotein." Conklin D.C., Rixon M.W., Kuestner R.E., Maurer M.F., Whitmore T.E., Millar R.P. Biochim. Biophys. Acta 1492:465-469(2000) [PubMed: 11004516] [Abstract] 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: 10662555] [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: 11013075] [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: 11030346] [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: 11707068] [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: 11042152] [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: 16303743] [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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 11118221] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH DEK; RNPS1; SRRM1 AND THOC4.
[14]	"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: 11707413] [Abstract] Cited for: INTERACTION WITH THOC4 AND THE EXON JUNCTION COMPLEX.
[15]	"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: 11546873] [Abstract] Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
[16]	"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: 11546874] [Abstract] Cited for: IDENTIFICATION IN A POST-SPLICING COMPLEX WITH NXF1; UPF1; UPF2; UPF3A; UPF3B AND RNPS1.
[17]	"Translation is required to remove Y14 from mRNAs in the cytoplasm." Dostie J., Dreyfuss G. Curr. Biol. 12:1060-1067(2002) [PubMed: 12121612] [Abstract] Cited for: FUNCTION IN TRANSLATION, ASSOCIATION WITH POLYSOMES, RNA-BINDING.
[18]	"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: 11991638] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[19]	"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: 12944400] [Abstract] Cited for: INTERACTION WITH BAT1; RNPS1; SRRM1 AND THOC4.
[20]	"Y14 and hUpf3b form an NMD-activating complex." Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E. Mol. Cell 11:939-949(2003) [PubMed: 12718880] [Abstract] Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH RENT3B.
[21]	"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: 12730685] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAGOH.
[22]	"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: 14968132] [Abstract] Cited for: INTERACTION WITH WIBG.
[23]	"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: 14625303] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC) WITH RNPS1 AND SRRM1.
[24]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[26]	"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: 16209946] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF 82-GLU-GLU-83; 106-LEU--ARG-108; LEU-118 AND 149-CYS-PHE-150.
[27]	"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: 16170325] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX.
[28]	"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: 16314458] [Abstract] Cited for: IDENTIFICATION IN THE CORE EXON JUNCTION COMPLEX, IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, MASS SPECTROMETRY.
[29]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-166 AND SER-168, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"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: 18026120] [Abstract] Cited for: INTERACTION WITH WIBG.
[32]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-56, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[34]	"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: 19409878] [Abstract] Cited for: FUNCTION IN MRNA TRANSLATION.
[35]	"Disassembly of exon junction complexes by PYM." Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W. Cell 137:536-548(2009) [PubMed: 19410547] [Abstract] Cited for: INTERACTION WITH WIBG.
[36]	"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: 19324961] [Abstract] Cited for: SUBCELLULAR LOCATION.
[37]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[38]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]	"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: 12781131] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-155 IN COMPLEX WITH MAGOH.
[40]	"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: 16923391] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 66-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND AMP-PNP.
[41]	"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: 16931718] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 64-154 IN THE EJC COMPLEX WITH CASC3; EIF4A3; MAGOH AND ADP-NP.
[42]	"Mechanism of ATP turnover inhibition in the EJC." Nielsen K.H., Chamieh H., Andersen C.B., Fredslund F., Hamborg K., Le Hir H., Andersen G.R. RNA 15:67-75(2009) [PubMed: 19033377] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00001757.
IPI00216659.

RefSeq

NP_005096.1. NM_005105.3.

UniGene

Hs.591455.
Hs.728824.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9Y5S9.

SMR

Q9Y5S9. Positions 12-155.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33070N.

IntAct

Q9Y5S9. 30 interactions.

MINT

MINT-265248.

STRING

Q9Y5S9.

Protein family/group databases

TCDB

3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.

PTM databases

PhosphoSite

Q9Y5S9.

Polymorphism databases

DMDM

10720244.

Proteomic databases

PRIDE

Q9Y5S9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000048915; ENSMUSP00000044548; ENSMUSG00000038374.
ENST00000330165; ENSP00000333001; ENSG00000131795.

GeneID

9939.

KEGG

hsa:9939.

UCSC

uc001ent.1. human.
uc001enu.1. human.

Organism-specific databases

CTD

9939.

GeneCards

GC01P145507.

H-InvDB

HIX0000976.

HGNC

HGNC:9905. RBM8A.

HPA

CAB012803.
HPA018403.

MIM

605313. gene.

neXtProt

NX_Q9Y5S9.

PharmGKB

PA34270.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19287.

GeneTree

ENSGT00550000074641.

HOGENOM

HBG756718.

HOVERGEN

HBG055173.

InParanoid

Q9Y5S9.

OMA

FVTSIHE.

OrthoDB

EOG42822W.

PhylomeDB

Q9Y5S9.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q9Y5S9.

Bgee

Q9Y5S9.

CleanEx

HS_RBM8A.

Genevestigator

Q9Y5S9.

GermOnline

ENSG00000131795. Homo sapiens.

Family and domain databases

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR008111. RNA-bd_8.
IPR000504. RRM_dom.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

KO

K12876.

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

PRINTS

PR01738. RNABINDINGM8.

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

37498.

PMAP-CutDB

Q9Y5S9.

SOURCE

Search...

Entry information

Entry name

RBM8A_HUMAN

Accession

Primary (citable) accession number: Q9Y5S9
Secondary accession number(s): B3KQI9 , Q6FHD1, Q6IQ40, Q9GZX8, Q9NZI4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.