Q9BRP8 (WIBG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Partner of Y14 and mago

Alternative name(s):
Protein wibg homolog

Gene names

Name:	WIBG
Synonyms:	PYM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by Ref.5, while Ref.8 did not detect RNA-binding activity independently of the EJC. Ref.6 Ref.8
Subunit structure	Interacts (via N-terminus) with MAGOH and RBM8A; the interaction is direct. Associates (eIF2A-like region) with the 40S ribosomal subunit and the 48S preinitiation complex. Ref.5 Ref.6 Ref.8
Subcellular location	Cytoplasm. Nucleus › nucleolus. Nucleus › nucleoplasm. Note: Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1. Ref.5 Ref.6
Domain	The eIF2A-like region shares sequence similarity with eIF2A and mediates the interaction with the 40S ribosomal subunit and the 48S preinitiation complex. Ref.6
Sequence similarities	Belongs to the wibg family.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Translation regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of translation Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA exon-exon junction complex Inferred from direct assay Ref.6. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW ribosome binding Inferred from direct assay Ref.6Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRNP	P04156	1	EBI-2352802,EBI-977302
RPL23	P62829	1	EBI-2352802,EBI-353303

Alternative products

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

Isoform 1 (identifier: Q9BRP8-1)

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: Q9BRP8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MEAAGSPAATET → MATPYVTDETG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	Partner of Y14 and mago		PRO_0000287285
Regions
	Region	1 – 33	33	Required for interaction with MAGOH and RBM8A
	Region	152 – 204	53	eIF2A-like
	Coiled coil	82 – 116	35	Potential
	Coiled coil	145 – 204	60	Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.9
	Modified residue	6	1	Phosphoserine Ref.9
	Modified residue	64	1	Phosphoserine Ref.7
	Modified residue	72	1	Phosphothreonine Ref.7
Natural variations
	Alternative sequence	1 – 12	12	MEAAG…AATET → MATPYVTDETG in isoform 2.		VSP_025430
	Natural variant	66	1	E → Q. Corresponds to variant rs3802998 [ dbSNP | Ensembl ].		VAR_032297
Experimental info
	Sequence conflict	147	1	T → S in CAD30677. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 087B901279007C05	FASTA	204	22,656
	10 20 30 40 50 60 MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP 70 80 90 100 110 120 PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE 130 140 150 160 170 180 TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS 190 200 KEQLEKLARR RALEEELEDL ELGL
	Isoform 2 [UniParc]. Checksum: 67BA3B0E86D8C581	FASTA	203	22,705
	10 20 30 40 50 60 MATPYVTDET GGKYIASTQR PDGTWRKQRR VKEGYVPQEE VPVYENKYVK FFKSKPELPP 70 80 90 100 110 120 GLSPEATAPV TPSRPEGGEP GLSKTAKRNL KRKEKRRQQQ EKGEAEALSR TLDKVSLEET 130 140 150 160 170 180 AQLPSAPQGS RAAPTAASDQ PDSAATTEKA KKIKNLKKKL RQVEELQQRI QAGEVSQPSK 190 200 EQLEKLARRR ALEEELEDLE LGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export." Gatfield D., Izaurralde E. J. Cell Biol. 159:579-588(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: B-cell and Pancreas.
[5]	"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: SUBCELLULAR LOCATION, INTERACTION WITH MAGOH AND RBM8A, RNA-BINDING.
[6]	"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: FUNCTION, SUBCELLULAR LOCATION, DOMAIN EIF2A-LIKE, INTERACTION WITH MAGOH; RBM8A AND RIBOSOME.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-72, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: FUNCTION, INTERACTION WITH MAGOH; RBM8A AND RIBOSOME.
[9]	"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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ459406 mRNA. Translation: CAD30677.1. AK096922 mRNA. Translation: BAC04897.1. AC023055 Genomic DNA. No translation available. AC025162 Genomic DNA. No translation available. BC006135 mRNA. Translation: AAH06135.1. BC014976 mRNA. Translation: AAH14976.1.
IPI	IPI00305092. IPI00790634.
RefSeq	NP_001137325.1. NM_001143853.1. NP_115721.1. NM_032345.2.
UniGene	Hs.505687. Hs.524488.
3D structure databases
ProteinModelPortal	Q9BRP8.
SMR	Q9BRP8. Positions 7-38.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48413N.
IntAct	Q9BRP8. 7 interactions.
MINT	MINT-3060675.
STRING	9606.ENSP00000386156.
PTM databases
PhosphoSite	Q9BRP8.
Polymorphism databases
DMDM	74732911.
Proteomic databases
PaxDb	Q9BRP8.
PRIDE	Q9BRP8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000398213; ENSP00000381271; ENSG00000170473. ENST00000408946; ENSP00000386156; ENSG00000170473.
GeneID	84305.
KEGG	hsa:84305.
UCSC	uc001sie.1. human. uc001sif.1. human.
Organism-specific databases
CTD	84305.
GeneCards	GC12M056295.
HGNC	HGNC:30258. WIBG.
HPA	HPA046200.
neXtProt	NX_Q9BRP8.
PharmGKB	PA142670574.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG114683.
HOGENOM	HOG000215176.
HOVERGEN	HBG097451.
InParanoid	Q9BRP8.
KO	K14294.
OMA	QPSKEQL.
OrthoDB	EOG48GW4M.
PhylomeDB	Q9BRP8.
Gene expression databases
ArrayExpress	Q9BRP8.
Bgee	Q9BRP8.
CleanEx	HS_WIBG.
Genevestigator	Q9BRP8.
Family and domain databases
InterPro	IPR015362. EJC_Pym. [Graphical view]
Pfam	PF09282. Mago-bind. 1 hit. [Graphical view]
SUPFAM	SSF101931. EJC_Pym. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	84305.
NextBio	73984.

Entry information

Entry name

WIBG_HUMAN

Accession

Primary (citable) accession number: Q9BRP8
Secondary accession number(s): B6ZDM5, Q8IXJ8, Q8N8E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 81 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.