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Q9BRP8 (WIBG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Partner of Y14 and mago
Alternative name(s):
Protein wibg homolog
Gene names
Name:WIBG
Synonyms:PYM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceEvidence 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.9 did not detect RNA-binding activity independently of the EJC. Ref.6 Ref.9

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.9

Subcellular location

Cytoplasm. Nucleusnucleolus. Nucleusnucleoplasm. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORF57Q2HR754EBI-2352802,EBI-6884751From a different organism.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Partner of Y14 and mago
PRO_0000287285

Regions

Region1 – 3333Required for interaction with MAGOH and RBM8A
Region152 – 20453eIF2A-like
Coiled coil82 – 11635 Potential
Coiled coil145 – 20460 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.10
Modified residue61Phosphoserine Ref.10
Modified residue641Phosphoserine Ref.7
Modified residue721Phosphothreonine Ref.7

Natural variations

Alternative sequence1 – 1212MEAAG…AATET → MATPYVTDETG in isoform 2.
VSP_025430
Natural variant661E → Q.
Corresponds to variant rs3802998 [ dbSNP | Ensembl ].
VAR_032297

Experimental info

Sequence conflict1471T → S in CAD30677. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 087B901279007C05

FASTA20422,656
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 67BA3B0E86D8C581
Show »

FASTA20322,705

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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.
[10]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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.
RefSeqNP_001137325.1. NM_001143853.1.
NP_115721.1. NM_032345.2.
UniGeneHs.505687.
Hs.524488.

3D structure databases

ProteinModelPortalQ9BRP8.
SMRQ9BRP8. Positions 6-38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124031. 50 interactions.
DIPDIP-48413N.
IntActQ9BRP8. 9 interactions.
MINTMINT-3060675.
STRING9606.ENSP00000386156.

PTM databases

PhosphoSiteQ9BRP8.

Proteomic databases

PaxDbQ9BRP8.
PRIDEQ9BRP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398213; ENSP00000381271; ENSG00000170473. [Q9BRP8-2]
ENST00000408946; ENSP00000386156; ENSG00000170473. [Q9BRP8-1]
GeneID84305.
KEGGhsa:84305.
UCSCuc001sie.1. human. [Q9BRP8-2]
uc001sif.1. human. [Q9BRP8-1]

Organism-specific databases

CTD84305.
GeneCardsGC12M056295.
HGNCHGNC:30258. WIBG.
HPAHPA046200.
neXtProtNX_Q9BRP8.
PharmGKBPA142670574.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG114683.
HOGENOMHOG000215176.
HOVERGENHBG097451.
InParanoidQ9BRP8.
KOK14294.
OMAEVSQPSK.
OrthoDBEOG7HMS3N.
PhylomeDBQ9BRP8.
TreeFamTF324615.

Gene expression databases

ArrayExpressQ9BRP8.
BgeeQ9BRP8.
CleanExHS_WIBG.
GenevestigatorQ9BRP8.

Family and domain databases

InterProIPR015362. EJC_Pym.
[Graphical view]
PfamPF09282. Mago-bind. 1 hit.
[Graphical view]
SUPFAMSSF101931. SSF101931. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi84305.
NextBio73984.
PROQ9BRP8.

Entry information

Entry nameWIBG_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM