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Q9BRP8

- WIBG_HUMAN

UniProt

Q9BRP8 - WIBG_HUMAN

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Protein

Partner of Y14 and mago

Gene

WIBG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 PubMed:14968132, while PubMed:19410547 did not detect RNA-binding activity independently of the EJC.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. ribosome binding Source: UniProtKB

GO - Biological processi

  1. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  2. positive regulation of translation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Nonsense-mediated mRNA decay, Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Partner of Y14 and mago
Alternative name(s):
Protein wibg homolog
Gene namesi
Name:WIBG
Synonyms:PYM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30258. WIBG.

Subcellular locationi

Cytoplasm. Nucleusnucleolus. Nucleusnucleoplasm
Note: Shuttles between the nucleus and the cytoplasm. Nuclear export is mediated by XPO1/CRM1.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. exon-exon junction complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142670574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Partner of Y14 and magoPRO_0000287285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei64 – 641Phosphoserine1 Publication
Modified residuei72 – 721Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BRP8.
PaxDbiQ9BRP8.
PRIDEiQ9BRP8.

PTM databases

PhosphoSiteiQ9BRP8.

Expressioni

Gene expression databases

BgeeiQ9BRP8.
CleanExiHS_WIBG.
ExpressionAtlasiQ9BRP8. baseline and differential.
GenevestigatoriQ9BRP8.

Organism-specific databases

HPAiHPA046200.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORF57Q2HR754EBI-2352802,EBI-6884751From a different organism.

Protein-protein interaction databases

BioGridi124031. 50 interactions.
DIPiDIP-48413N.
IntActiQ9BRP8. 10 interactions.
MINTiMINT-3060675.
STRINGi9606.ENSP00000386156.

Structurei

3D structure databases

ProteinModelPortaliQ9BRP8.
SMRiQ9BRP8. Positions 6-38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3333Required for interaction with MAGOH and RBM8AAdd
BLAST
Regioni152 – 20453eIF2A-likeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili82 – 11635Sequence AnalysisAdd
BLAST
Coiled coili145 – 20460Sequence AnalysisAdd
BLAST

Domaini

The eIF2A-like region shares sequence similarity with eIF2A and mediates the interaction with the 40S ribosomal subunit and the 48S preinitiation complex.1 Publication

Sequence similaritiesi

Belongs to the wibg family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG114683.
GeneTreeiENSGT00730000111107.
HOGENOMiHOG000215176.
HOVERGENiHBG097451.
InParanoidiQ9BRP8.
KOiK14294.
OMAiQQKIPGC.
OrthoDBiEOG7HMS3N.
PhylomeDBiQ9BRP8.
TreeFamiTF324615.

Family and domain databases

InterProiIPR015362. EJC_Pym.
[Graphical view]
PfamiPF09282. Mago-bind. 1 hit.
[Graphical view]
SUPFAMiSSF101931. SSF101931. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BRP8-1) [UniParc]FASTAAdd to Basket

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

        10         20         30         40         50
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV
60 70 80 90 100
KFFKSKPELP PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ
110 120 130 140 150
QEKGEAEALS RTLDKVSLEE TAQLPSAPQG SRAAPTAASD QPDSAATTEK
160 170 180 190 200
AKKIKNLKKK LRQVEELQQR IQAGEVSQPS KEQLEKLARR RALEEELEDL

ELGL
Length:204
Mass (Da):22,656
Last modified:June 1, 2001 - v1
Checksum:i087B901279007C05
GO
Isoform 2 (identifier: Q9BRP8-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:203
Mass (Da):22,705
Checksum:i67BA3B0E86D8C581
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471T → S in CAD30677. (PubMed:12438415)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti66 – 661E → Q.
Corresponds to variant rs3802998 [ dbSNP | Ensembl ].
VAR_032297

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212MEAAG…AATET → MATPYVTDETG in isoform 2. 1 PublicationVSP_025430Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41795.1. [Q9BRP8-1]
CCDS44916.1. [Q9BRP8-2]
RefSeqiNP_001137325.1. NM_001143853.1. [Q9BRP8-2]
NP_115721.1. NM_032345.2. [Q9BRP8-1]
UniGeneiHs.505687.
Hs.524488.

Genome annotation databases

EnsembliENST00000398213; ENSP00000381271; ENSG00000170473. [Q9BRP8-2]
ENST00000408946; ENSP00000386156; ENSG00000170473. [Q9BRP8-1]
GeneIDi84305.
KEGGihsa:84305.
UCSCiuc001sie.1. human. [Q9BRP8-2]
uc001sif.1. human. [Q9BRP8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41795.1. [Q9BRP8-1 ]
CCDS44916.1. [Q9BRP8-2 ]
RefSeqi NP_001137325.1. NM_001143853.1. [Q9BRP8-2 ]
NP_115721.1. NM_032345.2. [Q9BRP8-1 ]
UniGenei Hs.505687.
Hs.524488.

3D structure databases

ProteinModelPortali Q9BRP8.
SMRi Q9BRP8. Positions 6-38.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124031. 50 interactions.
DIPi DIP-48413N.
IntActi Q9BRP8. 10 interactions.
MINTi MINT-3060675.
STRINGi 9606.ENSP00000386156.

PTM databases

PhosphoSitei Q9BRP8.

Proteomic databases

MaxQBi Q9BRP8.
PaxDbi Q9BRP8.
PRIDEi Q9BRP8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000398213 ; ENSP00000381271 ; ENSG00000170473 . [Q9BRP8-2 ]
ENST00000408946 ; ENSP00000386156 ; ENSG00000170473 . [Q9BRP8-1 ]
GeneIDi 84305.
KEGGi hsa:84305.
UCSCi uc001sie.1. human. [Q9BRP8-2 ]
uc001sif.1. human. [Q9BRP8-1 ]

Organism-specific databases

CTDi 84305.
GeneCardsi GC12M056295.
HGNCi HGNC:30258. WIBG.
HPAi HPA046200.
neXtProti NX_Q9BRP8.
PharmGKBi PA142670574.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG114683.
GeneTreei ENSGT00730000111107.
HOGENOMi HOG000215176.
HOVERGENi HBG097451.
InParanoidi Q9BRP8.
KOi K14294.
OMAi QQKIPGC.
OrthoDBi EOG7HMS3N.
PhylomeDBi Q9BRP8.
TreeFami TF324615.

Miscellaneous databases

ChiTaRSi WIBG. human.
GenomeRNAii 84305.
NextBioi 73984.
PROi Q9BRP8.

Gene expression databases

Bgeei Q9BRP8.
CleanExi HS_WIBG.
ExpressionAtlasi Q9BRP8. baseline and differential.
Genevestigatori Q9BRP8.

Family and domain databases

InterProi IPR015362. EJC_Pym.
[Graphical view ]
Pfami PF09282. Mago-bind. 1 hit.
[Graphical view ]
SUPFAMi SSF101931. SSF101931. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiWIBG_HUMAN
AccessioniPrimary (citable) accession number: Q9BRP8
Secondary accession number(s): B6ZDM5, Q8IXJ8, Q8N8E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 94 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3