Full text data of WIBG
WIBG
(PYM)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Partner of Y14 and mago (Protein wibg homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Partner of Y14 and mago (Protein wibg homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRP8
ID WIBG_HUMAN Reviewed; 204 AA.
AC Q9BRP8; B6ZDM5; Q8IXJ8; Q8N8E7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Partner of Y14 and mago;
DE AltName: Full=Protein wibg homolog;
GN Name=WIBG; Synonyms=PYM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12438415; DOI=10.1083/jcb.200207128;
RA Gatfield D., Izaurralde E.;
RT "REF1/Aly and the additional exon junction complex proteins are
RT dispensable for nuclear mRNA export.";
RL J. Cell Biol. 159:579-588(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH MAGOH AND RBM8A, AND
RP RNA-BINDING.
RX PubMed=14968132; DOI=10.1038/sj.embor.7400091;
RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E.,
RA Conti E.;
RT "Molecular insights into the interaction of PYM with the Mago-Y14 core
RT of the exon junction complex.";
RL EMBO Rep. 5:304-310(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN EIF2A-LIKE, AND INTERACTION
RP WITH MAGOH; RBM8A AND RIBOSOME.
RX PubMed=18026120; DOI=10.1038/nsmb1321;
RA Diem M.D., Chan C.C., Younis I., Dreyfuss G.;
RT "PYM binds the cytoplasmic exon-junction complex and ribosomes to
RT enhance translation of spliced mRNAs.";
RL Nat. Struct. Mol. Biol. 14:1173-1179(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAGOH; RBM8A AND RIBOSOME.
RX PubMed=19410547; DOI=10.1016/j.cell.2009.02.042;
RA Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.;
RT "Disassembly of exon junction complexes by PYM.";
RL Cell 137:536-548(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Key regulator of the exon junction complex (EJC), a
CC multiprotein complex that associates immediately upstream of the
CC exon-exon junction on mRNAs and serves as a positional landmarks
CC for the intron exon structure of genes and directs post-
CC transcriptional processes in the cytoplasm such as mRNA export,
CC nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC
CC disassembly factor, allowing translation-dependent EJC removal and
CC recycling by disrupting mature EJC from spliced mRNAs. Its
CC association with the 40S ribosomal subunit probably prevents a
CC translation-independent disassembly of the EJC from spliced mRNAs,
CC by restricting its activity to mRNAs that have been translated.
CC Interferes with NMD and enhances translation of spliced mRNAs,
CC probably by antagonizing EJC functions. May bind RNA; the
CC relevance of RNA-binding remains unclear in vivo, RNA-binding was
CC detected by PubMed:14968132, while PubMed:19410547 did not detect
CC RNA-binding activity independently of the EJC.
CC -!- SUBUNIT: Interacts (via N-terminus) with MAGOH and RBM8A; the
CC interaction is direct. Associates (eIF2A-like region) with the 40S
CC ribosomal subunit and the 48S preinitiation complex.
CC -!- INTERACTION:
CC Q2HR75:ORF57 (xeno); NbExp=4; IntAct=EBI-2352802, EBI-6884751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus,
CC nucleoplasm. Note=Shuttles between the nucleus and the cytoplasm.
CC Nuclear export is mediated by XPO1/CRM1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRP8-2; Sequence=VSP_025430;
CC -!- DOMAIN: The eIF2A-like region shares sequence similarity with
CC eIF2A and mediates the interaction with the 40S ribosomal subunit
CC and the 48S preinitiation complex.
CC -!- SIMILARITY: Belongs to the wibg family.
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DR EMBL; AJ459406; CAD30677.1; -; mRNA.
DR EMBL; AK096922; BAC04897.1; -; mRNA.
DR EMBL; AC023055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006135; AAH06135.1; -; mRNA.
DR EMBL; BC014976; AAH14976.1; -; mRNA.
DR RefSeq; NP_001137325.1; NM_001143853.1.
DR RefSeq; NP_115721.1; NM_032345.2.
DR UniGene; Hs.505687; -.
DR UniGene; Hs.524488; -.
DR ProteinModelPortal; Q9BRP8; -.
DR SMR; Q9BRP8; 6-38.
DR DIP; DIP-48413N; -.
DR IntAct; Q9BRP8; 8.
DR MINT; MINT-3060675; -.
DR STRING; 9606.ENSP00000386156; -.
DR PhosphoSite; Q9BRP8; -.
DR DMDM; 74732911; -.
DR PaxDb; Q9BRP8; -.
DR PRIDE; Q9BRP8; -.
DR Ensembl; ENST00000398213; ENSP00000381271; ENSG00000170473.
DR Ensembl; ENST00000408946; ENSP00000386156; ENSG00000170473.
DR GeneID; 84305; -.
DR KEGG; hsa:84305; -.
DR UCSC; uc001sif.1; human.
DR CTD; 84305; -.
DR GeneCards; GC12M056295; -.
DR HGNC; HGNC:30258; WIBG.
DR HPA; HPA046200; -.
DR neXtProt; NX_Q9BRP8; -.
DR PharmGKB; PA142670574; -.
DR eggNOG; NOG114683; -.
DR HOGENOM; HOG000215176; -.
DR HOVERGEN; HBG097451; -.
DR InParanoid; Q9BRP8; -.
DR KO; K14294; -.
DR OMA; EVSQPSK; -.
DR OrthoDB; EOG7HMS3N; -.
DR PhylomeDB; Q9BRP8; -.
DR GenomeRNAi; 84305; -.
DR NextBio; 73984; -.
DR PRO; PR:Q9BRP8; -.
DR ArrayExpress; Q9BRP8; -.
DR Bgee; Q9BRP8; -.
DR CleanEx; HS_WIBG; -.
DR Genevestigator; Q9BRP8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR InterPro; IPR015362; EJC_Pym.
DR Pfam; PF09282; Mago-bind; 1.
DR SUPFAM; SSF101931; SSF101931; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1 204 Partner of Y14 and mago.
FT /FTId=PRO_0000287285.
FT REGION 1 33 Required for interaction with MAGOH and
FT RBM8A.
FT REGION 152 204 eIF2A-like.
FT COILED 82 116 Potential.
FT COILED 145 204 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 Phosphoserine.
FT MOD_RES 64 64 Phosphoserine.
FT MOD_RES 72 72 Phosphothreonine.
FT VAR_SEQ 1 12 MEAAGSPAATET -> MATPYVTDETG (in isoform
FT 2).
FT /FTId=VSP_025430.
FT VARIANT 66 66 E -> Q (in dbSNP:rs3802998).
FT /FTId=VAR_032297.
FT CONFLICT 147 147 T -> S (in Ref. 1; CAD30677).
SQ SEQUENCE 204 AA; 22656 MW; 087B901279007C05 CRC64;
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP
PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE
TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS
KEQLEKLARR RALEEELEDL ELGL
//
ID WIBG_HUMAN Reviewed; 204 AA.
AC Q9BRP8; B6ZDM5; Q8IXJ8; Q8N8E7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 85.
DE RecName: Full=Partner of Y14 and mago;
DE AltName: Full=Protein wibg homolog;
GN Name=WIBG; Synonyms=PYM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12438415; DOI=10.1083/jcb.200207128;
RA Gatfield D., Izaurralde E.;
RT "REF1/Aly and the additional exon junction complex proteins are
RT dispensable for nuclear mRNA export.";
RL J. Cell Biol. 159:579-588(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH MAGOH AND RBM8A, AND
RP RNA-BINDING.
RX PubMed=14968132; DOI=10.1038/sj.embor.7400091;
RA Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E.,
RA Conti E.;
RT "Molecular insights into the interaction of PYM with the Mago-Y14 core
RT of the exon junction complex.";
RL EMBO Rep. 5:304-310(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN EIF2A-LIKE, AND INTERACTION
RP WITH MAGOH; RBM8A AND RIBOSOME.
RX PubMed=18026120; DOI=10.1038/nsmb1321;
RA Diem M.D., Chan C.C., Younis I., Dreyfuss G.;
RT "PYM binds the cytoplasmic exon-junction complex and ribosomes to
RT enhance translation of spliced mRNAs.";
RL Nat. Struct. Mol. Biol. 14:1173-1179(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-72, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAGOH; RBM8A AND RIBOSOME.
RX PubMed=19410547; DOI=10.1016/j.cell.2009.02.042;
RA Gehring N.H., Lamprinaki S., Kulozik A.E., Hentze M.W.;
RT "Disassembly of exon junction complexes by PYM.";
RL Cell 137:536-548(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Key regulator of the exon junction complex (EJC), a
CC multiprotein complex that associates immediately upstream of the
CC exon-exon junction on mRNAs and serves as a positional landmarks
CC for the intron exon structure of genes and directs post-
CC transcriptional processes in the cytoplasm such as mRNA export,
CC nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC
CC disassembly factor, allowing translation-dependent EJC removal and
CC recycling by disrupting mature EJC from spliced mRNAs. Its
CC association with the 40S ribosomal subunit probably prevents a
CC translation-independent disassembly of the EJC from spliced mRNAs,
CC by restricting its activity to mRNAs that have been translated.
CC Interferes with NMD and enhances translation of spliced mRNAs,
CC probably by antagonizing EJC functions. May bind RNA; the
CC relevance of RNA-binding remains unclear in vivo, RNA-binding was
CC detected by PubMed:14968132, while PubMed:19410547 did not detect
CC RNA-binding activity independently of the EJC.
CC -!- SUBUNIT: Interacts (via N-terminus) with MAGOH and RBM8A; the
CC interaction is direct. Associates (eIF2A-like region) with the 40S
CC ribosomal subunit and the 48S preinitiation complex.
CC -!- INTERACTION:
CC Q2HR75:ORF57 (xeno); NbExp=4; IntAct=EBI-2352802, EBI-6884751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus,
CC nucleoplasm. Note=Shuttles between the nucleus and the cytoplasm.
CC Nuclear export is mediated by XPO1/CRM1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRP8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRP8-2; Sequence=VSP_025430;
CC -!- DOMAIN: The eIF2A-like region shares sequence similarity with
CC eIF2A and mediates the interaction with the 40S ribosomal subunit
CC and the 48S preinitiation complex.
CC -!- SIMILARITY: Belongs to the wibg family.
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DR EMBL; AJ459406; CAD30677.1; -; mRNA.
DR EMBL; AK096922; BAC04897.1; -; mRNA.
DR EMBL; AC023055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006135; AAH06135.1; -; mRNA.
DR EMBL; BC014976; AAH14976.1; -; mRNA.
DR RefSeq; NP_001137325.1; NM_001143853.1.
DR RefSeq; NP_115721.1; NM_032345.2.
DR UniGene; Hs.505687; -.
DR UniGene; Hs.524488; -.
DR ProteinModelPortal; Q9BRP8; -.
DR SMR; Q9BRP8; 6-38.
DR DIP; DIP-48413N; -.
DR IntAct; Q9BRP8; 8.
DR MINT; MINT-3060675; -.
DR STRING; 9606.ENSP00000386156; -.
DR PhosphoSite; Q9BRP8; -.
DR DMDM; 74732911; -.
DR PaxDb; Q9BRP8; -.
DR PRIDE; Q9BRP8; -.
DR Ensembl; ENST00000398213; ENSP00000381271; ENSG00000170473.
DR Ensembl; ENST00000408946; ENSP00000386156; ENSG00000170473.
DR GeneID; 84305; -.
DR KEGG; hsa:84305; -.
DR UCSC; uc001sif.1; human.
DR CTD; 84305; -.
DR GeneCards; GC12M056295; -.
DR HGNC; HGNC:30258; WIBG.
DR HPA; HPA046200; -.
DR neXtProt; NX_Q9BRP8; -.
DR PharmGKB; PA142670574; -.
DR eggNOG; NOG114683; -.
DR HOGENOM; HOG000215176; -.
DR HOVERGEN; HBG097451; -.
DR InParanoid; Q9BRP8; -.
DR KO; K14294; -.
DR OMA; EVSQPSK; -.
DR OrthoDB; EOG7HMS3N; -.
DR PhylomeDB; Q9BRP8; -.
DR GenomeRNAi; 84305; -.
DR NextBio; 73984; -.
DR PRO; PR:Q9BRP8; -.
DR ArrayExpress; Q9BRP8; -.
DR Bgee; Q9BRP8; -.
DR CleanEx; HS_WIBG; -.
DR Genevestigator; Q9BRP8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR InterPro; IPR015362; EJC_Pym.
DR Pfam; PF09282; Mago-bind; 1.
DR SUPFAM; SSF101931; SSF101931; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding; Translation regulation.
FT CHAIN 1 204 Partner of Y14 and mago.
FT /FTId=PRO_0000287285.
FT REGION 1 33 Required for interaction with MAGOH and
FT RBM8A.
FT REGION 152 204 eIF2A-like.
FT COILED 82 116 Potential.
FT COILED 145 204 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 6 6 Phosphoserine.
FT MOD_RES 64 64 Phosphoserine.
FT MOD_RES 72 72 Phosphothreonine.
FT VAR_SEQ 1 12 MEAAGSPAATET -> MATPYVTDETG (in isoform
FT 2).
FT /FTId=VSP_025430.
FT VARIANT 66 66 E -> Q (in dbSNP:rs3802998).
FT /FTId=VAR_032297.
FT CONFLICT 147 147 T -> S (in Ref. 1; CAD30677).
SQ SEQUENCE 204 AA; 22656 MW; 087B901279007C05 CRC64;
MEAAGSPAAT ETGKYIASTQ RPDGTWRKQR RVKEGYVPQE EVPVYENKYV KFFKSKPELP
PGLSPEATAP VTPSRPEGGE PGLSKTAKRN LKRKEKRRQQ QEKGEAEALS RTLDKVSLEE
TAQLPSAPQG SRAAPTAASD QPDSAATTEK AKKIKNLKKK LRQVEELQQR IQAGEVSQPS
KEQLEKLARR RALEEELEDL ELGL
//