Full text data of RBMX
RBMX
(HNRPG, RBMXP1)
[Confidence: low (only semi-automatic identification from reviews)]
RNA-binding motif protein, X chromosome (Glycoprotein p43; Heterogeneous nuclear ribonucleoprotein G; hnRNP G; RNA-binding motif protein, X chromosome, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RNA-binding motif protein, X chromosome (Glycoprotein p43; Heterogeneous nuclear ribonucleoprotein G; hnRNP G; RNA-binding motif protein, X chromosome, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P38159
ID RBMX_HUMAN Reviewed; 391 AA.
AC P38159; B4E3U4; D3DWH0; E9PG86; Q5JQ67; Q8N8Y7; Q969R3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 3.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Glycoprotein p43;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=RBMX; Synonyms=HNRPG, RBMXP1;
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), AND GLYCOSYLATION.
RC TISSUE=Mammary gland;
RX PubMed=7692398; DOI=10.1093/nar/21.18.4210;
RA Soulard M., Della Valle V., Siomi M., Pinol-Roma S., Codogno P.,
RA Bauvy C., Belli M., Lacroix J.-C., Monod G., Dreyfuss G.,
RA Larsen C.-J.;
RT "hnRNP G: sequence and characterization of a glycosylated RNA-binding
RT protein.";
RL Nucleic Acids Res. 21:4210-4217(1993).
RN [2]
RP SEQUENCE REVISION.
RA Venables J.P., Larsen C.-J.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=11420617; DOI=10.1007/s00335001-0003-z;
RA Lingenfelter P.A., Delbridge M.L., Thomas S., Hoekstra H.E.,
RA Mitchell M.J., Graves J.A., Disteche C.M.;
RT "Expression and conservation of processed copies of the RBMX gene.";
RL Mamm. Genome 12:538-545(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lin T.-Y., Chiou S.-H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [9]
RP PROTEIN SEQUENCE OF 1-30; 34-41; 50-63; 81-93; 126-144; 188-195;
RP 204-210; 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1 AND VAL-2, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP INTERACTION WITH KHDRBS3.
RC TISSUE=Testis;
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B.,
RA Wu J., Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [12]
RP FUNCTION, INTERACTION WITH TRA2B, AND RNA-BINDING.
RX PubMed=12165565; DOI=10.1093/hmg/11.17.2037;
RA Hofmann Y., Wirth B.;
RT "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via
RT direct interaction with Htra2-beta1.";
RL Hum. Mol. Genet. 11:2037-2049(2002).
RN [13]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12761049; DOI=10.1093/hmg/ddg136;
RA Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.;
RT "HnRNP G and Tra2beta: opposite effects on splicing matched by
RT antagonism in RNA binding.";
RL Hum. Mol. Genet. 12:1337-1348(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP FUNCTION, MUTAGENESIS OF LYS-22, AND TISSUE SPECIFICITY.
RX PubMed=16707624; DOI=10.1158/1078-0432.CCR-05-2656;
RA Shin K.H., Kang M.K., Kim R.H., Christensen R., Park N.H.;
RT "Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive
RT effect against oral squamous cell carcinoma cells.";
RL Clin. Cancer Res. 12:3222-3228(2006).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; NCOA5 AND
RP PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [17]
RP FUNCTION, AND INTERACTION WITH ERAP1.
RX PubMed=18445477; DOI=10.1016/j.bbrc.2008.04.103;
RA Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.;
RT "An association between RBMX, a heterogeneous nuclear
RT ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release.";
RL Biochem. Biophys. Res. Commun. 371:505-509(2008).
RN [18]
RP FUNCTION, CHROMATIN ASSOCIATION, AND MUTAGENESIS OF LYS-22.
RX PubMed=18541147; DOI=10.1016/j.bbrc.2008.05.175;
RA Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.;
RT "hnRNP G elicits tumor-suppressive activity in part by upregulating
RT the expression of Txnip.";
RL Biochem. Biophys. Res. Commun. 372:880-885(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-329 AND SER-332,
RP AND MASS 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 [20]
RP FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX, INTERACTION
RP WITH CLK2; KHDRBS2; SAFB; TRA2B AND YTHDC1, AND SUBCELLULAR LOCATION.
RX PubMed=19282290; DOI=10.1074/jbc.M901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N.,
RA Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H.,
RA Sperling J., Sperling R., Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site
RT selection by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=21327109; DOI=10.4161/nucl.1.1.10857;
RA Kanhoush R., Beenders B., Perrin C., Moreau J., Bellini M.,
RA Penrad-Mobayed M.;
RT "Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA
RT binding and targeting nascent transcripts.";
RL Nucleus 1:109-122(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-352, AND MASS
RP 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 [25]
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).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-332 AND SER-352,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: RNA-binding protein that plays several role in the
CC regulation of pre- and post-transcriptional processes. Implicated
CC in tissue-specific regulation of gene transcription and
CC alternative splicing of several pre-mRNAs. Binds to and stimulates
CC transcription from the tumor suppressor TXNIP gene promoter; may
CC thus be involved in tumor suppression. When associated with SAFB,
CC binds to and stimulates transcription from the SREBF1 promoter.
CC Associates with nascent mRNAs transcribed by RNA polymerase II.
CC Component of the supraspliceosome complex that regulates pre-mRNA
CC alternative splice site selection. Can either activate or suppress
CC exon inclusion; acts additively with TRA2B to promote exon 7
CC inclusion of the survival motor neuron SMN2. Represses the
CC splicing of MAPT/Tau exon 10. Binds preferentially to single-
CC stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
CC single-stranded conformation; probably binds RNA as a homodimer.
CC Binds non-specifically to pre-mRNAs. Plays also a role in the
CC cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-
CC beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains
CC and the release of TNFR1 exosome-like vesicles to the
CC extracellular compartment.
CC -!- SUBUNIT: Homomultimer. Interacts with SAFB/SAFB1 (By similarity).
CC Found in the supraspliceosome complex. Identified in the
CC spliceosome C complex. Interacts with KHDRBS3. Forms a complex
CC with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with
CC CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the
CC interaction is RNA-independent.
CC -!- INTERACTION:
CC P61978:HNRNPK; NbExp=3; IntAct=EBI-743526, EBI-304185;
CC Q5VWX1:KHDRBS2; NbExp=2; IntAct=EBI-743526, EBI-742808;
CC Q9JKL7:Srek1 (xeno); NbExp=3; IntAct=EBI-743526, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC Localizes in numerous small granules in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P38159-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P38159-2; Sequence=VSP_042203;
CC Name=3;
CC IsoId=P38159-3; Sequence=VSP_043650, VSP_043651;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed strongly in oral keratinocytes, but
CC only weakly detected in oral squamous cell carcinomas (at protein
CC level).
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for
CC splice site selection, indicating that its splicing activity does
CC not require direct binding to RNA (By similarity).
CC -!- PTM: O-glycosylated.
CC -!- PTM: Arg-185 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Cleavage of initiator Met is partial. If Met-1 is not
CC removed, it is acetylated. If it is removed, Val-2 is acetylated.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; Z23064; CAA80599.1; -; mRNA.
DR EMBL; AF266723; AAK58567.1; -; Genomic_DNA.
DR EMBL; AF266720; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AF266721; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AF266722; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AY464692; AAR28036.1; -; mRNA.
DR EMBL; AK096015; BAC04674.1; -; mRNA.
DR EMBL; AK304868; BAG65606.1; -; mRNA.
DR EMBL; AL683813; CAI39448.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88453.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88454.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88455.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88457.1; -; Genomic_DNA.
DR EMBL; BC006550; AAH06550.1; -; mRNA.
DR EMBL; BC007435; AAH07435.1; -; mRNA.
DR RefSeq; NP_001158275.1; NM_001164803.1.
DR RefSeq; NP_002130.2; NM_002139.3.
DR UniGene; Hs.380118; -.
DR UniGene; Hs.710162; -.
DR ProteinModelPortal; P38159; -.
DR SMR; P38159; 1-105.
DR DIP; DIP-34447N; -.
DR IntAct; P38159; 45.
DR MINT; MINT-5000999; -.
DR STRING; 9606.ENSP00000359645; -.
DR PhosphoSite; P38159; -.
DR DMDM; 23503093; -.
DR SWISS-2DPAGE; P38159; -.
DR PaxDb; P38159; -.
DR PRIDE; P38159; -.
DR DNASU; 27316; -.
DR Ensembl; ENST00000320676; ENSP00000359645; ENSG00000147274.
DR Ensembl; ENST00000431446; ENSP00000411989; ENSG00000147274.
DR GeneID; 27316; -.
DR KEGG; hsa:27316; -.
DR UCSC; uc004fae.2; human.
DR CTD; 27316; -.
DR GeneCards; GC0XM135951; -.
DR HGNC; HGNC:9910; RBMX.
DR MIM; 300199; gene.
DR neXtProt; NX_P38159; -.
DR PharmGKB; PA34277; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000070250; -.
DR HOVERGEN; HBG063314; -.
DR InParanoid; P38159; -.
DR KO; K12885; -.
DR OMA; GMARSRY; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; P38159; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RBMX; human.
DR GeneWiki; RBMX; -.
DR GenomeRNAi; 27316; -.
DR NextBio; 50322; -.
DR PRO; PR:P38159; -.
DR ArrayExpress; P38159; -.
DR Bgee; P38159; -.
DR CleanEx; HS_RBMX; -.
DR Genevestigator; P38159; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Glycoprotein; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
KW Tumor suppressor.
FT CHAIN 1 391 RNA-binding motif protein, X chromosome.
FT /FTId=PRO_0000081854.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 391 RNA-binding motif protein, X chromosome,
FT N-terminally processed.
FT /FTId=PRO_0000304582.
FT DOMAIN 8 86 RRM.
FT REGION 186 236 Necessary for the association to nascent
FT RNAPII transcripts and nuclear
FT localization.
FT REGION 333 391 Necessary for RNA-binding.
FT MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein G; alternate.
FT MOD_RES 2 2 N-acetylvaline; in Heterogeneous nuclear
FT ribonucleoprotein G, N-terminally
FT processed.
FT MOD_RES 30 30 N6-acetyllysine.
FT MOD_RES 88 88 Phosphoserine.
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT MOD_RES 352 352 Phosphoserine.
FT VAR_SEQ 45 57 Missing (in isoform 2).
FT /FTId=VSP_042203.
FT VAR_SEQ 73 196 SLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGR
FT GGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPP
FT PRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPR
FT R -> LLYHVEEIVMEVHLEGNRCPLVEMFICPQEMMGILL
FT KTAIQAEITQVLVILEIMHHHHEIILTVIMVIPVHVMTIHQ
FT EDIAIEMDMVVIVTIQIIQVEVPTEIHMRVMVGDFAHYGRG
FT VLIDSQ (in isoform 3).
FT /FTId=VSP_043650.
FT VAR_SEQ 197 391 Missing (in isoform 3).
FT /FTId=VSP_043651.
FT MUTAGEN 22 22 K->A: Promotes cell proliferation.
FT Inhibits transcriptional up-regulation of
FT the TXNIP promoter.
FT CONFLICT 259 259 G -> E (in Ref. 1; CAA80599).
SQ SEQUENCE 391 AA; 42332 MW; 904FEB9BFC573546 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR
APVSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP
RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y
//
ID RBMX_HUMAN Reviewed; 391 AA.
AC P38159; B4E3U4; D3DWH0; E9PG86; Q5JQ67; Q8N8Y7; Q969R3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 3.
DT 22-JAN-2014, entry version 155.
DE RecName: Full=RNA-binding motif protein, X chromosome;
DE AltName: Full=Glycoprotein p43;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
DE Short=hnRNP G;
DE Contains:
DE RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
GN Name=RBMX; Synonyms=HNRPG, RBMXP1;
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), AND GLYCOSYLATION.
RC TISSUE=Mammary gland;
RX PubMed=7692398; DOI=10.1093/nar/21.18.4210;
RA Soulard M., Della Valle V., Siomi M., Pinol-Roma S., Codogno P.,
RA Bauvy C., Belli M., Lacroix J.-C., Monod G., Dreyfuss G.,
RA Larsen C.-J.;
RT "hnRNP G: sequence and characterization of a glycosylated RNA-binding
RT protein.";
RL Nucleic Acids Res. 21:4210-4217(1993).
RN [2]
RP SEQUENCE REVISION.
RA Venables J.P., Larsen C.-J.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=11420617; DOI=10.1007/s00335001-0003-z;
RA Lingenfelter P.A., Delbridge M.L., Thomas S., Hoekstra H.E.,
RA Mitchell M.J., Graves J.A., Disteche C.M.;
RT "Expression and conservation of processed copies of the RBMX gene.";
RL Mamm. Genome 12:538-545(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lin T.-Y., Chiou S.-H.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Kidney, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [9]
RP PROTEIN SEQUENCE OF 1-30; 34-41; 50-63; 81-93; 126-144; 188-195;
RP 204-210; 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT MET-1 AND VAL-2, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [10]
RP INTERACTION WITH KHDRBS3.
RC TISSUE=Testis;
RX PubMed=10332027; DOI=10.1093/hmg/8.6.959;
RA Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B.,
RA Wu J., Cooke H.J., Artzt K., Eperon I.C.;
RT "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
RT binding protein implicated in spermatogenesis.";
RL Hum. Mol. Genet. 8:959-969(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL C COMPLEX.
RX PubMed=11991638; DOI=10.1017/S1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [12]
RP FUNCTION, INTERACTION WITH TRA2B, AND RNA-BINDING.
RX PubMed=12165565; DOI=10.1093/hmg/11.17.2037;
RA Hofmann Y., Wirth B.;
RT "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via
RT direct interaction with Htra2-beta1.";
RL Hum. Mol. Genet. 11:2037-2049(2002).
RN [13]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12761049; DOI=10.1093/hmg/ddg136;
RA Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.;
RT "HnRNP G and Tra2beta: opposite effects on splicing matched by
RT antagonism in RNA binding.";
RL Hum. Mol. Genet. 12:1337-1348(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP FUNCTION, MUTAGENESIS OF LYS-22, AND TISSUE SPECIFICITY.
RX PubMed=16707624; DOI=10.1158/1078-0432.CCR-05-2656;
RA Shin K.H., Kang M.K., Kim R.H., Christensen R., Park N.H.;
RT "Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive
RT effect against oral squamous cell carcinoma cells.";
RL Clin. Cancer Res. 12:3222-3228(2006).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; NCOA5 AND
RP PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [17]
RP FUNCTION, AND INTERACTION WITH ERAP1.
RX PubMed=18445477; DOI=10.1016/j.bbrc.2008.04.103;
RA Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.;
RT "An association between RBMX, a heterogeneous nuclear
RT ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release.";
RL Biochem. Biophys. Res. Commun. 371:505-509(2008).
RN [18]
RP FUNCTION, CHROMATIN ASSOCIATION, AND MUTAGENESIS OF LYS-22.
RX PubMed=18541147; DOI=10.1016/j.bbrc.2008.05.175;
RA Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.;
RT "hnRNP G elicits tumor-suppressive activity in part by upregulating
RT the expression of Txnip.";
RL Biochem. Biophys. Res. Commun. 372:880-885(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-329 AND SER-332,
RP AND MASS 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 [20]
RP FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX, INTERACTION
RP WITH CLK2; KHDRBS2; SAFB; TRA2B AND YTHDC1, AND SUBCELLULAR LOCATION.
RX PubMed=19282290; DOI=10.1074/jbc.M901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N.,
RA Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H.,
RA Sperling J., Sperling R., Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site
RT selection by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=21327109; DOI=10.4161/nucl.1.1.10857;
RA Kanhoush R., Beenders B., Perrin C., Moreau J., Bellini M.,
RA Penrad-Mobayed M.;
RT "Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA
RT binding and targeting nascent transcripts.";
RL Nucleus 1:109-122(2010).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-352, AND MASS
RP 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 [25]
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).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-332 AND SER-352,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: RNA-binding protein that plays several role in the
CC regulation of pre- and post-transcriptional processes. Implicated
CC in tissue-specific regulation of gene transcription and
CC alternative splicing of several pre-mRNAs. Binds to and stimulates
CC transcription from the tumor suppressor TXNIP gene promoter; may
CC thus be involved in tumor suppression. When associated with SAFB,
CC binds to and stimulates transcription from the SREBF1 promoter.
CC Associates with nascent mRNAs transcribed by RNA polymerase II.
CC Component of the supraspliceosome complex that regulates pre-mRNA
CC alternative splice site selection. Can either activate or suppress
CC exon inclusion; acts additively with TRA2B to promote exon 7
CC inclusion of the survival motor neuron SMN2. Represses the
CC splicing of MAPT/Tau exon 10. Binds preferentially to single-
CC stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
CC single-stranded conformation; probably binds RNA as a homodimer.
CC Binds non-specifically to pre-mRNAs. Plays also a role in the
CC cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-
CC beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains
CC and the release of TNFR1 exosome-like vesicles to the
CC extracellular compartment.
CC -!- SUBUNIT: Homomultimer. Interacts with SAFB/SAFB1 (By similarity).
CC Found in the supraspliceosome complex. Identified in the
CC spliceosome C complex. Interacts with KHDRBS3. Forms a complex
CC with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with
CC CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the
CC interaction is RNA-independent.
CC -!- INTERACTION:
CC P61978:HNRNPK; NbExp=3; IntAct=EBI-743526, EBI-304185;
CC Q5VWX1:KHDRBS2; NbExp=2; IntAct=EBI-743526, EBI-742808;
CC Q9JKL7:Srek1 (xeno); NbExp=3; IntAct=EBI-743526, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Component of ribonucleosomes.
CC Localizes in numerous small granules in the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P38159-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P38159-2; Sequence=VSP_042203;
CC Name=3;
CC IsoId=P38159-3; Sequence=VSP_043650, VSP_043651;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed strongly in oral keratinocytes, but
CC only weakly detected in oral squamous cell carcinomas (at protein
CC level).
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for
CC splice site selection, indicating that its splicing activity does
CC not require direct binding to RNA (By similarity).
CC -!- PTM: O-glycosylated.
CC -!- PTM: Arg-185 is dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Cleavage of initiator Met is partial. If Met-1 is not
CC removed, it is acetylated. If it is removed, Val-2 is acetylated.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
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DR EMBL; Z23064; CAA80599.1; -; mRNA.
DR EMBL; AF266723; AAK58567.1; -; Genomic_DNA.
DR EMBL; AF266720; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AF266721; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AF266722; AAK58567.1; JOINED; Genomic_DNA.
DR EMBL; AY464692; AAR28036.1; -; mRNA.
DR EMBL; AK096015; BAC04674.1; -; mRNA.
DR EMBL; AK304868; BAG65606.1; -; mRNA.
DR EMBL; AL683813; CAI39448.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88453.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88454.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88455.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88457.1; -; Genomic_DNA.
DR EMBL; BC006550; AAH06550.1; -; mRNA.
DR EMBL; BC007435; AAH07435.1; -; mRNA.
DR RefSeq; NP_001158275.1; NM_001164803.1.
DR RefSeq; NP_002130.2; NM_002139.3.
DR UniGene; Hs.380118; -.
DR UniGene; Hs.710162; -.
DR ProteinModelPortal; P38159; -.
DR SMR; P38159; 1-105.
DR DIP; DIP-34447N; -.
DR IntAct; P38159; 45.
DR MINT; MINT-5000999; -.
DR STRING; 9606.ENSP00000359645; -.
DR PhosphoSite; P38159; -.
DR DMDM; 23503093; -.
DR SWISS-2DPAGE; P38159; -.
DR PaxDb; P38159; -.
DR PRIDE; P38159; -.
DR DNASU; 27316; -.
DR Ensembl; ENST00000320676; ENSP00000359645; ENSG00000147274.
DR Ensembl; ENST00000431446; ENSP00000411989; ENSG00000147274.
DR GeneID; 27316; -.
DR KEGG; hsa:27316; -.
DR UCSC; uc004fae.2; human.
DR CTD; 27316; -.
DR GeneCards; GC0XM135951; -.
DR HGNC; HGNC:9910; RBMX.
DR MIM; 300199; gene.
DR neXtProt; NX_P38159; -.
DR PharmGKB; PA34277; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000070250; -.
DR HOVERGEN; HBG063314; -.
DR InParanoid; P38159; -.
DR KO; K12885; -.
DR OMA; GMARSRY; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; P38159; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RBMX; human.
DR GeneWiki; RBMX; -.
DR GenomeRNAi; 27316; -.
DR NextBio; 50322; -.
DR PRO; PR:P38159; -.
DR ArrayExpress; P38159; -.
DR Bgee; P38159; -.
DR CleanEx; HS_RBMX; -.
DR Genevestigator; P38159; -.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Glycoprotein; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
KW Tumor suppressor.
FT CHAIN 1 391 RNA-binding motif protein, X chromosome.
FT /FTId=PRO_0000081854.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 391 RNA-binding motif protein, X chromosome,
FT N-terminally processed.
FT /FTId=PRO_0000304582.
FT DOMAIN 8 86 RRM.
FT REGION 186 236 Necessary for the association to nascent
FT RNAPII transcripts and nuclear
FT localization.
FT REGION 333 391 Necessary for RNA-binding.
FT MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
FT nuclear ribonucleoprotein G; alternate.
FT MOD_RES 2 2 N-acetylvaline; in Heterogeneous nuclear
FT ribonucleoprotein G, N-terminally
FT processed.
FT MOD_RES 30 30 N6-acetyllysine.
FT MOD_RES 88 88 Phosphoserine.
FT MOD_RES 329 329 Phosphoserine.
FT MOD_RES 332 332 Phosphoserine.
FT MOD_RES 352 352 Phosphoserine.
FT VAR_SEQ 45 57 Missing (in isoform 2).
FT /FTId=VSP_042203.
FT VAR_SEQ 73 196 SLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGR
FT GGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPP
FT PRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPR
FT R -> LLYHVEEIVMEVHLEGNRCPLVEMFICPQEMMGILL
FT KTAIQAEITQVLVILEIMHHHHEIILTVIMVIPVHVMTIHQ
FT EDIAIEMDMVVIVTIQIIQVEVPTEIHMRVMVGDFAHYGRG
FT VLIDSQ (in isoform 3).
FT /FTId=VSP_043650.
FT VAR_SEQ 197 391 Missing (in isoform 3).
FT /FTId=VSP_043651.
FT MUTAGEN 22 22 K->A: Promotes cell proliferation.
FT Inhibits transcriptional up-regulation of
FT the TXNIP promoter.
FT CONFLICT 259 259 G -> E (in Ref. 1; CAA80599).
SQ SEQUENCE 391 AA; 42332 MW; 904FEB9BFC573546 CRC64;
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA
DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGRGGSGGTR
GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR
APVSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD
YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP
PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP
RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y
//
MIM
300199
*RECORD*
*FIELD* NO
300199
*FIELD* TI
*300199 RNA-BINDING MOTIF PROTEIN, X CHROMOSOME; RBMX
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN G; HNRNPG
read moreRNA-BINDING MOTIF PROTEIN, X CHROMOSOME, RETROGENE, INCLUDED; RBMXRT,
INCLUDED;;
RNA-BINDING MOTIF PROTEIN, X CHROMOSOME, PSEUDOGENE 1, INCLUDED; RBMXP1,
INCLUDED
*FIELD* TX
CLONING
Le Coniat et al. (1992) cloned a cDNA encoding a nuclear 43-kD
glycoprotein, identified as the G hnRNP protein. They designated the
gene HNRPG. The HNRPG cDNA has 60% homology with RBMY1A1.
Mazeyrat et al. (1999) isolated and sequenced 2 Rbmx mouse cDNA clones,
which they named Rbmx1 and Rbmx2, with distinct 3-prime ends. RT-PCR
showed that both Rbmx transcripts are ubiquitously expressed. Mazeyrat
et al. (1999) concluded that, based on the absence of intronic sequence,
the mouse Hnrpg gene is a retroposon derived from Rbmx.
GENE FUNCTION
The genes on the human Y chromosome fall into 2 classes with distinct
evolutionary origins. Widely expressed, single-copy genes with X
homologs that escape inactivation (X-Y shared genes) derive from the
ancient proto X-Y chromosome pair. Testis-specific, multicopy genes with
no X homologs originate from autosomes and have accumulated on a
'selfish Y' because of their male-specific function. Copies of genes in
the RBMY gene family (see RBMY1A1, 400006) are candidate spermatogenesis
genes because they are found in all 3 azoospermia factor (AZF) deletion
intervals on the human Yq, which are associated with oligospermia or
azoospermia (Vogt et al., 1997). An active X-borne homolog of the
Y-borne RBMY gene was demonstrated in humans and marsupials by Delbridge
et al. (1999) and in the mouse by Mazeyrat et al. (1999). Delbridge et
al. (1999) stated that, like other gene pairs on the X and Y chromosomes
(e.g., DFFRX/DFFRY; see 400005), RBMX retained a widespread function and
RBMY evolved a male-specific function in spermatogenesis. Thus, RBMY1A1,
far from belonging to a 'second class' of testis-specific elements, is a
diverged X-Y shared gene.
Venables et al. (2000) used a yeast 2-hybrid system to show that the
RBMY gene product hnRNPG and a novel testis-specific relative (termed
hnRNPG-T) interact with Tra2-beta (TRA2B; 602719), an activator of
pre-mRNA splicing that is ubiquitous but highly expressed in testis. The
RBMY gene product and Tra2-beta colocalized in 2 major domains in human
spermatocyte nuclei. Incubation with the protein interaction domain of
the RBMY gene product inhibited splicing in vitro of a specific pre-mRNA
substrate containing an essential enhancer bound by Tra2-beta. The
RNA-binding domain of RBM affected 5-prime splice site selection. The
authors concluded that the hnRNPG family of proteins is involved in
pre-mRNA splicing and hypothesized that RBM may be involved in
Tra2-beta-dependent splicing in spermatocytes.
Using in vivo splicing assays, Hofmann and Wirth (2002) identified
hnRNPG and its paralog RBM as splicing factors that promoted the
inclusion of SMN2 (601627) exon 7. Both hnRNPG and RBM nonspecifically
bound RNA, but directly and specifically bound Htra2-beta1, an SR-like
splicing factor which stimulates inclusion of exon 7 through a direct
interaction with SMN2 exon 7 pre-mRNA. Using deletion mutants of hnRNPG,
the authors demonstrated a specific protein-protein interaction of
hnRNPG with Htra2-beta1, which mediated the inclusion of SMN2 exon 7
rather than the nonspecific interaction of hnRNPG with SMN pre-mRNA.
These trans-acting splicing factors were also effective on endogenous
SMN2 transcripts and increased the endogenous SMN protein level. The
authors presented a model of how exon 7 mRNA processing may be regulated
by these splicing factors.
Nasim et al. (2003) showed that HNRNPG and the splicing activator
protein TRA2B have opposite effects upon the incorporation of several
exons, and that both are capable of acting as either an activator or a
repressor. HNRNPG acts via a specific sequence to repress the skeletal
muscle-specific exon (SK) of human slow skeletal alpha-tropomyosin
(TPM3; 191030), and stimulates inclusion of the alternative nonmuscle
exon. The binding of HNRNPG to the exon is antagonized by TRA2B. The 2
proteins also have opposite effects upon a dystrophin (300377)
pseudoexon. This exon was incorporated to a higher level in patient
heart muscle than skeletal muscle, causing X-linked dilated
cardiomyopathy. Cotransfection with HNRNPG repressed incorporation in
cardiac myoblasts, whereas TRA2B increased it in skeletal myoblasts. The
authors proposed that the HNRNPG/TRA2B ratio may contribute to cellular
splicing preferences, and that the higher proportion of HNRNPG in
skeletal muscle may play a role in preventing the incorporation of the
pseudoexon and thus in preventing skeletal muscle dystrophy.
MAPPING
Delbridge et al. (1999) mapped the RBMX gene to human Xq26 by FISH. By
PCR analysis of human/mouse hybrid cell lines, Mazeyrat et al. (1999)
demonstrated mapping of the HNRPG-homologous structural gene to the
human X chromosome. By FISH, they mapped the mouse Rbmx gene to XA3-XA5,
a region sharing homology of synteny with human Xq26. Mazeyrat et al.
(1999) localized the Hnrpg retroposon, which they renamed Rbmxrt, to
mouse chromosome 14.
- PSEUDOGENES
Le Coniat et al. (1992) had mapped the HNRPG gene to chromosome 6p12 by
radioactive in situ hybridization. Delbridge et al. (1999) found that
the HNRPG locus on 6p12 represents a processed pseudogene and considered
it likely that this and other intronless copies with nucleotide homology
to the HNRPG cDNA on chromosomes 1, 4, 9, 11, and the X chromosome were
derived by retrotransposition from RBMY-like sequence on the human X
chromosome. They suggested that the erroneous localization of the HNRPG
cDNA probably occurred because of the preferential hybridization of the
cDNA clone to the processed pseudogene on chromosome 6. Delbridge et al.
(1999) proposed that the HNRPG locus be renamed RBMXP1.
*FIELD* RF
1. Delbridge, M. L.; Lingenfelter, P. A.; Disteche, C. M.; Marshall
Graves, J. A.: The candidate spermatogenesis gene RBMY has a homologue
on the human X chromosome. (Letter) Nature Genet. 22: 223-224, 1999.
2. Hofmann, Y.; Wirth, B.: hnRNP-G promotes exon 7 inclusion of survival
motor neuron (SMN) via direct interaction with Htra2-beta1. Hum.
Molec. Genet. 11: 2037-2049, 2002.
3. Le Coniat, M.; Soulard, M.; Della Valle, V.; Larsen, C.-J.; Berger,
R.: Localization of the human gene encoding heterogeneous nuclear
RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12. Hum. Genet. 88:
593-595, 1992.
4. Mazeyrat, S.; Saut, N.; Mattei, M.-G.; Mitchell, M. J.: RBMY evolved
on the Y chromosome from a ubiquitously transcribed X-Y identical
gene. (Letter) Nature Genet. 22: 224-226, 1999.
5. Nasim, M. T.; Chernova, T. K.; Chowdhury, H. M.; Yue, B.-G.; Eperon,
I. C.: HnRNP G and Tra2-beta: opposite effects on splicing matched
by antagonism in RNA binding. Hum. Molec. Genet. 12: 1337-1348,
2003. Note: Erratum: Hum. Molec. Genet. 12: 1941 only, 2003.
6. Venables, J. P.; Elliott, D. J.; Makarova, O. V.; Makarov, E. M.;
Cooke, H. J.; Eperon, I. C.: RBMY, a probable human spermatogenesis
factor, and other hnRNP G proteins interact with Tra2-beta and affect
splicing. Hum. Molec. Genet. 9: 685-694, 2000.
7. Vogt, P. H.; Affara, N.; Davey, P.; Hammer, M.; Jobling, M. A.;
Lau, Y. F.; Mitchell, M.; Schempp, W.; Tyler-Smith, C.; Williams,
G.; Yen, P.; Rappold, G. A: Report of the Third International Workshop
on Y Chromosome Mapping 1997. Heidelberg, Germany, April 13-16, 1997. Cytogenet.
Cell Genet. 79: 1-20, 1997.
*FIELD* CN
George E. Tiller - updated: 3/11/2005
George E. Tiller - updated: 7/11/2003
George E. Tiller - updated: 4/18/2000
Anne M. Lopez - updated: 6/30/1999
*FIELD* CD
Victor A. McKusick: 6/29/1999
*FIELD* ED
terry: 04/04/2013
alopez: 3/11/2005
cwells: 7/11/2003
alopez: 4/18/2000
alopez: 2/21/2000
carol: 7/1/1999
carol: 6/30/1999
alopez: 6/29/1999
*RECORD*
*FIELD* NO
300199
*FIELD* TI
*300199 RNA-BINDING MOTIF PROTEIN, X CHROMOSOME; RBMX
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN G; HNRNPG
read moreRNA-BINDING MOTIF PROTEIN, X CHROMOSOME, RETROGENE, INCLUDED; RBMXRT,
INCLUDED;;
RNA-BINDING MOTIF PROTEIN, X CHROMOSOME, PSEUDOGENE 1, INCLUDED; RBMXP1,
INCLUDED
*FIELD* TX
CLONING
Le Coniat et al. (1992) cloned a cDNA encoding a nuclear 43-kD
glycoprotein, identified as the G hnRNP protein. They designated the
gene HNRPG. The HNRPG cDNA has 60% homology with RBMY1A1.
Mazeyrat et al. (1999) isolated and sequenced 2 Rbmx mouse cDNA clones,
which they named Rbmx1 and Rbmx2, with distinct 3-prime ends. RT-PCR
showed that both Rbmx transcripts are ubiquitously expressed. Mazeyrat
et al. (1999) concluded that, based on the absence of intronic sequence,
the mouse Hnrpg gene is a retroposon derived from Rbmx.
GENE FUNCTION
The genes on the human Y chromosome fall into 2 classes with distinct
evolutionary origins. Widely expressed, single-copy genes with X
homologs that escape inactivation (X-Y shared genes) derive from the
ancient proto X-Y chromosome pair. Testis-specific, multicopy genes with
no X homologs originate from autosomes and have accumulated on a
'selfish Y' because of their male-specific function. Copies of genes in
the RBMY gene family (see RBMY1A1, 400006) are candidate spermatogenesis
genes because they are found in all 3 azoospermia factor (AZF) deletion
intervals on the human Yq, which are associated with oligospermia or
azoospermia (Vogt et al., 1997). An active X-borne homolog of the
Y-borne RBMY gene was demonstrated in humans and marsupials by Delbridge
et al. (1999) and in the mouse by Mazeyrat et al. (1999). Delbridge et
al. (1999) stated that, like other gene pairs on the X and Y chromosomes
(e.g., DFFRX/DFFRY; see 400005), RBMX retained a widespread function and
RBMY evolved a male-specific function in spermatogenesis. Thus, RBMY1A1,
far from belonging to a 'second class' of testis-specific elements, is a
diverged X-Y shared gene.
Venables et al. (2000) used a yeast 2-hybrid system to show that the
RBMY gene product hnRNPG and a novel testis-specific relative (termed
hnRNPG-T) interact with Tra2-beta (TRA2B; 602719), an activator of
pre-mRNA splicing that is ubiquitous but highly expressed in testis. The
RBMY gene product and Tra2-beta colocalized in 2 major domains in human
spermatocyte nuclei. Incubation with the protein interaction domain of
the RBMY gene product inhibited splicing in vitro of a specific pre-mRNA
substrate containing an essential enhancer bound by Tra2-beta. The
RNA-binding domain of RBM affected 5-prime splice site selection. The
authors concluded that the hnRNPG family of proteins is involved in
pre-mRNA splicing and hypothesized that RBM may be involved in
Tra2-beta-dependent splicing in spermatocytes.
Using in vivo splicing assays, Hofmann and Wirth (2002) identified
hnRNPG and its paralog RBM as splicing factors that promoted the
inclusion of SMN2 (601627) exon 7. Both hnRNPG and RBM nonspecifically
bound RNA, but directly and specifically bound Htra2-beta1, an SR-like
splicing factor which stimulates inclusion of exon 7 through a direct
interaction with SMN2 exon 7 pre-mRNA. Using deletion mutants of hnRNPG,
the authors demonstrated a specific protein-protein interaction of
hnRNPG with Htra2-beta1, which mediated the inclusion of SMN2 exon 7
rather than the nonspecific interaction of hnRNPG with SMN pre-mRNA.
These trans-acting splicing factors were also effective on endogenous
SMN2 transcripts and increased the endogenous SMN protein level. The
authors presented a model of how exon 7 mRNA processing may be regulated
by these splicing factors.
Nasim et al. (2003) showed that HNRNPG and the splicing activator
protein TRA2B have opposite effects upon the incorporation of several
exons, and that both are capable of acting as either an activator or a
repressor. HNRNPG acts via a specific sequence to repress the skeletal
muscle-specific exon (SK) of human slow skeletal alpha-tropomyosin
(TPM3; 191030), and stimulates inclusion of the alternative nonmuscle
exon. The binding of HNRNPG to the exon is antagonized by TRA2B. The 2
proteins also have opposite effects upon a dystrophin (300377)
pseudoexon. This exon was incorporated to a higher level in patient
heart muscle than skeletal muscle, causing X-linked dilated
cardiomyopathy. Cotransfection with HNRNPG repressed incorporation in
cardiac myoblasts, whereas TRA2B increased it in skeletal myoblasts. The
authors proposed that the HNRNPG/TRA2B ratio may contribute to cellular
splicing preferences, and that the higher proportion of HNRNPG in
skeletal muscle may play a role in preventing the incorporation of the
pseudoexon and thus in preventing skeletal muscle dystrophy.
MAPPING
Delbridge et al. (1999) mapped the RBMX gene to human Xq26 by FISH. By
PCR analysis of human/mouse hybrid cell lines, Mazeyrat et al. (1999)
demonstrated mapping of the HNRPG-homologous structural gene to the
human X chromosome. By FISH, they mapped the mouse Rbmx gene to XA3-XA5,
a region sharing homology of synteny with human Xq26. Mazeyrat et al.
(1999) localized the Hnrpg retroposon, which they renamed Rbmxrt, to
mouse chromosome 14.
- PSEUDOGENES
Le Coniat et al. (1992) had mapped the HNRPG gene to chromosome 6p12 by
radioactive in situ hybridization. Delbridge et al. (1999) found that
the HNRPG locus on 6p12 represents a processed pseudogene and considered
it likely that this and other intronless copies with nucleotide homology
to the HNRPG cDNA on chromosomes 1, 4, 9, 11, and the X chromosome were
derived by retrotransposition from RBMY-like sequence on the human X
chromosome. They suggested that the erroneous localization of the HNRPG
cDNA probably occurred because of the preferential hybridization of the
cDNA clone to the processed pseudogene on chromosome 6. Delbridge et al.
(1999) proposed that the HNRPG locus be renamed RBMXP1.
*FIELD* RF
1. Delbridge, M. L.; Lingenfelter, P. A.; Disteche, C. M.; Marshall
Graves, J. A.: The candidate spermatogenesis gene RBMY has a homologue
on the human X chromosome. (Letter) Nature Genet. 22: 223-224, 1999.
2. Hofmann, Y.; Wirth, B.: hnRNP-G promotes exon 7 inclusion of survival
motor neuron (SMN) via direct interaction with Htra2-beta1. Hum.
Molec. Genet. 11: 2037-2049, 2002.
3. Le Coniat, M.; Soulard, M.; Della Valle, V.; Larsen, C.-J.; Berger,
R.: Localization of the human gene encoding heterogeneous nuclear
RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12. Hum. Genet. 88:
593-595, 1992.
4. Mazeyrat, S.; Saut, N.; Mattei, M.-G.; Mitchell, M. J.: RBMY evolved
on the Y chromosome from a ubiquitously transcribed X-Y identical
gene. (Letter) Nature Genet. 22: 224-226, 1999.
5. Nasim, M. T.; Chernova, T. K.; Chowdhury, H. M.; Yue, B.-G.; Eperon,
I. C.: HnRNP G and Tra2-beta: opposite effects on splicing matched
by antagonism in RNA binding. Hum. Molec. Genet. 12: 1337-1348,
2003. Note: Erratum: Hum. Molec. Genet. 12: 1941 only, 2003.
6. Venables, J. P.; Elliott, D. J.; Makarova, O. V.; Makarov, E. M.;
Cooke, H. J.; Eperon, I. C.: RBMY, a probable human spermatogenesis
factor, and other hnRNP G proteins interact with Tra2-beta and affect
splicing. Hum. Molec. Genet. 9: 685-694, 2000.
7. Vogt, P. H.; Affara, N.; Davey, P.; Hammer, M.; Jobling, M. A.;
Lau, Y. F.; Mitchell, M.; Schempp, W.; Tyler-Smith, C.; Williams,
G.; Yen, P.; Rappold, G. A: Report of the Third International Workshop
on Y Chromosome Mapping 1997. Heidelberg, Germany, April 13-16, 1997. Cytogenet.
Cell Genet. 79: 1-20, 1997.
*FIELD* CN
George E. Tiller - updated: 3/11/2005
George E. Tiller - updated: 7/11/2003
George E. Tiller - updated: 4/18/2000
Anne M. Lopez - updated: 6/30/1999
*FIELD* CD
Victor A. McKusick: 6/29/1999
*FIELD* ED
terry: 04/04/2013
alopez: 3/11/2005
cwells: 7/11/2003
alopez: 4/18/2000
alopez: 2/21/2000
carol: 7/1/1999
carol: 6/30/1999
alopez: 6/29/1999