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RNA-binding motif protein, X chromosome (Glycoprotein p43) (Heterogeneous nuclear ribonucleoprotein G) (hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]

 RBMX_HUMAN              Reviewed;         391 AA.
P38159; B4E3U4; D3DWH0; E9PG86; Q5JQ67; Q8N8Y7; Q969R3;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 3.
25-OCT-2017, entry version 198.
RecName: Full=RNA-binding motif protein, X chromosome;
AltName: Full=Glycoprotein p43;
AltName: Full=Heterogeneous nuclear ribonucleoprotein G;
Short=hnRNP G;
Contains:
RecName: Full=RNA-binding motif protein, X chromosome, N-terminally processed;
Name=RBMX; Synonyms=HNRPG, RBMXP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GLYCOSYLATION.
TISSUE=Mammary gland;
PubMed=7692398; DOI=10.1093/nar/21.18.4210;
Soulard M., Della Valle V., Siomi M., Pinol-Roma S., Codogno P.,
Bauvy C., Belli M., Lacroix J.-C., Monod G., Dreyfuss G.,
Larsen C.-J.;
"hnRNP G: sequence and characterization of a glycosylated RNA-binding
protein.";
Nucleic Acids Res. 21:4210-4217(1993).
[2]
SEQUENCE REVISION.
Venables J.P., Larsen C.-J.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=11420617; DOI=10.1007/s00335001-0003-z;
Lingenfelter P.A., Delbridge M.L., Thomas S., Hoekstra H.E.,
Mitchell M.J., Graves J.A., Disteche C.M.;
"Expression and conservation of processed copies of the RBMX gene.";
Mamm. Genome 12:538-545(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lin T.-Y., Chiou S.-H.;
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Kidney, and Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 1-30; 34-41; 50-63; 81-93; 126-144; 188-195;
204-210; 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT MET-1 AND VAL-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
Submitted (JUL-2007) to UniProtKB.
[10]
INTERACTION WITH KHDRBS3.
TISSUE=Testis;
PubMed=10332027; DOI=10.1093/hmg/8.6.959;
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B.,
Wu J., Cooke H.J., Artzt K., Eperon I.C.;
"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-
binding protein implicated in spermatogenesis.";
Hum. Mol. Genet. 8:959-969(1999).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[12]
FUNCTION, INTERACTION WITH TRA2B, AND RNA-BINDING.
PubMed=12165565; DOI=10.1093/hmg/11.17.2037;
Hofmann Y., Wirth B.;
"hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via
direct interaction with Htra2-beta1.";
Hum. Mol. Genet. 11:2037-2049(2002).
[13]
FUNCTION, AND RNA-BINDING.
PubMed=12761049; DOI=10.1093/hmg/ddg136;
Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.;
"HnRNP G and Tra2beta: opposite effects on splicing matched by
antagonism in RNA binding.";
Hum. Mol. Genet. 12:1337-1348(2003).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
FUNCTION, MUTAGENESIS OF LYS-22, AND TISSUE SPECIFICITY.
PubMed=16707624; DOI=10.1158/1078-0432.CCR-05-2656;
Shin K.H., Kang M.K., Kim R.H., Christensen R., Park N.H.;
"Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive
effect against oral squamous cell carcinoma cells.";
Clin. Cancer Res. 12:3222-3228(2006).
[16]
IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; NCOA5 AND
PPP1CA.
PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K.,
Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
"The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
G.";
Biochim. Biophys. Acta 1774:1339-1350(2007).
[17]
FUNCTION, AND INTERACTION WITH ERAP1.
PubMed=18445477; DOI=10.1016/j.bbrc.2008.04.103;
Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.;
"An association between RBMX, a heterogeneous nuclear
ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release.";
Biochem. Biophys. Res. Commun. 371:505-509(2008).
[18]
FUNCTION, CHROMATIN ASSOCIATION, AND MUTAGENESIS OF LYS-22.
PubMed=18541147; DOI=10.1016/j.bbrc.2008.05.175;
Shin K.H., Kim R.H., Kim R.H., Kang M.K., Park N.H.;
"hnRNP G elicits tumor-suppressive activity in part by upregulating
the expression of Txnip.";
Biochem. Biophys. Res. Commun. 372:880-885(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-329 AND SER-332,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
FUNCTION, IDENTIFICATION IN THE SUPRASPLICEOSOME COMPLEX, INTERACTION
WITH CLK2; KHDRBS2; SAFB; TRA2B AND YTHDC1, AND SUBCELLULAR LOCATION.
PubMed=19282290; DOI=10.1074/jbc.M901026200;
Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N.,
Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H.,
Sperling J., Sperling R., Stamm S.;
"Heterogeneous nuclear ribonucleoprotein G regulates splice site
selection by binding to CC(A/C)-rich regions in pre-mRNA.";
J. Biol. Chem. 284:14303-14315(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=21327109; DOI=10.4161/nucl.1.1.10857;
Kanhoush R., Beenders B., Perrin C., Moreau J., Bellini M.,
Penrad-Mobayed M.;
"Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA
binding and targeting nascent transcripts.";
Nucleus 1:109-122(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-352, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-332 AND SER-352,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-91; SER-165;
SER-174; SER-261; SER-328; SER-330 AND SER-332, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[30]
INVOLVEMENT IN MRXS11.
PubMed=25256757; DOI=10.1111/cge.12511;
Shashi V., Xie P., Schoch K., Goldstein D.B., Howard T.D., Berry M.N.,
Schwartz C.E., Cronin K., Sliwa S., Allen A., Need A.C.;
"The RBMX gene as a candidate for the Shashi X-linked intellectual
disability syndrome.";
Clin. Genet. 88:386-390(2015).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-80 AND LYS-86, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[34]
STRUCTURE BY NMR OF 1-90.
Joint center for structural genomics (JCSG);
"NMR structure of the first RRM domain of the protein RBM39 from Homo
sapiens.";
Submitted (MAR-2014) to the PDB data bank.
-!- FUNCTION: RNA-binding protein that plays several role in the
regulation of pre- and post-transcriptional processes. Implicated
in tissue-specific regulation of gene transcription and
alternative splicing of several pre-mRNAs. Binds to and stimulates
transcription from the tumor suppressor TXNIP gene promoter; may
thus be involved in tumor suppression. When associated with SAFB,
binds to and stimulates transcription from the SREBF1 promoter.
Associates with nascent mRNAs transcribed by RNA polymerase II.
Component of the supraspliceosome complex that regulates pre-mRNA
alternative splice site selection. Can either activate or suppress
exon inclusion; acts additively with TRA2B to promote exon 7
inclusion of the survival motor neuron SMN2. Represses the
splicing of MAPT/Tau exon 10. Binds preferentially to single-
stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
single-stranded conformation; probably binds RNA as a homodimer.
Binds non-specifically to pre-mRNAs. Plays also a role in the
cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-
beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains
and the release of TNFR1 exosome-like vesicles to the
extracellular compartment. {ECO:0000269|PubMed:12165565,
ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:16707624,
ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:18541147,
ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:21327109}.
-!- SUBUNIT: Homomultimer. Interacts with SAFB/SAFB1 (By similarity).
Found in the supraspliceosome complex. Identified in the
spliceosome C complex. Interacts with KHDRBS3. Forms a complex
with ILF2, ILF3, YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with
CLK2, KHDRBS2, SAFB, TRA2B and YTHDC1. Interacts with ERAP1; the
interaction is RNA-independent. {ECO:0000250,
ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:17890166,
ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:19282290}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-743526, EBI-743526;
Q9NRW3:APOBEC3C; NbExp=5; IntAct=EBI-743526, EBI-1044593;
Q14011:CIRBP; NbExp=4; IntAct=EBI-743526, EBI-538850;
P49761:CLK3; NbExp=3; IntAct=EBI-743526, EBI-745579;
P61978:HNRNPK; NbExp=11; IntAct=EBI-743526, EBI-304185;
P61978-2:HNRNPK; NbExp=4; IntAct=EBI-743526, EBI-7060731;
Q5VWX1:KHDRBS2; NbExp=13; IntAct=EBI-743526, EBI-742808;
O75525:KHDRBS3; NbExp=3; IntAct=EBI-743526, EBI-722504;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-743526, EBI-739832;
Q96A72:MAGOHB; NbExp=3; IntAct=EBI-743526, EBI-746778;
Q96AH0:NABP1; NbExp=5; IntAct=EBI-743526, EBI-2889252;
Q8WWY3:PRPF31; NbExp=7; IntAct=EBI-743526, EBI-1567797;
P79522:PRR3; NbExp=5; IntAct=EBI-743526, EBI-2803328;
P98179:RBM3; NbExp=5; IntAct=EBI-743526, EBI-2949699;
P0DJD3:RBMY1A1; NbExp=3; IntAct=EBI-743526, EBI-8638511;
P0DJD3-2:RBMY1A1; NbExp=6; IntAct=EBI-743526, EBI-11994018;
Q15415:RBMY1J; NbExp=7; IntAct=EBI-743526, EBI-8642021;
Q96HH0:ROBO3; NbExp=3; IntAct=EBI-743526, EBI-10288358;
P09012:SNRPA; NbExp=3; IntAct=EBI-743526, EBI-607085;
Q9JKL7:Srek1 (xeno); NbExp=3; IntAct=EBI-743526, EBI-6452221;
P62995:TRA2B; NbExp=3; IntAct=EBI-743526, EBI-725485;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19282290,
ECO:0000269|PubMed:21327109}. Note=Component of ribonucleosomes.
Localizes in numerous small granules in the nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P38159-1; Sequence=Displayed;
Name=2;
IsoId=P38159-2; Sequence=VSP_042203;
Name=3;
IsoId=P38159-3; Sequence=VSP_043650, VSP_043651;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed strongly in oral keratinocytes, but
only weakly detected in oral squamous cell carcinomas (at protein
level). {ECO:0000269|PubMed:16707624}.
-!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for
splice site selection, indicating that its splicing activity does
not require direct binding to RNA. {ECO:0000250}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:7692398}.
-!- PTM: Arg-185 is dimethylated, probably to asymmetric
dimethylarginine.
-!- PTM: Cleavage of initiator Met is partial. If Met-1 is not
removed, it is acetylated. If it is removed, Val-2 is acetylated.
{ECO:0000269|Ref.9}.
-!- DISEASE: Mental retardation, X-linked, syndromic, 11 (MRXS11)
[MIM:300238]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRXS11 patients manifest moderate
intellectual disability and craniofacial dysmorphism.
{ECO:0000269|PubMed:25256757}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z23064; CAA80599.1; -; mRNA.
EMBL; AF266723; AAK58567.1; -; Genomic_DNA.
EMBL; AF266720; AAK58567.1; JOINED; Genomic_DNA.
EMBL; AF266721; AAK58567.1; JOINED; Genomic_DNA.
EMBL; AF266722; AAK58567.1; JOINED; Genomic_DNA.
EMBL; AY464692; AAR28036.1; -; mRNA.
EMBL; AK096015; BAC04674.1; -; mRNA.
EMBL; AK304868; BAG65606.1; -; mRNA.
EMBL; AL683813; CAI39448.1; -; Genomic_DNA.
EMBL; CH471150; EAW88453.1; -; Genomic_DNA.
EMBL; CH471150; EAW88454.1; -; Genomic_DNA.
EMBL; CH471150; EAW88455.1; -; Genomic_DNA.
EMBL; CH471150; EAW88457.1; -; Genomic_DNA.
EMBL; BC006550; AAH06550.1; -; mRNA.
EMBL; BC007435; AAH07435.1; -; mRNA.
CCDS; CCDS14661.1; -. [P38159-1]
CCDS; CCDS55510.1; -. [P38159-3]
RefSeq; NP_001158275.1; NM_001164803.1. [P38159-3]
RefSeq; NP_002130.2; NM_002139.3. [P38159-1]
UniGene; Hs.380118; -.
UniGene; Hs.710162; -.
PDB; 2MB0; NMR; -; B=1-95.
PDB; 2MKS; NMR; -; A=1-90.
PDBsum; 2MB0; -.
PDBsum; 2MKS; -.
ProteinModelPortal; P38159; -.
SMR; P38159; -.
BioGrid; 118134; 159.
CORUM; P38159; -.
DIP; DIP-34447N; -.
IntAct; P38159; 94.
MINT; MINT-5000999; -.
STRING; 9606.ENSP00000359645; -.
iPTMnet; P38159; -.
PhosphoSitePlus; P38159; -.
SwissPalm; P38159; -.
BioMuta; RBMX; -.
DMDM; 23503093; -.
SWISS-2DPAGE; P38159; -.
EPD; P38159; -.
MaxQB; P38159; -.
PaxDb; P38159; -.
PeptideAtlas; P38159; -.
PRIDE; P38159; -.
TopDownProteomics; P38159-1; -. [P38159-1]
DNASU; 27316; -.
Ensembl; ENST00000320676; ENSP00000359645; ENSG00000147274. [P38159-1]
Ensembl; ENST00000431446; ENSP00000411989; ENSG00000147274. [P38159-3]
GeneID; 27316; -.
KEGG; hsa:27316; -.
UCSC; uc004fae.4; human. [P38159-1]
CTD; 27316; -.
DisGeNET; 27316; -.
EuPathDB; HostDB:ENSG00000147274.14; -.
GeneCards; RBMX; -.
HGNC; HGNC:9910; RBMX.
HPA; HPA057707; -.
MalaCards; RBMX; -.
MIM; 300199; gene.
MIM; 300238; phenotype.
neXtProt; NX_P38159; -.
OpenTargets; ENSG00000147274; -.
PharmGKB; PA34277; -.
eggNOG; ENOG410IHG3; Eukaryota.
eggNOG; ENOG4111GI6; LUCA.
GeneTree; ENSGT00710000106295; -.
HOGENOM; HOG000276235; -.
HOVERGEN; HBG063314; -.
InParanoid; P38159; -.
KO; K12885; -.
OMA; DPGACFK; -.
OrthoDB; EOG091G13K0; -.
PhylomeDB; P38159; -.
TreeFam; TF331833; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
ChiTaRS; RBMX; human.
GeneWiki; RBMX; -.
GenomeRNAi; 27316; -.
PRO; PR:P38159; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000147274; -.
CleanEx; HS_RBMX; -.
ExpressionAtlas; P38159; baseline and differential.
Genevisible; P38159; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; NAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0006376; P:mRNA splice site selection; IEA:Ensembl.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR012604; RBM1CTR.
InterPro; IPR000504; RRM_dom.
InterPro; IPR003954; RRM_dom_euk.
Pfam; PF08081; RBM1CTR; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SMART; SM00361; RRM_1; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Direct protein sequencing; Glycoprotein;
Isopeptide bond; Mental retardation; Methylation; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
Ribonucleoprotein; RNA-binding; Spliceosome; Transcription;
Tumor suppressor; Ubl conjugation.
CHAIN 1 391 RNA-binding motif protein, X chromosome.
/FTId=PRO_0000081854.
INIT_MET 1 1 Removed; alternate. {ECO:0000269|Ref.9}.
CHAIN 2 391 RNA-binding motif protein, X chromosome,
N-terminally processed.
/FTId=PRO_0000304582.
DOMAIN 8 86 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 186 236 Necessary for the association to nascent
RNAPII transcripts and nuclear
localization.
REGION 333 391 Necessary for RNA-binding.
MOD_RES 1 1 N-acetylmethionine; in Heterogeneous
nuclear ribonucleoprotein G; alternate.
{ECO:0000269|Ref.9}.
MOD_RES 2 2 N-acetylvaline; in Heterogeneous nuclear
ribonucleoprotein G, N-terminally
processed. {ECO:0000269|Ref.9}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q91VM5}.
MOD_RES 125 125 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q9WV02}.
MOD_RES 144 144 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WV02}.
MOD_RES 164 164 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WV02}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 172 172 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9WV02}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 332 332 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 86 86 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 45 57 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042203.
VAR_SEQ 73 196 SLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGR
GGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPP
PRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPR
R -> LLYHVEEIVMEVHLEGNRCPLVEMFICPQEMMGILL
KTAIQAEITQVLVILEIMHHHHEIILTVIMVIPVHVMTIHQ
EDIAIEMDMVVIVTIQIIQVEVPTEIHMRVMVGDFAHYGRG
VLIDSQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043650.
VAR_SEQ 197 391 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043651.
MUTAGEN 22 22 K->A: Promotes cell proliferation.
Inhibits transcriptional up-regulation of
the TXNIP promoter.
{ECO:0000269|PubMed:16707624,
ECO:0000269|PubMed:18541147}.
CONFLICT 259 259 G -> E (in Ref. 1; CAA80599).
{ECO:0000305}.
STRAND 9 13 {ECO:0000244|PDB:2MB0}.
HELIX 21 28 {ECO:0000244|PDB:2MB0}.
TURN 29 31 {ECO:0000244|PDB:2MB0}.
STRAND 34 39 {ECO:0000244|PDB:2MB0}.
TURN 43 45 {ECO:0000244|PDB:2MB0}.
STRAND 50 58 {ECO:0000244|PDB:2MB0}.
HELIX 61 66 {ECO:0000244|PDB:2MB0}.
STRAND 67 74 {ECO:0000244|PDB:2MKS}.
STRAND 80 83 {ECO:0000244|PDB:2MB0}.
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


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