RBMX_HUMAN
ID RBMX_HUMAN Reviewed; 391 AA.
AC P38159; B4E3U4; D3DWH0; E9PG86; Q5JQ67; Q8N8Y7; Q969R3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 3.
DT 03-AUG-2022, entry version 230.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Bauvy C.,
RA Belli M., Lacroix J.-C., Monod G., Dreyfuss G., 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., Mitchell M.J.,
RA 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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; 204-210;
RP 283-292; 299-317 AND 332-339, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT MET-1 AND VAL-2, AND IDENTIFICATION BY 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., Wu J.,
RA 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 SPLICEOSOMAL
RP 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 antagonism
RT in RNA binding.";
RL Hum. Mol. Genet. 12:1337-1348(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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 effect
RT 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., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-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 ribonucleoprotein,
RT 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 the
RT 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 WITH
RP 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., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-91; SER-165; SER-174;
RP SER-261; SER-328; SER-330 AND SER-332, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [29]
RP INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [31]
RP INVOLVEMENT IN MRXS11.
RX PubMed=25256757; DOI=10.1111/cge.12511;
RA Shashi V., Xie P., Schoch K., Goldstein D.B., Howard T.D., Berry M.N.,
RA Schwartz C.E., Cronin K., Sliwa S., Allen A., Need A.C.;
RT "The RBMX gene as a candidate for the Shashi X-linked intellectual
RT disability syndrome.";
RL Clin. Genet. 88:386-390(2015).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-80, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-80 AND LYS-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [35]
RP STRUCTURE BY NMR OF 1-90.
RG Joint center for structural genomics (JCSG);
RT "NMR structure of the first RRM domain of the protein RBM39 from Homo
RT sapiens.";
RL Submitted (MAR-2014) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein that plays several role in the regulation
CC of pre- and post-transcriptional processes. Implicated in tissue-
CC specific regulation of gene transcription and alternative splicing of
CC several pre-mRNAs. Binds to and stimulates transcription from the tumor
CC suppressor TXNIP gene promoter; may thus be involved in tumor
CC suppression. When associated with SAFB, binds to and stimulates
CC transcription from the SREBF1 promoter. Associates with nascent mRNAs
CC transcribed by RNA polymerase II. Component of the supraspliceosome
CC complex that regulates pre-mRNA alternative splice site selection. Can
CC either activate or suppress exon inclusion; acts additively with TRA2B
CC to promote exon 7 inclusion of the survival motor neuron SMN2.
CC Represses the splicing of MAPT/Tau exon 10. Binds preferentially to
CC single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a
CC single-stranded conformation; probably binds RNA as a homodimer. Binds
CC non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic
CC TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated
CC inducible proteolytic cleavage of TNFR1 ectodomains and the release of
CC TNFR1 exosome-like vesicles to the extracellular compartment.
CC {ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:12761049,
CC ECO:0000269|PubMed:16707624, ECO:0000269|PubMed:18445477,
CC ECO:0000269|PubMed:18541147, ECO:0000269|PubMed:19282290,
CC ECO:0000269|PubMed:21327109}.
CC -!- SUBUNIT: Homomultimer. Interacts with SAFB/SAFB1 (By similarity). Found
CC in the supraspliceosome complex. Identified in the spliceosome C
CC complex. Interacts with KHDRBS3. Forms a complex with ILF2, ILF3,
CC YLPM1, KHDRBS1, NCOA5 and PPP1CA. Interacts with CLK2, KHDRBS2, SAFB,
CC TRA2B and YTHDC1. Interacts with ERAP1; the interaction is RNA-
CC independent (PubMed:18445477). Interacts with PPIA/CYPA
CC (PubMed:25678563). {ECO:0000250|UniProtKB:Q9WV02,
CC ECO:0000269|PubMed:10332027, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12165565, ECO:0000269|PubMed:17890166,
CC ECO:0000269|PubMed:18445477, ECO:0000269|PubMed:19282290,
CC ECO:0000269|PubMed:25678563}.
CC -!- INTERACTION:
CC P38159; Q9NRW3: APOBEC3C; NbExp=6; IntAct=EBI-743526, EBI-1044593;
CC P38159; Q14011: CIRBP; NbExp=4; IntAct=EBI-743526, EBI-538850;
CC P38159; P49761: CLK3; NbExp=3; IntAct=EBI-743526, EBI-745579;
CC P38159; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-743526, EBI-1054315;
CC P38159; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-743526, EBI-741032;
CC P38159; P35637: FUS; NbExp=5; IntAct=EBI-743526, EBI-400434;
CC P38159; P61978: HNRNPK; NbExp=11; IntAct=EBI-743526, EBI-304185;
CC P38159; P61978-2: HNRNPK; NbExp=8; IntAct=EBI-743526, EBI-7060731;
CC P38159; Q5VWX1: KHDRBS2; NbExp=10; IntAct=EBI-743526, EBI-742808;
CC P38159; O75525: KHDRBS3; NbExp=4; IntAct=EBI-743526, EBI-722504;
CC P38159; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-743526, EBI-739832;
CC P38159; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-743526, EBI-746778;
CC P38159; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-743526, EBI-2858213;
CC P38159; Q96AH0: NABP1; NbExp=6; IntAct=EBI-743526, EBI-2889252;
CC P38159; Q9GZU5: NYX; NbExp=3; IntAct=EBI-743526, EBI-12744849;
CC P38159; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-743526, EBI-10329013;
CC P38159; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-743526, EBI-1567797;
CC P38159; P79522: PRR3; NbExp=6; IntAct=EBI-743526, EBI-2803328;
CC P38159; P98179: RBM3; NbExp=7; IntAct=EBI-743526, EBI-2949699;
CC P38159; P38159: RBMX; NbExp=6; IntAct=EBI-743526, EBI-743526;
CC P38159; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-743526, EBI-8638511;
CC P38159; P0DJD3-2: RBMY1A1; NbExp=4; IntAct=EBI-743526, EBI-11994018;
CC P38159; A6NEQ0: RBMY1E; NbExp=3; IntAct=EBI-743526, EBI-11958200;
CC P38159; Q15415: RBMY1J; NbExp=6; IntAct=EBI-743526, EBI-8642021;
CC P38159; Q96HH0: ROBO3; NbExp=3; IntAct=EBI-743526, EBI-10288358;
CC P38159; P09012: SNRPA; NbExp=3; IntAct=EBI-743526, EBI-607085;
CC P38159; P84103: SRSF3; NbExp=3; IntAct=EBI-743526, EBI-372557;
CC P38159; Q13242: SRSF9; NbExp=3; IntAct=EBI-743526, EBI-2949710;
CC P38159; Q13148: TARDBP; NbExp=3; IntAct=EBI-743526, EBI-372899;
CC P38159; P62995: TRA2B; NbExp=4; IntAct=EBI-743526, EBI-725485;
CC P38159; Q9JKL7: Srek1; Xeno; NbExp=3; IntAct=EBI-743526, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19282290,
CC ECO:0000269|PubMed:21327109}. 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 -!- TISSUE SPECIFICITY: Expressed strongly in oral keratinocytes, but only
CC weakly detected in oral squamous cell carcinomas (at protein level).
CC {ECO:0000269|PubMed:16707624}.
CC -!- DOMAIN: The RRM domain is necessary for RNA-binding, but not for splice
CC site selection, indicating that its splicing activity does not require
CC direct binding to RNA. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:7692398}.
CC -!- PTM: Arg-185 is dimethylated, probably to asymmetric dimethylarginine.
CC -!- PTM: Cleavage of initiator Met is partial. If Met-1 is not removed, it
CC is acetylated. If it is removed, Val-2 is acetylated.
CC {ECO:0000269|Ref.9}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 11
CC (MRXS11) [MIM:300238]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC MRXS11 patients manifest moderate intellectual disability and
CC craniofacial dysmorphism. {ECO:0000269|PubMed:25256757}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS14661.1; -. [P38159-1]
DR CCDS; CCDS55510.1; -. [P38159-3]
DR RefSeq; NP_001158275.1; NM_001164803.1. [P38159-3]
DR RefSeq; NP_002130.2; NM_002139.3. [P38159-1]
DR PDB; 2MB0; NMR; -; B=1-95.
DR PDB; 2MKS; NMR; -; A=1-90.
DR PDBsum; 2MB0; -.
DR PDBsum; 2MKS; -.
DR AlphaFoldDB; P38159; -.
DR BMRB; P38159; -.
DR SMR; P38159; -.
DR BioGRID; 118134; 319.
DR CORUM; P38159; -.
DR DIP; DIP-34447N; -.
DR IntAct; P38159; 146.
DR MINT; P38159; -.
DR STRING; 9606.ENSP00000359645; -.
DR GlyGen; P38159; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P38159; -.
DR PhosphoSitePlus; P38159; -.
DR SwissPalm; P38159; -.
DR BioMuta; RBMX; -.
DR DMDM; 23503093; -.
DR SWISS-2DPAGE; P38159; -.
DR EPD; P38159; -.
DR jPOST; P38159; -.
DR MassIVE; P38159; -.
DR MaxQB; P38159; -.
DR PaxDb; P38159; -.
DR PeptideAtlas; P38159; -.
DR PRIDE; P38159; -.
DR ProteomicsDB; 55284; -. [P38159-1]
DR ProteomicsDB; 55285; -. [P38159-2]
DR ProteomicsDB; 55286; -. [P38159-3]
DR TopDownProteomics; P38159-1; -. [P38159-1]
DR ABCD; P38159; 1 sequenced antibody.
DR Antibodypedia; 30459; 156 antibodies from 27 providers.
DR DNASU; 27316; -.
DR Ensembl; ENST00000320676.11; ENSP00000359645.3; ENSG00000147274.14. [P38159-1]
DR Ensembl; ENST00000431446.7; ENSP00000411989.3; ENSG00000147274.14. [P38159-3]
DR GeneID; 27316; -.
DR KEGG; hsa:27316; -.
DR MANE-Select; ENST00000320676.11; ENSP00000359645.3; NM_002139.4; NP_002130.2.
DR UCSC; uc004fae.4; human. [P38159-1]
DR CTD; 27316; -.
DR DisGeNET; 27316; -.
DR GeneCards; RBMX; -.
DR HGNC; HGNC:9910; RBMX.
DR HPA; ENSG00000147274; Low tissue specificity.
DR MalaCards; RBMX; -.
DR MIM; 300199; gene.
DR MIM; 300238; phenotype.
DR neXtProt; NX_P38159; -.
DR OpenTargets; ENSG00000147274; -.
DR PharmGKB; PA34277; -.
DR VEuPathDB; HostDB:ENSG00000147274; -.
DR eggNOG; ENOG502QS9N; Eukaryota.
DR GeneTree; ENSGT00940000153425; -.
DR HOGENOM; CLU_1395869_0_0_1; -.
DR InParanoid; P38159; -.
DR OMA; AKYHEGF; -.
DR OrthoDB; 1248417at2759; -.
DR PhylomeDB; P38159; -.
DR TreeFam; TF331833; -.
DR PathwayCommons; P38159; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; P38159; -.
DR BioGRID-ORCS; 27316; 433 hits in 680 CRISPR screens.
DR ChiTaRS; RBMX; human.
DR GeneWiki; RBMX; -.
DR GenomeRNAi; 27316; -.
DR Pharos; P38159; Tbio.
DR PRO; PR:P38159; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P38159; protein.
DR Bgee; ENSG00000147274; Expressed in ventricular zone and 180 other tissues.
DR ExpressionAtlas; P38159; baseline and differential.
DR Genevisible; P38159; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; NAS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
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:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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 by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012604; RBM1CTR.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF08081; RBM1CTR; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Glycoprotein; Intellectual disability;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Transcription; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..391
FT /note="RNA-binding motif protein, X chromosome"
FT /id="PRO_0000081854"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|Ref.9"
FT CHAIN 2..391
FT /note="RNA-binding motif protein, X chromosome, N-
FT terminally processed"
FT /id="PRO_0000304582"
FT DOMAIN 8..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 61..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..236
FT /note="Necessary for the association to nascent RNAPII
FT transcripts and nuclear localization"
FT REGION 333..391
FT /note="Necessary for RNA-binding"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Heterogeneous nuclear
FT ribonucleoprotein G; alternate"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 2
FT /note="N-acetylvaline; in Heterogeneous nuclear
FT ribonucleoprotein G, N-terminally processed"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 144
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV02"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 45..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042203"
FT VAR_SEQ 73..196
FT /note="SLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPS
FT RGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPV
FT SRGRDSYGGPPRR -> LLYHVEEIVMEVHLEGNRCPLVEMFICPQEMMGILLKTAIQA
FT EITQVLVILEIMHHHHEIILTVIMVIPVHVMTIHQEDIAIEMDMVVIVTIQIIQVEVPT
FT EIHMRVMVGDFAHYGRGVLIDSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043650"
FT VAR_SEQ 197..391
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043651"
FT MUTAGEN 22
FT /note="K->A: Promotes cell proliferation. Inhibits
FT transcriptional up-regulation of the TXNIP promoter."
FT /evidence="ECO:0000269|PubMed:16707624,
FT ECO:0000269|PubMed:18541147"
FT CONFLICT 259
FT /note="G -> E (in Ref. 1; CAA80599)"
FT /evidence="ECO:0000305"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:2MB0"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2MB0"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2MB0"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2MB0"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2MB0"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:2MB0"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:2MB0"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:2MKS"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:2MB0"
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
