RBM15_HUMAN
ID RBM15_HUMAN Reviewed; 977 AA.
AC Q96T37; A1A693; Q3ZB86; Q4V760; Q5D058; Q5T613; Q86VW9; Q96PE4; Q96SC5;
AC Q96SC6; Q96SC9; Q96SD0; Q96T38; Q9BRA5; Q9H6R8; Q9H9Y0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=RNA-binding protein 15 {ECO:0000305};
DE AltName: Full=One-twenty two protein 1 {ECO:0000303|PubMed:16129689};
DE AltName: Full=RNA-binding motif protein 15 {ECO:0000303|PubMed:11431691};
GN Name=RBM15 {ECO:0000303|PubMed:11431691, ECO:0000312|HGNC:HGNC:14959};
GN Synonyms=OTT {ECO:0000303|PubMed:16129689},
GN OTT1 {ECO:0000303|PubMed:16129689};
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] (ISOFORMS 1; 2 AND 3), AND CHROMOSOMAL
RP TRANSLOCATION WITH MKL1.
RX PubMed=11431691; DOI=10.1038/90054;
RA Ma Z., Morris S.W., Valentine V., Li M., Herbrick J.-A., Cui X., Bouman D.,
RA Li Y., Mehta P.K., Nizetic D., Kaneko Y., Chan G.C.F., Chan L.C.,
RA Squire J., Scherer S.W., Hitzler J.K.;
RT "Fusion of two novel genes, RBM15 and MKL1, in the t(1;22)(p13;q13) of
RT acute megakaryoblastic leukemia.";
RL Nat. Genet. 28:220-221(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CHROMOSOMAL
RP TRANSLOCATION WITH MKL1.
RX PubMed=11344311; DOI=10.1073/pnas.101001498;
RA Mercher T., Coniat M.B.-L., Monni R., Mauchauffe M., Khac F.N., Gressin L.,
RA Mugneret F., Leblanc T., Dastugue N., Berger R., Bernard O.A.;
RT "Involvement of a human gene related to the Drosophila spen gene in the
RT recurrent t(1;22) translocation of acute megakaryocytic leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:5776-5779(2001).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hepatoma, and Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 21-977 (ISOFORM 1).
RC TISSUE=Melanoma, and Testis;
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 [7]
RP INTERACTION WITH EBV BSFL2/BMLF1 (MICROBIAL INFECTION).
RX PubMed=16129689; DOI=10.1074/jbc.m501725200;
RA Hiriart E., Gruffat H., Buisson M., Mikaelian I., Keppler S., Meresse P.,
RA Mercher T., Bernard O.A., Sergeant A., Manet E.;
RT "Interaction of the Epstein-Barr virus mRNA export factor EB2 with human
RT Spen proteins SHARP, OTT1, and a novel member of the family, OTT3, links
RT Spen proteins with splicing regulation and mRNA export.";
RL J. Biol. Chem. 280:36935-36945(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568; SER-622 AND SER-700, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION (ISOFORM 4),
RP RNA-BINDING, AND INTERACTION WITH NXF1.
RX PubMed=17001072; DOI=10.1074/jbc.m608745200;
RA Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V.,
RA Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.;
RT "RNA-binding motif protein 15 binds to the RNA transport element RTE and
RT provides a direct link to the NXF1 export pathway.";
RL J. Biol. Chem. 281:36915-36928(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-568; SER-670 AND SER-674, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-259; SER-292;
RP SER-294; THR-568; SER-670; SER-674; SER-741 AND SER-935, AND IDENTIFICATION
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19786495; DOI=10.1093/nar/gkp782;
RA Zolotukhin A.S., Uranishi H., Lindtner S., Bear J., Pavlakis G.N.,
RA Felber B.K.;
RT "Nuclear export factor RBM15 facilitates the access of DBP5 to mRNA.";
RL Nucleic Acids Res. 37:7151-7162(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670 AND SER-674, AND
RP IDENTIFICATION BY 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-450, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-210; SER-257;
RP SER-259; SER-294; SER-365; THR-568; SER-622; SER-670; SER-765 AND SER-935,
RP AND 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 [20]
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 [21]
RP SUBCELLULAR LOCATION.
RX PubMed=19586903; DOI=10.1074/jbc.m109.040113;
RA Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J.,
RA Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.;
RT "The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the
RT nuclear export receptor NXF1.";
RL J. Biol. Chem. 284:26106-26116(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-294; THR-568;
RP SER-741 AND SER-765, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP INTERACTION WITH SETD1B, AND MUTAGENESIS OF LYS-795; LYS-898 AND PHE-923.
RX PubMed=22927943; DOI=10.1371/journal.pone.0042965;
RA Lee J.H., Skalnik D.G.;
RT "Rbm15-Mkl1 interacts with the Setd1b histone H3-Lys4 methyltransferase via
RT a SPOC domain that is required for cytokine-independent proliferation.";
RL PLoS ONE 7:E42965-E42965(2012).
RN [24]
RP IDENTIFICATION IN A MACOM-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=24100041; DOI=10.1074/jbc.m113.500397;
RA Horiuchi K., Kawamura T., Iwanari H., Ohashi R., Naito M., Kodama T.,
RA Hamakubo T.;
RT "Identification of Wilms' tumor 1-associating protein complex and its role
RT in alternative splicing and the cell cycle.";
RL J. Biol. Chem. 288:33292-33302(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-208; SER-253;
RP SER-257; SER-259; SER-292; SER-294; THR-568; SER-622; SER-656; SER-670;
RP SER-674; SER-700; SER-741; SER-765; SER-767; SER-781 AND SER-935, AND
RP IDENTIFICATION BY MASS 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-257; SER-259;
RP TYR-266; SER-292; SER-294; THR-568; SER-670; SER-674; SER-700 AND SER-741,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP FUNCTION, METHYLATION AT ARG-578, UBIQUITINATION, INTERACTION WITH SF3B1,
RP AND MUTAGENESIS OF 574-ARG--ARG-578 AND ARG-578.
RX PubMed=26575292; DOI=10.7554/elife.07938;
RA Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A.,
RA Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X.,
RA Zhou W., Laha S., Abdel-Wahab O., Levine R.L., Raffel G., Liu Y., Chen D.,
RA Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.;
RT "Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15
RT controls RNA splicing.";
RL Elife 4:0-0(2015).
RN [28]
RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN THE WMM COMPLEX.
RX PubMed=27602518; DOI=10.1038/nature19342;
RA Patil D.P., Chen C.K., Pickering B.F., Chow A., Jackson C., Guttman M.,
RA Jaffrey S.R.;
RT "m(6)A RNA methylation promotes XIST-mediated transcriptional repression.";
RL Nature 537:369-373(2016).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246; LYS-406; LYS-420; LYS-445
RP AND LYS-744, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
CC -!- FUNCTION: RNA-binding protein that acts as a key regulator of N6-
CC methyladenosine (m6A) methylation of RNAs, thereby regulating different
CC processes, such as hematopoietic cell homeostasis, alternative splicing
CC of mRNAs and X chromosome inactivation mediated by Xist RNA
CC (PubMed:27602518). Associated component of the WMM complex, a complex
CC that mediates N6-methyladenosine (m6A) methylation of RNAs, a
CC modification that plays a role in the efficiency of mRNA splicing and
CC RNA processing (By similarity). Plays a key role in m6A methylation,
CC possibly by binding target RNAs and recruiting the WMM complex
CC (PubMed:27602518). Involved in random X inactivation mediated by Xist
CC RNA: acts by binding Xist RNA and recruiting the WMM complex, which
CC mediates m6A methylation, leading to target YTHDC1 reader on Xist RNA
CC and promoting transcription repression activity of Xist
CC (PubMed:27602518). Required for the development of multiple tissues,
CC such as the maintenance of the homeostasis of long-term hematopoietic
CC stem cells and for megakaryocyte (MK) and B-cell differentiation (By
CC similarity). Regulates megakaryocyte differentiation by regulating
CC alternative splicing of genes important for megakaryocyte
CC differentiation; probably regulates alternative splicing via m6A
CC regulation (PubMed:26575292). Required for placental vascular branching
CC morphogenesis and embryonic development of the heart and spleen (By
CC similarity). Acts as a regulator of thrombopoietin response in
CC hematopoietic stem cells by regulating alternative splicing of MPL (By
CC similarity). May also function as an mRNA export factor, stimulating
CC export and expression of RTE-containing mRNAs which are present in many
CC retrotransposons that require to be exported prior to splicing
CC (PubMed:17001072, PubMed:19786495). High affinity binding of pre-mRNA
CC to RBM15 may allow targeting of the mRNP to the export helicase DBP5 in
CC a manner that is independent of splicing-mediated NXF1 deposition,
CC resulting in export prior to splicing (PubMed:17001072,
CC PubMed:19786495). May be implicated in HOX gene regulation
CC (PubMed:11344311). {ECO:0000250|UniProtKB:Q0VBL3,
CC ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495,
CC ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:27602518,
CC ECO:0000305|PubMed:11344311}.
CC -!- SUBUNIT: Component of the WMM complex, a N6-methyltransferase complex
CC composed of a catalytic subcomplex, named MAC, and of an associated
CC subcomplex, named MACOM (PubMed:27602518). The MAC subcomplex is
CC composed of METTL3 and METTL14 (PubMed:27602518). The MACOM subcomplex
CC is composed of WTAP, ZC3H13, CBLL1/HAKAI, VIRMA, and, in some cases of
CC RBM15 (RBM15 or RBM15B) (PubMed:27602518). Also a component of a MACOM-
CC like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1,
CC VIRMA, RBM15, BCLAF1 and THRAP3 (PubMed:24100041). Interacts with RBPJ
CC (By similarity). Interacts (via SPOC domain) with SETD1B
CC (PubMed:22927943). Interacts with NXF1, the interaction is required to
CC promote mRNA export (PubMed:17001072). Interacts with SF3B1
CC (PubMed:26575292). {ECO:0000250|UniProtKB:Q0VBL3,
CC ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:22927943,
CC ECO:0000269|PubMed:24100041, ECO:0000269|PubMed:26575292,
CC ECO:0000269|PubMed:27602518}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC BSFL2/BMLF1. {ECO:0000269|PubMed:16129689}.
CC -!- INTERACTION:
CC Q96T37; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-2514922, EBI-739580;
CC Q96T37; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-2514922, EBI-744115;
CC Q96T37; Q92841: DDX17; NbExp=5; IntAct=EBI-2514922, EBI-746012;
CC Q96T37; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-2514922, EBI-741037;
CC Q96T37; Q8IVL1: NAV2; NbExp=3; IntAct=EBI-2514922, EBI-741200;
CC Q96T37-3; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-12041043, EBI-11743294;
CC Q96T37-3; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-12041043, EBI-947459;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19586903,
CC ECO:0000269|PubMed:24100041}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17001072, ECO:0000269|PubMed:19786495,
CC ECO:0000269|PubMed:24100041}. Nucleus envelope
CC {ECO:0000269|PubMed:19586903}. Nucleus membrane
CC {ECO:0000269|PubMed:19786495}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19786495}. Note=Colocalizes at the nuclear pore
CC with DBP5 and NXF1. {ECO:0000269|PubMed:19786495}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1; Synonyms=RBM15s+ae;
CC IsoId=Q96T37-1; Sequence=Displayed;
CC Name=2; Synonyms=RBM15L;
CC IsoId=Q96T37-2; Sequence=VSP_005811;
CC Name=3; Synonyms=RBM15S;
CC IsoId=Q96T37-3; Sequence=VSP_005812;
CC Name=4;
CC IsoId=Q96T37-4; Sequence=VSP_053877, VSP_005811;
CC -!- PTM: Methylated at Arg-578 by PRMT1, leading to promote ubiquitination
CC by CNOT4 and subsequent degradation by the proteasome.
CC {ECO:0000269|PubMed:26575292}.
CC -!- PTM: Ubiquitinated by CNOT4 following methylation at Arg-578 by PRMT1.
CC {ECO:0000269|PubMed:26575292}.
CC -!- DISEASE: Note=A chromosomal aberration involving RBM15 may be a cause
CC of acute megakaryoblastic leukemia. Translocation t(1;22)(p13;q13) with
CC MKL1. Although both reciprocal fusion transcripts are detected in acute
CC megakaryoblastic leukemia (AMKL, FAB-M7), the RBM15-MKL1 chimeric
CC protein has all the putative functional domains encoded by each gene
CC and is the candidate oncogene. {ECO:0000269|PubMed:11344311,
CC ECO:0000269|PubMed:11431691}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation of
CC isoform 2. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RRM Spen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14088.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15185.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OTTID175.html";
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DR EMBL; AF368062; AAK54722.1; -; mRNA.
DR EMBL; AF368063; AAK54723.1; -; mRNA.
DR EMBL; AF368064; AAK54724.1; -; mRNA.
DR EMBL; AF364035; AAK56920.1; ALT_TERM; mRNA.
DR EMBL; AJ303089; CAC38828.1; ALT_TERM; mRNA.
DR EMBL; AJ303090; CAC38829.1; ALT_TERM; mRNA.
DR EMBL; AJ297259; CAC38861.1; -; Genomic_DNA.
DR EMBL; AJ297259; CAC38862.1; -; Genomic_DNA.
DR EMBL; AK022541; BAB14088.1; ALT_INIT; mRNA.
DR EMBL; AK025596; BAB15185.1; ALT_INIT; mRNA.
DR EMBL; AL355488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56439.1; -; Genomic_DNA.
DR EMBL; BC006397; AAH06397.2; -; mRNA.
DR EMBL; BC047479; AAH47479.1; -; mRNA.
DR EMBL; BC062316; AAH62316.1; -; mRNA.
DR EMBL; BC098140; AAH98140.1; -; mRNA.
DR EMBL; BC103493; AAI03494.1; -; mRNA.
DR EMBL; BC103507; AAI03508.1; -; mRNA.
DR EMBL; BK005915; DAA05818.1; -; mRNA.
DR CCDS; CCDS59198.1; -. [Q96T37-3]
DR CCDS; CCDS822.1; -. [Q96T37-1]
DR RefSeq; NP_001188474.1; NM_001201545.1. [Q96T37-3]
DR RefSeq; NP_073605.4; NM_022768.4. [Q96T37-1]
DR AlphaFoldDB; Q96T37; -.
DR SMR; Q96T37; -.
DR BioGRID; 122293; 137.
DR CORUM; Q96T37; -.
DR IntAct; Q96T37; 38.
DR MINT; Q96T37; -.
DR STRING; 9606.ENSP00000358799; -.
DR GlyGen; Q96T37; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96T37; -.
DR PhosphoSitePlus; Q96T37; -.
DR SwissPalm; Q96T37; -.
DR BioMuta; RBM15; -.
DR DMDM; 32363506; -.
DR EPD; Q96T37; -.
DR jPOST; Q96T37; -.
DR MassIVE; Q96T37; -.
DR MaxQB; Q96T37; -.
DR PaxDb; Q96T37; -.
DR PeptideAtlas; Q96T37; -.
DR PRIDE; Q96T37; -.
DR ProteomicsDB; 78180; -. [Q96T37-1]
DR ProteomicsDB; 78181; -. [Q96T37-2]
DR ProteomicsDB; 78182; -. [Q96T37-3]
DR Antibodypedia; 4448; 136 antibodies from 26 providers.
DR DNASU; 64783; -.
DR Ensembl; ENST00000369784.9; ENSP00000358799.3; ENSG00000162775.17. [Q96T37-1]
DR Ensembl; ENST00000487146.8; ENSP00000473552.3; ENSG00000162775.17. [Q96T37-3]
DR Ensembl; ENST00000602849.1; ENSP00000473638.1; ENSG00000162775.17. [Q96T37-2]
DR Ensembl; ENST00000618772.4; ENSP00000483133.1; ENSG00000162775.17. [Q96T37-1]
DR Ensembl; ENST00000652342.2; ENSP00000498328.1; ENSG00000162775.17. [Q96T37-4]
DR Ensembl; ENST00000652747.1; ENSP00000498634.1; ENSG00000162775.17. [Q96T37-3]
DR GeneID; 64783; -.
DR KEGG; hsa:64783; -.
DR MANE-Select; ENST00000369784.9; ENSP00000358799.3; NM_022768.5; NP_073605.4.
DR UCSC; uc001dzl.1; human. [Q96T37-1]
DR CTD; 64783; -.
DR DisGeNET; 64783; -.
DR GeneCards; RBM15; -.
DR HGNC; HGNC:14959; RBM15.
DR HPA; ENSG00000162775; Tissue enhanced (bone).
DR MalaCards; RBM15; -.
DR MIM; 606077; gene.
DR neXtProt; NX_Q96T37; -.
DR OpenTargets; ENSG00000162775; -.
DR Orphanet; 402023; Megakaryoblastic acute myeloid leukemia with t(1;22)(p13;q13).
DR PharmGKB; PA34264; -.
DR VEuPathDB; HostDB:ENSG00000162775; -.
DR eggNOG; KOG0112; Eukaryota.
DR GeneTree; ENSGT00940000158161; -.
DR InParanoid; Q96T37; -.
DR OMA; YVCFRTP; -.
DR OrthoDB; 367857at2759; -.
DR PhylomeDB; Q96T37; -.
DR TreeFam; TF315637; -.
DR PathwayCommons; Q96T37; -.
DR SignaLink; Q96T37; -.
DR SIGNOR; Q96T37; -.
DR BioGRID-ORCS; 64783; 107 hits in 1083 CRISPR screens.
DR ChiTaRS; RBM15; human.
DR GeneWiki; RBM15; -.
DR GenomeRNAi; 64783; -.
DR Pharos; Q96T37; Tbio.
DR PRO; PR:Q96T37; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96T37; protein.
DR Bgee; ENSG00000162775; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; Q96T37; baseline and differential.
DR Genevisible; Q96T37; HS.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0036396; C:RNA N6-methyladenosine methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0060674; P:placenta blood vessel development; IEA:Ensembl.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0045652; P:regulation of megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
DR GO; GO:0048536; P:spleen development; IEA:Ensembl.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd12553; RRM1_RBM15; 1.
DR CDD; cd12555; RRM2_RBM15; 1.
DR CDD; cd12557; RRM3_RBM15; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034470; RBM15_RRM1.
DR InterPro; IPR034472; RBM15_RRM2.
DR InterPro; IPR034473; RBM15_RRM3.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR012921; SPOC_C.
DR InterPro; IPR010912; SPOC_met.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF07744; SPOC; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS50917; SPOC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Alternative splicing;
KW Chromosomal rearrangement; Host-virus interaction; Isopeptide bond;
KW Membrane; Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..977
FT /note="RNA-binding protein 15"
FT /id="PRO_0000081777"
FT DOMAIN 170..252
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 374..451
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 455..529
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 777..956
FT /note="SPOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00249"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 954..955
FT /note="Breakpoint for translocation to form RBM15-MKL1"
FT /evidence="ECO:0000269|PubMed:11344311,
FT ECO:0000269|PubMed:11431691"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 266
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 450
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 578
FT /note="Asymmetric dimethylarginine; alternate; by PRMT1"
FT /evidence="ECO:0000269|PubMed:26575292"
FT MOD_RES 578
FT /note="Omega-N-methylarginine; alternate; by PRMT1"
FT /evidence="ECO:0000269|PubMed:26575292"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 744
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_053877"
FT VAR_SEQ 955..977
FT /note="GFGFQIGVRYENKKRENLALTLL -> AKLVEQRMKIWNSKL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11431691,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005812"
FT VAR_SEQ 956..977
FT /note="FGFQIGVRYENKKRENLALTLL -> AS (in isoform 2 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11431691"
FT /id="VSP_005811"
FT MUTAGEN 574..578
FT /note="RDRDR->KDKDK: Decreased, but not abolished
FT methylation by PRMT1."
FT /evidence="ECO:0000269|PubMed:26575292"
FT MUTAGEN 578
FT /note="R->K: Decreased methylation by PRMT1, leading to
FT decreased ubiquitination by CNOT4."
FT /evidence="ECO:0000269|PubMed:26575292"
FT MUTAGEN 795
FT /note="K->A: Disrupts interaction with SETD1B."
FT /evidence="ECO:0000269|PubMed:22927943"
FT MUTAGEN 898
FT /note="K->A: Disrupts interaction with SETD1B."
FT /evidence="ECO:0000269|PubMed:22927943"
FT MUTAGEN 923
FT /note="F->A: Disrupts interaction with SETD1B."
FT /evidence="ECO:0000269|PubMed:22927943"
FT CONFLICT 99
FT /note="H -> L (in Ref. 1; AAK54722/AAK54723/AAK54724 and 3;
FT BAB14088)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> N (in Ref. 6; AAI03494)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="R -> G (in Ref. 1; AAK54722/AAK54723/AAK54724 and 3;
FT BAB14088)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 107189 MW; FB26AFE246E40282 CRC64;
MRTAGRDPVP RRSPRWRRAV PLCETSAGRR VTQLRGDDLR RPATMKGKER SPVKAKRSRG
GEDSTSRGER SKKLGGSGGS NGSSSGKTDS GGGSRRSLHL DKSSSRGGSR EYDTGGGSSS
SRLHSYSSPS TKNSSGGGES RSSSRGGGGE SRSSGAASSA PGGGDGAEYK TLKISELGSQ
LSDEAVEDGL FHEFKRFGDV SVKISHLSGS GSGDERVAFV NFRRPEDARA AKHARGRLVL
YDRPLKIEAV YVSRRRSRSP LDKDTYPPSA SVVGASVGGH RHPPGGGGGQ RSLSPGGAAL
GYRDYRLQQL ALGRLPPPPP PPLPRDLERE RDYPFYERVR PAYSLEPRVG AGAGAAPFRE
VDEISPEDDQ RANRTLFLGN LDITVTESDL RRAFDRFGVI TEVDIKRPSR GQTSTYGFLK
FENLDMSHRA KLAMSGKIII RNPIKIGYGK ATPTTRLWVG GLGPWVPLAA LAREFDRFGT
IRTIDYRKGD SWAYIQYESL DAAHAAWTHM RGFPLGGPDR RLRVDFADTE HRYQQQYLQP
LPLTHYELVT DAFGHRAPDP LRGARDRTPP LLYRDRDRDL YPDSDWVPPP PPVRERSTRT
AATSVPAYEP LDSLDRRRDG WSLDRDRGDR DLPSSRDQPR KRRLPEESGG RHLDRSPESD
RPRKRHCAPS PDRSPELSSS RDRYNSDNDR SSRLLLERPS PIRDRRGSLE KSQGDKRDRK
NSASAERDRK HRTTAPTEGK SPLKKEDRSD GSAPSTSTAS SKLKSPSQKQ DGGTAPVASA
SPKLCLAWQG MLLLKNSNFP SNMHLLQGDL QVASSLLVEG STGGKVAQLK ITQRLRLDQP
KLDEVTRRIK VAGPNGYAIL LAVPGSSDSR SSSSSAASDT ATSTQRPLRN LVSYLKQKQA
AGVISLPVGG NKDKENTGVL HAFPPCEFSQ QFLDSPAKAL AKSEEDYLVM IIVRGFGFQI
GVRYENKKRE NLALTLL
