RBM39_HUMAN
ID RBM39_HUMAN Reviewed; 530 AA.
AC Q14498; A2RRD3; A5D8W2; B0BLV3; E1P5S0; E1P5S1; Q14499;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=RNA-binding protein 39 {ECO:0000303|PubMed:28302793};
DE AltName: Full=CAPER alpha {ECO:0000303|PubMed:24795046, ECO:0000303|PubMed:28437394};
DE Short=CAPERalpha {ECO:0000303|PubMed:24795046, ECO:0000303|PubMed:28437394};
DE AltName: Full=Hepatocellular carcinoma protein 1 {ECO:0000303|PubMed:8227358};
DE AltName: Full=RNA-binding motif protein 39;
DE AltName: Full=RNA-binding region-containing protein 2;
DE AltName: Full=Splicing factor HCC1;
GN Name=RBM39 {ECO:0000303|PubMed:28302793, ECO:0000312|HGNC:HGNC:15923};
GN Synonyms=HCC1 {ECO:0000303|PubMed:8227358}, RNPC2;
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 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=8227358; DOI=10.1172/jci116848;
RA Imai H., Chan E.K.L., Kiyosawa K., Fu X.-D., Tan E.M.;
RT "Novel nuclear autoantigen with splicing factor motifs identified with
RT antibody from hepatocellular carcinoma.";
RL J. Clin. Invest. 92:2419-2426(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [6]
RP PROTEIN SEQUENCE OF 2-17; 154-163; 168-178; 218-232; 268-289; 292-305;
RP 307-319; 330-356 AND 478-494, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP FUNCTION.
RX PubMed=15694343; DOI=10.1016/j.molcel.2004.12.025;
RA Dowhan D.H., Hong E.P., Auboeuf D., Dennis A.P., Wilson M.M., Berget S.M.,
RA O'Malley B.W.;
RT "Steroid hormone receptor coactivation and alternative RNA splicing by
RT U2AF65-related proteins CAPERalpha and CAPERbeta.";
RL Mol. Cell 17:429-439(2005).
RN [8]
RP INTERACTION WITH RSRC1.
RX PubMed=15798186; DOI=10.1128/mcb.25.8.2969-2980.2005;
RA Cazalla D., Newton K., Caceres J.F.;
RT "A novel SR-related protein is required for the second step of pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 25:2969-2980(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-95; SER-97; SER-100; SER-136;
RP SER-334; SER-337 AND SER-341, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-341, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-136 AND SER-341, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-136 AND THR-146, 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-117; SER-121;
RP SER-136; SER-337 AND SER-341, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY
RP 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-119 AND LYS-244, 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 [21]
RP FUNCTION, UBIQUITINATION, VARIANT VAL-268, AND CHARACTERIZATION OF VARIANT
RP VAL-268.
RX PubMed=28437394; DOI=10.1038/nchembio.2363;
RA Uehara T., Minoshima Y., Sagane K., Sugi N.H., Mitsuhashi K.O.,
RA Yamamoto N., Kamiyama H., Takahashi K., Kotake Y., Uesugi M., Yokoi A.,
RA Inoue A., Yoshida T., Mabuchi M., Tanaka A., Owa T.;
RT "Selective degradation of splicing factor CAPERalpha by anticancer
RT sulfonamides.";
RL Nat. Chem. Biol. 13:675-680(2017).
RN [22]
RP FUNCTION, UBIQUITINATION, VARIANTS LEU-265; ARG-268; GLU-268; TRP-268;
RP VAL-268; GLN-271; GLY-271 AND SER-272, AND CHARACTERIZATION OF VARIANTS
RP LEU-265; ARG-268; TRP-268; VAL-268; GLN-271 AND SER-272.
RX PubMed=28302793; DOI=10.1126/science.aal3755;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RT "Anticancer sulfonamides target splicing by inducing RBM39 degradation via
RT recruitment to DCAF15.";
RL Science 356:0-0(2017).
RN [23]
RP ERRATUM OF PUBMED:28302793.
RX PubMed=28546157; DOI=10.1126/science.aan7977;
RA Han T., Goralski M., Gaskill N., Capota E., Kim J., Ting T.C., Xie Y.,
RA Williams N.S., Nijhawan D.;
RL Science 356:0-0(2017).
RN [24]
RP UBIQUITINATION.
RX PubMed=31693891; DOI=10.1016/j.celrep.2019.09.079;
RA Ting T.C., Goralski M., Klein K., Wang B., Kim J., Xie Y., Nijhawan D.;
RT "Aryl sulfonamides degrade RBM39 and RBM23 by recruitment to CRL4-DCAF15.";
RL Cell Rep. 29:1499-1510(2019).
RN [25]
RP FUNCTION.
RX PubMed=31271494; DOI=10.15252/embr.201847604;
RA Tari M., Manceau V., de Matha Salone J., Kobayashi A., Pastre D.,
RA Maucuer A.;
RT "U2AF65 assemblies drive sequence-specific splice site recognition.";
RL EMBO Rep. 20:E47604-E47604(2019).
RN [26]
RP STRUCTURE BY NMR OF 235-331.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of CAPER RRM2 domain.";
RL Submitted (SEP-2007) to the PDB data bank.
RN [27]
RP STRUCTURE BY NMR OF 144-234.
RA Serrano P., Wuthrich K., Geralt M., Dutta S.K.;
RT "NMR structure of the first RRM domain of the protein RBM39 from Homo
RT sapiens.";
RL Submitted (DEC-2013) to the PDB data bank.
RN [28]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 417-530 IN COMPLEX WITH SF3B1,
RP AND FUNCTION.
RX PubMed=24795046; DOI=10.1074/jbc.m114.558825;
RA Loerch S., Maucuer A., Manceau V., Green M.R., Kielkopf C.L.;
RT "Cancer-relevant splicing factor CAPERalpha engages the essential splicing
RT factor SF3b155 in a specific ternary complex.";
RL J. Biol. Chem. 289:17325-17337(2014).
RN [29] {ECO:0007744|PDB:6Q0R, ECO:0007744|PDB:6Q0V, ECO:0007744|PDB:6Q0W}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 250-332 IN COMPLEX WITH DCAF15,
RP AND UBIQUITINATION.
RX PubMed=31686031; DOI=10.1038/s41589-019-0378-3;
RA Faust T.B., Yoon H., Nowak R.P., Donovan K.A., Li Z., Cai Q.,
RA Eleuteri N.A., Zhang T., Gray N.S., Fischer E.S.;
RT "Structural complementarity facilitates E7820-mediated degradation of RBM39
RT by DCAF15.";
RL Nat. Chem. Biol. 16:7-14(2020).
RN [30] {ECO:0007744|PDB:6SJ7, ECO:0007744|PDB:6UD7, ECO:0007744|PDB:6UE5}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 91-171 IN COMPLEX WITH DCAF15,
RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS) IN COMPLEX WITH DCAF15,
RP IDENTIFICATION IN THE DCX(DCAF15) COMPLEX, VARIANTS LEU-265; TRP-268 AND
RP VAL-268, AND CHARACTERIZATION OF VARIANTS LEU-265; TRP-268 AND VAL-268.
RX PubMed=31819272; DOI=10.1038/s41589-019-0411-6;
RA Bussiere D.E., Xie L., Srinivas H., Shu W., Burke A., Be C., Zhao J.,
RA Godbole A., King D., Karki R.G., Hornak V., Xu F., Cobb J., Carte N.,
RA Frank A.O., Frommlet A., Graff P., Knapp M., Fazal A., Okram B., Jiang S.,
RA Michellys P.Y., Beckwith R., Voshol H., Wiesmann C., Solomon J.M.,
RA Paulk J.;
RT "Structural basis of indisulam-mediated RBM39 recruitment to DCAF15 E3
RT ligase complex.";
RL Nat. Chem. Biol. 16:15-23(2020).
RN [31] {ECO:0007744|PDB:6PAI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 235-331 IN COMPLEX WITH DCAF15.
RX PubMed=31693911; DOI=10.1016/j.str.2019.10.005;
RA Du X., Volkov O.A., Czerwinski R.M., Tan H., Huerta C., Morton E.R.,
RA Rizzi J.P., Wehn P.M., Xu R., Nijhawan D., Wallace E.M.;
RT "Structural basis and kinetic pathway of RBM39 recruitment to DCAF15 by a
RT sulfonamide molecular glue E7820.";
RL Structure 27:1625-1633(2019).
CC -!- FUNCTION: RNA-binding protein that acts as a pre-mRNA splicing factor
CC (PubMed:15694343, PubMed:31271494, PubMed:28437394, PubMed:28302793,
CC PubMed:24795046). Acts by promoting exon inclusion via regulation of
CC exon cassette splicing (PubMed:31271494). Also acts as a
CC transcriptional coactivator for steroid nuclear receptors ESR1/ER-alpha
CC and ESR2/ER-beta, and JUN/AP-1, independently of the pre-mRNA splicing
CC factor activity (By similarity). {ECO:0000250|UniProtKB:Q8VH51,
CC ECO:0000269|PubMed:15694343, ECO:0000269|PubMed:24795046,
CC ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394,
CC ECO:0000269|PubMed:31271494}.
CC -!- SUBUNIT: Interacts with NCOA6 and JUN. Interacts with ESR1 and ESR2, in
CC the presence of estradiol (E2) (By similarity). Interacts with RSRC1
CC (via Arg/Ser-rich domain) (PubMed:15798186). Interacts with SF3B1
CC (PubMed:24795046). Interacts with ZNF106 (via N-terminus) (By
CC similarity). {ECO:0000250|UniProtKB:Q8VH51,
CC ECO:0000269|PubMed:15798186, ECO:0000269|PubMed:24795046}.
CC -!- INTERACTION:
CC Q14498; Q96MA6: AK8; NbExp=3; IntAct=EBI-395290, EBI-8466265;
CC Q14498; Q66PJ3-3: ARL6IP4; NbExp=3; IntAct=EBI-395290, EBI-10248982;
CC Q14498; P49760: CLK2; NbExp=9; IntAct=EBI-395290, EBI-750020;
CC Q14498; P68400: CSNK2A1; NbExp=3; IntAct=EBI-395290, EBI-347804;
CC Q14498; P67870: CSNK2B; NbExp=3; IntAct=EBI-395290, EBI-348169;
CC Q14498; Q92997: DVL3; NbExp=3; IntAct=EBI-395290, EBI-739789;
CC Q14498; A0A024RA76: hCG_1744368; NbExp=3; IntAct=EBI-395290, EBI-10180729;
CC Q14498; Q9C086: INO80B; NbExp=3; IntAct=EBI-395290, EBI-715611;
CC Q14498; Q7Z7F0: KHDC4; NbExp=3; IntAct=EBI-395290, EBI-751942;
CC Q14498; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-395290, EBI-10176379;
CC Q14498; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395290, EBI-21591415;
CC Q14498; Q6ZUT1: NKAPD1; NbExp=6; IntAct=EBI-395290, EBI-3920396;
CC Q14498; Q6ZUT1-2: NKAPD1; NbExp=3; IntAct=EBI-395290, EBI-10180231;
CC Q14498; Q15365: PCBP1; NbExp=2; IntAct=EBI-395290, EBI-946095;
CC Q14498; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-395290, EBI-713786;
CC Q14498; P78424: POU6F2; NbExp=3; IntAct=EBI-395290, EBI-12029004;
CC Q14498; Q13427: PPIG; NbExp=3; IntAct=EBI-395290, EBI-396072;
CC Q14498; O75400-2: PRPF40A; NbExp=6; IntAct=EBI-395290, EBI-5280197;
CC Q14498; O00422: SAP18; NbExp=9; IntAct=EBI-395290, EBI-1044156;
CC Q14498; O00560: SDCBP; NbExp=3; IntAct=EBI-395290, EBI-727004;
CC Q14498; Q15427: SF3B4; NbExp=3; IntAct=EBI-395290, EBI-348469;
CC Q14498; Q8WXA9: SREK1; NbExp=3; IntAct=EBI-395290, EBI-1044237;
CC Q14498; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-395290, EBI-10268630;
CC Q14498; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-395290, EBI-539478;
CC Q14498; P78362: SRPK2; NbExp=10; IntAct=EBI-395290, EBI-593303;
CC Q14498; A7MD48: SRRM4; NbExp=3; IntAct=EBI-395290, EBI-3867173;
CC Q14498; Q05519: SRSF11; NbExp=3; IntAct=EBI-395290, EBI-1051785;
CC Q14498; Q05519-2: SRSF11; NbExp=5; IntAct=EBI-395290, EBI-11975029;
CC Q14498; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-395290, EBI-741515;
CC Q14498; Q8TBK6: ZCCHC10; NbExp=4; IntAct=EBI-395290, EBI-597063;
CC Q14498-2; Q15365: PCBP1; NbExp=2; IntAct=EBI-11032687, EBI-946095;
CC Q14498-3; Q96MA6: AK8; NbExp=3; IntAct=EBI-6654703, EBI-8466265;
CC Q14498-3; Q8N9N5: BANP; NbExp=3; IntAct=EBI-6654703, EBI-744695;
CC Q14498-3; Q8TCP9: FAM200A; NbExp=3; IntAct=EBI-6654703, EBI-2799179;
CC Q14498-3; Q08379: GOLGA2; NbExp=3; IntAct=EBI-6654703, EBI-618309;
CC Q14498-3; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-6654703, EBI-10172004;
CC Q14498-3; Q7Z7F0: KHDC4; NbExp=3; IntAct=EBI-6654703, EBI-751942;
CC Q14498-3; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-6654703, EBI-9089060;
CC Q14498-3; Q9UH92: MLX; NbExp=3; IntAct=EBI-6654703, EBI-741109;
CC Q14498-3; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-6654703, EBI-713786;
CC Q14498-3; Q04864: REL; NbExp=3; IntAct=EBI-6654703, EBI-307352;
CC Q14498-3; O00422: SAP18; NbExp=3; IntAct=EBI-6654703, EBI-1044156;
CC Q14498-3; P23497: SP100; NbExp=3; IntAct=EBI-6654703, EBI-751145;
CC Q14498-3; Q05519: SRSF11; NbExp=3; IntAct=EBI-6654703, EBI-1051785;
CC Q14498-3; O15209: ZBTB22; NbExp=3; IntAct=EBI-6654703, EBI-723574;
CC Q14498-3; Q8TBK6: ZCCHC10; NbExp=3; IntAct=EBI-6654703, EBI-597063;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:8227358}.
CC Note=Concentrated in nuclear speckles (PubMed:8227358). Colocalizes
CC with the core spliceosomal snRNP proteins (PubMed:8227358).
CC {ECO:0000269|PubMed:8227358}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HCC1.4;
CC IsoId=Q14498-1; Sequence=Displayed;
CC Name=2; Synonyms=HCC1.3;
CC IsoId=Q14498-2; Sequence=VSP_005820;
CC Name=3;
CC IsoId=Q14498-3; Sequence=VSP_043375;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in pancreas,
CC skeletal muscle, lung and brain (PubMed:8227358). Expressed at
CC intermediate level in kidney, liver and heart (PubMed:8227358).
CC {ECO:0000269|PubMed:8227358}.
CC -!- PTM: Aryl sulfonamide anticancer drugs, such as indisulam (E7070) or
CC E7820, promote ubiquitination and subsequent degradation by the
CC DCX(DCAF15) complex (PubMed:31693891, PubMed:28437394,
CC PubMed:28302793). RBM39 degradation results in splicing defects and
CC death in cancer cell lines (PubMed:31693891, PubMed:28437394,
CC PubMed:28302793). Aryl sulfonamide anticancer drugs change the
CC substrate specificity of DCAF15 by acting as a molecular glue that
CC promotes binding between DCAF15 and weak affinity interactor RBM39
CC (PubMed:31686031, PubMed:31819272). {ECO:0000269|PubMed:28302793,
CC ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:31686031,
CC ECO:0000269|PubMed:31693891, ECO:0000269|PubMed:31819272}.
CC -!- MISCELLANEOUS: Antibodies against RBM39 are present in sera from a
CC patient with hepatocellular carcinoma who developed several
CC autoantibodies. {ECO:0000269|PubMed:8227358}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; L10910; AAA16346.1; -; mRNA.
DR EMBL; L10911; AAA16347.1; -; mRNA.
DR EMBL; AK299678; BAG61586.1; -; mRNA.
DR EMBL; AL357374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76159.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76161.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76162.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76163.1; -; Genomic_DNA.
DR EMBL; BC131543; AAI31544.1; -; mRNA.
DR EMBL; BC141835; AAI41836.1; -; mRNA.
DR EMBL; BC158172; AAI58173.1; -; mRNA.
DR CCDS; CCDS13265.1; -. [Q14498-2]
DR CCDS; CCDS13266.1; -. [Q14498-1]
DR CCDS; CCDS56186.1; -. [Q14498-3]
DR PIR; I55595; I55595.
DR RefSeq; NP_001229528.1; NM_001242599.1. [Q14498-3]
DR RefSeq; NP_001229529.1; NM_001242600.1.
DR RefSeq; NP_004893.1; NM_004902.3. [Q14498-2]
DR RefSeq; NP_909122.1; NM_184234.2. [Q14498-1]
DR PDB; 2JRS; NMR; -; A=235-331.
DR PDB; 2MHN; NMR; -; A=144-234.
DR PDB; 4OO6; X-ray; 2.70 A; B=73-99.
DR PDB; 4OZ0; X-ray; 2.20 A; A/B=417-530.
DR PDB; 4OZ1; X-ray; 1.74 A; A/B=417-530.
DR PDB; 4YUD; X-ray; 1.28 A; A=144-234.
DR PDB; 6PAI; X-ray; 2.90 A; D=235-331.
DR PDB; 6Q0R; X-ray; 2.90 A; D=250-332.
DR PDB; 6Q0V; X-ray; 2.90 A; D=250-332.
DR PDB; 6Q0W; X-ray; 2.90 A; D=250-332.
DR PDB; 6SJ7; EM; 3.54 A; C=91-171.
DR PDB; 6UD7; X-ray; 2.30 A; C=91-171.
DR PDB; 6UE5; X-ray; 2.61 A; C=91-171.
DR PDBsum; 2JRS; -.
DR PDBsum; 2MHN; -.
DR PDBsum; 4OO6; -.
DR PDBsum; 4OZ0; -.
DR PDBsum; 4OZ1; -.
DR PDBsum; 4YUD; -.
DR PDBsum; 6PAI; -.
DR PDBsum; 6Q0R; -.
DR PDBsum; 6Q0V; -.
DR PDBsum; 6Q0W; -.
DR PDBsum; 6SJ7; -.
DR PDBsum; 6UD7; -.
DR PDBsum; 6UE5; -.
DR AlphaFoldDB; Q14498; -.
DR BMRB; Q14498; -.
DR SMR; Q14498; -.
DR BioGRID; 114952; 920.
DR CORUM; Q14498; -.
DR DIP; DIP-32928N; -.
DR IntAct; Q14498; 107.
DR MINT; Q14498; -.
DR STRING; 9606.ENSP00000253363; -.
DR ChEMBL; CHEMBL4680031; -.
DR GlyGen; Q14498; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14498; -.
DR MetOSite; Q14498; -.
DR PhosphoSitePlus; Q14498; -.
DR SwissPalm; Q14498; -.
DR BioMuta; RBM39; -.
DR DMDM; 28201880; -.
DR EPD; Q14498; -.
DR jPOST; Q14498; -.
DR MassIVE; Q14498; -.
DR MaxQB; Q14498; -.
DR PaxDb; Q14498; -.
DR PeptideAtlas; Q14498; -.
DR PRIDE; Q14498; -.
DR ProteomicsDB; 60005; -. [Q14498-1]
DR ProteomicsDB; 60006; -. [Q14498-2]
DR ProteomicsDB; 60007; -. [Q14498-3]
DR Antibodypedia; 459; 238 antibodies from 28 providers.
DR DNASU; 9584; -.
DR Ensembl; ENST00000253363.11; ENSP00000253363.6; ENSG00000131051.24. [Q14498-1]
DR Ensembl; ENST00000361162.10; ENSP00000354437.6; ENSG00000131051.24. [Q14498-2]
DR Ensembl; ENST00000528062.7; ENSP00000436747.2; ENSG00000131051.24. [Q14498-3]
DR GeneID; 9584; -.
DR KEGG; hsa:9584; -.
DR MANE-Select; ENST00000253363.11; ENSP00000253363.6; NM_184234.3; NP_909122.1.
DR UCSC; uc002xeb.4; human. [Q14498-1]
DR CTD; 9584; -.
DR DisGeNET; 9584; -.
DR GeneCards; RBM39; -.
DR HGNC; HGNC:15923; RBM39.
DR HPA; ENSG00000131051; Low tissue specificity.
DR MIM; 604739; gene.
DR neXtProt; NX_Q14498; -.
DR OpenTargets; ENSG00000131051; -.
DR PharmGKB; PA34450; -.
DR VEuPathDB; HostDB:ENSG00000131051; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000154468; -.
DR InParanoid; Q14498; -.
DR OMA; GRDNDKG; -.
DR OrthoDB; 873705at2759; -.
DR PhylomeDB; Q14498; -.
DR TreeFam; TF320448; -.
DR PathwayCommons; Q14498; -.
DR SignaLink; Q14498; -.
DR SIGNOR; Q14498; -.
DR BioGRID-ORCS; 9584; 717 hits in 1094 CRISPR screens.
DR ChiTaRS; RBM39; human.
DR EvolutionaryTrace; Q14498; -.
DR GeneWiki; RBM39; -.
DR GenomeRNAi; 9584; -.
DR Pharos; Q14498; Tbio.
DR PRO; PR:Q14498; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q14498; protein.
DR Bgee; ENSG00000131051; Expressed in right uterine tube and 172 other tissues.
DR ExpressionAtlas; Q14498; baseline and differential.
DR Genevisible; Q14498; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0050733; F:RS domain binding; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 3.
DR IDEAL; IID00567; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR029123; RBM39_linker.
DR InterPro; IPR006509; RBM39_SF.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF15519; RBM39linker; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01622; SF-CC1; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..530
FT /note="RNA-binding protein 39"
FT /id="PRO_0000081814"
FT DOMAIN 153..230
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 250..328
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 445..508
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..406
FT /note="Interaction with JUN"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 291..355
FT /note="Activating domain"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 355..406
FT /note="Interaction with ESR1 and ESR2"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT REGION 406..530
FT /note="Interaction with NCOA6"
FT /evidence="ECO:0000250|UniProtKB:Q8VH51"
FT COMPBIAS 9..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..92
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 95
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 100..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043375"
FT VAR_SEQ 392..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8227358"
FT /id="VSP_005820"
FT VARIANT 2
FT /note="A -> V (in dbSNP:rs1803701)"
FT /id="VAR_015228"
FT VARIANT 265
FT /note="M -> L (associated with resistance to anticancer
FT indisulam; decreased interaction with the DCX(DCAF15)
FT complex in presence of indisulam; abolished degradation by
FT the DCX(DCAF15) complex in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083212"
FT VARIANT 268
FT /note="G -> E (associated with resistance to anticancer
FT indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083213"
FT VARIANT 268
FT /note="G -> R (associated with resistance to anticancer
FT indisulam; abolished degradation by the DCX(DCAF15) complex
FT in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083214"
FT VARIANT 268
FT /note="G -> V (associated with resistance to anticancer
FT indisulam; decreased interaction with the DCX(DCAF15)
FT complex in presence of indisulam; abolished degradation by
FT the DCX(DCAF15) complex in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793,
FT ECO:0000269|PubMed:28437394"
FT /id="VAR_083215"
FT VARIANT 268
FT /note="G -> W (associated with resistance to anticancer
FT indisulam; decreased interaction with the DCX(DCAF15)
FT complex in presence of indisulam; abolished degradation by
FT the DCX(DCAF15) complex in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083216"
FT VARIANT 271
FT /note="E -> G (associated with resistance to anticancer
FT indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083217"
FT VARIANT 271
FT /note="E -> Q (associated with resistance to anticancer
FT indisulam; abolished degradation by the DCX(DCAF15) complex
FT in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083218"
FT VARIANT 272
FT /note="P -> S (associated with resistance to anticancer
FT indisulam; abolished degradation by the DCX(DCAF15) complex
FT in presence of indisulam)"
FT /evidence="ECO:0000269|PubMed:28302793"
FT /id="VAR_083219"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:4YUD"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:4YUD"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:4YUD"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4YUD"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4YUD"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2MHN"
FT STRAND 195..203
FT /evidence="ECO:0007829|PDB:4YUD"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:4YUD"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:4YUD"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:4YUD"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2JRS"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6UD7"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 288..300
FT /evidence="ECO:0007829|PDB:6UD7"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6PAI"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6UD7"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:4OZ1"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:4OZ1"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:4OZ1"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:4OZ1"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:4OZ1"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:4OZ1"
FT HELIX 481..491
FT /evidence="ECO:0007829|PDB:4OZ1"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:4OZ1"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:4OZ1"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:4OZ1"
SQ SEQUENCE 530 AA; 59380 MW; 0CC610356D4AA040 CRC64;
MADDIDIEAM LEAPYKKDEN KLSSANGHEE RSKKRKKSKS RSRSHERKRS KSKERKRSRD
RERKKSKSRE RKRSRSKERR RSRSRSRDRR FRGRYRSPYS GPKFNSAIRG KIGLPHSIKL
SRRRSRSKSP FRKDKSPVRE PIDNLTPEER DARTVFCMQL AARIRPRDLE EFFSTVGKVR
DVRMISDRNS RRSKGIAYVE FVDVSSVPLA IGLTGQRVLG VPIIVQASQA EKNRAAAMAN
NLQKGSAGPM RLYVGSLHFN ITEDMLRGIF EPFGRIESIQ LMMDSETGRS KGYGFITFSD
SECAKKALEQ LNGFELAGRP MKVGHVTERT DASSASSFLD SDELERTGID LGTTGRLQLM
ARLAEGTGLQ IPPAAQQALQ MSGSLAFGAV AEFSFVIDLQ TRLSQQTEAS ALAAAASVQP
LATQCFQLSN MFNPQTEEEV GWDTEIKDDV IEECNKHGGV IHIYVDKNSA QGNVYVKCPS
IAAAIAAVNA LHGRWFAGKM ITAAYVPLPT YHNLFPDSMT ATQLLVPSRR
