YTDC1_HUMAN
ID YTDC1_HUMAN Reviewed; 727 AA.
AC Q96MU7; Q4W5Q3; Q7Z622; Q8TF35;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=YTH domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Splicing factor YT521 {ECO:0000303|PubMed:12755701};
DE Short=YT521-B {ECO:0000303|PubMed:12755701};
GN Name=YTHDC1 {ECO:0000312|HGNC:HGNC:30626};
GN Synonyms=KIAA1966 {ECO:0000303|PubMed:11853319},
GN YT521 {ECO:0000303|PubMed:12755701};
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-727 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [5]
RP INTERACTION WITH EMD.
RX PubMed=12755701; DOI=10.1046/j.1432-1033.2003.03617.x;
RA Wilkinson F.L., Holaska J.M., Zhang Z., Sharma A., Manilal S., Holt I.,
RA Stamm S., Wilson K.L., Morris G.E.;
RT "Emerin interacts in vitro with the splicing-associated factor, YT521-B.";
RL Eur. J. Biochem. 270:2459-2466(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-315; SER-317;
RP SER-318; SER-320 AND SER-424, 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 [9]
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 [10]
RP INTERACTION WITH RBMX.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-148; SER-308;
RP SER-424 AND SER-435, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-120; SER-308;
RP SER-424 AND SER-545, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; THR-148 AND SER-308, AND
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-96, 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 [16]
RP FUNCTION, RNA-BINDING, AND MUTAGENESIS OF ASN-367; LEU-380 AND MET-438.
RX PubMed=26318451; DOI=10.1074/jbc.m115.680389;
RA Xu C., Liu K., Ahmed H., Loppnau P., Schapira M., Min J.;
RT "structural basis for the discriminative recognition of N6-methyladenosine
RT RNA by the human YT521-B homology domain family of proteins.";
RL J. Biol. Chem. 290:24902-24913(2015).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SRSF3 AND SRSF10, AND
RP MUTAGENESIS OF TRP-377 AND TRP-428.
RX PubMed=26876937; DOI=10.1016/j.molcel.2016.01.012;
RA Xiao W., Adhikari S., Dahal U., Chen Y.S., Hao Y.J., Sun B.F., Sun H.Y.,
RA Li A., Ping X.L., Lai W.Y., Wang X., Ma H.L., Huang C.M., Yang Y.,
RA Huang N., Jiang G.B., Wang H.L., Zhou Q., Wang X.J., Zhao Y.L., Yang Y.G.;
RT "Nuclear m(6)A reader YTHDC1 regulates mRNA splicing.";
RL Mol. Cell 61:507-519(2016).
RN [18]
RP FUNCTION, AND RNA-BINDING.
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 [19]
RP FUNCTION, AND INTERACTION WITH SRSF3 AND ZCCHC8.
RX PubMed=28984244; DOI=10.7554/elife.31311;
RA Roundtree I.A., Luo G.Z., Zhang Z., Wang X., Zhou T., Cui Y., Sha J.,
RA Huang X., Guerrero L., Xie P., He E., Shen B., He C.;
RT "YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs.";
RL Elife 6:0-0(2017).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-96, AND IDENTIFICATION BY MASS
RP 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 STRUCTURE BY NMR OF 334-509, RNA-BINDING, SUBCELLULAR LOCATION, FUNCTION,
RP AND MUTAGENESIS OF LYS-361; SER-362; TRP-377; LEU-387; LEU-399; PHE-401;
RP SER-402; PHE-409; GLY-411; TRP-428; TRP-447; ASN-466; ARG-475 AND ASP-476.
RX PubMed=20167602; DOI=10.1074/jbc.m110.104711;
RA Zhang Z., Theler D., Kaminska K.H., Hiller M., de la Grange P., Pudimat R.,
RA Rafalska I., Heinrich B., Bujnicki J.M., Allain F.H., Stamm S.;
RT "The YTH domain is a novel RNA binding domain.";
RL J. Biol. Chem. 285:14701-14710(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 345-509 IN COMPLEX WITH
RP N6-METHYLADENOSINE (M6A)-CONTAINING RNA, FUNCTION, RNA-BINDING, AND
RP MUTAGENESIS OF TRP-377; TRP-428 AND ARG-475.
RX PubMed=25242552; DOI=10.1038/nchembio.1654;
RA Xu C., Wang X., Liu K., Roundtree I.A., Tempel W., Li Y., Lu Z., He C.,
RA Min J.;
RT "Structural basis for selective binding of m6A RNA by the YTHDC1 YTH
RT domain.";
RL Nat. Chem. Biol. 10:927-929(2014).
RN [23] {ECO:0007744|PDB:6RT4, ECO:0007744|PDB:6RT5, ECO:0007744|PDB:6RT6, ECO:0007744|PDB:6RT7}
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 345-509 IN COMPLEX WITH
RP N6-METHYLADENOSINE (M6A)-CONTAINING RNA.
RX PubMed=31670957; DOI=10.1021/acs.jctc.9b00987;
RA Li Y., Bedi R.K., Wiedmer L., Huang D., Sledz P., Caflisch A.;
RT "Flexible binding of m6A reader protein YTHDC1 to its preferred RNA
RT motif.";
RL J. Chem. Theory Comput. 15:7004-7014(2019).
RN [24] {ECO:0007744|PDB:6WE8, ECO:0007744|PDB:6WE9, ECO:0007744|PDB:6WEA}
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 345-509 IN COMPLEX WITH
RP N6-METHYLADENOSINE (M6A)-CONTAINING SINGLE-STRANDED DNA, AND FUNCTION.
RX PubMed=32663306; DOI=10.1093/nar/gkaa604;
RA Woodcock C.B., Horton J.R., Zhou J., Bedford M.T., Blumenthal R.M.,
RA Zhang X., Cheng X.;
RT "Biochemical and structural basis for YTH domain of human YTHDC1 binding to
RT methylated adenine in DNA.";
RL Nucleic Acids Res. 48:10329-10341(2020).
CC -!- FUNCTION: Regulator of alternative splicing that specifically
CC recognizes and binds N6-methyladenosine (m6A)-containing RNAs
CC (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244).
CC M6A is a modification present at internal sites of mRNAs and some non-
CC coding RNAs and plays a role in the efficiency of mRNA splicing,
CC processing and stability (PubMed:25242552, PubMed:26318451). Acts as a
CC key regulator of exon-inclusion or exon-skipping during alternative
CC splicing via interaction with mRNA splicing factors SRSF3 and SRSF10
CC (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes
CC recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A
CC sites, leading to exon-inclusion during alternative splicing
CC (PubMed:26876937). In contrast, interaction with SRSF3 prevents
CC interaction with SRSF10, a splicing factor that promotes exon skipping:
CC this prevents SRSF10 from binding to its mRNA-binding sites close to
CC m6A-containing regions, leading to inhibit exon skipping during
CC alternative splicing (PubMed:26876937). May also regulate alternative
CC splice site selection (PubMed:20167602). Also involved in nuclear
CC export of m6A-containing mRNAs via interaction with SRSF3: interaction
CC with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and
CC NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S-
CC adenosyl-L-methionine homeostasis by regulating expression of MAT2A
CC transcripts, probably by binding m6A-containing MAT2A mRNAs (By
CC similarity). Also recognizes and binds m6A on other RNA molecules
CC (PubMed:27602518). Involved in random X inactivation mediated by Xist
CC RNA: recognizes and binds m6A-containing Xist and promotes
CC transcription repression activity of Xist (PubMed:27602518). Also
CC recognizes and binds m6A-containing single-stranded DNA
CC (PubMed:32663306). Involved in germline development: required for
CC spermatogonial development in males and oocyte growth and maturation in
CC females, probably via its role in alternative splicing (By similarity).
CC {ECO:0000250|UniProtKB:E9Q5K9, ECO:0000269|PubMed:20167602,
CC ECO:0000269|PubMed:25242552, ECO:0000269|PubMed:26318451,
CC ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:27602518,
CC ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:32663306}.
CC -!- SUBUNIT: Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By
CC similarity). Interacts with SRSF3 (PubMed:26876937, PubMed:28984244).
CC Interacts with SRSF7 (By similarity). Interacts with SRSF10
CC (PubMed:26876937). Interacts with CPSF6 (By similarity). Interacts with
CC KHDRBS1/SAM68 (By similarity). Interacts with TRA2B (By similarity).
CC Interacts with KHDRBS3 (By similarity). Interacts with EMD
CC (PubMed:12755701). Interacts with RBMX (PubMed:19282290). Interacts
CC with ZCCHC8 (PubMed:28984244). {ECO:0000250|UniProtKB:E9Q5K9,
CC ECO:0000250|UniProtKB:Q9QY02, ECO:0000269|PubMed:12755701,
CC ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:26876937,
CC ECO:0000269|PubMed:28984244}.
CC -!- INTERACTION:
CC Q96MU7; O15084: ANKRD28; NbExp=3; IntAct=EBI-2849854, EBI-359567;
CC Q96MU7; P49760: CLK2; NbExp=6; IntAct=EBI-2849854, EBI-750020;
CC Q96MU7; Q92997: DVL3; NbExp=6; IntAct=EBI-2849854, EBI-739789;
CC Q96MU7; P61978: HNRNPK; NbExp=4; IntAct=EBI-2849854, EBI-304185;
CC Q96MU7; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-2849854, EBI-7060731;
CC Q96MU7; Q5VWX1: KHDRBS2; NbExp=6; IntAct=EBI-2849854, EBI-742808;
CC Q96MU7; O75525: KHDRBS3; NbExp=6; IntAct=EBI-2849854, EBI-722504;
CC Q96MU7; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-2849854, EBI-12012928;
CC Q96MU7; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-2849854, EBI-2339674;
CC Q96MU7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2849854, EBI-79165;
CC Q96MU7; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-2849854, EBI-11994018;
CC Q96MU7; Q15415: RBMY1J; NbExp=6; IntAct=EBI-2849854, EBI-8642021;
CC Q96MU7; Q15287: RNPS1; NbExp=3; IntAct=EBI-2849854, EBI-395959;
CC Q96MU7; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-2849854, EBI-742426;
CC Q96MU7; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-2849854, EBI-539478;
CC Q96MU7; P78362: SRPK2; NbExp=4; IntAct=EBI-2849854, EBI-593303;
CC Q96MU7; P62995: TRA2B; NbExp=4; IntAct=EBI-2849854, EBI-725485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20167602}. Nucleus
CC speckle {ECO:0000269|PubMed:26876937}. Note=Localizes to a novel
CC subnuclear structure, the YT bodies. {ECO:0000250|UniProtKB:Q9QY02}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96MU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96MU7-2; Sequence=VSP_006818;
CC -!- DOMAIN: The YTH domain mediates RNA-binding.
CC {ECO:0000269|PubMed:20167602}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q9QY02}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY41024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB71181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK056430; BAB71181.1; ALT_INIT; mRNA.
DR EMBL; AC074378; AAY41024.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC041119; AAH41119.1; -; mRNA.
DR EMBL; BC053863; AAH53863.1; -; mRNA.
DR EMBL; AB075846; BAB85552.1; -; mRNA.
DR CCDS; CCDS33992.1; -. [Q96MU7-1]
DR CCDS; CCDS3522.2; -. [Q96MU7-2]
DR RefSeq; NP_001026902.1; NM_001031732.3. [Q96MU7-1]
DR RefSeq; NP_001317627.1; NM_001330698.1.
DR RefSeq; NP_588611.2; NM_133370.3. [Q96MU7-2]
DR PDB; 2YUD; NMR; -; A=337-509.
DR PDB; 4R3H; X-ray; 1.90 A; A/B=345-509.
DR PDB; 4R3I; X-ray; 1.80 A; A=345-509.
DR PDB; 6RT4; X-ray; 1.49 A; A/B=345-509.
DR PDB; 6RT5; X-ray; 2.30 A; B/C=345-509.
DR PDB; 6RT6; X-ray; 1.46 A; B/C=345-509.
DR PDB; 6RT7; X-ray; 1.73 A; B/C=345-509.
DR PDB; 6SYZ; X-ray; 2.28 A; A/B=345-509.
DR PDB; 6SZ1; X-ray; 1.75 A; A/B=345-509.
DR PDB; 6SZ2; X-ray; 1.52 A; A/B=345-509.
DR PDB; 6SZ3; X-ray; 1.28 A; A/B=345-509.
DR PDB; 6SZL; X-ray; 1.45 A; A/B=345-509.
DR PDB; 6SZN; X-ray; 1.47 A; A/B=345-509.
DR PDB; 6SZR; X-ray; 1.64 A; A/B=345-509.
DR PDB; 6SZT; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6SZX; X-ray; 1.17 A; A/B=345-509.
DR PDB; 6SZY; X-ray; 1.79 A; A/B=345-509.
DR PDB; 6T01; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6T02; X-ray; 1.10 A; A/B=345-509.
DR PDB; 6T03; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6T04; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6T05; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6T06; X-ray; 2.40 A; A/B=345-509.
DR PDB; 6T07; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6T08; X-ray; 1.41 A; A/B=345-509.
DR PDB; 6T09; X-ray; 1.75 A; A/B=345-509.
DR PDB; 6T0A; X-ray; 2.02 A; A/B=345-509.
DR PDB; 6T0C; X-ray; 2.03 A; A/B=345-509.
DR PDB; 6T0D; X-ray; 1.43 A; A/B=345-509.
DR PDB; 6T0O; X-ray; 1.71 A; A/B=345-509.
DR PDB; 6T0X; X-ray; 1.36 A; A/B=345-509.
DR PDB; 6T0Z; X-ray; 1.43 A; A/B=345-509.
DR PDB; 6T10; X-ray; 1.48 A; A/B=345-509.
DR PDB; 6T11; X-ray; 1.49 A; A/B=345-509.
DR PDB; 6T12; X-ray; 1.46 A; A/B=345-509.
DR PDB; 6WE8; X-ray; 1.18 A; A/B=345-509.
DR PDB; 6WE9; X-ray; 1.59 A; A/C=345-509.
DR PDB; 6WEA; X-ray; 1.80 A; A/B/C/D=345-509.
DR PDB; 6YKE; X-ray; 1.52 A; A/B=345-509.
DR PDB; 6YKI; X-ray; 1.30 A; A/B=345-509.
DR PDB; 6YKJ; X-ray; 1.60 A; A/B=345-509.
DR PDB; 6YKZ; X-ray; 1.20 A; A/B=345-509.
DR PDB; 6YL0; X-ray; 1.20 A; A/B=345-509.
DR PDB; 6YL8; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YL9; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YM2; X-ray; 1.70 A; A/B=345-509.
DR PDB; 6YM6; X-ray; 1.20 A; A/B=345-509.
DR PDB; 6YM8; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YNI; X-ray; 1.36 A; A/B=345-509.
DR PDB; 6YNJ; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YNK; X-ray; 1.30 A; A/B=345-509.
DR PDB; 6YNL; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YNM; X-ray; 1.50 A; A/B=345-509.
DR PDB; 6YNN; X-ray; 1.20 A; A/B=345-509.
DR PDB; 6YNO; X-ray; 1.40 A; A/B=345-509.
DR PDB; 6YNP; X-ray; 1.10 A; A/B=345-509.
DR PDB; 6YOQ; X-ray; 1.30 A; A/B=345-509.
DR PDB; 6ZCM; X-ray; 1.24 A; A/B=345-509.
DR PDB; 6ZCN; X-ray; 1.60 A; A/B=345-509.
DR PDB; 6ZD9; X-ray; 1.51 A; A/B=345-509.
DR PDB; 7L4X; X-ray; 1.79 A; B=345-509.
DR PDB; 7L4Y; X-ray; 1.79 A; B=345-509.
DR PDB; 7P87; X-ray; 1.30 A; A/B=345-509.
DR PDB; 7P88; X-ray; 1.50 A; A/B=345-509.
DR PDB; 7P8A; X-ray; 1.70 A; A/B=345-509.
DR PDB; 7P8B; X-ray; 1.20 A; A/B=345-509.
DR PDB; 7P8F; X-ray; 1.50 A; A/B=345-509.
DR PDB; 7PJ7; X-ray; 1.41 A; A/B=345-509.
DR PDB; 7PJ8; X-ray; 1.40 A; A/B=345-509.
DR PDB; 7PJ9; X-ray; 1.72 A; A/B=345-509.
DR PDB; 7PJA; X-ray; 1.85 A; A/B=345-509.
DR PDB; 7PJB; X-ray; 1.90 A; A/B=345-509.
DR PDB; 7PJP; X-ray; 1.61 A; A/B=345-509.
DR PDB; 7PJQ; X-ray; 1.20 A; A/B=345-509.
DR PDB; 7PO6; X-ray; 1.77 A; A/B/C=345-509.
DR PDBsum; 2YUD; -.
DR PDBsum; 4R3H; -.
DR PDBsum; 4R3I; -.
DR PDBsum; 6RT4; -.
DR PDBsum; 6RT5; -.
DR PDBsum; 6RT6; -.
DR PDBsum; 6RT7; -.
DR PDBsum; 6SYZ; -.
DR PDBsum; 6SZ1; -.
DR PDBsum; 6SZ2; -.
DR PDBsum; 6SZ3; -.
DR PDBsum; 6SZL; -.
DR PDBsum; 6SZN; -.
DR PDBsum; 6SZR; -.
DR PDBsum; 6SZT; -.
DR PDBsum; 6SZX; -.
DR PDBsum; 6SZY; -.
DR PDBsum; 6T01; -.
DR PDBsum; 6T02; -.
DR PDBsum; 6T03; -.
DR PDBsum; 6T04; -.
DR PDBsum; 6T05; -.
DR PDBsum; 6T06; -.
DR PDBsum; 6T07; -.
DR PDBsum; 6T08; -.
DR PDBsum; 6T09; -.
DR PDBsum; 6T0A; -.
DR PDBsum; 6T0C; -.
DR PDBsum; 6T0D; -.
DR PDBsum; 6T0O; -.
DR PDBsum; 6T0X; -.
DR PDBsum; 6T0Z; -.
DR PDBsum; 6T10; -.
DR PDBsum; 6T11; -.
DR PDBsum; 6T12; -.
DR PDBsum; 6WE8; -.
DR PDBsum; 6WE9; -.
DR PDBsum; 6WEA; -.
DR PDBsum; 6YKE; -.
DR PDBsum; 6YKI; -.
DR PDBsum; 6YKJ; -.
DR PDBsum; 6YKZ; -.
DR PDBsum; 6YL0; -.
DR PDBsum; 6YL8; -.
DR PDBsum; 6YL9; -.
DR PDBsum; 6YM2; -.
DR PDBsum; 6YM6; -.
DR PDBsum; 6YM8; -.
DR PDBsum; 6YNI; -.
DR PDBsum; 6YNJ; -.
DR PDBsum; 6YNK; -.
DR PDBsum; 6YNL; -.
DR PDBsum; 6YNM; -.
DR PDBsum; 6YNN; -.
DR PDBsum; 6YNO; -.
DR PDBsum; 6YNP; -.
DR PDBsum; 6YOQ; -.
DR PDBsum; 6ZCM; -.
DR PDBsum; 6ZCN; -.
DR PDBsum; 6ZD9; -.
DR PDBsum; 7L4X; -.
DR PDBsum; 7L4Y; -.
DR PDBsum; 7P87; -.
DR PDBsum; 7P88; -.
DR PDBsum; 7P8A; -.
DR PDBsum; 7P8B; -.
DR PDBsum; 7P8F; -.
DR PDBsum; 7PJ7; -.
DR PDBsum; 7PJ8; -.
DR PDBsum; 7PJ9; -.
DR PDBsum; 7PJA; -.
DR PDBsum; 7PJB; -.
DR PDBsum; 7PJP; -.
DR PDBsum; 7PJQ; -.
DR PDBsum; 7PO6; -.
DR AlphaFoldDB; Q96MU7; -.
DR BMRB; Q96MU7; -.
DR SMR; Q96MU7; -.
DR BioGRID; 124871; 180.
DR IntAct; Q96MU7; 64.
DR MINT; Q96MU7; -.
DR STRING; 9606.ENSP00000339245; -.
DR GlyGen; Q96MU7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96MU7; -.
DR PhosphoSitePlus; Q96MU7; -.
DR SwissPalm; Q96MU7; -.
DR BioMuta; YTHDC1; -.
DR DMDM; 47606762; -.
DR EPD; Q96MU7; -.
DR jPOST; Q96MU7; -.
DR MassIVE; Q96MU7; -.
DR MaxQB; Q96MU7; -.
DR PaxDb; Q96MU7; -.
DR PeptideAtlas; Q96MU7; -.
DR PRIDE; Q96MU7; -.
DR ProteomicsDB; 77413; -. [Q96MU7-1]
DR ProteomicsDB; 77414; -. [Q96MU7-2]
DR Antibodypedia; 52214; 101 antibodies from 23 providers.
DR DNASU; 91746; -.
DR Ensembl; ENST00000344157.9; ENSP00000339245.4; ENSG00000083896.13. [Q96MU7-1]
DR Ensembl; ENST00000355665.7; ENSP00000347888.3; ENSG00000083896.13. [Q96MU7-2]
DR Ensembl; ENST00000613637.3; ENSP00000484604.1; ENSG00000275272.4. [Q96MU7-2]
DR Ensembl; ENST00000615500.4; ENSP00000479213.1; ENSG00000275272.4. [Q96MU7-1]
DR GeneID; 91746; -.
DR KEGG; hsa:91746; -.
DR MANE-Select; ENST00000344157.9; ENSP00000339245.4; NM_001031732.4; NP_001026902.1.
DR UCSC; uc003hdx.4; human. [Q96MU7-1]
DR CTD; 91746; -.
DR DisGeNET; 91746; -.
DR GeneCards; YTHDC1; -.
DR HGNC; HGNC:30626; YTHDC1.
DR HPA; ENSG00000083896; Low tissue specificity.
DR neXtProt; NX_Q96MU7; -.
DR OpenTargets; ENSG00000083896; -.
DR PharmGKB; PA143485673; -.
DR VEuPathDB; HostDB:ENSG00000083896; -.
DR eggNOG; KOG1902; Eukaryota.
DR GeneTree; ENSGT00940000155803; -.
DR InParanoid; Q96MU7; -.
DR OMA; CHTSTVY; -.
DR OrthoDB; 1523119at2759; -.
DR PhylomeDB; Q96MU7; -.
DR TreeFam; TF325590; -.
DR PathwayCommons; Q96MU7; -.
DR SignaLink; Q96MU7; -.
DR SIGNOR; Q96MU7; -.
DR BioGRID-ORCS; 91746; 448 hits in 1082 CRISPR screens.
DR ChiTaRS; YTHDC1; human.
DR EvolutionaryTrace; Q96MU7; -.
DR GeneWiki; YTHDC1; -.
DR GenomeRNAi; 91746; -.
DR Pharos; Q96MU7; Tbio.
DR PRO; PR:Q96MU7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96MU7; protein.
DR Bgee; ENSG00000083896; Expressed in calcaneal tendon and 100 other tissues.
DR ExpressionAtlas; Q96MU7; baseline and differential.
DR Genevisible; Q96MU7; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048160; P:primary follicle stage; IEA:Ensembl.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 2.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..727
FT /note="YTH domain-containing protein 1"
FT /id="PRO_0000223076"
FT DOMAIN 355..492
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 361..363
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:31670957,
FT ECO:0007744|PDB:6RT4, ECO:0007744|PDB:6RT5,
FT ECO:0007744|PDB:6RT6, ECO:0007744|PDB:6RT7"
FT BINDING 377..378
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:25242552,
FT ECO:0000269|PubMed:31670957, ECO:0007744|PDB:6RT4,
FT ECO:0007744|PDB:6RT5, ECO:0007744|PDB:6RT6,
FT ECO:0007744|PDB:6RT7"
FT BINDING 428
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:25242552"
FT BINDING 476
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000269|PubMed:31670957,
FT ECO:0007744|PDB:6RT4, ECO:0007744|PDB:6RT5,
FT ECO:0007744|PDB:6RT6, ECO:0007744|PDB:6RT7"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY02"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 308
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 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 325..342
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006818"
FT VARIANT 183
FT /note="H -> R (in dbSNP:rs3813832)"
FT /id="VAR_053746"
FT MUTAGEN 361
FT /note="K->L: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 362
FT /note="S->A: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 367
FT /note="N->D: Abolished binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT MUTAGEN 377
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs. Abolishes binding to m6A-containing mRNAs;
FT when associated with A-428."
FT /evidence="ECO:0000269|PubMed:25242552,
FT ECO:0000269|PubMed:26876937"
FT MUTAGEN 377
FT /note="W->D: Abolishes RNA-binding and ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 380
FT /note="L->T: Reduced binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT MUTAGEN 387
FT /note="L->E: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 399
FT /note="L->E: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 401
FT /note="F->D: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 402
FT /note="S->A: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 409
FT /note="F->D: Abolishes RNA-binding and ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 411
FT /note="G->I: Abolishes RNA-binding and ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 428
FT /note="W->A: Abolishes binding to N6-methyladenosine (m6A)-
FT containing RNAs. Abolishes binding to m6A-containing mRNAs;
FT when associated with A-377."
FT /evidence="ECO:0000269|PubMed:25242552,
FT ECO:0000269|PubMed:26876937"
FT MUTAGEN 428
FT /note="W->D: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 438
FT /note="M->A: Reduced binding to N6-methyladenosine (m6A)-
FT containing RNAs."
FT /evidence="ECO:0000269|PubMed:26318451"
FT MUTAGEN 447
FT /note="W->D: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 466
FT /note="N->D: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 475
FT /note="R->A: Reduced binding affinity for N6-
FT methyladenosine (m6A)-containing RNAs by 100-fold."
FT /evidence="ECO:0000269|PubMed:25242552"
FT MUTAGEN 475
FT /note="R->D: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT MUTAGEN 475
FT /note="R->F: Reduced binding affinity for N6-
FT methyladenosine (m6A)-containing RNAs by 9-fold."
FT /evidence="ECO:0000269|PubMed:25242552"
FT MUTAGEN 476
FT /note="D->K: Does not affect ability to influence
FT alternative splice site selection."
FT /evidence="ECO:0000269|PubMed:20167602"
FT CONFLICT 619
FT /note="H -> Q (in Ref. 1; BAB71181)"
FT /evidence="ECO:0000305"
FT HELIX 346..352
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:6T02"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:6YNP"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:7PJ7"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 442..449
FT /evidence="ECO:0007829|PDB:6T02"
FT HELIX 455..458
FT /evidence="ECO:0007829|PDB:6T02"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2YUD"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:6RT5"
FT HELIX 482..491
FT /evidence="ECO:0007829|PDB:6T02"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:2YUD"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:6T02"
SQ SEQUENCE 727 AA; 84700 MW; 536032FD44582EAF CRC64;
MAADSREEKD GELNVLDDIL TEVPEQDDEL YNPESEQDKN EKKGSKRKSD RMESTDTKRQ
KPSVHSRQLV SKPLSSSVSN NKRIVSTKGK SATEYKNEEY QRSERNKRLD ADRKIRLSSS
ASREPYKNQP EKTCVRKRDP ERRAKSPTPD GSERIGLEVD RRASRSSQSS KEEVNSEEYG
SDHETGSSGS SDEQGNNTEN EEEGVEEDVE EDEEVEEDAE EDEEVDEDGE EEEEEEEEEE
EEEEEEEEEY EQDERDQKEE GNDYDTRSEA SDSGSESVSF TDGSVRSGSG TDGSDEKKKE
RKRARGISPI VFDRSGSSAS ESYAGSEKKH EKLSSSVRAV RKDQTSKLKY VLQDARFFLI
KSNNHENVSL AKAKGVWSTL PVNEKKLNLA FRSARSVILI FSVRESGKFQ GFARLSSESH
HGGSPIHWVL PAGMSAKMLG GVFKIDWICR RELPFTKSAH LTNPWNEHKP VKIGRDGQEI
ELECGTQLCL LFPPDESIDL YQVIHKMRHK RRMHSQPRSR GRPSRREPVR DVGRRRPEDY
DIHNSRKKPR IDYPPEFHQR PGYLKDPRYQ EVDRRFSGVR RDVFLNGSYN DYVREFHNMG
PPPPWQGMPP YPGMEQPPHH PYYQHHAPPP QAHPPYSGHH PVPHEARYRD KRVHDYDMRV
DDFLRRTQAV VSGRRSRPRE RDRERERDRP RDNRRDRERD RGRDRERERE RLCDRDRDRG
ERGRYRR
