YTDC2_HUMAN
ID YTDC2_HUMAN Reviewed; 1430 AA.
AC Q9H6S0; B2RP66;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=3'-5' RNA helicase YTHDC2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:29033321};
DE AltName: Full=YTH domain-containing protein 2 {ECO:0000303|PubMed:29033321};
DE Short=hYTHDC2 {ECO:0000303|PubMed:29033321};
GN Name=YTHDC2 {ECO:0000303|PubMed:29033321, ECO:0000312|HGNC:HGNC:24721};
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 GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 730-1430, AND VARIANT GLN-1409.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1089, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1202, AND IDENTIFICATION BY
RP 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 [10]
RP FUNCTION, AND RNA-BINDING.
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, RNA-BINDING, INTERACTION WITH XRN1,
RP AND MUTAGENESIS OF GLU-317 AND TRP-1360.
RX PubMed=29033321; DOI=10.1016/j.molcel.2017.09.021;
RA Wojtas M.N., Pandey R.R., Mendel M., Homolka D., Sachidanandam R.,
RA Pillai R.S.;
RT "Regulation of m6A transcripts by the 3'-5' RNA helicase YTHDC2 is
RT essential for a successful meiotic program in the mammalian germline.";
RL Mol. Cell 68:374-387(2017).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=29087293; DOI=10.7554/elife.26116;
RA Bailey A.S., Batista P.J., Gold R.S., Chen Y.G., de Rooij D.G., Chang H.Y.,
RA Fuller M.T.;
RT "The conserved RNA helicase YTHDC2 regulates the transition from
RT proliferation to differentiation in the germline.";
RL Elife 6:0-0(2017).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH XRN1.
RX PubMed=29970596; DOI=10.1261/rna.064238.117;
RA Kretschmer J., Rao H., Hackert P., Sloan K.E., Hoebartner C.,
RA Bohnsack M.T.;
RT "The m6A reader protein YTHDC2 interacts with the small ribosomal subunit
RT and the 5'-3' exoribonuclease XRN1.";
RL RNA 24:1339-1350(2018).
RN [14]
RP INTERACTION WITH ZCCHC4.
RX PubMed=31799605; DOI=10.1093/nar/gkz1147;
RA Pinto R., Vaagboe C.B., Jakobsson M.E., Kim Y., Baltissen M.P.,
RA O'Donohue M.F., Guzman U.H., Malecki J.M., Wu J., Kirpekar F., Olsen J.V.,
RA Gleizes P.E., Vermeulen M., Leidel S.A., Slupphaug G., Falnes P.O.;
RT "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine
RT modification of 28S ribosomal RNA.";
RL Nucleic Acids Res. 48:830-846(2020).
RN [15]
RP STRUCTURE BY NMR OF 1288-1421.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the YTH domain in YTH domain-containing protein 2.";
RL Submitted (OCT-2007) to the PDB data bank.
RN [16] {ECO:0007744|PDB:6K6U}
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1286-1426.
RX PubMed=31472957; DOI=10.1016/j.bbrc.2019.08.107;
RA Ma C., Liao S., Zhu Z.;
RT "Crystal structure of human YTHDC2 YTH domain.";
RL Biochem. Biophys. Res. Commun. 518:678-684(2019).
CC -!- FUNCTION: 3'-5' RNA helicase that plays a key role in the male and
CC female germline by promoting transition from mitotic to meiotic
CC divisions in stem cells (PubMed:26318451, PubMed:29033321,
CC PubMed:29970596). Specifically recognizes and binds N6-methyladenosine
CC (m6A)-containing RNAs, a modification present at internal sites of
CC mRNAs and some non-coding RNAs that plays a role in the efficiency of
CC RNA processing and stability (PubMed:26318451, PubMed:29033321).
CC Essential for ensuring a successful progression of the meiotic program
CC in the germline by regulating the level of m6A-containing RNAs (By
CC similarity). Acts by binding and promoting degradation of m6A-
CC containing mRNAs: the 3'-5' RNA helicase activity is required for this
CC process and RNA degradation may be mediated by XRN1 exoribonuclease
CC (PubMed:29033321). Required for both spermatogenesis and oogenesis (By
CC similarity). {ECO:0000250|UniProtKB:B2RR83,
CC ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:29033321,
CC ECO:0000269|PubMed:29970596}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:29033321};
CC -!- SUBUNIT: Interacts with MEIOC; binds transcripts that regulate the
CC mitotic cell cycle inhibiting progression into metaphase, thereby
CC allowing meiotic prophase to proceed normally (By similarity).
CC Interacts (via ANK repeats) with XRN1 (PubMed:29033321,
CC PubMed:29970596). Interacts with ZCCHC4 (PubMed:31799605). Associates
CC with the small ribosomal subunit (PubMed:29970596).
CC {ECO:0000250|UniProtKB:B2RR83, ECO:0000269|PubMed:29033321,
CC ECO:0000269|PubMed:29970596, ECO:0000269|PubMed:31799605}.
CC -!- INTERACTION:
CC Q9H6S0; Q15306: IRF4; NbExp=2; IntAct=EBI-1057466, EBI-751345;
CC Q9H6S0; Q99J34: Irak1; Xeno; NbExp=2; IntAct=EBI-1057466, EBI-6117042;
CC Q9H6S0; A2AG06: Meioc; Xeno; NbExp=2; IntAct=EBI-1057466, EBI-11664020;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2RR83}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:29970596}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (PubMed:29087293). Not detected
CC in spermatogonia next to the tubule wall but is strongly expressed in
CC spermatocytes, suggesting that it is up-regulated in germ cells upon
CC entry into meiosis (PubMed:29087293). {ECO:0000269|PubMed:29087293}.
CC -!- DOMAIN: The YTH domain mediates RNA-binding. It recognizes and binds
CC N6-methyladenosine (m6A)-containing RNAs.
CC {ECO:0000269|PubMed:29033321}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC093208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137285; AAI37286.1; -; mRNA.
DR EMBL; AK025593; BAB15183.1; ALT_INIT; mRNA.
DR CCDS; CCDS4113.1; -.
DR RefSeq; NP_073739.3; NM_022828.4.
DR RefSeq; XP_016865219.1; XM_017009730.1.
DR PDB; 2YU6; NMR; -; A=1288-1421.
DR PDB; 6K6U; X-ray; 2.27 A; A/B=1286-1426.
DR PDB; 6LR2; NMR; -; A=1288-1421.
DR PDBsum; 2YU6; -.
DR PDBsum; 6K6U; -.
DR PDBsum; 6LR2; -.
DR AlphaFoldDB; Q9H6S0; -.
DR SMR; Q9H6S0; -.
DR BioGRID; 122321; 188.
DR IntAct; Q9H6S0; 58.
DR MINT; Q9H6S0; -.
DR STRING; 9606.ENSP00000161863; -.
DR GlyGen; Q9H6S0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H6S0; -.
DR PhosphoSitePlus; Q9H6S0; -.
DR BioMuta; YTHDC2; -.
DR DMDM; 239938805; -.
DR EPD; Q9H6S0; -.
DR jPOST; Q9H6S0; -.
DR MassIVE; Q9H6S0; -.
DR MaxQB; Q9H6S0; -.
DR PaxDb; Q9H6S0; -.
DR PeptideAtlas; Q9H6S0; -.
DR PRIDE; Q9H6S0; -.
DR ProteomicsDB; 81025; -.
DR Antibodypedia; 48855; 39 antibodies from 16 providers.
DR DNASU; 64848; -.
DR Ensembl; ENST00000161863.9; ENSP00000161863.4; ENSG00000047188.16.
DR GeneID; 64848; -.
DR KEGG; hsa:64848; -.
DR MANE-Select; ENST00000161863.9; ENSP00000161863.4; NM_022828.5; NP_073739.3.
DR UCSC; uc003kqn.4; human.
DR CTD; 64848; -.
DR DisGeNET; 64848; -.
DR GeneCards; YTHDC2; -.
DR HGNC; HGNC:24721; YTHDC2.
DR HPA; ENSG00000047188; Low tissue specificity.
DR MIM; 616530; gene.
DR neXtProt; NX_Q9H6S0; -.
DR OpenTargets; ENSG00000047188; -.
DR PharmGKB; PA134912676; -.
DR VEuPathDB; HostDB:ENSG00000047188; -.
DR eggNOG; KOG0920; Eukaryota.
DR eggNOG; KOG0922; Eukaryota.
DR eggNOG; KOG1902; Eukaryota.
DR GeneTree; ENSGT00940000155826; -.
DR HOGENOM; CLU_001832_1_6_1; -.
DR InParanoid; Q9H6S0; -.
DR OMA; WQNLFIK; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q9H6S0; -.
DR TreeFam; TF318311; -.
DR PathwayCommons; Q9H6S0; -.
DR SignaLink; Q9H6S0; -.
DR BioGRID-ORCS; 64848; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; YTHDC2; human.
DR EvolutionaryTrace; Q9H6S0; -.
DR GenomeRNAi; 64848; -.
DR Pharos; Q9H6S0; Tbio.
DR PRO; PR:Q9H6S0; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H6S0; protein.
DR Bgee; ENSG00000047188; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q9H6S0; baseline and differential.
DR Genevisible; Q9H6S0; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR GO; GO:0034458; F:3'-5' RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:AgBase.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070063; F:RNA polymerase binding; IPI:AgBase.
DR GO; GO:0051729; P:germline cell cycle switching, mitotic to meiotic cell cycle; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048599; P:oocyte development; ISS:UniProtKB.
DR GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase.
DR GO; GO:0070555; P:response to interleukin-1; IDA:AgBase.
DR GO; GO:0034612; P:response to tumor necrosis factor; IDA:AgBase.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR CDD; cd06007; R3H_DEXH_helicase; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034083; R3H_DEXH_helicase.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR031083; YTHDC2-like.
DR PANTHER; PTHR18934:SF100; PTHR18934:SF100; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF04146; YTH; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; ATP-binding; Cytoplasm; Differentiation;
KW Helicase; Hydrolase; Meiosis; Nucleotide-binding; Oogenesis;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Spermatogenesis.
FT CHAIN 1..1430
FT /note="3'-5' RNA helicase YTHDC2"
FT /id="PRO_0000249340"
FT DOMAIN 38..106
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 203..369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REPEAT 506..538
FT /note="ANK 1"
FT REPEAT 539..571
FT /note="ANK 2"
FT DOMAIN 612..784
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1288..1418
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1164..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 316..319
FT /note="DEAH box"
FT COMPBIAS 1164..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1294..1296
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:0000250|UniProtKB:Q9Y5A9"
FT BINDING 1310
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:0000250|UniProtKB:Q96MU7"
FT BINDING 1360
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:0000250|UniProtKB:Q96MU7"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RR83"
FT MOD_RES 1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RR83"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2RR83"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 652
FT /note="S -> N (in dbSNP:rs10071816)"
FT /id="VAR_058002"
FT VARIANT 1409
FT /note="L -> Q (in dbSNP:rs1132528)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_058003"
FT MUTAGEN 317
FT /note="E->A: Abolished 3'-5' RNA helicase activity."
FT /evidence="ECO:0000269|PubMed:29033321"
FT MUTAGEN 1360
FT /note="W->A: Abolished ability to bind N6-methyladenosine
FT (m6A)-containing RNAs."
FT /evidence="ECO:0000269|PubMed:29033321"
FT CONFLICT 860
FT /note="I -> V (in Ref. 3; BAB15183)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="L -> S (in Ref. 3; BAB15183)"
FT /evidence="ECO:0000305"
FT CONFLICT 1230
FT /note="Q -> R (in Ref. 3; BAB15183)"
FT /evidence="ECO:0000305"
FT STRAND 1287..1296
FT /evidence="ECO:0007829|PDB:6K6U"
FT HELIX 1298..1307
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1309..1311
FT /evidence="ECO:0007829|PDB:2YU6"
FT HELIX 1314..1326
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1327..1336
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1339..1342
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1345..1348
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1352..1354
FT /evidence="ECO:0007829|PDB:2YU6"
FT STRAND 1369..1375
FT /evidence="ECO:0007829|PDB:6K6U"
FT HELIX 1381..1384
FT /evidence="ECO:0007829|PDB:6K6U"
FT HELIX 1390..1392
FT /evidence="ECO:0007829|PDB:6K6U"
FT STRAND 1404..1406
FT /evidence="ECO:0007829|PDB:2YU6"
FT HELIX 1408..1416
FT /evidence="ECO:0007829|PDB:6K6U"
FT HELIX 1417..1420
FT /evidence="ECO:0007829|PDB:6K6U"
SQ SEQUENCE 1430 AA; 160248 MW; A0C3B45771A3DE16 CRC64;
MSRPSSVSPR QPAPGGGGGG GPSPCGPGGG GRAKGLKDIR IDEEVKIAVN IALERFRYGD
QREMEFPSSL TSTERAFIHR LSQSLGLVSK SKGKGANRYL TVKKKDGSET AHAMMTCNLT
HNTKHAVRSL IQRFPVTNKE RTELLPKTER GNVFAVEAEN REMSKTSGRL NNGIPQIPVK
RGESEFDSFR QSLPVFEKQE EIVKIIKENK VVLIVGETGS GKTTQIPQFL LDDCFKNGIP
CRIFCTQPRR LAAIAVAERV AAERRERIGQ TIGYQIRLES RVSPKTLLTF CTNGVLLRTL
MAGDSTLSTV THVIVDEVHE RDRFSDFLLT KLRDLLQKHP TLKLILSSAA LDVNLFIRYF
GSCPVIYIQG RPFEVKEMFL EDILRTTGYT NKEMLKYKKE KQQEEKQQTT LTEWYSAQEN
SFKPESQRQR TVLNVTDEYD LLDDGGDAVF SQLTEKDVNC LEPWLIKEMD ACLSDIWLHK
DIDAFAQVFH LILTENVSVD YRHSETSATA LMVAAGRGFA SQVEQLISMG ANVHSKASNG
WMALDWAKHF GQTEIVDLLE SYSATLEFGN LDESSLVQTN GSDLSAEDRE LLKAYHHSFD
DEKVDLDLIM HLLYNICHSC DAGAVLIFLP GYDEIVGLRD RILFDDKRFA DSTHRYQVFM
LHSNMQTSDQ KKVLKNPPAG VRKIILSTNI AETSITVNDV VFVIDSGKVK EKSFDALNFV
TMLKMVWISK ASAIQRKGRA GRCRPGICFR LFSRLRFQNM LEFQTPELLR MPLQELCLHT
KLLAPVNCPI ADFLMKAPEP PPALIVRNAV QMLKTIDAMD TWEDLTELGY HLADLPVEPH
LGKMVLCAVV LKCLDPILTI ACTLAYRDPF VLPTQASQKR AAMLCRKRFT AGAFSDHMAL
LRAFQAWQKA RSDGWERAFC EKNFLSQATM EIIIGMRTQL LGQLRASGFV RARGGGDIRD
VNTNSENWAV VKAALVAGMY PNLVHVDREN LVLTGPKEKK VRFHPASVLS QPQYKKIPPA
NGQAAAIKAL PTDWLIYDEM TRAHRIANIR CCSAVTPVTI LVFCGPARLA SNALQEPSSF
RVDGIPNDSS DSEMEDKTTA NLAALKLDEW LHFTLEPEAA SLLLQLRQKW HSLFLRRMRA
PSKPWSQVDE ATIRAIIAVL STEEQSAGLQ QPSGIGQRPR PMSSEELPLA SSWRSNNSRK
SSADTEFSDE CTTAERVLMK SPSPALHPPQ KYKDRGILHP KRGTEDRSDQ SSLKSTDSSS
YPSPCASPSP PSSGKGSKSP SPRPNMPVRY FIMKSSNLRN LEISQQKGIW STTPSNERKL
NRAFWESSIV YLVFSVQGSG HFQGFSRMSS EIGREKSQDW GSAGLGGVFK VEWIRKESLP
FQFAHHLLNP WNDNKKVQIS RDGQELEPLV GEQLLQLWER LPLGEKNTTD
