YTHD2_MOUSE
ID YTHD2_MOUSE Reviewed; 579 AA.
AC Q91YT7; Q3TWU3; Q8BM70; Q8K325;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=YTH domain-containing family protein 2 {ECO:0000305};
GN Name=Ythdf2 {ECO:0000303|PubMed:28867294, ECO:0000312|MGI:MGI:2444233};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=28867294; DOI=10.1016/j.molcel.2017.08.003;
RA Ivanova I., Much C., Di Giacomo M., Azzi C., Morgan M., Moreira P.N.,
RA Monahan J., Carrieri C., Enright A.J., O'Carroll D.;
RT "The RNA m(6)A reader YTHDF2 is essential for the post-transcriptional
RT regulation of the maternal transcriptome and oocyte competence.";
RL Mol. Cell 0:0-0(2017).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30065315; DOI=10.1038/s41422-018-0072-0;
RA Li Z., Qian P., Shao W., Shi H., He X.C., Gogol M., Yu Z., Wang Y., Qi M.,
RA Zhu Y., Perry J.M., Zhang K., Tao F., Zhou K., Hu D., Han Y., Zhao C.,
RA Alexander R., Xu H., Chen S., Peak A., Hall K., Peterson M., Perera A.,
RA Haug J.S., Parmely T., Li H., Shen B., Zeitlinger J., He C., Li L.;
RT "Suppression of m6A reader Ythdf2 promotes hematopoietic stem cell
RT expansion.";
RL Cell Res. 28:904-917(2018).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30150673; DOI=10.1038/s41422-018-0082-y;
RA Wang H., Zuo H., Liu J., Wen F., Gao Y., Zhu X., Liu B., Xiao F., Wang W.,
RA Huang G., Shen B., Ju Z.;
RT "Loss of YTHDF2-mediated m6A-dependent mRNA clearance facilitates
RT hematopoietic stem cell regeneration.";
RL Cell Res. 28:1035-1038(2018).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29855337; DOI=10.1186/s13059-018-1436-y;
RA Li M., Zhao X., Wang W., Shi H., Pan Q., Lu Z., Perez S.P., Suganthan R.,
RA He C., Bjoeraas M., Klungland A.;
RT "Ythdf2-mediated m6A mRNA clearance modulates neural development in mice.";
RL Genome Biol. 19:RESEARCH69.1-RESEARCH69.16(2018).
RN [10]
RP FUNCTION.
RX PubMed=30559377; DOI=10.1038/s41590-018-0275-z;
RA Winkler R., Gillis E., Lasman L., Safra M., Geula S., Soyris C.,
RA Nachshon A., Tai-Schmiedel J., Friedman N., Le-Trilling V.T.K.,
RA Trilling M., Mandelboim M., Hanna J.H., Schwartz S., Stern-Ginossar N.;
RT "m6A modification controls the innate immune response to infection by
RT targeting type I interferons.";
RL Nat. Immunol. 20:173-182(2019).
RN [11]
RP FUNCTION, AND INTERACTION WITH CNOT1.
RX PubMed=32905781; DOI=10.1016/j.celrep.2020.108120;
RA Liu J., Gao M., Xu S., Chen Y., Wu K., Liu H., Wang J., Yang X., Wang J.,
RA Liu W., Bao X., Chen J.;
RT "YTHDF2/3 are required for somatic reprogramming through different RNA
RT deadenylation pathways.";
RL Cell Rep. 32:108120-108120(2020).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31959747; DOI=10.1038/s41419-020-2235-4;
RA Huang T., Liu Z., Zheng Y., Feng T., Gao Q., Zeng W.;
RT "YTHDF2 promotes spermagonial adhesion through modulating MMPs decay via
RT m6A/mRNA pathway.";
RL Cell Death Dis. 11:37-37(2020).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32943573; DOI=10.1101/gad.340695.120;
RA Lasman L., Krupalnik V., Viukov S., Mor N., Aguilera-Castrejon A.,
RA Schneir D., Bayerl J., Mizrahi O., Peles S., Tawil S., Sathe S.,
RA Nachshon A., Shani T., Zerbib M., Kilimnik I., Aigner S., Shankar A.,
RA Mueller J.R., Schwartz S., Stern-Ginossar N., Yeo G.W., Geula S.,
RA Novershtern N., Hanna J.H.;
RT "Context-dependent functional compensation between Ythdf m6A reader
RT proteins.";
RL Genes Dev. 34:1373-1391(2020).
CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC containing RNAs, and regulates their stability (PubMed:28867294,
CC PubMed:29855337, PubMed:32943573). M6A is a modification present at
CC internal sites of mRNAs and some non-coding RNAs and plays a role in
CC mRNA stability and processing (PubMed:28867294, PubMed:29855337,
CC PubMed:32943573). Acts as a regulator of mRNA stability by promoting
CC degradation of m6A-containing mRNAs via interaction with the CCR4-NOT
CC and ribonuclease P/MRP complexes, depending on the context
CC (PubMed:29855337, PubMed:30065315, PubMed:32943573, PubMed:32905781).
CC The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing
CC mRNAs targets and act redundantly to mediate mRNA degradation and
CC cellular differentiation (PubMed:32943573). M6A-containing mRNAs
CC containing a binding site for RIDA/HRSP12 (5'-GGUUC-3') are
CC preferentially degraded by endoribonucleolytic cleavage: cooperative
CC binding of RIDA/HRSP12 and YTHDF2 to transcripts leads to recruitment
CC of the ribonuclease P/MRP complex (By similarity). Other m6A-containing
CC mRNAs undergo deadenylation via direct interaction between YTHDF2 and
CC CNOT1, leading to recruitment of the CCR4-NOT and subsequent
CC deadenylation of m6A-containing mRNAs (PubMed:32905781). Required
CC maternally to regulate oocyte maturation: probably acts by binding to
CC m6A-containing mRNAs, thereby regulating maternal transcript dosage
CC during oocyte maturation, which is essential for the competence of
CC oocytes to sustain early zygotic development (PubMed:28867294). Also
CC required during spermatogenesis: regulates spermagonial adhesion by
CC promoting degradation of m6A-containing transcripts coding for matrix
CC metallopeptidases (PubMed:31959747). Also involved in hematopoietic
CC stem cells specification by binding to m6A-containing mRNAs, leading to
CC promote their degradation (PubMed:30065315, PubMed:30150673). Also acts
CC as a regulator of neural development by promoting m6A-dependent
CC degradation of neural development-related mRNA targets
CC (PubMed:29855337). Inhibits neural specification of induced pluripotent
CC stem cells by binding to methylated neural-specific mRNAs and promoting
CC their degradation, thereby restraining neural differentiation (By
CC similarity). Regulates circadian regulation of hepatic lipid
CC metabolism: acts by promoting m6A-dependent degradation of PPARA
CC transcripts (By similarity). Regulates the innate immune response to
CC infection by inhibiting the type I interferon response: acts by binding
CC to m6A-containing IFNB transcripts and promoting their degradation
CC (PubMed:30559377). May also act as a promoter of cap-independent mRNA
CC translation following heat shock stress: upon stress, relocalizes to
CC the nucleus and specifically binds mRNAs with some m6A methylation mark
CC at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby
CC promoting cap-independent mRNA translation (By similarity). Regulates
CC mitotic entry by promoting the phase-specific m6A-dependent degradation
CC of WEE1 transcripts (By similarity). Promotes formation of phase-
CC separated membraneless compartments, such as P-bodies or stress
CC granules, by undergoing liquid-liquid phase separation upon binding to
CC mRNAs containing multiple m6A-modified residues: polymethylated mRNAs
CC act as a multivalent scaffold for the binding of YTHDF proteins,
CC juxtaposing their disordered regions and thereby leading to phase
CC separation (By similarity). The resulting mRNA-YTHDF complexes then
CC partition into different endogenous phase-separated membraneless
CC compartments, such as P-bodies, stress granules or neuronal RNA
CC granules (By similarity). May also recognize and bind RNAs modified by
CC C5-methylcytosine (m5C) and act as a regulator of rRNA processing (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y5A9,
CC ECO:0000269|PubMed:28867294, ECO:0000269|PubMed:29855337,
CC ECO:0000269|PubMed:30065315, ECO:0000269|PubMed:30150673,
CC ECO:0000269|PubMed:30559377, ECO:0000269|PubMed:31959747,
CC ECO:0000269|PubMed:32905781, ECO:0000269|PubMed:32943573}.
CC -!- SUBUNIT: Interacts with CNOT1; interaction is direct and promotes
CC recruitment of the CCR4-NOT complex (PubMed:32905781). Interacts with
CC YTHDF3 (By similarity). Interacts with RIDA/HRSP12; interaction leads
CC to recruitment of the ribonuclease P/MRP complex (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5A9, ECO:0000269|PubMed:32905781}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:28867294,
CC ECO:0000305|PubMed:32943573}. Cytoplasm, P-body
CC {ECO:0000250|UniProtKB:Q9Y5A9}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9Y5A9}. Nucleus {ECO:0000269|PubMed:32943573}.
CC Note=Localizes to the cytosol and relocates to the nucleus following
CC heat shock stress. Can partition into different structures: into P-
CC bodies in unstressed cells, and into stress granules during stress.
CC {ECO:0000250|UniProtKB:Q9Y5A9}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC testis. {ECO:0000269|PubMed:28867294}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the germline during gametogenesis:
CC expressed at all stages of spermatogenesis, with elevated expression
CC observed in pachytene spermatocytes (PubMed:28867294). During
CC oogenesis, expressed at all stages of folliculogenesis: expressed both
CC in the oocyte and in somatic granulosa cells (PubMed:28867294). Also
CC expressed during oocyte maturation, with abundant expression in
CC germinal vesicle as well as in meiosis II oocytes (PubMed:28867294).
CC {ECO:0000269|PubMed:28867294}.
CC -!- DOMAIN: The disordered regions have the ability to interact with each
CC other and to 'phase separate' into liquid droplets within the cytosol
CC following binding to mRNAs containing multiple m6A-modified residues.
CC This leads to the partition of m6A-containing mRNAs into membraneless
CC compartments, where mRNAs may be stored, degraded or used to transport
CC mRNAs to dendritic arbors in neurons. {ECO:0000250|UniProtKB:Q9Y5A9}.
CC -!- PTM: Ubiquitinated by the SCF(SKP2) complex, leading to its
CC degradation. {ECO:0000250|UniProtKB:Q9Y5A9}.
CC -!- DISRUPTION PHENOTYPE: Female are infertile despite successful ovulation
CC (PubMed:28867294, PubMed:32943573). Corpora lutea is present in
CC ovaries, indicating that ovulation has occurred (PubMed:28867294).
CC Defects during oocyte maturation are probably caused by the
CC deregulation of some transcripts, leading to an arrest prior to or at
CC the two-cell stage, with various cytokinesis defects observed in the
CC two-cell embryos (PubMed:28867294). Males are hypofertile because of
CC mild degenerative changes in the seminiferous tubules, including large
CC scattered vacuoles in Sertoli cells and severe loss of sperm in the
CC cauda epididymis (PubMed:32943573). Conditional deletion in embryos
CC leads to lethality at late embryonic developmental stages, caused by
CC defects in neural development (PubMed:29855337). Conditional deletion
CC in spermatogonia leads to impaired spermatogonial proliferation caused
CC by decreased cell spread (PubMed:31959747). The proliferation and
CC differentiation capabilities of neural stem/progenitor cell (NSPC)
CC decrease significantly in conditional deletion mutant embryos
CC (PubMed:29855337). Conditional deletion in hematopoietic stem cells
CC promotes hematopoietic stem cell expansion (PubMed:30065315,
CC PubMed:30150673). Mice lacking Ythdf1, Ythdf2 and Ythdf3 display early
CC embryonic lethality and show defects in embryonic stem cell
CC differentiation (PubMed:32943573). {ECO:0000269|PubMed:28867294,
CC ECO:0000269|PubMed:29855337, ECO:0000269|PubMed:30065315,
CC ECO:0000269|PubMed:30150673, ECO:0000269|PubMed:31959747,
CC ECO:0000269|PubMed:32943573}.
CC -!- SIMILARITY: Belongs to the YTHDF family. YTHDF2 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Previous studies suggested the 3 different paralogs (YTHDF1,
CC YTHDF2 and YTHDF3) have unique functions with limited redundancy (By
CC similarity). However, later studies showed that YTHDF1, YTHDF2 and
CC YTHDF3 paralogs have redundant functions to a profound extent and
CC directly promote degradation of m6A-containing mRNAs (PubMed:32943573).
CC {ECO:0000250|UniProtKB:Q9Y5A9, ECO:0000269|PubMed:32943573}.
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DR EMBL; AK031616; BAC27480.1; -; mRNA.
DR EMBL; AK034655; BAC28785.1; -; mRNA.
DR EMBL; AK083882; BAC39048.1; -; mRNA.
DR EMBL; AK150350; BAE29487.1; -; mRNA.
DR EMBL; AK150669; BAE29751.1; -; mRNA.
DR EMBL; AK151392; BAE30361.1; -; mRNA.
DR EMBL; AK151862; BAE30751.1; -; mRNA.
DR EMBL; AK159548; BAE35173.1; -; mRNA.
DR EMBL; BX537301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30120.1; -; Genomic_DNA.
DR EMBL; BC014797; AAH14797.1; -; mRNA.
DR EMBL; BC028994; AAH28994.1; -; mRNA.
DR CCDS; CCDS18719.1; -.
DR RefSeq; NP_663368.3; NM_145393.4.
DR AlphaFoldDB; Q91YT7; -.
DR SMR; Q91YT7; -.
DR BioGRID; 229450; 11.
DR IntAct; Q91YT7; 2.
DR STRING; 10090.ENSMUSP00000120414; -.
DR iPTMnet; Q91YT7; -.
DR PhosphoSitePlus; Q91YT7; -.
DR EPD; Q91YT7; -.
DR jPOST; Q91YT7; -.
DR MaxQB; Q91YT7; -.
DR PaxDb; Q91YT7; -.
DR PeptideAtlas; Q91YT7; -.
DR PRIDE; Q91YT7; -.
DR ProteomicsDB; 298484; -.
DR Antibodypedia; 30989; 141 antibodies from 28 providers.
DR DNASU; 213541; -.
DR Ensembl; ENSMUST00000152796; ENSMUSP00000120414; ENSMUSG00000040025.
DR GeneID; 213541; -.
DR KEGG; mmu:213541; -.
DR UCSC; uc008vas.2; mouse.
DR CTD; 51441; -.
DR MGI; MGI:2444233; Ythdf2.
DR VEuPathDB; HostDB:ENSMUSG00000040025; -.
DR eggNOG; KOG1901; Eukaryota.
DR GeneTree; ENSGT00940000156761; -.
DR HOGENOM; CLU_022715_0_0_1; -.
DR InParanoid; Q91YT7; -.
DR OMA; RTNGFGD; -.
DR OrthoDB; 1523251at2759; -.
DR PhylomeDB; Q91YT7; -.
DR TreeFam; TF323736; -.
DR BioGRID-ORCS; 213541; 16 hits in 70 CRISPR screens.
DR ChiTaRS; Ythdf2; mouse.
DR PRO; PR:Q91YT7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91YT7; protein.
DR Bgee; ENSMUSG00000040025; Expressed in maxillary prominence and 252 other tissues.
DR ExpressionAtlas; Q91YT7; baseline and differential.
DR Genevisible; Q91YT7; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0098508; P:endothelial to hematopoietic transition; ISS:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; IMP:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:0070925; P:organelle assembly; ISS:UniProtKB.
DR GO; GO:1903679; P:positive regulation of cap-independent translational initiation; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IMP:UniProtKB.
DR GO; GO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:2000232; P:regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0007284; P:spermatogonial cell division; IMP:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 1.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Differentiation;
KW Immunity; Innate immunity; Mitosis; Nucleus; Oogenesis; Phosphoprotein;
KW Reference proteome; RNA-binding; Spermatogenesis; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT CHAIN 2..579
FT /note="YTH domain-containing family protein 2"
FT /id="PRO_0000425544"
FT DOMAIN 410..544
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..384
FT /note="Localization to mRNA processing bodies (P-bodies)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT REGION 247..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..579
FT /note="Interaction with m6A-containing mRNAs"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..418
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 422
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 432..433
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 462
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 486
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 491
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z739"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT CONFLICT 82
FT /note="A -> P (in Ref. 4; AAH28994)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> V (in Ref. 1; BAE35173)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="A -> V (in Ref. 1; BAE35173)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="Q -> R (in Ref. 1; BAC28785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 62280 MW; 9D79DF630593C7AB CRC64;
MSASSLLEQR PKGQGNKVQN GSVHQKDGLN DDDFEPYLSP QARPNNAYTA MSDSYLPSYY
SPSIGFSYSL GEAAWSTGGD TAMPYLTSYG QLSNGEPHFL PDAMFGQPGA LGSTPFLGQH
GFNFFPSGID FSAWGNNSSQ GQSTQSSGYS SNYAYAPSSL GGAMIDGQSA FANETLNKAP
GMNTIDQGMA ALKLGSTEVA SSVPKVVGSA VGSGSITSNI VASSSLPPAT IAPPKPASWA
DIASKPAKQQ PKLKTKNGIA GSSLPPPPIK HNMDIGTWDN KGPVAKAPSQ ALVQNIGQPT
QGSPQPVGQQ ANNSPPVAQA SVGQQTQPLP PPPPQPAQLS VQQQAAQPTR WVAPRNRGSG
FGHNGVDGNG VGQSQAGSGS TPSEPHPVLE KLRSINNYNP KDFDWNLKHG RVFIIKSYSE
DDIHRSIKYN IWCSTEHGNK RLDAAYRSMN GKGPVYLLFS VNGSGHFCGV AEMKSAVDYN
TCAGVWSQDK WKGRFDVRWI FVKDVPNSQL RHIRLENNEN KPVTNSRDTQ EVPLEKAKQV
LKIIASYKHT TSIFDDFSHY EKRQEEEESV KKERQGRGK
