ID   YTHD3_HUMAN             Reviewed;         585 AA.
AC   Q7Z739; B3KXL4; Q63Z37; Q659A3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=YTH domain-containing family protein 3 {ECO:0000305};
DE            Short=DF3 {ECO:0000303|PubMed:31292544, ECO:0000303|PubMed:32492408};
GN   Name=YTHDF3 {ECO:0000303|PubMed:28106072,
GN   ECO:0000312|HGNC:HGNC:26465};
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].
RC   TISSUE=Tongue;
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 MRNA].
RC   TISSUE=Skeletal muscle, and Spinal cord;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 256-271; 408-414 AND 534-542, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RA   Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [6]
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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP   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   [9]
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   [10]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=22575960; DOI=10.1038/nature11112;
RA   Dominissini D., Moshitch-Moshkovitz S., Schwartz S., Salmon-Divon M.,
RA   Ungar L., Osenberg S., Cesarkas K., Jacob-Hirsch J., Amariglio N.,
RA   Kupiec M., Sorek R., Rechavi G.;
RT   "Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq.";
RL   Nature 485:201-206(2012).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [13]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=24284625; DOI=10.1038/nature12730;
RA   Wang X., Lu Z., Gomez A., Hon G.C., Yue Y., Han D., Fu Y., Parisien M.,
RA   Dai Q., Jia G., Ren B., Pan T., He C.;
RT   "N-methyladenosine-dependent regulation of messenger RNA stability.";
RL   Nature 505:117-120(2014).
RN   [14]
RP   INDUCTION.
RX   PubMed=26458103; DOI=10.1038/nature15377;
RA   Zhou J., Wan J., Gao X., Zhang X., Jaffrey S.R., Qian S.B.;
RT   "Dynamic m(6)A mRNA methylation directs translational control of heat shock
RT   response.";
RL   Nature 526:591-594(2015).
RN   [15]
RP   RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YTHDF1
RP   AND YTHDF2.
RX   PubMed=28106072; DOI=10.1038/cr.2017.15;
RA   Shi H., Wang X., Lu Z., Zhao B.S., Ma H., Hsu P.J., Liu C., He C.;
RT   "YTHDF3 facilitates translation and decay of N(6)-methyladenosine-modified
RT   RNA.";
RL   Cell Res. 27:315-328(2017).
RN   [16]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=28106076; DOI=10.1038/cr.2017.10;
RA   Li A., Chen Y.S., Ping X.L., Yang X., Xiao W., Yang Y., Sun H.Y., Zhu Q.,
RA   Baidya P., Wang X., Bhattarai D.P., Zhao Y.L., Sun B.F., Yang Y.G.;
RT   "Cytoplasmic m(6)A reader YTHDF3 promotes mRNA translation.";
RL   Cell Res. 27:444-447(2017).
RN   [17]
RP   RNA-BINDING, AND FUNCTION.
RX   PubMed=28281539; DOI=10.1038/cr.2017.31;
RA   Yang Y., Fan X., Mao M., Song X., Wu P., Zhang Y., Jin Y., Yang Y.,
RA   Chen L., Wang Y., Wong C.C., Xiao X., Wang Z.;
RT   "Extensive translation of circular RNAs driven by N(6)-methyladenosine.";
RL   Cell Res. 27:626-641(2017).
RN   [18]
RP   FUNCTION.
RX   PubMed=31388144; DOI=10.1038/s41422-019-0210-3;
RA   Gao Y., Pei G., Li D., Li R., Shao Y., Zhang Q.C., Li P.;
RT   "Multivalent m6A motifs promote phase separation of YTHDF proteins.";
RL   Cell Res. 29:767-769(2019).
RN   [19]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=31292544; DOI=10.1038/s41586-019-1374-1;
RA   Ries R.J., Zaccara S., Klein P., Olarerin-George A., Namkoong S.,
RA   Pickering B.F., Patil D.P., Kwak H., Lee J.H., Jaffrey S.R.;
RT   "m6A enhances the phase separation potential of mRNA.";
RL   Nature 571:424-428(2019).
RN   [20]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE CCR4-NOT COMPLEX.
RX   PubMed=32492408; DOI=10.1016/j.cell.2020.05.012;
RA   Zaccara S., Jaffrey S.R.;
RT   "A unified model for the function of YTHDF proteins in regulating m6A-
RT   modified mRNA.";
RL   Cell 181:1582-1595(2020).
RN   [21]
RP   FUNCTION.
RX   PubMed=32194978; DOI=10.1038/s41421-020-0144-4;
RA   Zheng Q., Gan H., Yang F., Yao Y., Hao F., Hong L., Jin L.;
RT   "Cytoplasmic m1A reader YTHDF3 inhibits trophoblast invasion by
RT   downregulation of m1A-methylated IGF1R.";
RL   Cell Discov. 6:12-12(2020).
RN   [22]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=32451507; DOI=10.1038/s41589-020-0524-y;
RA   Fu Y., Zhuang X.;
RT   "m6A-binding YTHDF proteins promote stress granule formation.";
RL   Nat. Chem. Biol. 16:955-963(2020).
RN   [23]
RP   PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX   PubMed=32053707; DOI=10.1371/journal.ppat.1008305;
RA   Jurczyszak D., Zhang W., Terry S.N., Kehrer T., Bermudez Gonzalez M.C.,
RA   McGregor E., Mulder L.C.F., Eckwahl M.J., Pan T., Simon V.;
RT   "HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral
RT   particle.";
RL   PLoS Pathog. 16:e1008305-e1008305(2020).
RN   [24] {ECO:0007744|PDB:6ZOT}
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 392-571 IN COMPLEX WITH
RP   N6-METHYLADENOSINE (M6A)-CONTAINING RNA.
RX   PubMed=33073985; DOI=10.1021/acs.jcim.0c01029;
RA   Li Y., Bedi R.K., Moroz-Omori E.V., Caflisch A.;
RT   "Structural and dynamic insights into redundant function of YTHDF
RT   proteins.";
RL   J. Chem. Inf. Model. 60:5932-5935(2020).
CC   -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC       containing RNAs, and regulates their stability (PubMed:28106072,
CC       PubMed:28106076, PubMed:28281539, PubMed:32492408). M6A is a
CC       modification present at internal sites of mRNAs and some non-coding
CC       RNAs and plays a role in mRNA stability and processing
CC       (PubMed:22575960, PubMed:24284625, PubMed:28106072, PubMed:28281539,
CC       PubMed:32492408). Acts as a regulator of mRNA stability by promoting
CC       degradation of m6A-containing mRNAs via interaction with the CCR4-NOT
CC       complex or PAN3 (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2
CC       and YTHDF3) share m6A-containing mRNAs targets and act redundantly to
CC       mediate mRNA degradation and cellular differentiation (PubMed:28106072,
CC       PubMed:28106076, PubMed:32492408). Acts as a negative regulator of type
CC       I interferon response by down-regulating interferon-stimulated genes
CC       (ISGs) expression: acts by binding to FOXO3 mRNAs (By similarity).
CC       Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification
CC       (By similarity). Can also act as a regulator of mRNA stability in
CC       cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting
CC       their degradation (PubMed:28106072). Recognizes and binds m6A-
CC       containing circular RNAs (circRNAs); circRNAs are generated through
CC       back-splicing of pre-mRNAs, a non-canonical splicing process promoted
CC       by dsRNA structures across circularizing exons (PubMed:28281539).
CC       Promotes formation of phase-separated membraneless compartments, such
CC       as P-bodies or stress granules, by undergoing liquid-liquid phase
CC       separation upon binding to mRNAs containing multiple m6A-modified
CC       residues: polymethylated mRNAs act as a multivalent scaffold for the
CC       binding of YTHDF proteins, juxtaposing their disordered regions and
CC       thereby leading to phase separation (PubMed:31388144, PubMed:31292544,
CC       PubMed:32451507). The resulting mRNA-YTHDF complexes then partition
CC       into different endogenous phase-separated membraneless compartments,
CC       such as P-bodies, stress granules or neuronal RNA granules
CC       (PubMed:31292544). May also recognize and bind N1-methyladenosine
CC       (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to
CC       m1A-methylated transcripts of IGF1R, promoting their degradation
CC       (PubMed:32194978). {ECO:0000250|UniProtKB:Q8BYK6,
CC       ECO:0000269|PubMed:22575960, ECO:0000269|PubMed:24284625,
CC       ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:28106076,
CC       ECO:0000269|PubMed:28281539, ECO:0000269|PubMed:31292544,
CC       ECO:0000269|PubMed:31388144, ECO:0000269|PubMed:32194978,
CC       ECO:0000269|PubMed:32451507, ECO:0000269|PubMed:32492408}.
CC   -!- FUNCTION: Has some antiviral activity against HIV-1 virus: incorporated
CC       into HIV-1 particles in a nucleocapsid-dependent manner and reduces
CC       viral infectivity in the next cycle of infection (PubMed:32053707). May
CC       interfere with this early step of the viral life cycle by binding to
CC       N6-methyladenosine (m6A) modified sites on the HIV-1 RNA genome
CC       (PubMed:32053707). {ECO:0000269|PubMed:32053707}.
CC   -!- SUBUNIT: Interacts with CNOT1; promoting recruitment of the CCR4-NOT
CC       complex (PubMed:32492408). Interacts with YTHDF1 (PubMed:28106072).
CC       Interacts with YTHDF2 (PubMed:28106072). Interacts with PAN3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8BYK6,
CC       ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:32492408}.
CC   -!- INTERACTION:
CC       Q7Z739; Q9UNN5: FAF1; NbExp=3; IntAct=EBI-2849837, EBI-718246;
CC       Q7Z739; PRO_0000038596 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-2849837, EBI-6179727;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:32492408,
CC       ECO:0000305|PubMed:28106072}. Cytoplasm, P-body
CC       {ECO:0000269|PubMed:32492408}. Cytoplasm, Stress granule
CC       {ECO:0000269|PubMed:32451507}.
CC   -!- INDUCTION: Following heat shock stress. {ECO:0000269|PubMed:26458103}.
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       (PubMed:31292544). This leads to the partition of m6A-containing mRNAs
CC       into membraneless compartments, where mRNAs may be stored, degraded or
CC       used to transport mRNAs to dendritic arbors in neurons
CC       (PubMed:31292544). {ECO:0000269|PubMed:31292544}.
CC   -!- PTM: (Microbial infection) Proteolytically cleaved by HIV-1 protease
CC       when incorporated into HIV-1 particles in a nucleocapsid-dependent-
CC       manner. Cleavage by HIV-1 protease probably ensures optimal infectivity
CC       of the mature virion. {ECO:0000269|PubMed:32053707}.
CC   -!- SIMILARITY: Belongs to the YTHDF family. YTHDF3 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was initially reported to act as a regulator of mRNA
CC       translation efficiency in cooperation with YTHDF1 by binding to m6A-
CC       containing mRNAs and interacting with 40S and 60S ribosome subunits
CC       (PubMed:28106072, PubMed:28106076, PubMed:28281539). These studies
CC       suggested that the 3 different paralogs (YTHDF1, YTHDF2 and YTHDF3)
CC       have unique functions with limited redundancy (PubMed:28106072,
CC       PubMed:28106076, PubMed:28281539). However, later studies showed that
CC       YTHDF1, YTHDF2 and YTHDF3 paralogs have redundant functions to a
CC       profound extent and directly promote degradation of m6A-containing
CC       mRNAs (PubMed:32492408). The effect on translation efficiency observed
CC       earlier is probably indirect (PubMed:32492408).
CC       {ECO:0000269|PubMed:28106072, ECO:0000269|PubMed:28106076,
CC       ECO:0000269|PubMed:28281539, ECO:0000269|PubMed:32492408}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=On the benefits of disorder
CC       - Issue 238 of August 2021;
CC       URL="https://web.expasy.org/spotlight/back_issues/238/";
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DR   EMBL; AK127574; BAG54526.1; -; mRNA.
DR   EMBL; AL832005; CAH56224.1; -; mRNA.
DR   EMBL; BX537996; CAH56480.1; -; mRNA.
DR   EMBL; CH471068; EAW86867.1; -; Genomic_DNA.
DR   EMBL; BC052970; AAH52970.1; -; mRNA.
DR   CCDS; CCDS75747.1; -.
DR   RefSeq; NP_001264742.1; NM_001277813.1.
DR   RefSeq; NP_001264743.1; NM_001277814.1.
DR   RefSeq; NP_001264744.1; NM_001277815.1.
DR   RefSeq; NP_001264745.1; NM_001277816.1.
DR   RefSeq; NP_001264746.1; NM_001277817.1.
DR   RefSeq; NP_001264747.1; NM_001277818.1.
DR   RefSeq; NP_689971.4; NM_152758.5.
DR   PDB; 6ZOT; X-ray; 2.70 A; A/B=392-571.
DR   PDBsum; 6ZOT; -.
DR   AlphaFoldDB; Q7Z739; -.
DR   SMR; Q7Z739; -.
DR   BioGRID; 128997; 226.
DR   IntAct; Q7Z739; 37.
DR   MINT; Q7Z739; -.
DR   STRING; 9606.ENSP00000478490; -.
DR   GlyConnect; 1905; 4 N-Linked glycans (2 sites), 1 O-Linked glycan (1 site).
DR   GlyGen; Q7Z739; 15 sites, 3 N-linked glycans (2 sites), 2 O-linked glycans (13 sites).
DR   iPTMnet; Q7Z739; -.
DR   MetOSite; Q7Z739; -.
DR   PhosphoSitePlus; Q7Z739; -.
DR   BioMuta; YTHDF3; -.
DR   DMDM; 74738853; -.
DR   EPD; Q7Z739; -.
DR   jPOST; Q7Z739; -.
DR   MassIVE; Q7Z739; -.
DR   MaxQB; Q7Z739; -.
DR   PeptideAtlas; Q7Z739; -.
DR   PRIDE; Q7Z739; -.
DR   ProteomicsDB; 69483; -.
DR   Antibodypedia; 24763; 145 antibodies from 22 providers.
DR   DNASU; 253943; -.
DR   Ensembl; ENST00000539294.6; ENSP00000473496.2; ENSG00000185728.17.
DR   GeneID; 253943; -.
DR   KEGG; hsa:253943; -.
DR   MANE-Select; ENST00000539294.6; ENSP00000473496.2; NM_152758.6; NP_689971.4.
DR   UCSC; uc033bnj.2; human.
DR   CTD; 253943; -.
DR   DisGeNET; 253943; -.
DR   GeneCards; YTHDF3; -.
DR   HGNC; HGNC:26465; YTHDF3.
DR   HPA; ENSG00000185728; Low tissue specificity.
DR   MIM; 618669; gene.
DR   neXtProt; NX_Q7Z739; -.
DR   OpenTargets; ENSG00000185728; -.
DR   PharmGKB; PA134976395; -.
DR   VEuPathDB; HostDB:ENSG00000185728; -.
DR   eggNOG; KOG1901; Eukaryota.
DR   GeneTree; ENSGT00940000158777; -.
DR   HOGENOM; CLU_022715_1_1_1; -.
DR   InParanoid; Q7Z739; -.
DR   OMA; GAYRSMG; -.
DR   OrthoDB; 1523251at2759; -.
DR   PhylomeDB; Q7Z739; -.
DR   PathwayCommons; Q7Z739; -.
DR   SignaLink; Q7Z739; -.
DR   BioGRID-ORCS; 253943; 9 hits in 264 CRISPR screens.
DR   ChiTaRS; YTHDF3; human.
DR   GeneWiki; YTHDF3; -.
DR   GenomeRNAi; 253943; -.
DR   Pharos; Q7Z739; Tbio.
DR   PRO; PR:Q7Z739; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q7Z739; protein.
DR   Bgee; ENSG00000185728; Expressed in endothelial cell and 212 other tissues.
DR   ExpressionAtlas; Q7Z739; baseline and differential.
DR   Genevisible; Q7Z739; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR   GO; GO:0000932; C:P-body; IDA:UniProtKB.
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:0043022; F:ribosome binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0061157; P:mRNA destabilization; IDA:UniProtKB.
DR   GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0070925; P:organelle assembly; IDA:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR   GO; GO:0045948; P:positive regulation of translational initiation; IDA:UniProtKB.
DR   GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
DR   GO; GO:1901163; P:regulation of trophoblast cell migration; IMP:UniProtKB.
DR   GO; GO:0034063; P:stress granule assembly; IDA: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   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Host-virus interaction; Phosphoprotein; Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..585
FT                   /note="YTH domain-containing family protein 3"
FT                   /id="PRO_0000230991"
FT   DOMAIN          416..550
FT                   /note="YTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..333
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         422..424
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:33073985,
FT                   ECO:0007744|PDB:6ZOT"
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:0000250|UniProtKB:Q9Y5A9"
FT   BINDING         438..439
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:33073985,
FT                   ECO:0007744|PDB:6ZOT"
FT   BINDING         468
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         492
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:33073985,
FT                   ECO:0007744|PDB:6ZOT"
FT   BINDING         497
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:33073985,
FT                   ECO:0007744|PDB:6ZOT"
FT   SITE            157..158
FT                   /note="(Microbial infection) Cleavage; by HIV-1 protease"
FT                   /evidence="ECO:0000269|PubMed:32053707"
FT   SITE            538..539
FT                   /note="(Microbial infection) Cleavage; by HIV-1 protease"
FT                   /evidence="ECO:0000305|PubMed:32053707"
FT   SITE            570..571
FT                   /note="(Microbial infection) Cleavage; by HIV-1 protease"
FT                   /evidence="ECO:0000305|PubMed:32053707"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CONFLICT        139
FT                   /note="S -> R (in Ref. 2; CAH56224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="P -> S (in Ref. 2; CAH56224)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        532
FT                   /note="S -> P (in Ref. 2; CAH56480)"
FT                   /evidence="ECO:0000305"
FT   HELIX           393..401
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          417..425
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           426..435
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           442..455
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          461..467
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          470..479
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          484..486
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   STRAND          500..512
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           513..515
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   TURN            516..518
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   TURN            522..525
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           529..531
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           540..552
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           559..562
FT                   /evidence="ECO:0007829|PDB:6ZOT"
FT   HELIX           563..568
FT                   /evidence="ECO:0007829|PDB:6ZOT"
SQ   SEQUENCE   585 AA;  63861 MW;  C7021FE48DEA441E CRC64;
     MSATSVDQRP KGQGNKVSVQ NGSIHQKDAV NDDDFEPYLS SQTNQSNSYP PMSDPYMPSY
     YAPSIGFPYS LGEAAWSTAG DQPMPYLTTY GQMSNGEHHY IPDGVFSQPG ALGNTPPFLG
     QHGFNFFPGN ADFSTWGTSG SQGQSTQSSA YSSSYGYPPS SLGRAITDGQ AGFGNDTLSK
     VPGISSIEQG MTGLKIGGDL TAAVTKTVGT ALSSSGMTSI ATNSVPPVSS AAPKPTSWAA
     IARKPAKPQP KLKPKGNVGI GGSAVPPPPI KHNMNIGTWD EKGSVVKAPP TQPVLPPQTI
     IQQPQPLIQP PPLVQSQLPQ QQPQPPQPQQ QQGPQPQAQP HQVQPQQQQL QNRWVAPRNR
     GAGFNQNNGA GSENFGLGVV PVSASPSSVE VHPVLEKLKA INNYNPKDFD WNLKNGRVFI
     IKSYSEDDIH RSIKYSIWCS TEHGNKRLDA AYRSLNGKGP LYLLFSVNGS GHFCGVAEMK
     SVVDYNAYAG VWSQDKWKGK FEVKWIFVKD VPNNQLRHIR LENNDNKPVT NSRDTQEVPL
     EKAKQVLKII ATFKHTTSIF DDFAHYEKRQ EEEEAMRRER NRNKQ
//
