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Showing Protein YTH domain-containing family protein 3 (HMDBP13975)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP13975
Secondary Accession Numbers None
Name YTH domain-containing family protein 3
Synonyms
  1. DF3
Gene Name YTHDF3
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:28106072, PubMed:28106076, PubMed:28281539, PubMed:32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:22575960, PubMed:24284625, PubMed:28106072, PubMed:28281539, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex or PAN3 (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:28106076, PubMed:32492408). Acts as a negative regulator of type I interferon response by down-regulating interferon-stimulated genes (ISGs) expression: acts by binding to FOXO3 mRNAs (By similarity). Binds to FOXO3 mRNAs independently of METTL3-mediated m6A modification (By similarity). Can also act as a regulator of mRNA stability in cooperation with YTHDF2 by binding to m6A-containing mRNA and promoting their degradation (PubMed:28106072). Recognizes and binds m6A-containing circular RNAs (circRNAs); circRNAs are generated through back-splicing of pre-mRNAs, a non-canonical splicing process promoted by dsRNA structures across circularizing exons (PubMed:28281539). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31388144, PubMed:31292544, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). May also recognize and bind N1-methyladenosine (m1A)-containing mRNAs: inhibits trophoblast invasion by binding to m1A-methylated transcripts of IGF1R, promoting their degradation (PubMed:32194978).Has some antiviral activity against HIV-1 virus: incorporated into HIV-1 particles in a nucleocapsid-dependent manner and reduces viral infectivity in the next cycle of infection (PubMed:32053707). May interfere with this early step of the viral life cycle by binding to N6-methyladenosine (m6A) modified sites on the HIV-1 RNA genome (PubMed:32053707).
Pathways Not Available
Reactions Not Available
GO Classification
Biological Process
regulation of mRNA stability
mRNA destabilization
negative regulation of type I interferon-mediated signaling pathway
regulation of trophoblast cell migration
positive regulation of translational initiation
stress granule assembly
positive regulation of translation
viral reproduction
organelle assembly
Cellular Component
cytosol
cytoplasmic mRNA processing body
cytoplasm
cytoplasmic stress granule
Molecular Function
ribosome binding
N6-methyladenosine-containing RNA binding
RNA binding
mRNA binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 585
Molecular Weight 63861.0
Theoretical pI 9.041
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q7Z739
UniProtKB/Swiss-Prot Entry Name YTHD3_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  17. Zaccara S, Jaffrey SR: A Unified Model for the Function of YTHDF Proteins in Regulating m(6)A-Modified mRNA. Cell. 2020 Jun 25;181(7):1582-1595.e18. doi: 10.1016/j.cell.2020.05.012. Epub 2020 Jun 2. [PubMed:32492408 ]
  18. Zheng Q, Gan H, Yang F, Yao Y, Hao F, Hong L, Jin L: Cytoplasmic m(1)A reader YTHDF3 inhibits trophoblast invasion by downregulation of m(1)A-methylated IGF1R. Cell Discov. 2020 Mar 10;6:12. doi: 10.1038/s41421-020-0144-4. eCollection 2020. [PubMed:32194978 ]
  19. Fu Y, Zhuang X: m(6)A-binding YTHDF proteins promote stress granule formation. Nat Chem Biol. 2020 Sep;16(9):955-963. doi: 10.1038/s41589-020-0524-y. Epub 2020 May 25. [PubMed:32451507 ]
  20. Jurczyszak D, Zhang W, Terry SN, Kehrer T, Bermudez Gonzalez MC, McGregor E, Mulder LCF, Eckwahl MJ, Pan T, Simon V: HIV protease cleaves the antiviral m6A reader protein YTHDF3 in the viral particle. PLoS Pathog. 2020 Feb 13;16(2):e1008305. doi: 10.1371/journal.ppat.1008305. eCollection 2020 Feb. [PubMed:32053707 ]
  21. Li Y, Bedi RK, Moroz-Omori EV, Caflisch A: Structural and Dynamic Insights into Redundant Function of YTHDF Proteins. J Chem Inf Model. 2020 Dec 28;60(12):5932-5935. doi: 10.1021/acs.jcim.0c01029. Epub 2020 Oct 19. [PubMed:33073985 ]