UniProt functional annotation for Q96MU7



	UniProt functional annotation for Q96MU7

UniProt code: Q96MU7.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244). M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S- adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). {ECO:0000250|UniProtKB:E9Q5K9, ECO:0000269|PubMed:20167602, ECO:0000269|PubMed:25242552, ECO:0000269|PubMed:26318451, ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:27602518, ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:32663306}.

Subunit: Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By similarity). Interacts with SRSF3 (PubMed:26876937, PubMed:28984244). Interacts with SRSF7 (By similarity). Interacts with SRSF10 (PubMed:26876937). Interacts with CPSF6 (By similarity). Interacts with KHDRBS1/SAM68 (By similarity). Interacts with TRA2B (By similarity). Interacts with KHDRBS3 (By similarity). Interacts with EMD (PubMed:12755701). Interacts with RBMX (PubMed:19282290). Interacts with ZCCHC8 (PubMed:28984244). {ECO:0000250|UniProtKB:E9Q5K9, ECO:0000250|UniProtKB:Q9QY02, ECO:0000269|PubMed:12755701, ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:28984244}.

Subcellular location: Nucleus {ECO:0000269|PubMed:20167602}. Nucleus speckle {ECO:0000269|PubMed:26876937}. Note=Localizes to a novel subnuclear structure, the YT bodies. {ECO:0000250|UniProtKB:Q9QY02}.

Domain: The YTH domain mediates RNA-binding. {ECO:0000269|PubMed:20167602}.

Ptm: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q9QY02}.

Sequence caution: Sequence=AAY41024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=BAB71181.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:25242552, PubMed:26318451, PubMed:26876937, PubMed:28984244). M6A is a modification present at internal sites of mRNAs and some non- coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability (PubMed:25242552, PubMed:26318451). Acts as a key regulator of exon-inclusion or exon-skipping during alternative splicing via interaction with mRNA splicing factors SRSF3 and SRSF10 (PubMed:26876937). Specifically binds m6A-containing mRNAs and promotes recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A sites, leading to exon-inclusion during alternative splicing (PubMed:26876937). In contrast, interaction with SRSF3 prevents interaction with SRSF10, a splicing factor that promotes exon skipping: this prevents SRSF10 from binding to its mRNA-binding sites close to m6A-containing regions, leading to inhibit exon skipping during alternative splicing (PubMed:26876937). May also regulate alternative splice site selection (PubMed:20167602). Also involved in nuclear export of m6A-containing mRNAs via interaction with SRSF3: interaction with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export (PubMed:28984244). Involved in S- adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts, probably by binding m6A-containing MAT2A mRNAs (By similarity). Also recognizes and binds m6A on other RNA molecules (PubMed:27602518). Involved in random X inactivation mediated by Xist RNA: recognizes and binds m6A-containing Xist and promotes transcription repression activity of Xist (PubMed:27602518). Also recognizes and binds m6A-containing single-stranded DNA (PubMed:32663306). Involved in germline development: required for spermatogonial development in males and oocyte growth and maturation in females, probably via its role in alternative splicing (By similarity). {ECO:0000250\|UniProtKB:E9Q5K9, ECO:0000269\|PubMed:20167602, ECO:0000269\|PubMed:25242552, ECO:0000269\|PubMed:26318451, ECO:0000269\|PubMed:26876937, ECO:0000269\|PubMed:27602518, ECO:0000269\|PubMed:28984244, ECO:0000269\|PubMed:32663306}.


Subunit:		Interacts with SRSF1 (By similarity). Interacts with SRSF2 (By similarity). Interacts with SRSF3 (PubMed:26876937, PubMed:28984244). Interacts with SRSF7 (By similarity). Interacts with SRSF10 (PubMed:26876937). Interacts with CPSF6 (By similarity). Interacts with KHDRBS1/SAM68 (By similarity). Interacts with TRA2B (By similarity). Interacts with KHDRBS3 (By similarity). Interacts with EMD (PubMed:12755701). Interacts with RBMX (PubMed:19282290). Interacts with ZCCHC8 (PubMed:28984244). {ECO:0000250\|UniProtKB:E9Q5K9, ECO:0000250\|UniProtKB:Q9QY02, ECO:0000269\|PubMed:12755701, ECO:0000269\|PubMed:19282290, ECO:0000269\|PubMed:26876937, ECO:0000269\|PubMed:28984244}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:20167602}. Nucleus speckle {ECO:0000269\|PubMed:26876937}. Note=Localizes to a novel subnuclear structure, the YT bodies. {ECO:0000250\|UniProtKB:Q9QY02}.
Domain:		The YTH domain mediates RNA-binding. {ECO:0000269\|PubMed:20167602}.
Ptm:		Tyrosine phosphorylated. {ECO:0000250\|UniProtKB:Q9QY02}.
Sequence caution:		Sequence=AAY41024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; Sequence=BAB71181.1; Type=Erroneous initiation; Evidence={ECO:0000305};