UniProt functional annotation for P09651



	UniProt functional annotation for P09651

UniProt code: P09651.

Organism: Homo sapiens (Human).

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

Function: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection (PubMed:17371836). May bind to specific miRNA hairpins (PubMed:28431233). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). {ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:31498791}.

Function: (Microbial infection) May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681}.

Function: (Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis. {ECO:0000269|PubMed:17229681}.

Subunit: Identified in the spliceosome C complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with SEPT6 (PubMed:17229681). Interacts with C9orf72 (PubMed:24549040). Interacts with KHDRBS1 (PubMed:17371836). Interacts with UBQLN2 (PubMed:25616961). Interacts with PPIA/CYPA (PubMed:25678563). {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17229681, ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:24549040, ECO:0000269|PubMed:25616961, ECO:0000269|PubMed:25678563}.

Subunit: (Microbial infection) Interacts with HCV NS5B and with the 5'- UTR and 3'-UTR of HCV RNA. {ECO:0000269|PubMed:17229681}.

Subunit: (Microbial infection) May interact with SARS-CoV Nucleoprotein. {ECO:0000305|PubMed:15862300}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:17289661). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:17229681}. Note=(Microbial infection) In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV- replication dependent manner. {ECO:0000269|PubMed:17229681}.

Ptm: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.

Ptm: Sumoylated. {ECO:0000269|PubMed:15161980}.

Disease: Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269|PubMed:23455423}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269|PubMed:23455423, ECO:0000269|PubMed:27694260}. Note=The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous: [Isoform A1-A]: Is twenty times more abundant than isoform A1-B. {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:		Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and may modulate splice site selection (PubMed:17371836). May bind to specific miRNA hairpins (PubMed:28431233). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). {ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:28431233, ECO:0000269\|PubMed:31498791}.



Function:		(Microbial infection) May play a role in HCV RNA replication. {ECO:0000269\|PubMed:17229681}.



Function:		(Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis. {ECO:0000269\|PubMed:17229681}.


Subunit:		Identified in the spliceosome C complex (PubMed:11991638). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661). Interacts with SEPT6 (PubMed:17229681). Interacts with C9orf72 (PubMed:24549040). Interacts with KHDRBS1 (PubMed:17371836). Interacts with UBQLN2 (PubMed:25616961). Interacts with PPIA/CYPA (PubMed:25678563). {ECO:0000269\|PubMed:11991638, ECO:0000269\|PubMed:17229681, ECO:0000269\|PubMed:17289661, ECO:0000269\|PubMed:17371836, ECO:0000269\|PubMed:24549040, ECO:0000269\|PubMed:25616961, ECO:0000269\|PubMed:25678563}.
Subunit:		(Microbial infection) Interacts with HCV NS5B and with the 5'- UTR and 3'-UTR of HCV RNA. {ECO:0000269\|PubMed:17229681}.
Subunit:		(Microbial infection) May interact with SARS-CoV Nucleoprotein. {ECO:0000305\|PubMed:15862300}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17289661, ECO:0000269\|PubMed:27694260}. Cytoplasm {ECO:0000269\|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:17289661). {ECO:0000269\|PubMed:17289661, ECO:0000269\|PubMed:27694260}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:17229681}. Note=(Microbial infection) In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV- replication dependent manner. {ECO:0000269\|PubMed:17229681}.
Ptm:		Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.
Ptm:		Sumoylated. {ECO:0000269\|PubMed:15161980}.
Disease:		Inclusion body myopathy with early-onset Paget disease with or without frontotemporal dementia 3 (IBMPFD3) [MIM:615424]: An autosomal dominant disease characterized by disabling muscle weakness clinically resembling to limb girdle muscular dystrophy, osteolytic bone lesions consistent with Paget disease, and premature frontotemporal dementia. Clinical features show incomplete penetrance. {ECO:0000269\|PubMed:23455423}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Amyotrophic lateral sclerosis 20 (ALS20) [MIM:615426]: A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. {ECO:0000269\|PubMed:23455423, ECO:0000269\|PubMed:27694260}. Note=The disease is caused by variants affecting the gene represented in this entry.
Miscellaneous:		[Isoform A1-A]: Is twenty times more abundant than isoform A1-B. {ECO:0000305}.