UniProt functional annotation for Q8TEQ6



	UniProt functional annotation for Q8TEQ6

UniProt code: Q8TEQ6.

Organism: Homo sapiens (Human).

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

Function: Required for the assembly of the SMN complex that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:16857593, PubMed:18984161, PubMed:20513430). Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (PubMed:18984161). GEMIN5 acts as the snRNA-binding protein of the SMN complex (PubMed:11714716, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601). Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.25). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887). {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:16857593, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:20513430, ECO:0000269|PubMed:25911097, ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601, ECO:0000269|Ref.25}.

Subunit: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:20513430, PubMed:27507887). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:11714716, PubMed:20513430). Interacts directly with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE (PubMed:11714716). Identified in a SMN complex that contains GEMIN2/SIP1 (PubMed:19377484). Interacts with cytosolic DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887). Interacts with SNRNP70 and HNRNPU (PubMed:27507887). Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit (PubMed:27507887). Interacts with the ribosomal subunits RPL3 and RPL4 (PubMed:27507887). {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:20513430, ECO:0000269|PubMed:27507887}.

Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:11714716}. Nucleus, gem {ECO:0000269|PubMed:11714716}. Cytoplasm {ECO:0000269|PubMed:11714716, ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:20513430, ECO:0000269|PubMed:25911097, ECO:0000269|PubMed:27507887}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm. {ECO:0000269|PubMed:11714716}.

Domain: The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.25). The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit (PubMed:27507887). {ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007, ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601, ECO:0000269|Ref.25}.

Similarity: Belongs to the WD repeat gemin-5 family. {ECO:0000305}.

Sequence caution: Sequence=BAB84892.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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:		Required for the assembly of the SMN complex that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:16857593, PubMed:18984161, PubMed:20513430). Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (PubMed:18984161). GEMIN5 acts as the snRNA-binding protein of the SMN complex (PubMed:11714716, PubMed:16857593, PubMed:19377484, PubMed:19750007, PubMed:20513430, PubMed:27834343, PubMed:27881600, PubMed:27881601). Binds to the 7-methylguanosine cap of RNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.25). Binds to the 3'-UTR of SMN1 mRNA and regulates its translation; does not affect mRNA stability (PubMed:25911097). May play a role in the regulation of protein synthesis via its interaction with ribosomes (PubMed:27507887). {ECO:0000269\|PubMed:11714716, ECO:0000269\|PubMed:16857593, ECO:0000269\|PubMed:18984161, ECO:0000269\|PubMed:19377484, ECO:0000269\|PubMed:19750007, ECO:0000269\|PubMed:20513430, ECO:0000269\|PubMed:25911097, ECO:0000269\|PubMed:27507887, ECO:0000269\|PubMed:27834343, ECO:0000269\|PubMed:27881600, ECO:0000269\|PubMed:27881601, ECO:0000269\|Ref.25}.


Subunit:		Part of the core SMN complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP (PubMed:20513430, PubMed:27507887). Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:11714716, PubMed:20513430). Interacts directly with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE (PubMed:11714716). Identified in a SMN complex that contains GEMIN2/SIP1 (PubMed:19377484). Interacts with cytosolic DDX20/GEMIN3 and GEMIN4 (PubMed:19750007, PubMed:27507887). Interacts with SNRNP70 and HNRNPU (PubMed:27507887). Identified in a complex with 80S ribosomes; binds to the 60S large ribosomal subunit (PubMed:27507887). Interacts with the ribosomal subunits RPL3 and RPL4 (PubMed:27507887). {ECO:0000269\|PubMed:11714716, ECO:0000269\|PubMed:18984161, ECO:0000269\|PubMed:19377484, ECO:0000269\|PubMed:19750007, ECO:0000269\|PubMed:20513430, ECO:0000269\|PubMed:27507887}.
Subcellular location:		Nucleus, nucleoplasm {ECO:0000269\|PubMed:11714716}. Nucleus, gem {ECO:0000269\|PubMed:11714716}. Cytoplasm {ECO:0000269\|PubMed:11714716, ECO:0000269\|PubMed:19750007, ECO:0000269\|PubMed:20513430, ECO:0000269\|PubMed:25911097, ECO:0000269\|PubMed:27507887}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm. {ECO:0000269\|PubMed:11714716}.
Domain:		The WD repeat domain mediates binding to U1 snRNA and to U4 snRNA (PubMed:19377484, PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601). The WD repeat domain also mediates binding to the 7-methylguanosine cap that is found both on mRNA and snRNA molecules (PubMed:19750007, PubMed:27834343, PubMed:27881600, PubMed:27881601, Ref.25). The regions that bind snRNA molecules and the isolated 7-methylguanosine cap overlap at least partially (PubMed:27834343, PubMed:27881600, PubMed:27881601). Besides, the WD repeat domain mediates interaction with the 60S large ribosomal subunit (PubMed:27507887). {ECO:0000269\|PubMed:19377484, ECO:0000269\|PubMed:19750007, ECO:0000269\|PubMed:27507887, ECO:0000269\|PubMed:27834343, ECO:0000269\|PubMed:27881600, ECO:0000269\|PubMed:27881601, ECO:0000269\|Ref.25}.
Similarity:		Belongs to the WD repeat gemin-5 family. {ECO:0000305}.
Sequence caution:		Sequence=BAB84892.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};