GEMIN5
entrez
25929
canonical
uniprot
Q8TEQ6
canonical
ensembl
ENSG00000082516
resolver
ensp
ENSP00000285873
resolver
enst
ENST00000285873
resolver
genesymbol
GEMIN5
resolver
hgnc
HGNC:20043
resolver
uniprot
B7ZLC9
resolver
uniprot
Q14CV0
resolver
uniprot
Q58EZ8
resolver
uniprot
Q8WWV4
resolver
uniprot
Q969W4
resolver
uniprot
Q9H9K3
resolver
uniprot
Q9UFI5
resolver
uniprot_entry
B7ZLC9_HUMAN
resolver
uniprot_entry
GEMI5_HUMAN
resolver
uniprot_entry
Q58EZ8_HUMAN
resolver
uniprot_sec
Q14CV0
resolver
uniprot_sec
Q8WWV4
resolver
uniprot_sec
Q969W4
resolver
uniprot_sec
Q9H9K3
resolver
uniprot_sec
Q9UFI5
resolver
amino_acid_sequence
MGQEPRTLPPSPNWYCARCSDAVPGGLFGFAARTSVFLVRVGPGAGESPGTPPFRVIGELVGHTERVSGFTFSHHPGQYNLCATSSDDGTVKIWDVETKTVVTEHALHQHTISTLHWSPRVKDLIVSGDEKGVVFCYWFNRNDSQHLFIEPRTIFCLTCSPHHEDLVAIGYKDGIVVIIDISKKGEVIHRLRGHDDEIHSIAWCPLPGEDCLSINQEETSEEAEITNGNAVAQAPVTKGCYLATGSKDQTIRIWSCSRGRGVMILKLPFLKRRGGGIDPTVKERLWLTLHWPSNQPTQLVSSCFGGELLQWDLTQSWRRKYTLFSASSEGQNHSRIVFNLCPLQTEDDKQLLLSTSMDRDVKCWDIATLECSWTLPSLGGFAYSLAFSSVDIGSLAIGVGDGMIRVWNTLSIKNNYDVKNFWQGVKSKVTALCWHPTKEGCLAFGTDDGKVGLYDTYSNKPPQISSTYHKKTVYTLAWGPPVPPMSLGGEGDRPSLALYSCGGEGIVLQHNPWKLSGEAFDINKLIRDTNSIKYKLPVHTEISWKADGKIMALGNEDGSIEIFQIPNLKLICTIQQHHKLVNTISWHHEHGSQPELSYLMASGSNNAVIYVHNLKTVIESSPESPVTITEPYRTLSGHTAKITSVAWSPHHDGRLVSASYDGTAQVWDALREEPLCNFRGHRGRLLCVAWSPLDPDCIYSGADDFCVHKWLTSMQDHSRPPQGKKSIELEKKRLSQPKAKPKKKKKPTLRTPVKLESIDGNEEESMKENSGPVENGVSDQEGEEQAREPELPCGLAPAVSREPVICTPVSSGFEKSKVTINNKVILLKKEPPKEKPETLIKKRKARSLLPLSTSLDHRSKEELHQDCLVLATAKHSRELNEDVSADVEERFHLGLFTDRATLYRMIDIEGKGHLENGHPELFHQLMLWKGDLKGVLQTAAERGELTDNLVAMAPAAGYHVWLWAVEAFAKQLCFQDQYVKAASHLLSIHKVYEAVELLKSNHFYREAIAIAKARLRPEDPVLKDLYLSWGTVLERDGHYAVAAKCYLGATCAYDAAKVLAKKGDAASLRTAAELAAIVGEDELSASLALRCAQELLLANNWVGAQEALQLHESLQGQRLVFCLLELLSRHLEEKQLSEGKSSSSYHTWNTGTEGPFVERVTAVWKSIFSLDTPEQYQEAFQKLQNIKYPSATNNTPAKQLLLHICHDLTLAVLSQQMASWDEAVQALLRAVVRSYDSGSFTIMQEVYSAFLPDGCDHLRDKLGDHQSPATPAFKSLEAFFLYGRLYEFWWSLSRPCPNSSVWVRAGHRTLSVEPSQQLDTASTEETDPETSQPEPNRPSELDLRLTEEGERMLSTFKELFSEKHASLQNSQRTVAEVQETLAEMIRQHQKSQLCKSTANGPDKNEPEVEAEQPLCSSQSQCKEEKNEPLSLPELTKRLTEANQRMAKFPESIKAWPFPDVLECCLVLLLIRSHFPGCLAQEMQQQAQELLQKYGNTKTYRRHCQTFCM
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with cerebellar atrophy and motor dysfunction (NEDCAM) [MIM:619333]: An autosomal recessive disorder characterized by global developmental delay with predominantly motor abnormalities, axial hypotonia with decreased or absent reflexes, gait ataxia and appendicular spasticity. Affected individuals have cognitive impairment and speech delay. Brain imaging shows cerebellar atrophy. {ECO:0000269|PubMed:33963192}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:16857593, PubMed:18984161, PubMed:20513430, PubMed:33963192). 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 (Sm core). 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). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. Within the SMN complex, GEMIN5 recognizes and delivers the small nuclear RNAs (snRNAs) to the SMN complex (PubMed:11714716, PubMed:16314521, 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.27). 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:16314521, 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|PubMed:33963192, ECO:0000269|Ref.27}.
uniprot
proteins
mass_dalton
168589
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="W->A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes."; /evidence="ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601"; MUTAGEN 15; /note="Y->A: Abolishes interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. No effect on interaction with 80S ribosomes."; /evidence="ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600, ECO:0000269|PubMed:27881601"; MUTAGEN 33; /note="R->A: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881601"; MUTAGEN 197; /note="E->A: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881600"; MUTAGEN 271..273; /note="KRR->AAA: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex."; /evidence="ECO:0000269|PubMed:19377484"; MUTAGEN 286; /note="W->A: Abolishes interaction with U4 snRNA. Abolishes interaction with the 7-methylguanosine cap of RNA molecules. No effect on interaction with SMN complex."; /evidence="ECO:0000269|PubMed:19377484, ECO:0000269|PubMed:19750007"; MUTAGEN 290; /note="H->A: No effect in interaction with U4 snRNA. No effect on interaction with SMN complex."; /evidence="ECO:0000269|PubMed:19377484"; MUTAGEN 335; /note="R->E: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881601"; MUTAGEN 359; /note="R->A: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881601"; MUTAGEN 381; /note="F->A: Strongly decreases interaction with U4 snRNA. No effect on interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules. Abolishes interaction with 80S ribosomes."; /evidence="ECO:0000269|PubMed:27507887, ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600"; MUTAGEN 381; /note="F->D: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881601"; MUTAGEN 422; /note="W->E: Abolishes interaction with U4 snRNA."; /evidence="ECO:0000269|PubMed:27881601"; MUTAGEN 474; /note="Y->A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules."; /evidence="ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600"; MUTAGEN 641; /note="K->A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules."; /evidence="ECO:0000269|PubMed:27834343, ECO:0000269|PubMed:27881600"; MUTAGEN 660; /note="Y->A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules."; /evidence="ECO:0000269|PubMed:27834343"; MUTAGEN 684; /note="R->A: Abolishes interaction with the isolated 7-methylguanosine cap that is normally part of RNA molecules."; /evidence="ECO:0000269|PubMed:27834343
uniprot
proteins
protein_family
WD repeat gemin-5 family
uniprot
proteins
pubmed
11714716
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16314521
uniprot
proteins
pubmed
16857593
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17178713
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18984161
uniprot
proteins
pubmed
19377484
uniprot
proteins
pubmed
19750007
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20513430
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25911097
uniprot
proteins
pubmed
27507887
uniprot
proteins
pubmed
27834343
uniprot
proteins
pubmed
27881600
uniprot
proteins
pubmed
27881601
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
33963192
uniprot
proteins
sequence_length
1508
uniprot
proteins
subcellular_location
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}.
uniprot
proteins