Q16637
uniprot
Q16637
canonical
amino_acid_sequence
MAMSSGGSGGGVPEQEDSVLFRRGTGQSDDSDIWDDTALIKAYDKAVASFKHALKNGDICETSGKPKTTPKRKPAKKNKSQKKNTAASLQQWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNAQENENESQVSTDESENSRSPGNKSDNIKPKSAPWNSFLPPPPPMPGPRLGPGKPGLKFNGPPPPPPPPPPHLLSCWLPPFPSGPPIIPPPPPICPDSLDDADALGSMLISWYMSGYHTGYYMGFRQNQKEGRCSHSLN
uniprot
proteins
disease_involvement
DISEASE: Spinal muscular atrophy 1 (SMA1) [MIM:253300]: A form of spinal muscular atrophy, a group of neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Autosomal recessive forms are classified according to the age of onset, the maximum muscular activity achieved, and survivorship. The severity of the disease is mainly determined by the copy number of SMN2, a copy gene which predominantly produces exon 7-skipped transcripts and only low amount of full-length transcripts that encode for a protein identical to SMN1. Only about 4% of SMA patients bear one SMN1 copy with an intragenic mutation. SMA1 is a severe form, with onset before 6 months of age. SMA1 patients never achieve the ability to sit. {ECO:0000269|PubMed:10500148, ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:15249625, ECO:0000269|PubMed:15580564, ECO:0000269|PubMed:21088113, ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:22101937, ECO:0000269|PubMed:23022347, ECO:0000269|PubMed:33754639, ECO:0000269|PubMed:7813012, ECO:0000269|PubMed:9147655}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 2 (SMA2) [MIM:253550]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. It has intermediate severity, with onset between 6 and 18 months. Patients do not reach the motor milestone of standing, and survive into adulthood. {ECO:0000269|PubMed:10732802, ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:21088113, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 3 (SMA3) [MIM:253400]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is after 18 months. Patients develop ability to stand and walk and survive into adulthood. {ECO:0000269|PubMed:10732817, ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:9158159, ECO:0000269|PubMed:9837824}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinal muscular atrophy 4 (SMA4) [MIM:271150]: An autosomal recessive form of spinal muscular atrophy, a neuromuscular disorder characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. Onset is in adulthood, disease progression is slow, and patients can stand and walk. {ECO:0000269|PubMed:7658877, ECO:0000269|PubMed:8551862}. 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:18984161, PubMed:9845364). 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) (PubMed:18984161). 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). Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (PubMed:17178713, PubMed:21816274, PubMed:22101937). 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 (PubMed:31799625). Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development (PubMed:23063131). Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs). {ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:22101937, ECO:0000269|PubMed:23063131, ECO:0000269|PubMed:26700805, ECO:0000269|PubMed:31799625, ECO:0000269|PubMed:9845364}.
uniprot
proteins
mass_dalton
31849
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="W->A: Impairs GEMIN2 binding."; /evidence="ECO:0000269|PubMed:22607171"; MUTAGEN 39; /note="L->A: Impairs GEMIN2 binding."; /evidence="ECO:0000269|PubMed:22607171"; MUTAGEN 43; /note="Y->A: Impairs GEMIN2 binding."; /evidence="ECO:0000269|PubMed:22607171"; MUTAGEN 44; /note="D->A: Impairs GEMIN2 binding."; /evidence="ECO:0000269|PubMed:21816274"; MUTAGEN 46; /note="A->N: Impairs GEMIN2 binding."; /evidence="ECO:0000269|PubMed:22607171"; MUTAGEN 92; /note="W->S: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 102; /note="W->L,V: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 109; /note="Y->H: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 127; /note="Y->L,F: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 130; /note="Y->D: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 132; /note="N->D,S: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 134..136; /note="EEQ->SEV: Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:22101937"; MUTAGEN 134; /note="E->K: Impairs SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4. Abolishes interaction with SNRPD1 and SNRPD3. Impairs binding to substrate containing dimethylated arginine."; /evidence="ECO:0000269|PubMed:11135666, ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:21088113, ECO:0000269|PubMed:21389246, ECO:0000269|PubMed:22101937, ECO:0000269|PubMed:29061699"; MUTAGEN 260; /note="L->S: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 263; /note="M->R,T,A: Impairs homooligomerization and GEMIN8 binding."; /evidence="ECO:0000269|PubMed:23022347, ECO:0000269|PubMed:33754639"; MUTAGEN 264; /note="L->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 266; /note="S->P: Impairs homooligomerization and GEMIN8 binding."; /evidence="ECO:0000269|PubMed:23022347, ECO:0000269|PubMed:33754639"; MUTAGEN 267; /note="W->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 268; /note="Y->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 271; /note="G->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 272; /note="Y->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 273; /note="H->R: Impairs GEMIN8 binding."; /evidence="ECO:0000269|PubMed:33754639"; MUTAGEN 274; /note="T->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 275; /note="G->A: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347"; MUTAGEN 279; /note="G->E: Impairs homooligomerization."; /evidence="ECO:0000269|PubMed:23022347
uniprot
proteins
protein_family
SMN family
uniprot
proteins
pubmed
10500148
uniprot
proteins
pubmed
10732802
uniprot
proteins
pubmed
10732817
uniprot
proteins
pubmed
11135666
uniprot
proteins
pubmed
11283611
uniprot
proteins
pubmed
11551898
uniprot
proteins
pubmed
11574476
uniprot
proteins
pubmed
11641277
uniprot
proteins
pubmed
12065586
uniprot
proteins
pubmed
12067652
uniprot
proteins
pubmed
12095920
uniprot
proteins
pubmed
12628254
uniprot
proteins
pubmed
12975319
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14715275
uniprot
proteins
pubmed
15249625
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15580564
uniprot
proteins
pubmed
16087681
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17103222
uniprot
proteins
pubmed
17178713
uniprot
proteins
pubmed
17487921
uniprot
proteins
pubmed
18093976
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18984161
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21072240
uniprot
proteins
pubmed
21088113
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21389246
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21609790
uniprot
proteins
pubmed
21700224
uniprot
proteins
pubmed
21816274
uniprot
proteins
pubmed
22101937
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22607171
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23022347
uniprot
proteins
pubmed
23063131
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25737013
uniprot
proteins
pubmed
26092730
uniprot
proteins
pubmed
26700805
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29061699
uniprot
proteins
pubmed
31799625
uniprot
proteins
pubmed
33754639
uniprot
proteins
pubmed
7552146
uniprot
proteins
pubmed
7639755
uniprot
proteins
pubmed
7658877
uniprot
proteins
pubmed
7813012
uniprot
proteins
pubmed
8551862
uniprot
proteins
pubmed
8670859
uniprot
proteins
pubmed
8838816
uniprot
proteins
pubmed
9147655
uniprot
proteins
pubmed
9158159
uniprot
proteins
pubmed
9259265
uniprot
proteins
pubmed
9323129
uniprot
proteins
pubmed
9503025
uniprot
proteins
pubmed
9837824
uniprot
proteins
pubmed
9845364
uniprot
proteins
sequence_length
294
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, gem {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:8670859, ECO:0000305|PubMed:12067652}. Nucleus, Cajal body {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:21072240, ECO:0000305|PubMed:12067652}. Cytoplasm {ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:8670859, ECO:0000305|PubMed:12067652}. Cytoplasmic granule {ECO:0000269|PubMed:14715275}. Perikaryon {ECO:0000269|PubMed:18093976}. Cell projection, neuron projection {ECO:0000269|PubMed:18093976}. Cell projection, axon {ECO:0000250|UniProtKB:P97801}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P97801}. Note=Colocalizes with actin and at the Z-line of skeletal muscle (By similarity). Under stress conditions colocalizes with RPP20/POP7 in punctuated cytoplasmic granules (PubMed:14715275). Colocalized and redistributed with ZPR1 from the cytoplasm to nuclear gems (Gemini of coiled bodies) and Cajal bodies (PubMed:11283611). Colocalizes with FMR1 in cytoplasmic granules in the soma and neurite cell processes (PubMed:18093976). {ECO:0000250|UniProtKB:P97801, ECO:0000269|PubMed:11283611, ECO:0000269|PubMed:14715275, ECO:0000269|PubMed:18093976}.
uniprot
proteins