SIGMAR1
entrez
10280
canonical
uniprot
Q99720
canonical
ensembl
ENSG00000147955
resolver
ensp
ENSP00000277010
resolver
ensp
ENSP00000368170
resolver
ensp
ENSP00000420022
resolver
ensp
ENSP00000505305
resolver
ensp
ENSP00000505588
resolver
ensp
ENSP00000505634
resolver
ensp
ENSP00000505742
resolver
enst
ENST00000680244
resolver
enst
ENST00000680277
resolver
enst
ENST00000680730
resolver
genesymbol
SIGMAR1
resolver
genesymbol_syn
OPRS1
resolver
genesymbol_syn
SRBP
resolver
hgnc
HGNC:8157
resolver
uniprot
A0A7P0T8Z4
resolver
uniprot
A0A7P0T9D5
resolver
uniprot
A0A7P0Z4C2
resolver
uniprot
B4DR71
resolver
uniprot
D3DRM7
resolver
uniprot
O00673
resolver
uniprot
O00725
resolver
uniprot
Q0Z9W6
resolver
uniprot
Q153Z1
resolver
uniprot
Q2TSD1
resolver
uniprot
Q53GN2
resolver
uniprot
Q7Z653
resolver
uniprot
Q8N7H3
resolver
uniprot
Q9NYX0
resolver
uniprot_entry
A0A7P0T8Z4_HUMAN
resolver
uniprot_entry
A0A7P0T9D5_HUMAN
resolver
uniprot_entry
A0A7P0Z4C2_HUMAN
resolver
uniprot_entry
B4DR71_HUMAN
resolver
uniprot_entry
SGMR1_HUMAN
resolver
uniprot_sec
D3DRM7
resolver
uniprot_sec
O00673
resolver
uniprot_sec
O00725
resolver
uniprot_sec
Q0Z9W6
resolver
uniprot_sec
Q153Z1
resolver
uniprot_sec
Q2TSD1
resolver
uniprot_sec
Q53GN2
resolver
uniprot_sec
Q7Z653
resolver
uniprot_sec
Q8N7H3
resolver
uniprot_sec
Q9NYX0
resolver
amino_acid_sequence
MQWAVGRRWAWAALLLAVAAVLTQVVWLWLGTQSFVFQREEIAQLARQYAGLDHELAFSRLIVELRRLHPGHVLPDEELQWVFVNAGGWMGAMCLLHASLSEYVLLFGTALGSRGHSGRYWAEISDTIISGTFHQWREGTTKSEVFYPGETVVHGPGEATAVEWGPNTWMVEYGRGVIPSTLAFALADTVFSTQDFLTLFYTLRSYARGLRLELTTYLFGQDP
uniprot
proteins
disease_involvement
DISEASE: Amyotrophic lateral sclerosis 16, juvenile (ALS16) [MIM:614373]: 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:21842496}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, autosomal recessive 2 (HMNR2) [MIM:605726]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMNR2 is characterized by onset of distal muscle weakness and wasting affecting the lower and upper limbs in the first decade. {ECO:0000269|PubMed:26078401, ECO:0000269|PubMed:27629094}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:16472803, ECO:0000269|PubMed:9341151}.
uniprot
proteins
mass_dalton
25128
uniprot
proteins
mutagenesis
MUTAGEN 123; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 126; /note="D->G: Reduces ligand-binding. No effect on subcellular localization."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 138; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 144; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 150; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 158; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 163; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 172; /note="E->G: Reduces ligand-binding. No effect on subcellular localization."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 188; /note="D->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 195; /note="D->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895"; MUTAGEN 213; /note="E->G: No effect on ligand-binding."; /evidence="ECO:0000269|PubMed:11476895
uniprot
proteins
protein_family
ERG2 family
uniprot
proteins
pubmed
10087012
uniprot
proteins
pubmed
10406945
uniprot
proteins
pubmed
11476895
uniprot
proteins
pubmed
11687279
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15298647
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16472803
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21842496
uniprot
proteins
pubmed
22292588
uniprot
proteins
pubmed
23314020
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25647032
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26078401
uniprot
proteins
pubmed
27042935
uniprot
proteins
pubmed
27629094
uniprot
proteins
pubmed
8954936
uniprot
proteins
pubmed
9341151
uniprot
proteins
pubmed
9453537
uniprot
proteins
sequence_length
223
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:10406945}. Nucleus outer membrane {ECO:0000269|PubMed:10406945}. Nucleus envelope {ECO:0000269|PubMed:11476895, ECO:0000269|PubMed:9341151}. Cytoplasmic vesicle {ECO:0000269|PubMed:10406945}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10406945}. Membrane {ECO:0000269|PubMed:11476895, ECO:0000269|PubMed:27042935, ECO:0000269|PubMed:9341151}; Single-pass membrane protein {ECO:0000269|PubMed:27042935}. Lipid droplet {ECO:0000250|UniProtKB:O55242}. Cell junction. Cell membrane {ECO:0000269|PubMed:23314020}. Cell projection, growth cone. Postsynaptic density membrane {ECO:0000269|PubMed:23314020}. Note=During interphase, detected at the inner and outer nuclear membrane and the endoplasmic reticulum. Detected on cytoplasmic vesicles during mitosis (PubMed:10406945). Targeted to lipid droplets, cholesterol and galactosylceramide-enriched domains of the endoplasmic reticulum. Accumulation at the endoplasmic reticulum is prominent in alpha-motor neurons of patients with amyotrophic lateral sclerosis (PubMed:23314020). Enriched at cell-cell communication regions, growth cone and postsynaptic structures. Localization is modulated by ligand-binding. In motor neurons it is enriched at cholinergic postsynaptic densities (By similarity). {ECO:0000250|UniProtKB:O55242, ECO:0000269|PubMed:10406945, ECO:0000269|PubMed:23314020}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..30; /note="Helical"; /evidence="ECO:0000269|PubMed:27042935
uniprot
proteins