BSCL2
entrez
26580
canonical
uniprot
Q96G97
canonical
ensembl
ENSG00000168000
resolver
ensp
ENSP00000278893
resolver
ensp
ENSP00000354032
resolver
ensp
ENSP00000384080
resolver
ensp
ENSP00000385332
resolver
ensp
ENSP00000505838
resolver
ensp
ENSP00000524177
resolver
enst
ENST00000405837
resolver
enst
ENST00000854118
resolver
genesymbol
BSCL2
resolver
hgnc
HGNC:15832
resolver
uniprot
A0A024R541
resolver
uniprot
A0A024R549
resolver
uniprot
G3XAE4
resolver
uniprot
J3KQ12
resolver
uniprot
Q567S1
resolver
uniprot
Q96SV1
resolver
uniprot
Q9BSQ0
resolver
uniprot_entry
A0A024R549_HUMAN
resolver
uniprot_entry
BSCL2_HUMAN
resolver
uniprot_entry
J3KQ12_HUMAN
resolver
uniprot_sec
A0A024R541
resolver
uniprot_sec
G3XAE4
resolver
uniprot_sec
Q567S1
resolver
uniprot_sec
Q96SV1
resolver
uniprot_sec
Q9BSQ0
resolver
amino_acid_sequence
MVNDPPVPALLWAQEVGQVLAGRARRLLLQFGVLFCTILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDSSTTSLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNFTFLSVIVLFSYMQWVWGGIWPRHRFSLQVNIRKRDNSRKEVQRRISAHQPGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDQQPLSGEEELEPEASDGSGSWEDAALLTEANLPAPAPASASAPVLETLGSSEPAGGALRQRPTCSSS
uniprot
proteins
disease_involvement
DISEASE: Lipodystrophy, congenital generalized, 2 (CGL2) [MIM:269700]: A form of congenital generalized lipodystrophy, a metabolic disorder characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. Inheritance is autosomal recessive. {ECO:0000269|PubMed:11479539, ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30901948}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spastic paraplegia 17, autosomal dominant (SPG17) [MIM:270685]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG17 is characterized by prominent amyotrophy of the hand muscles, the presence of mild to severe pyramidal tract signs and spastic paraplegia. SPG17 is a motor neuron disease overlapping with distal spinal muscular atrophy type 5. {ECO:0000269|PubMed:14981520, ECO:0000269|PubMed:17663003, ECO:0000269|PubMed:18585921, ECO:0000269|PubMed:24604904}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, autosomal dominant 13 (HMND13) [MIM:619112]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. HMND13 is characterized by distal muscular atrophy primarily affecting the upper limbs. Lower limb involvement may occur at the same time or later. Clinical features are highly variable even within families, and include poor fine hand motor skills, difficulty walking, foot deformities, spasticity and hyperreflexia. Some HMND13 patients show axonal peripheral neuropathy and distal sensory impairment. HMND13 inheritance is autosomal dominant with incomplete penetrance. {ECO:0000269|PubMed:14981520, ECO:0000269|PubMed:17663003}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Encephalopathy, progressive, with or without lipodystrophy (PELD) [MIM:615924]: A neurodegenerative disease characterized by developmental regression of motor and cognitive skills in the first years of life, often leading to death in the first decade, hyperactive behavior, seizures, tremor and ataxic gait. Patients may show a mild or typical lipodystrophic appearance. {ECO:0000269|PubMed:23564749}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Mediates the formation of lipid droplets during the differentiation and maturation of adipocytes (PubMed:19278620, PubMed:21533227, PubMed:27564575, PubMed:30293840, PubMed:31708432). Together with LDAF1, defines the sites of lipid droplet formation in the endoplasmic reticulum and promotes the aggregation of triacylglycerol molecules to form the core of a lipid droplet (nucleation) in the endoplasmic reticulum and drive budding of lipid droplets into the cytoplasm (PubMed:31708432). BSCL2 and LDAF1 also regulate protein and lipid delivery from the endoplasmic reticulum into growing lipid droplets (PubMed:27879284, PubMed:31178403). During early adipogenesis, BSCL2 inhibits GPAT3 and GPAT4 activity, thereby preventing phosphatidic acid accumulation that could antagonize PPARG and block differentiation (By similarity). This inhibition is then relieved by ADIG during adipocyte maturation, allowing expansion of lipid droplets (By similarity). Regulates the maturation of ZFYVE1-positive nascent lipid droplets and the function of the RAB18-ZFYVE1 complex in mediating the formation of endoplasmic reticulum-lipid droplet contacts (PubMed:30970241). Binds anionic phospholipids including phosphatidic acid (PubMed:30293840). {ECO:0000250|UniProtKB:Q9Z2E9, ECO:0000269|PubMed:19278620, ECO:0000269|PubMed:21533227, ECO:0000269|PubMed:27564575, ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30293840, ECO:0000269|PubMed:30970241, ECO:0000269|PubMed:31178403, ECO:0000269|PubMed:31708432}.
uniprot
proteins
mass_dalton
44392
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="H->R: Loss of oligomerization and function in lipid droplet formation; when associated with A-70; A-151; D-156; D-169 and A-175."; /evidence="ECO:0000269|PubMed:30293840"; MUTAGEN 70; /note="Y->A: Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-151; D-156; D-169 and A-175."; /evidence="ECO:0000269|PubMed:30293840"; MUTAGEN 151; /note="Y->A: Loss of oligomerization and function in lipid droplet biogenesis; when associated with R-67; A-70; D-156; D-169 and A-175."; /evidence="ECO:0000269|PubMed:30293840"; MUTAGEN 156; /note="L->D: Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-169 and A-175."; /evidence="ECO:0000269|PubMed:30293840"; MUTAGEN 169; /note="L->D: Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-156 and A-175."; /evidence="ECO:0000269|PubMed:30293840"; MUTAGEN 175; /note="Q->A: Loss of oligomerization and function in lipid droplet formation; when associated with R-67; A-70; A-151; D-156 and D-169."; /evidence="ECO:0000269|PubMed:30293840
uniprot
proteins
protein_family
Seipin family
uniprot
proteins
pubmed
11479539
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14981520
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16574104
uniprot
proteins
pubmed
17663003
uniprot
proteins
pubmed
18458148
uniprot
proteins
pubmed
18585921
uniprot
proteins
pubmed
19278620
uniprot
proteins
pubmed
21533227
uniprot
proteins
pubmed
23564749
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24604904
uniprot
proteins
pubmed
27564575
uniprot
proteins
pubmed
27879284
uniprot
proteins
pubmed
30293840
uniprot
proteins
pubmed
30901948
uniprot
proteins
pubmed
30970241
uniprot
proteins
pubmed
31178403
uniprot
proteins
pubmed
31708432
uniprot
proteins
sequence_length
398
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14981520, ECO:0000269|PubMed:16574104, ECO:0000269|PubMed:18458148, ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:27879284, ECO:0000269|PubMed:30970241}. Note=Localizes at endoplasmic reticulum-lipid droplets (ER-LD) contact sites. {ECO:0000269|PubMed:27879284}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..56; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q9Z2E9"; TRANSMEM 222..261; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q9Z2E9
uniprot
proteins