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Protein Page:
BSCL2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BSCL2 Is a regulator of lipid catabolism essential for adipocyte differentiation. Necessary for correct lipid storage and lipid droplets maintenance. Defects in BSCL2 are the cause of congenital generalized lipodystrophy type 2 (CGL2). Congenital generalized lipodystrophy is an autosomal recessive disorder characterized by a near absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes. Defects in BSCL2 are the cause of spastic paraplegia type 17 (SPG17); also known as Silver spastic paraplegia syndrome. Spastic paraplegia is a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. 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. Defects in BSCL2 are a cause of distal hereditary motor neuronopathy type 5A (HMN5A); also known as distal hereditary motor neuropathy type V (DSMAV). A disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute 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. 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. Belongs to the seipin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; Membrane protein, integral
Cellular Component: integral to endoplasmic reticulum membrane
Biological Process: cell death; fat cell differentiation; sequestering of lipid; negative regulation of lipid catabolic process; lipid catabolic process
Reference #:  Q96G97 (UniProtKB)
Alt. Names/Synonyms: Berardinelli-Seip congenital lipodystrophy 2 (seipin); Bernardinelli-Seip congenital lipodystrophy 2 (seipin); Bernardinelli-Seip congenital lipodystrophy type 2 protein; BSCL2; FLJ16651; GNG3LG; HMN5; MGC4694; Seipin; SPG17
Gene Symbols: BSCL2
Molecular weight: 44,392 Da
Basal Isoelectric point: 5.07  Predict pI for various phosphorylation states
Select Structure to View Below

BSCL2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K93-ub VANVSLTkGGRDRVL
0 1 Y106-p VLMYGQPyRVtLELE
0 1 T109-p YGQPyRVtLELELPE
0 1 S144 GRIISTSSRSVMLHY
0 1 S146 IISTSSRSVMLHYRS
0 1 Y184-p QLLEVELyADYRENS
0 1 Y213-p RIQLYGAyLRIHAHF
0 3 S289-p KEVQRRIsAHQPGPE
0 1 S372-p APAPASAsAPVLETL
  mouse

 
K93 VANVSLAKSGRDRVL
Y106 VLMYGQPYRVTLELE
T109 YGQPYRVTLELELPE
S144-p GRIISTSsRsVMLHY
S146-p IISTSsRsVMLHYRS
Y184 QLLEVELYSDYRENS
Y213 RIQMYGAYLRIHAHF
S289 HGAPRRISRHQPGQE
L366 TSASASALAPETLGS
  rat

 
K93 VANVSLTKSGRDRVL
Y106 VLMYGQPYRVTLELE
T109 YGQPYRVTLELELPE
S144 GRIISTSSRSVMLHY
S146 IISTSSRSVMLHYRS
Y184 QLLEVELYSDYRENS
Y213 RVQMYGAYLRIHAHF
S289 HGAQRRISRHQPGQA
- under review  
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