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Protein Page:
StAR (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
StAR Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone. May interact with TSPO. Expressed in gonads, adrenal cortex and kidney. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial; Lipid binding protein; Carrier protein
Cellular Component: mitochondrial crista; neuron projection; cell soma; mitochondrial intermembrane space; cytosol
Molecular Function: cholesterol transporter activity; cholesterol binding
Biological Process: response to nicotine; steroid metabolic process; diterpenoid metabolic process; dibenzo-p-dioxin metabolic process; regulation of steroid biosynthetic process; estrogen biosynthetic process; biphenyl metabolic process; circadian sleep/wake cycle, REM sleep; negative regulation of neuron apoptosis; response to nutrient; response to corticosterone stimulus; response to drug; cholesterol metabolic process; bile acid biosynthetic process; progesterone biosynthetic process; insecticide metabolic process; positive regulation of neurogenesis; fractalkine metabolic process; phthalate metabolic process; male gonad development; intracellular cholesterol transport; response to herbicide; glucocorticoid metabolic process; response to ethanol; cellular response to insulin stimulus; response to hydrogen peroxide; response to estrogen stimulus; response to lead ion; C21-steroid hormone biosynthetic process; brain development; response to ionizing radiation; response to activity; steroid biosynthetic process; regulation of neuronal synaptic plasticity; phenol metabolic process
Reference #:  P49675 (UniProtKB)
Alt. Names/Synonyms: cholesterol trafficker; mitochondrial steroid acute regulatory protein; STAR; StAR-related lipid transfer (START) domain containing 1; STARD1; START domain containing 1; START domain-containing protein 1; steroid acute regulatory protein; steroidogenic acute regulator; steroidogenic acute regulatory protein; Steroidogenic acute regulatory protein, mitochondrial
Gene Symbols: STAR
Molecular weight: 31,914 Da
Basal Isoelectric point: 9.17  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

StAR

Protein Structure Not Found.


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Sites Implicated In
activity, induced: S195‑p

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 R15 LCAGSSYRHMRNMKG
3 1 S56-p INQVRRRssLLGsRL
4 1 S57-p NQVRRRssLLGsRLE
0 2 S61-p RRssLLGsRLEETLY
1 0 S100 QEGWKKESQQDNGDK
8 0 S195-p RCAKRRGsTCVLAGM
0 1 T204-p CVLAGMAtDFGNMPE
3 0 S233 VLHPLAGSPSKTKLT
0 1 K273-ac DFANHLRkRLESHPA
1 0 S277 HLRkRLESHPASEAR
  mouse

 
R15-m1 LCAGSSYrHMRNMKG
S55 MGQVRRRSSLLGSQL
S56 GQVRRRSSLLGSQLE
S60 RRSSLLGSQLEATLY
S99 QEGWKKESQQENGDE
S194-p RCTKRRGsTCVLAGM
T203 CVLAGMATHFGEMPE
S232-p VLHPLAGsPSKTKLT
K272 EFANHLRKRLEASPA
S277 LRKRLEASPASEAQC
  rat

 
R15 LCAGSSYRHMRNMKG
S55-p MGQVRRRssLLGSQL
S56-p GQVRRRssLLGSQLE
S60 RRssLLGSQLEATLY
S99-p QEGWKKEsQQENGDE
S194-p RCTKRRGsTCVLAGM
T203 CVLAGMATHFGEMPE
S232 VLHPLAGSPSKTKLT
K272 EFASHLRKRLEsSPA
S276-p HLRKRLEsSPASEAQ
  hamster

 
R15 LCAGSSYRHLRNMKG
S55-p ISQVRRRssLLGSQL
S56-p SQVRRRssLLGSQLE
S60 RRssLLGSQLEAALY
N99 QEGWKKENQQENGDE
S194-p RCAKRRGsTCVLAGI
T203 CVLAGIATHFGEMPE
S232 VLHPLAGSPSKTKFT
K272 EFANHLRKRLESSSA
S276 HLRKRLESSSASEAR
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