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Protein Page:
CYP46A1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CYP46A1 Involved in the turnover of cholesterol. It converts cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. Belongs to the cytochrome P450 family. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.13.98; Membrane protein, integral; Lipid Metabolism - primary bile acid biosynthesis; Oxidoreductase
Chromosomal Location of Human Ortholog: 14q32.1
Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; integral to membrane
Molecular Function: cholesterol 24-hydroxylase activity; heme binding; iron ion binding; steroid hydroxylase activity
Biological Process: bile acid biosynthetic process; cholesterol catabolic process; nervous system development; sterol metabolic process; xenobiotic metabolic process
Reference #:  Q9Y6A2 (UniProtKB)
Gene Symbols: CYP46A1
Molecular weight: 56,821 Da
Basal Isoelectric point: 9.15  Predict pI for various phosphorylation states
Select Structure to View Below

CYP46A1

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 K69 DVFLDWAKKYGPVVR
0 2 S146‑p RVIDLAFsRsSLVSL
0 1 S148‑p IDLAFsRsSLVSLME
0 1 R255 RFLRQVGRDWVQRRR
0 1 K339 VDEVIGSKRyLDFED
0 2 Y341‑p EVIGSKRyLDFEDLG
0 1 Y352‑p EDLGRLQyLsQVLKE
0 1 S354‑p LGRLQyLsQVLKESL
0 1 K358 QyLsQVLKESLRLYP
0 1 K422 RFGPGAPKPRFTYFP
0 1 K477 LQEQATLKPLDPVLC
  mouse

 
K69‑ub DVFLDWAkKYGPVVR
S146‑p KVMDLAFsRSSLVSL
S148 MDLAFsRSSLVSLME
K255‑ub RLLRQVGkDWVQRRR
K339‑ub VDEVVGSkRHLDYED
H341 EVVGSkRHLDYEDLG
Y352 EDLGRLQYLSQVLkE
S354 LGRLQYLSQVLkESL
K358‑ub QYLSQVLkESLRLYP
K422‑ub RFGPGAPkPRFTYFP
K477 LQEQATLKPLDPVLC
  rat

 
K69 DVFLDWAKKYGPVVR
S146 RVMDLAFSRSSLVSL
S148 MDLAFSRSSLVSLMG
K255 RLLRQVGKDWVQRRR
K339 VDEVVGSKRHLDYED
H341 EVVGSKRHLDYEDLG
Y352 EDLGRLQYLSQVLKE
S354 LGRLQYLSQVLKESL
K358 QYLSQVLKESLRLYP
K422 RFGPGAPKPRFTYFP
K477‑ub LQEQATLkPLDPVLC
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