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Protein Page:
ApoM (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
ApoM Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. Plasma protein. Expressed in liver and kidney. Belongs to the calycin superfamily. Lipocalin family. Highly divergent. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide
Cellular Component: integral to plasma membrane
Molecular Function: antioxidant activity; lipid transporter activity; phospholipid binding
Biological Process: cholesterol homeostasis; reverse cholesterol transport; response to glucose stimulus; lipoprotein metabolic process; cholesterol efflux
Reference #:  O95445 (UniProtKB)
Alt. Names/Synonyms: apo-M; apolipoprotein M; APOM; G3a; HSPC336; NG20
Gene Symbols: APOM
Molecular weight: 21,253 Da
Basal Isoelectric point: 5.66  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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ApoM

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 - gap
  mouse

 
K108-u TYRLTEGkGNMELRT
  rat

 
K108 TYHLTEGKGNTELRT
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