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Protein Page:
APOA1 (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
APOA1 Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. Interacts with APOA1BP and CLU. Component of a sperm activating protein complex (SPAP), consisting of APOA1, an immunoglobulin heavy chain, an immunoglobulin light chain and albumin. Interacts with NDRG1. Major protein of plasma HDL, also found in chylomicrons. Synthesized in the liver and small intestine. The oxidized form at Met-110 and Met-136 is increased in individuals with increased risk for coronary artery disease, such as in carrier of the eNOSa/b genotype and exposure to cigarette smoking. It is also present in increased levels in aortic lesions relative to native ApoA-I and increased levels are seen with increasing severity of disease. Belongs to the apolipoprotein A1/A4/E family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Endoplasmic reticulum; Motility/polarity/chemotaxis; Lipid-binding; Vesicle; Secreted; Cell development/differentiation
Chromosomal Location of Human Ortholog: 11q23-q24
Cellular Component: extracellular space; chylomicron; cell surface; endoplasmic reticulum lumen; endocytic vesicle; early endosome; extracellular region; plasma membrane; cytoplasmic vesicle; cytosol; nucleus; vesicle
Molecular Function: identical protein binding; protein binding; enzyme binding; phospholipid transporter activity; lipase inhibitor activity; chemorepellent activity; beta-amyloid binding; cholesterol transporter activity; cholesterol binding; phospholipid binding; phosphatidylcholine binding; high-density lipoprotein binding; apolipoprotein A-I receptor binding; apolipoprotein receptor binding
Biological Process: phototransduction, visible light; negative chemotaxis; negative regulation of lipase activity; axon regeneration in the peripheral nervous system; negative regulation of interleukin-1 beta secretion; sequestering of lipid; regulation of cholesterol absorption; transforming growth factor beta receptor signaling pathway; positive regulation of stress fiber formation; response to drug; platelet activation; cholesterol metabolic process; organ regeneration; regulation of Cdc42 protein signal transduction; adrenal gland development; positive regulation of hydrolase activity; positive regulation of Rho protein signal transduction; lipoprotein metabolic process; positive regulation of transferase activity; vitamin transport; cholesterol biosynthetic process; negative regulation of cytokine secretion during immune response; cholesterol homeostasis; lipoprotein biosynthetic process; response to estrogen stimulus; peptidyl-methionine modification; phosphatidylcholine biosynthetic process; positive regulation of lipoprotein lipase activity; blood vessel endothelial cell migration; cellular lipid metabolic process; platelet degranulation; phospholipid efflux; retinoid metabolic process; transmembrane transport; response to nutrient; phospholipid homeostasis; integrin-mediated signaling pathway; receptor-mediated endocytosis; positive regulation of fatty acid biosynthetic process; regulation of protein amino acid phosphorylation; cholesterol transport; protein stabilization; negative regulation of heterotypic cell-cell adhesion; protein amino acid oxidation; neurite regeneration; cholesterol efflux; G-protein coupled receptor protein signaling pathway; glucocorticoid metabolic process; reverse cholesterol transport; negative regulation of inflammatory response; endothelial cell proliferation; blood coagulation
Disease: Hypoalphalipoproteinemia, Primary; Amyloidosis, Familial Visceral
Reference #:  P02647 (UniProtKB)
Alt. Names/Synonyms: Apo-AI; ApoA-I; APOA1; Apolipoprotein A-I; Apolipoprotein A-I(1-242); Apolipoprotein A1; MGC117399
Gene Symbols: APOA1
Molecular weight: 30,778 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

APOA1

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


 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 K36 QSPWDRVKDLATVYV
0 1 K36 QSPWDRVKDLATVYV
0 1 K47 TVYVDVLKDSGRDYV
0 1 K47 TVYVDVLKDSGRDYV
0 1 K47 TVYVDVLKDSGRDYV
0 1 S55-p DSGRDYVsQFEGsAL
0 1 G59 DYVsQFEGsALGKQL
0 1 S60-p YVsQFEGsALGKQLN
0 1 A61 VsQFEGsALGKQLNL
0 1 S76 KLLDNWDSVTSTFSK
0 1 K112 GLRQEMSKDLEEVKA
0 1 K118 SKDLEEVKAKVQPYL
0 1 K120 DLEEVKAKVQPYLDD
0 1 K120 DLEEVKAKVQPYLDD
0 1 K130-ac PYLDDFQkKWQEEME
0 1 K130 PYLDDFQKKWQEEME
0 1 K130 PYLDDFQKKWQEEME
0 1 K131 YLDDFQkKWQEEMEL
0 1 Q133 DDFQkKWQEEMELYR
0 1 K142 EMELYRQKVEPLRAE
0 1 K142 EMELYRQKVEPLRAE
0 1 E152 PLRAELQEGARQKLH
0 1 K157 LQEGARQKLHELQEK
0 2 K157 LQEGARQKLHELQEK
0 1 S166-p HELQEKLsPLGEEMR
0 1 S166 HELQEKLSPLGEEMR
0 1 T185-p AHVDALRtHLAPYsD
0 1 H186 HVDALRtHLAPYsDE
0 3 S191-p RtHLAPYsDELRQRL
0 1 K206 AARLEALKENGGARL
0 2 K206 AARLEALKENGGARL
0 1 Y216-p GGARLAEyHAkAtEH
0 2 K219-ac RLAEyHAkAtEHLST
0 1 T221-p AEyHAkAtEHLSTLs
0 1 T221-ga AEyHAkAtEHLSTLs
0 1 S225 AkAtEHLSTLsEKAK
0 1 S228-ga tEHLSTLsEKAKPAL
0 1 - gap
0 1 S252-p VLESFKVsFLSALEE
0 1 E259 sFLSALEEYTkKLNT
0 1 E259 sFLSALEEYTkKLNT
0 1 T261 LSALEEYTkKLNTQ_
0 1 K262-ac SALEEYTkKLNTQ__
  mouse

 
K35 QSQWDKVKDFANVYV
K35-ub QSQWDKVkDFANVYV
K46-ac NVYVDAVkDSGRDYV
K46-ub NVYVDAVkDSGRDYV
K46-sc NVYVDAVkDSGRDYV
S54 DSGRDYVSQFEsSsL
S58-p DYVSQFEsSsLGQQL
S59 YVSQFEsSsLGQQLN
S60-p VSQFEsSsLGQQLNL
T75-p NLLENWDtLGSTVSQ
K111 WVRQEMNKDLEEVKQ
K117 NKDLEEVKQkVQPYL
K119 DLEEVKQKVQPYLDE
K119-ub DLEEVKQkVQPYLDE
K129 PYLDEFQKkWkEDVE
K129-ub PYLDEFQkkWkEDVE
K129-sc PYLDEFQkkWkEDVE
K130-ub YLDEFQkkWkEDVEL
K132-sc DEFQkkWkEDVELYR
K141 DVELYRQKVAPLGAE
K141-ub DVELYRQkVAPLGAE
E151 PLGAELQESARQkLQ
K156-ub LQESARQkLQELQGR
K156-ac LQESARQkLQELQGR
S165 QELQGRLSPVAEEFR
S165 QELQGRLSPVAEEFR
T184 THVDSLRTQLAPHSE
Q185 HVDSLRTQLAPHSEQ
S190 RTQLAPHSEQMRESL
K205 AQRLAELKSNPTLNE
K205-ub AQRLAELkSNPTLNE
Y213 SNPTLNEYHTRAKTH
R216 TLNEYHTRAKTHLKT
K218 NEYHTRAKTHLKTLG
K218 NEYHTRAKTHLKTLG
K222 TRAKTHLKTLGEKAR
G225 KTHLKTLGEKARPAL
Q249 MLETLKTQVQSVIDk
- gap
K256-ac QVQSVIDkASETLTA
K256-ub QVQSVIDkASETLTA
S258 QSVIDkASETLTAQ_
E259 SVIDkASETLTAQ__
  rat

 
K35-ac QSQWDRVkDFATVYV
K35 QSQWDRVKDFATVYV
K46 TVYVDAVKDSGRDYV
K46 TVYVDAVKDSGRDYV
K46 TVYVDAVKDSGRDYV
S54 DSGRDYVSQFESSTL
S58 DYVSQFESSTLGKQL
S59 YVSQFESSTLGKQLN
T60 VSQFESSTLGKQLNL
T75 NLLDNWDTLGSTVGR
K111-ac WLRNEMNkDLENVkQ
K117-ac NkDLENVkQkMQPHL
K119-ac DLENVkQkMQPHLDE
K119 DLENVkQKMQPHLDE
E129 PHLDEFQEKWNEEVE
E129 PHLDEFQEKWNEEVE
E129 PHLDEFQEKWNEEVE
K130 HLDEFQEKWNEEVEA
N132 DEFQEKWNEEVEAYR
K141-ac EVEAYRQkLEPLGTE
K141 EVEAYRQKLEPLGTE
K151-ac PLGTELHkNAkEMQR
K154 TELHkNAKEMQRHLk
K154-ac TELHkNAkEMQRHLk
K161 kEMQRHLKVVAEEFR
K161-ac kEMQRHLkVVAEEFR
A180 VNADALRAkFGLYSD
K181-ac NADALRAkFGLYSDQ
S186 RAkFGLYSDQMRENL
K201-ac AQRLTEIkNHPTLIE
K201 AQRLTEIKNHPTLIE
Y209 NHPTLIEYHTkASDH
K212-ac TLIEYHTkASDHLkT
S214 IEYHTkASDHLkTLG
S214 IEYHTkASDHLkTLG
K218-ac TkASDHLkTLGEKAK
G221 SDHLkTLGEKAKPAL
K245-ac VLEAWKAkIMSMIDE
- gap
E252 kIMSMIDEAkKKLNA
E252 kIMSMIDEAkKKLNA
K254-ac MSMIDEAkKKLNA__
K255 SMIDEAkKKLNA___
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