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Protein Page:
ACE (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
ACE Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. Genetic variations in ACE may be a cause of susceptibility to ischemic stroke (ISCHSTR); also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Defects in ACE are a cause of renal tubular dysgenesis (RTD). RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Genetic variations in ACE are associated with susceptibility to microvascular complications of diabetes type 3 (MVCD3). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Defects in ACE are a cause of susceptibility to intracerebral hemorrhage (ICH). A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. Belongs to the peptidase M2 family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.2.1.-; Protease; EC 3.4.15.1; Membrane protein, integral
Cellular Component: extracellular space; integral to membrane; extracellular region; plasma membrane; endosome; external side of plasma membrane
Molecular Function: peptidyl-dipeptidase activity; protein binding; metallopeptidase activity; zinc ion binding; carboxypeptidase activity; endopeptidase activity; bradykinin receptor binding; drug binding; actin binding; chloride ion binding
Biological Process: mononuclear cell proliferation; regulation of vasodilation; angiotensin mediated regulation of renal output; arachidonic acid secretion; angiotensin maturation; proteolysis; regulation of systemic arterial blood pressure by renin-angiotensin; regulation of smooth muscle cell migration; cellular protein metabolic process; regulation of blood pressure; regulation of vasoconstriction; peptide catabolic process; angiotensin catabolic process in blood; blood vessel remodeling; hormone catabolic process; kidney development
Reference #:  P12821 (UniProtKB)
Alt. Names/Synonyms: ACE; ACE1; angiotensin converting enzyme, somatic isoform; angiotensin I converting enzyme (peptidyl-dipeptidase A) 1; angiotensin I converting enzyme 1; Angiotensin-converting enzyme; Angiotensin-converting enzyme, soluble form; carboxycathepsin; CD143; CD143 antigen; DCP; DCP1; dipeptidyl carboxypeptidase 1; Dipeptidyl carboxypeptidase I; Kininase II; MGC26566; MVCD3; peptidase P; testicular ECA
Gene Symbols: ACE
Molecular weight: 149,715 Da
Basal Isoelectric point: 5.95  Predict pI for various phosphorylation states
Select Structure to View Below

ACE

Protein Structure Not Found.


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Sites Implicated In
exocytosis, altered: S1299‑p
intracellular localization: S1299‑p
molecular association, regulation: S1299‑p
protein degradation: S1299‑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

► Hide Isoforms
 
0 1 Q99 EFAEAWGQKAKELYE
0 1 Q99 EFAEAWGQKAKELYE
0 1 K100 FAEAWGQKAKELYEP
0 1 K136-ac SANLPLAkRQQyNAL
0 1 Y140-p PLAkRQQyNALLSNM
0 1 Y151-p LSNMSRIySTAKVCL
0 1 T697-p NMQIANHtLKYGTQA
0 1 T716-p VNQLQNTtIkRIIKK
0 1 K718-ub QLQNTtIkRIIKKVQ
0 1 S824-p GYVDAGDsWRSMYET
0 1 - gap
0 1 - gap
7 25 S1299-p SHGPQFGsEVELRHS
0 1 S1306 sEVELRHS_______
  ACE iso2  
- gap
- gap
- gap
- gap
- gap
- gap
T123 NMQIANHTLKYGTQA
T142 VNQLQNTTIKRIIKK
K144 QLQNTTIKRIIKKVQ
S250 GYVDAGDSWRSMYET
Y700-p GTREAPVyMSkRAAS
K703-ac EAPVyMSkRAASSGP
- gap
- gap
  mouse

 
K104-ac EFAEVWGkkAKELYE
K104 EFAEVWGKkAKELYE
K105-ac FAEVWGkkAKELYES
Q141 PANLPLAQRQQYNSL
Y145 PLAQRQQYNSLLSNM
Y156 LSNMSRIYSTGKVCF
T702 STEVSNHTLKYGTRA
S721 VSNFQNSSIKRIIKK
K723 NFQNSSIKRIIKKLQ
S829 GYTDAGDSWRSLYES
- gap
- gap
S1305-p HRGPQFGsEVELRHs
S1312-p sEVELRHs_______
  rat

 
K105 EFAEVWGKKAKELYE
K105-ub EFAEVWGkKAKELYE
K106 FAEVWGkKAKELYES
Q142 PANLPLTQRLQYNSL
Y146 PLTQRLQYNSLLSNM
Y157 LSNMSRIYSTGKVCF
T703 NKEVSNHTLKYGTWA
T722 VSNFQNSTIKRIIKK
K724 NFQNSTIKRIIKKVQ
S830 GYSDAGDSWRSSYES
- gap
- gap
S1306-p HRGPQFGsEVELRHs
S1313-p sEVELRHs_______
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