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Protein Page:
CST3 (human)
rdtyret
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
CST3 As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity. Defects in CST3 are the cause of amyloidosis type 6 (AMYL6); also known as hereditary cerebral hemorrhage with amyloidosis (HCHWA), cerebral amyloid angiopathy (CAA) or cerebroarterial amyloidosis Icelandic type. AMYL6 is a hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low. Genetic variations in CST3 are associated with age- related macular degeneration type 11 (ARMD11). ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. Belongs to the cystatin family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted; Inhibitor
Chromosomal Location of Human Ortholog: 20p11.21
Cellular Component: axon; basement membrane; cell soma; contractile fiber; endoplasmic reticulum; extracellular region; extracellular space; lysosome; multivesicular body; nuclear membrane; perinuclear region of cytoplasm
Molecular Function: beta-amyloid binding; cysteine protease inhibitor activity; endopeptidase inhibitor activity; identical protein binding; protease binding; protein binding
Biological Process: apoptosis; brain development; cell activation; cellular protein metabolic process; circadian sleep/wake cycle, REM sleep; defense response; embryo implantation; eye development; fibril organization and biogenesis; negative regulation of peptidase activity; negative regulation of proteolysis; positive regulation of cell proliferation; positive regulation of DNA replication; regulation of programmed cell death; regulation of tissue remodeling; response to axon injury; response to carbohydrate stimulus; response to drug; response to estradiol stimulus; response to hypoxia; response to nutrient levels; response to toxin; salivary gland development; Sertoli cell development
Disease: Cerebral Amyloid Angiopathy, Cst3-related; Macular Degeneration, Age-related, 11
Reference #:  P01034 (UniProtKB)
Alt. Names/Synonyms: ARMD11; bA218C14.4 (cystatin C); CST3; cystatin 3; cystatin C; Cystatin-3; Cystatin-C; CYTC; Gamma-trace; MGC117328; Neuroendocrine basic polypeptide; Post-gamma-globulin
Gene Symbols: CST3
Molecular weight: 15,799 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CST3

Protein Structure Not Found.


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Modification Sites and Domains  
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Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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 K62 FAVGEYNKASNDMYH
0 1 Y128 AFCSFQIYAVPWQGT
  mouse

 
K56‑ub FAVSEYNkGSNDAYH
Y122 ALCSFQIYSVPWKGT
  rat

 
K56 FAVSEYNKGSNDAYH
Y122‑p ALCSFQIySVPWKGT
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