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Protein Page:
TTR (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
TTR Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Defects in TTR are the cause of amyloidosis transthyretin-related (AMYL-TTR). A hereditary generalized amyloidosis due to transthyretin amyloid deposition. Protein fibrils can form in different tissues leading to amyloid polyneuropathies, amyloidotic cardiomyopathy, carpal tunnel syndrome, systemic senile amyloidosis. The disease includes leptomeningeal amyloidosis that is characterized by primary involvement of the central nervous system. Neuropathologic examination shows amyloid in the walls of leptomeningeal vessels, in pia arachnoid, and subpial deposits. Some patients also develop vitreous amyloid deposition that leads to visual impairment (oculoleptomeningeal amyloidosis). Clinical features include seizures, stroke-like episodes, dementia, psychomotor deterioration, variable amyloid deposition in the vitreous humor. Defects in TTR are a cause of hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE). It is a condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities. Defects in TTR are a cause of carpal tunnel syndrome type 1 (CTS1). It is a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis. Belongs to the transthyretin family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide
Cellular Component: extracellular space; protein complex; cytoplasm; extracellular region
Molecular Function: identical protein binding; protein binding; hormone binding; protein heterodimerization activity; hormone activity
Biological Process: phototransduction, visible light; extracellular matrix organization and biogenesis; retinol metabolic process; transport; retinoid metabolic process
Reference #:  P02766 (UniProtKB)
Alt. Names/Synonyms: ATTR; HsT2651; PALB; Prealbumin; prealbumin, amyloidosis type I; TBPA; thyroxine-binding prealbumin; Transthyretin; TTHY; TTR
Gene Symbols: TTR
Molecular weight: 15,887 Da
Basal Isoelectric point: 5.52  Predict pI for various phosphorylation states
Select Structure to View Below

TTR

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 K35 SKCPLMVKVLDAVRG
0 1 K35 SKCPLMVKVLDAVRG
0 1 K55 VAVHVFRKAADDTWE
0 1 K68 WEPFASGKTSESGEL
0 1 S72 ASGKTSESGELHGLT
0 1 E83 HGLTTEEEFVEGIYK
0 1 K96 YKVEIDTKSYWKALG
  mouse

 
K35-u SKCPLMVkVLDAVRG
K35-a SKCPLMVkVLDAVRG
K55-u VAVKVFKkTSEGSWE
K68-u WEPFASGkTAEsGEL
S72-p ASGkTAEsGELHGLT
K83-u HGLTTDEkFVEGVYR
K96-u YRVELDTkSYWKTLG
  rat

 
K35 SKCPLMVKVLDAVRG
K35 SKCPLMVKVLDAVRG
K55 VAVKVFKKTADGSWE
K68 WEPFASGKTAESGEL
S72 ASGKTAESGELHGLT
K83 HGLTTDEKFTEGVYR
K96 YRVELDTKSYWKALG
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