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UniProtKB - P02766 (TTHY_HUMAN)

Protein

Transthyretin

Gene

TTR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.1 Publication

Miscellaneous

Tetramer dissociation and partial unfolding leads to the formation of aggregates and amyloid fibrils. Small molecules that occupy at least one of the thyroid hormone binding sites stabilize the tetramer, and thereby stabilize the native state and protect against misfolding and the formation of amyloid fibrils.
Two binding sites for thyroxine are located in the channel. Less than 1% of plasma prealbumin molecules are normally involved in thyroxine transport. L-thyroxine binds to the transthyretin by an order of magnitude stronger than does the triiodo-L-thyronine. Thyroxine-binding globulin is the major carrier protein for thyroid hormones in man.
About 40% of plasma transthyretin circulates in a tight protein-protein complex with the plasma retinol-binding protein (RBP). The formation of the complex with RBP stabilizes the binding of retinol to RBP and decreases the glomerular filtration and renal catabolism of the relatively small RBP molecule. There is evidence for 2 binding sites for RBP, one possibly being a region that includes Ile-104, located on the outer surface of the transthyretin molecule.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei35Thyroid hormones1
Binding sitei74Thyroid hormones1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • hormone activity Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein heterodimerization activity Source: Ensembl
  • thyroid hormone binding Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHormone, Thyroid hormone
Biological processTransport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-6798695 Neutrophil degranulation
R-HSA-975634 Retinoid metabolism and transport
R-HSA-977225 Amyloid fiber formation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transthyretin
Alternative name(s):
ATTR
Prealbumin
TBPA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TTR
Synonyms:PALB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 18

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000118271.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:12405 TTR

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		176300 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P02766

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Amyloid, Cytoplasm, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Amyloidosis, transthyretin-related (AMYL-TTR)73 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:105210
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_00754730C → R in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918083EnsemblClinVar.1
Natural variantiVAR_03895932L → P in AMYL-TTR. 2 PublicationsCorresponds to variant dbSNP:rs121918094EnsemblClinVar.1
Natural variantiVAR_00754838D → E in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_00754938D → G in AMYL-TTR; leptomeningeal amyloidosis; leads to unfolding and exposure of N-118 to glycosylation by STT3B and subsequent degradation by the ERAD pathway. 2 PublicationsCorresponds to variant dbSNP:rs121918098EnsemblClinVar.1
Natural variantiVAR_00755040V → I in AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome. 2 PublicationsCorresponds to variant dbSNP:rs121918093EnsemblClinVar.1
Natural variantiVAR_03896143S → N in AMYL-TTR. 1 Publication1
Natural variantiVAR_00755144P → S in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs11541790EnsemblClinVar.1
Natural variantiVAR_01065848V → M in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00755250V → A in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs79977247EnsemblClinVar.1
Natural variantiVAR_03896250V → G in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs79977247EnsemblClinVar.1
Natural variantiVAR_00755350V → L in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs28933979EnsemblClinVar.1
Natural variantiVAR_00755450V → M in AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation. 10 PublicationsCorresponds to variant dbSNP:rs28933979EnsemblClinVar.1
Natural variantiVAR_00755553F → I in AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs121918068EnsemblClinVar.1
Natural variantiVAR_00755653F → L in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs121918068EnsemblClinVar.1
Natural variantiVAR_03896453F → V in AMYL-TTR; amyloid polyneuropathy. 4 Publications1
Natural variantiVAR_03896554R → T in AMYL-TTR. 1 Publication1
Natural variantiVAR_03896655K → N in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00755756A → P in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918077EnsemblClinVar.1
Natural variantiVAR_03896758D → A in AMYL-TTR. 2 Publications1
Natural variantiVAR_03896858D → V in AMYL-TTR. 2 Publications1
Natural variantiVAR_03896961W → L in AMYL-TTR. 1 Publication1
Natural variantiVAR_03897062E → D in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs11541796EnsemblClinVar.1
Natural variantiVAR_00755862E → G in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs11541796EnsemblClinVar.1
Natural variantiVAR_03897164F → S in AMYL-TTR. 2 PublicationsCorresponds to variant dbSNP:rs104894665EnsemblClinVar.1
Natural variantiVAR_00755965A → D in AMYL-TTR; amyloid cardiomyopathy. Corresponds to variant dbSNP:rs730881169EnsemblClinVar.1
Natural variantiVAR_03897265A → S in AMYL-TTR. 1 Publication1
Natural variantiVAR_00756065A → T in AMYL-TTR; amyloid cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121918078Ensembl.1
Natural variantiVAR_00756167G → A in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs121918090EnsemblClinVar.1
Natural variantiVAR_03897367G → E in AMYL-TTR. 2 Publications1
Natural variantiVAR_00756267G → R in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs387906523EnsemblClinVar.1
Natural variantiVAR_00756367G → V in AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome. 1
Natural variantiVAR_00756469T → A in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918081EnsemblClinVar.1
Natural variantiVAR_03897469T → I in AMYL-TTR. 2 Publications1
Natural variantiVAR_00756570S → I in AMYL-TTR; amyloid cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs121918080EnsemblClinVar.1
Natural variantiVAR_00756670S → R in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs386134269EnsemblClinVar.1
Natural variantiVAR_00756772S → P in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_03897573G → E in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs121918097EnsemblClinVar.1
Natural variantiVAR_00756874E → G in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_03897674E → K in AMYL-TTR; early-onset amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00756975L → P in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs121918079EnsemblClinVar.1
Natural variantiVAR_03897775L → Q in AMYL-TTR. 1 Publication1
Natural variantiVAR_00757078L → H in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918069EnsemblClinVar.1
Natural variantiVAR_00757178L → R in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918069EnsemblClinVar.1
Natural variantiVAR_00757279T → K in AMYL-TTR; amyloid cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs730881163EnsemblClinVar.1
Natural variantiVAR_00757380T → A in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. 4 PublicationsCorresponds to variant dbSNP:rs121918070EnsemblClinVar.1
Natural variantiVAR_03897881E → G in AMYL-TTR. 1 Publication1
Natural variantiVAR_00757481E → K in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918086EnsemblClinVar.1
Natural variantiVAR_00757584F → L in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918091EnsemblClinVar.1
Natural variantiVAR_00757688I → L in AMYL-TTR; amyloid cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121918085EnsemblClinVar.1
Natural variantiVAR_00757789Y → H in AMYL-TTR; leptomeningeal amyloidosis; vitreous amyloid in some patients. 1 PublicationCorresponds to variant dbSNP:rs121918100EnsemblClinVar.1
Natural variantiVAR_00757890K → N in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs267607160EnsemblClinVar.1
Natural variantiVAR_00757991V → A in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918084EnsemblClinVar.1
Natural variantiVAR_00758093I → V in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00758297S → Y in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs121918071EnsemblClinVar.1
Natural variantiVAR_03897998Y → F in AMYL-TTR. 2 PublicationsCorresponds to variant dbSNP:rs958191819Ensembl.1
Natural variantiVAR_007583104I → N in AMYL-TTR; vitrous amyloid. 1 Publication1
Natural variantiVAR_007584104I → S in AMYL-TTR; amyloid polyneuropathy; almost no RBP binding. 3 PublicationsCorresponds to variant dbSNP:rs121918072EnsemblClinVar.1
Natural variantiVAR_038980104I → T in AMYL-TTR. 1 Publication1
Natural variantiVAR_010659109E → K in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_007585109E → Q in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121918082EnsemblClinVar.1
Natural variantiVAR_007587111A → S in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_007588117A → G in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918087EnsemblClinVar.1
Natural variantiVAR_038982117A → S in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs267607161EnsemblClinVar.1
Natural variantiVAR_038984126T → N in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs1456101911Ensembl.1
Natural variantiVAR_038985127I → M in AMYL-TTR. 1 Publication1
Natural variantiVAR_007592127I → V in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918089EnsemblClinVar.1
Natural variantiVAR_007594131L → M in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs121918073EnsemblClinVar.1
Natural variantiVAR_007595134Y → C in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918075EnsemblClinVar.1
Natural variantiVAR_007596136Y → S in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs730881167EnsemblClinVar.1
Natural variantiVAR_038986140A → S in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs876658108EnsemblClinVar.1
Natural variantiVAR_038987142V → A in AMYL-TTR. 1 Publication1
Natural variantiVAR_007600142V → I in AMYL-TTR. 3 PublicationsCorresponds to variant dbSNP:rs76992529EnsemblClinVar.1
Natural variantiVAR_038988144N → S in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs144965179Ensembl.1
Hyperthyroxinemia, dystransthyretinemic (DTTRH)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities.
See also OMIM:145680
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007593129A → T in DTTRH; increased affinity for thyroxine. 2 PublicationsCorresponds to variant dbSNP:rs267607159EnsemblClinVar.1
Carpal tunnel syndrome 1 (CTS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:115430
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007598134Y → H in CTS1; amyloid deposit on carpal tunnel; patients show no other abnormalities. 1 PublicationCorresponds to variant dbSNP:rs121918088EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi107F → M: Loss of tetramerization; when associated with M-130. 1 Publication1
Mutagenesisi130L → M: Loss of tetramerization; when associated with M-107. 1 Publication1

Keywords - Diseasei

Amyloidosis, Disease mutation, Neuropathy

Organism-specific databases

DisGeNET

More...DisGeNETi		7276

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		TTR

MalaCards human disease database

More...MalaCardsi		TTR
MIMi105210 phenotype
115430 phenotype
145680 phenotype

Open Targets

More...OpenTargetsi		ENSG00000118271

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		85451 ATTRV122I amyloidosis
85447 ATTRV30M amyloidosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA37069

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3194

Drug and drug target database

More...DrugBanki		DB07201 (2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid
DB04474 1-Anilino-8-Naphthalene Sulfonate
DB07282 3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid
DB07240 3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid
DB06885 3-[({(1E)-[2-(trifluoromethyl)phenyl]methylidene}amino)oxy]propanoic acid
DB07176 5-aminonaphthalene-1-sulfonic acid
DB00586 Diclofenac
DB00255 Diethylstilbestrol
DB00861 Diflunisal
DB01093 Dimethyl sulfoxide
DB02266 Flufenamic Acid
DB05352 Fx-1006A
DB01645 Genistein
DB00451 Levothyroxine
DB00279 Liothyronine
DB01583 Liotrix
DB05235 NRP409
DB02179 O-Trifluoromethylphenyl Anthranilic Acid
DB03167 Pentabromophenol
DB02709 Resveratrol

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2851

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TTR

Domain mapping of disease mutations (DMDM)

More...DMDMi		136464

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 206 PublicationsAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003575521 – 147TransthyretinAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei624-carboxyglutamate; in a patient with Moyamoya disease1 Publication1
Modified residuei72PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi118N-linked (GlcNAc...) asparagine2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Not glycosylated under normal conditions. Following unfolding, caused for example by variant AMYL-TTR 'Gly-38', the cryptic Asn-118 site is exposed and glycosylated by STT3B-containing OST complex, leading to its degradation by the ER-associated degradation (ERAD) pathway.3 Publications

Keywords - PTMi

Gamma-carboxyglutamic acid, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P02766

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02766

MaxQB - The MaxQuant DataBase

More...MaxQBi		P02766

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P02766

PeptideAtlas

More...PeptideAtlasi		P02766

PRoteomics IDEntifications database

More...PRIDEi		P02766

ProteomicsDB human proteome resource

More...ProteomicsDBi		51586

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P02766

2D gel databases

DOSAC-COBS 2D-PAGE database

More...DOSAC-COBS-2DPAGEi		P02766

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		P02766

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P02766

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P02766

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P02766

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02766

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P02766

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P02766

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000118271 Expressed in 125 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

More...CleanExi		HS_TTR

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P02766 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02766 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB002517
CAB062567
CAB073406
HPA002550

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4.13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113127, 55 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P02766

Database of interacting proteins

More...DIPi		DIP-1083N

Protein interaction database and analysis system

More...IntActi		P02766, 51 interactors

Molecular INTeraction database

More...MINTi		P02766

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000237014

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P02766

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BM7X-ray2.00A/B21-147[»]
1BMZX-ray2.00A/B21-147[»]
1BZ8X-ray2.00A/B21-147[»]
1BZDX-ray1.90A/B21-147[»]
1BZEX-ray1.80A/B21-147[»]
1DVQX-ray2.00A/B21-144[»]
1DVSX-ray2.00A/B21-144[»]
1DVTX-ray1.90A/B21-144[»]
1DVUX-ray1.90A/B21-144[»]
1DVXX-ray2.00A/B21-144[»]
1DVYX-ray1.90A/B21-144[»]
1DVZX-ray1.90A/B21-144[»]
1E3FX-ray1.90A/B21-147[»]
1E4HX-ray1.80A/B21-147[»]
1E5AX-ray1.80A/B21-147[»]
1ETAX-ray1.701/221-147[»]
1ETBX-ray1.701/221-147[»]
1F41X-ray1.30A/B21-147[»]
1F64model-A21-147[»]
1F86X-ray1.10A/B30-144[»]
1FH2X-ray1.80A/B21-147[»]
1FHNX-ray1.75A/B21-147[»]
1G1OX-ray2.30A/B/C/D21-147[»]
1GKOX-ray2.10A/B/C/D21-147[»]
1ICTX-ray3.00A/B/C/D/E/F/G/H21-147[»]
1IIIX-ray2.00A/B21-147[»]
1IIKX-ray2.00A/B21-147[»]
1IJNX-ray1.70A/B21-147[»]
1QABX-ray3.20A/B/C/D21-147[»]
1QWHX-ray1.36A/B31-147[»]
1RLBX-ray3.10A/B/C/D21-147[»]
1SOKX-ray1.60A/B21-147[»]
1SOQX-ray2.10A/B/C/D21-147[»]
1THAX-ray2.00A/B21-147[»]
1THCX-ray2.30A/B21-147[»]
1TLMX-ray1.90A/B21-147[»]
1TSHX-ray1.70A/B21-147[»]
1TT6X-ray1.80A/B21-147[»]
1TTAX-ray1.70A/B21-147[»]
1TTBX-ray1.70A/B21-147[»]
1TTCX-ray1.70A/B21-147[»]
1TTRX-ray1.90A/B21-147[»]
1TYRX-ray1.80A/B21-147[»]
1TZ8X-ray1.85A/B/C/D21-147[»]
1U21X-ray1.69A/B21-147[»]
1X7SX-ray1.55A/B21-147[»]
1X7TX-ray1.60A/B21-147[»]
1Y1DX-ray1.70A/B21-147[»]
1Z7JX-ray2.20A/B21-147[»]
1ZCRX-ray1.80A/B21-147[»]
1ZD6X-ray1.90A/B21-147[»]
2B14X-ray2.00A/B21-147[»]
2B15X-ray1.70A/B21-147[»]
2B16X-ray1.75A/B21-147[»]
2B77X-ray1.70A/B21-147[»]
2B9AX-ray1.54A/B21-147[»]
2F7IX-ray1.60A/B21-147[»]
2F8IX-ray1.54A/B21-147[»]
2FBRX-ray1.46A/B21-147[»]
2FLMX-ray1.65A/B21-147[»]
2G3XX-ray1.58A/B21-147[»]
2G3ZX-ray1.90A/B21-147[»]
2G4EX-ray2.17A/B21-147[»]
2G4GX-ray1.85A/B21-147[»]
2G5UX-ray1.80A/B21-147[»]
2G9KX-ray1.85A/B21-147[»]
2GABX-ray1.85A/B21-147[»]
2H4EX-ray1.45A/B21-147[»]
2M5NNMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P125-135[»]
2NBONMR-A21-147[»]
2NBPNMR-A21-147[»]
2NOYX-ray1.80A/B21-147[»]
2PABX-ray1.80A/B21-147[»]
2QELX-ray2.29A/B/C/D21-147[»]
2QGBX-ray1.40A/B21-147[»]
2QGCX-ray1.30A/B21-147[»]
2QGDX-ray1.50A/B21-147[»]
2QGEX-ray1.45A/B21-147[»]
2ROXX-ray2.00A/B21-147[»]
2ROYX-ray2.20A/B21-147[»]
2TRHX-ray1.90A/B21-147[»]
2TRYX-ray2.00A/B21-147[»]
2WQAX-ray2.85A/B/C/D21-147[»]
3A4DX-ray2.00A/B21-147[»]
3A4EX-ray1.70A/B21-147[»]
3A4FX-ray1.99A/B21-147[»]
3B56X-ray1.55A/B21-147[»]
3BSZX-ray3.38A/B/C/D21-147[»]
3BT0X-ray1.59A/B21-147[»]
3CBRX-ray1.70A/B21-147[»]
3CFMX-ray1.60A/B30-147[»]
3CFNX-ray1.87A/B30-147[»]
3CFQX-ray2.09A/B30-147[»]
3CFTX-ray1.87A/B30-147[»]
3CN0X-ray1.52A/B21-147[»]
3CN1X-ray1.52A/B21-147[»]
3CN2X-ray1.52A/B21-147[»]
3CN3X-ray1.80A/B21-147[»]
3CN4X-ray1.40A/B21-147[»]
3CXFX-ray2.30A/B21-147[»]
3D2TX-ray1.85A/B21-147[»]
3D7PX-ray1.72A/B21-147[»]
3DGDX-ray1.38A/B/C/D21-147[»]
3DIDX-ray1.78A/B/C/D21-147[»]
3DJRX-ray2.02A/B21-147[»]
3DJSX-ray1.80A/B21-147[»]
3DJTX-ray2.30A/B21-147[»]
3DJZX-ray1.82A/B21-147[»]
3DK0X-ray1.87A/B21-147[»]
3DK2X-ray2.35A/B21-147[»]
3DO4X-ray2.40A/B/C/D/E/F/G/H21-147[»]
3ESNX-ray1.35A/B21-147[»]
3ESOX-ray1.31A/B21-147[»]
3ESPX-ray1.31A/B21-147[»]
3FC8X-ray1.85A/B21-144[»]
3FCBX-ray1.80A/B21-144[»]
3GLZX-ray1.78A/B21-147[»]
3GPSX-ray1.78A/B/C/D21-147[»]
3GRBX-ray1.75A/B/C/D21-147[»]
3GRGX-ray1.90A/B/C/D21-147[»]
3GS0X-ray1.85A/B21-147[»]
3GS4X-ray1.78A/B21-147[»]
3GS7X-ray1.80A/B21-147[»]
3HJ0X-ray1.34A/B21-147[»]
3I9AX-ray1.65A/B21-147[»]
3I9IX-ray1.80A/B30-145[»]
3I9PX-ray1.90A/B30-145[»]
3IMRX-ray1.70A/B21-147[»]
3IMSX-ray1.40A/B21-147[»]
3IMTX-ray1.40A/B21-147[»]
3IMUX-ray1.40A/B21-147[»]
3IMVX-ray1.47A/B21-147[»]
3IMWX-ray1.31A/B21-147[»]
3IPBX-ray1.90A/B21-147[»]
3IPEX-ray1.40A/B21-147[»]
3KGSX-ray1.80A/B21-147[»]
3KGTX-ray1.95A/B21-147[»]
3KGUX-ray1.85A/B21-147[»]
3M1OX-ray1.20A/B21-147[»]
3NEEX-ray1.55A/B30-145[»]
3NEOX-ray2.00A/B30-145[»]
3NESX-ray1.75A/B30-145[»]
3NEXX-ray1.70A/B30-145[»]
3NG5X-ray1.70A/B21-147[»]
3OZKX-ray1.90A/B21-147[»]
3OZLX-ray1.90A/B21-147[»]
3P3RX-ray1.25A/B21-147[»]
3P3SX-ray1.60A/B21-147[»]
3P3TX-ray1.45A/B21-147[»]
3P3UX-ray1.50A/B21-147[»]
3SSGX-ray2.00A21-147[»]
3TCTX-ray1.30A/B21-147[»]
3TFBX-ray2.03A/B30-145[»]
3U2IX-ray1.70A/B32-147[»]
3U2Jneutron diffraction2.00A/B32-147[»]
3W3BX-ray1.90A/B21-147[»]
4ABQX-ray1.70A/B21-144[»]
4ABUX-ray1.86A/B21-144[»]
4ABVX-ray1.80A/B21-144[»]
4ABWX-ray1.70A/B21-144[»]
4AC2X-ray1.81A/B21-144[»]
4AC4X-ray1.80A/B21-147[»]
4ACTX-ray1.80A/B21-147[»]
4ANKX-ray1.70A/B1-147[»]
4D7BX-ray1.15A/B21-147[»]
4DERX-ray1.90A/B30-145[»]
4DESX-ray1.75A/B30-145[»]
4DETX-ray2.05A/B30-145[»]
4DEUX-ray1.60A/B30-145[»]
4DEWX-ray1.90A/B1-147[»]
4FI6X-ray1.46A/B21-147[»]
4FI7X-ray1.40A/B21-147[»]
4FI8X-ray1.22A/B21-147[»]
4HIQX-ray1.18A/B21-147[»]
4HISX-ray1.20A/B21-147[»]
4HJSX-ray1.22A/B30-145[»]
4HJTX-ray1.45A/B21-147[»]
4HJUX-ray1.35A/B21-147[»]
4I85X-ray1.67A/B21-147[»]
4I87X-ray1.69A/B21-147[»]
4I89X-ray1.69A/B21-147[»]
4IIZX-ray2.10A/B21-147[»]
4IK6X-ray2.00A/B21-147[»]
4IK7X-ray2.10A/B21-147[»]
4IKIX-ray2.00A/B21-147[»]
4IKJX-ray2.10A/B21-147[»]
4IKKX-ray1.90A/B21-147[»]
4IKLX-ray1.90A/B21-147[»]
4KY2X-ray1.13A/B21-147[»]
4L1SX-ray1.50A/B21-147[»]
4L1TX-ray1.16A/B21-147[»]
4MASX-ray1.22A/B21-147[»]
4MRBX-ray1.27A/B21-147[»]
4MRCX-ray1.54A/B22-147[»]
4N85X-ray1.60A/B1-147[»]
4N86X-ray2.00A/B1-147[»]
4N87X-ray1.79A/B1-147[»]
4PM1X-ray1.23A/B21-147[»]
4PMEX-ray1.26A/B29-146[»]
4PMFX-ray1.35A/B29-145[»]
4PVLX-ray1.85A/B21-147[»]
4PVMOther2.00A/B21-147[»]
4PVNOther2.30A/B21-147[»]
4PWEX-ray1.40A/B1-147[»]
4PWFX-ray1.60A/B1-147[»]
4PWGX-ray1.80A/B1-147[»]
4PWHX-ray1.80A/B1-147[»]
4PWIX-ray1.49A/B1-147[»]
4PWJX-ray1.55A/B1-147[»]
4PWKX-ray1.59A/B1-147[»]
4QRFX-ray1.80A/B1-147[»]
4QXVX-ray1.12A/B21-147[»]
4QYAX-ray1.70A/B21-147[»]
4TKWX-ray1.80A/B29-147[»]
4TL4X-ray1.75A/B29-147[»]
4TL5X-ray1.44A/B29-147[»]
4TLKX-ray1.44A/B29-147[»]
4TLSX-ray1.35A/B29-147[»]
4TLTX-ray1.70A/B29-147[»]
4TLUX-ray1.75A/B29-147[»]
4TM9X-ray1.70A/B29-147[»]
4TNEX-ray1.55A/B29-147[»]
4TNFX-ray1.60A/B29-147[»]
4TNGX-ray1.60A/B29-147[»]
4TQ8X-ray1.52A/B21-147[»]
4TQHX-ray1.51A/B21-147[»]
4TQIX-ray1.25A/B21-147[»]
4TQPX-ray1.58A/B21-147[»]
4WNJX-ray1.40A/B21-147[»]
4WNSX-ray1.40A/B21-147[»]
4WO0X-ray1.34A/B21-147[»]
4Y9BX-ray1.40A/B1-147[»]
4Y9CX-ray1.49A/B1-147[»]
4Y9EX-ray1.49A/B1-147[»]
4Y9FX-ray1.50A/B1-147[»]
4Y9GX-ray1.89A/B1-147[»]
4YDMX-ray1.25A/B21-147[»]
4YDNX-ray1.35A/B21-147[»]
5A6IX-ray1.86A21-147[»]
5AKSX-ray1.25A/B21-147[»]
5AKTX-ray1.35A/B21-147[»]
5AKVX-ray1.52A/B21-147[»]
5AL0X-ray1.39A/B21-147[»]
5AL8X-ray1.50A/B21-147[»]
5AYTX-ray1.40A/B1-147[»]
5BOJX-ray1.75A/B21-147[»]
5CLXX-ray1.28A/B21-147[»]
5CLYX-ray1.23A/B21-147[»]
5CLZX-ray1.22A/B21-147[»]
5CM1X-ray1.22A/B21-147[»]
5CN3X-ray1.30A/B21-147[»]
5CNHX-ray1.42A/B21-147[»]
5CR1X-ray1.54A/B30-145[»]
5DEJX-ray1.37A/B30-145[»]
5DWPX-ray1.20A/B30-145[»]
5E23X-ray1.41A/B21-147[»]
5E4AX-ray1.33A/B10-146[»]
5E4OX-ray1.50A/B30-146[»]
5EN3X-ray1.25A/B21-147[»]
5EZPX-ray2.50A/B/C/D/E/F/G/H26-147[»]
5FO2X-ray1.45A/B21-147[»]
5FW6X-ray1.30A/B21-147[»]
5FW7X-ray1.20A/B21-147[»]
5FW8X-ray1.60A/B21-147[»]
5H0VX-ray1.58A/B/C/D31-147[»]
5H0WX-ray1.90A31-147[»]
5H0XX-ray1.57A/B31-147[»]
5H0YX-ray1.80A31-147[»]
5H0ZX-ray1.74A31-147[»]
5HJGX-ray1.40A/B21-147[»]
5IHHX-ray1.35A/B21-147[»]
5JIDX-ray1.20A/B21-147[»]
5JIMX-ray1.26A/B21-147[»]
5JIQX-ray1.45A/B21-147[»]
5K1JX-ray1.69A/B30-145[»]
5K1NX-ray1.81A/B30-147[»]
5L4FX-ray1.48A/B21-147[»]
5L4IX-ray1.45A/B21-147[»]
5L4JX-ray1.62A/B21-147[»]
5L4MX-ray1.58A/B21-147[»]
5LLLX-ray1.42A/B21-147[»]
5LLVX-ray1.70A/B/C/D21-147[»]
5N5QX-ray2.53A/B30-145[»]
5N62X-ray1.80A/B30-146[»]
5N7CX-ray2.45A/B30-145[»]
5OQ0X-ray1.94A21-147[»]
5TTRX-ray2.70A/B/C/D/E/F/G/H21-147[»]
5TZLX-ray1.40A/B21-147[»]
5U48X-ray1.50A/B21-147[»]
5U49X-ray2.22A21-147[»]
5U4AX-ray1.90A/B21-147[»]
5U4BX-ray1.45A/B21-147[»]
5U4CX-ray1.70A/B21-147[»]
5U4DX-ray1.55A/B21-147[»]
5U4EX-ray1.45A/B21-147[»]
5U4FX-ray1.50A/B21-147[»]
5U4GX-ray1.80A/B21-147[»]
6EP1X-ray1.30A/B30-144[»]
6GR7X-ray1.40A/B21-147[»]
6GRPX-ray1.60A/B21-147[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02766

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P02766

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02766

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni135 – 139Thyroid hormone binding5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Each monomer has two 4-stranded beta sheets and the shape of a prolate ellipsoid. Antiparallel beta-sheet interactions link monomers into dimers. A short loop from each monomer forms the main dimer-dimer interaction. These two pairs of loops separate the opposed, convex beta-sheets of the dimers to form an internal channel.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the transthyretin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3006 Eukaryota
COG2351 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153229

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000251776

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG000285

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02766

KEGG Orthology (KO)

More...KOi		K20731

Database of Orthologous Groups

More...OrthoDBi		720138at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02766

TreeFam database of animal gene trees

More...TreeFami		TF300210

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.180, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR023418 Thyroxine_BS
IPR030178 Transthyretin
IPR000895 Transthyretin/HIU_hydrolase
IPR023416 Transthyretin/HIU_hydrolase_d
IPR036817 Transthyretin/HIU_hydrolase_sf
IPR023419 Transthyretin_CS

The PANTHER Classification System

More...PANTHERi		PTHR10395 PTHR10395, 1 hit
PTHR10395:SF12 PTHR10395:SF12, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00576 Transthyretin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00189 TRNSTHYRETIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00095 TR_THY, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49472 SSF49472, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00768 TRANSTHYRETIN_1, 1 hit
PS00769 TRANSTHYRETIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P02766-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV 
        60         70         80         90        100
HVFRKAADDT WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK 
       110        120        130        140 
ALGISPFHEH AEVVFTANDS GPRRYTIAAL LSPYSYSTTA VVTNPKE
Length:147
Mass (Da):15,887
Last modified:March 20, 1987 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3A6AEBCBBA56BC44
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WT59A0A087WT59_HUMAN
Transthyretin
TTR
185Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WV45A0A087WV45_HUMAN
Transthyretin
TTR
139Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti41R → P in AAA98771 (PubMed:4054629).Curated1
Sequence conflicti147E → D in CAG33189 (Ref. 12) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00754626G → S Common polymorphism. 5 PublicationsCorresponds to variant dbSNP:rs1800458EnsemblClinVar.1
Natural variantiVAR_00754730C → R in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918083EnsemblClinVar.1
Natural variantiVAR_03895932L → P in AMYL-TTR. 2 PublicationsCorresponds to variant dbSNP:rs121918094EnsemblClinVar.1
Natural variantiVAR_03896033M → I1 Publication1
Natural variantiVAR_00754838D → E in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_00754938D → G in AMYL-TTR; leptomeningeal amyloidosis; leads to unfolding and exposure of N-118 to glycosylation by STT3B and subsequent degradation by the ERAD pathway. 2 PublicationsCorresponds to variant dbSNP:rs121918098EnsemblClinVar.1
Natural variantiVAR_00755040V → I in AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome. 2 PublicationsCorresponds to variant dbSNP:rs121918093EnsemblClinVar.1
Natural variantiVAR_03896143S → N in AMYL-TTR. 1 Publication1
Natural variantiVAR_00755144P → S in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs11541790EnsemblClinVar.1
Natural variantiVAR_01065848V → M in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00755250V → A in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs79977247EnsemblClinVar.1
Natural variantiVAR_03896250V → G in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs79977247EnsemblClinVar.1
Natural variantiVAR_00755350V → L in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs28933979EnsemblClinVar.1
Natural variantiVAR_00755450V → M in AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation. 10 PublicationsCorresponds to variant dbSNP:rs28933979EnsemblClinVar.1
Natural variantiVAR_03896353F → C in a patient with amyloidosis. 2 Publications1
Natural variantiVAR_00755553F → I in AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs121918068EnsemblClinVar.1
Natural variantiVAR_00755653F → L in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs121918068EnsemblClinVar.1
Natural variantiVAR_03896453F → V in AMYL-TTR; amyloid polyneuropathy. 4 Publications1
Natural variantiVAR_03896554R → T in AMYL-TTR. 1 Publication1
Natural variantiVAR_03896655K → N in AMYL-TTR; amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00755756A → P in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs121918077EnsemblClinVar.1
Natural variantiVAR_03896758D → A in AMYL-TTR. 2 Publications1
Natural variantiVAR_03896858D → V in AMYL-TTR. 2 Publications1
Natural variantiVAR_03896961W → L in AMYL-TTR. 1 Publication1
Natural variantiVAR_03897062E → D in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs11541796EnsemblClinVar.1
Natural variantiVAR_00755862E → G in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs11541796EnsemblClinVar.1
Natural variantiVAR_03897164F → S in AMYL-TTR. 2 PublicationsCorresponds to variant dbSNP:rs104894665EnsemblClinVar.1
Natural variantiVAR_00755965A → D in AMYL-TTR; amyloid cardiomyopathy. Corresponds to variant dbSNP:rs730881169EnsemblClinVar.1
Natural variantiVAR_03897265A → S in AMYL-TTR. 1 Publication1
Natural variantiVAR_00756065A → T in AMYL-TTR; amyloid cardiomyopathy. 2 PublicationsCorresponds to variant dbSNP:rs121918078Ensembl.1
Natural variantiVAR_00756167G → A in AMYL-TTR; amyloid polyneuropathy. 2 PublicationsCorresponds to variant dbSNP:rs121918090EnsemblClinVar.1
Natural variantiVAR_03897367G → E in AMYL-TTR. 2 Publications1
Natural variantiVAR_00756267G → R in AMYL-TTR; amyloid polyneuropathy. 1 PublicationCorresponds to variant dbSNP:rs387906523EnsemblClinVar.1
Natural variantiVAR_00756367G → V in AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome. 1
Natural variantiVAR_00756469T → A in AMYL-TTR; amyloid polyneuropathy. 3 PublicationsCorresponds to variant dbSNP:rs121918081EnsemblClinVar.1
Natural variantiVAR_03897469T → I in AMYL-TTR. 2 Publications1
Natural variantiVAR_00756570S → I in AMYL-TTR; amyloid cardiomyopathy. 1 PublicationCorresponds to variant dbSNP:rs121918080EnsemblClinVar.1
Natural variantiVAR_00756670S → R in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs386134269EnsemblClinVar.1
Natural variantiVAR_00756772S → P in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_03897573G → E in AMYL-TTR. 1 PublicationCorresponds to variant dbSNP:rs121918097EnsemblClinVar.1
Natural variantiVAR_00756874E → G in AMYL-TTR; amyloid polyneuropathy. 1
Natural variantiVAR_03897674E → K in AMYL-TTR; early-onset amyloid polyneuropathy. 1 Publication1
Natural variantiVAR_00756975L → P in AMYL-TTR; amyloid polyneuropathy. 4 PublicationsCorresponds to variant dbSNP:rs121918079EnsemblClinVar.1
Natural variantiVAR_03897775L → Q in AMYL-TTR. 1 Publication1
Natural variantiVAR_00757078L → H in AMYL-TTR; amyloid polyneuropathy. 1 Publication