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P02766 (TTHY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 182. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transthyretin
Alternative name(s):
ATTR
Prealbumin
TBPA
Gene names
Name:TTR
Synonyms:PALB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain. Ref.29

Subunit structure

Homotetramer. Dimer of dimers. In the homotetramer, subunits assemble around a central channel that can accommodate two ligand molecules. Interacts with RBP4. Ref.42 Ref.45 Ref.46 Ref.51 Ref.54 Ref.55

Subcellular location

Secreted. Cytoplasm Ref.9 Ref.29.

Tissue specificity

Detected in serum and cerebrospinal fluid (at protein level). Highly expressed in choroid plexus epithelial cells. Detected in retina pigment epithelium and liver. Ref.9 Ref.29

Domain

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.

Post-translational modification

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. Ref.33

Involvement in disease

Amyloidosis, transthyretin-related (AMYL-TTR) [MIM:105210]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.33 Ref.36 Ref.37 Ref.40 Ref.46 Ref.47 Ref.51 Ref.53 Ref.56 Ref.66 Ref.67 Ref.69 Ref.70 Ref.71 Ref.73 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.83 Ref.84 Ref.85 Ref.86 Ref.87 Ref.88 Ref.89 Ref.90 Ref.91 Ref.93 Ref.94 Ref.95 Ref.97 Ref.98 Ref.99 Ref.100 Ref.101 Ref.102 Ref.103 Ref.104 Ref.105 Ref.108 Ref.109 Ref.110 Ref.112 Ref.113 Ref.114 Ref.115 Ref.116 Ref.117 Ref.118 Ref.119 Ref.120 Ref.121 Ref.123 Ref.124 Ref.125 Ref.126 Ref.127 Ref.128 Ref.129 Ref.130

Hyperthyroxinemia dystransthyretinemic euthyroidal (HTDE) [MIM:145680]: A condition characterized by elevation of total and free thyroxine in healthy, euthyroid persons without detectable binding protein abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26

Carpal tunnel syndrome 1 (CTS1) [MIM:115430]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.96

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.

Sequence similarities

Belongs to the transthyretin family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Chain21 – 147127Transthyretin
PRO_0000035755

Regions

Region135 – 1395Thyroid hormone binding

Sites

Binding site351Thyroid hormones
Binding site741Thyroid hormones

Amino acid modifications

Modified residue6214-carboxyglutamate; in a patient with Moyamoya disease Ref.32
Glycosylation1181N-linked (GlcNAc...) Ref.31 Ref.33

Natural variations

Natural variant261G → S Common polymorphism. Ref.16 Ref.90 Ref.108 Ref.119 Ref.125
Corresponds to variant rs1800458 [ dbSNP | Ensembl ].
VAR_007546
Natural variant301C → R in AMYL-TTR; amyloid polyneuropathy. Ref.83
VAR_007547
Natural variant321L → P in AMYL-TTR. Ref.112 Ref.128
VAR_038959
Natural variant331M → I. Ref.128
VAR_038960
Natural variant381D → E in AMYL-TTR; amyloid polyneuropathy.
VAR_007548
Natural variant381D → 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. Ref.33 Ref.99
VAR_007549
Natural variant401V → I in AMYL-TTR; late-onset amyloid polyneuropathy with carpal tunnel syndrome. Ref.101 Ref.128
VAR_007550
Natural variant431S → N in AMYL-TTR. Ref.109
VAR_038961
Natural variant441P → S in AMYL-TTR; amyloid polyneuropathy. Ref.128
Corresponds to variant rs11541790 [ dbSNP | Ensembl ].
VAR_007551
Natural variant481V → M in AMYL-TTR; amyloid polyneuropathy. Ref.116
VAR_010658
Natural variant501V → A in AMYL-TTR; amyloid polyneuropathy. Ref.80 Ref.128
VAR_007552
Natural variant501V → G in AMYL-TTR. Ref.100
VAR_038962
Natural variant501V → L in AMYL-TTR; amyloid polyneuropathy. Ref.78 Ref.110
VAR_007553
Natural variant501V → M in AMYL-TTR; amyloid polyneuropathy; by far the most frequent mutation. Ref.5 Ref.6 Ref.17 Ref.18 Ref.20 Ref.36 Ref.37 Ref.46 Ref.97 Ref.120 Ref.128
Corresponds to variant rs28933979 [ dbSNP | Ensembl ].
VAR_007554
Natural variant531F → C in a patient with amyloidosis. Ref.122 Ref.125
VAR_038963
Natural variant531F → I in AMYL-TTR; Jewish 'SKO' amyloid polyneuropathy. Ref.66 Ref.90
VAR_007555
Natural variant531F → L in AMYL-TTR; amyloid polyneuropathy. Ref.22 Ref.75 Ref.120 Ref.128
VAR_007556
Natural variant531F → V in AMYL-TTR; amyloid polyneuropathy. Ref.110 Ref.120 Ref.124 Ref.128
VAR_038964
Natural variant541R → T in AMYL-TTR. Ref.102
VAR_038965
Natural variant551K → N in AMYL-TTR; amyloid polyneuropathy. Ref.97
VAR_038966
Natural variant561A → P in AMYL-TTR; amyloid polyneuropathy. Ref.128
VAR_007557
Natural variant581D → A in AMYL-TTR. Ref.110 Ref.119
VAR_038967
Natural variant581D → V in AMYL-TTR. Ref.120 Ref.129
VAR_038968
Natural variant611W → L in AMYL-TTR. Ref.119
VAR_038969
Natural variant621E → D in AMYL-TTR. Ref.103
Corresponds to variant rs11541796 [ dbSNP | Ensembl ].
VAR_038970
Natural variant621E → G in AMYL-TTR; amyloid polyneuropathy. Ref.23 Ref.71
Corresponds to variant rs11541796 [ dbSNP | Ensembl ].
VAR_007558
Natural variant641F → S in AMYL-TTR. Ref.107 Ref.119
VAR_038971
Natural variant651A → D in AMYL-TTR; amyloid cardiomyopathy.
VAR_007559
Natural variant651A → S in AMYL-TTR. Ref.115
VAR_038972
Natural variant651A → T in AMYL-TTR; amyloid cardiomyopathy. Ref.76 Ref.128
VAR_007560
Natural variant671G → A in AMYL-TTR; amyloid polyneuropathy. Ref.89 Ref.128
VAR_007561
Natural variant671G → E in AMYL-TTR. Ref.120 Ref.125
VAR_038973
Natural variant671G → R in AMYL-TTR; amyloid polyneuropathy. Ref.77
VAR_007562
Natural variant671G → V in AMYL-TTR; amyloid polyneuropathy with carpal tunnel syndrome.
VAR_007563
Natural variant691T → A in AMYL-TTR; amyloid polyneuropathy. Ref.82 Ref.97 Ref.128
VAR_007564
Natural variant691T → I in AMYL-TTR. Ref.113 Ref.128
VAR_038974
Natural variant701S → I in AMYL-TTR; amyloid cardiomyopathy. Ref.79
VAR_007565
Natural variant701S → R in AMYL-TTR; amyloid polyneuropathy. Ref.71 Ref.97 Ref.110 Ref.130
VAR_007566
Natural variant721S → P in AMYL-TTR; amyloid polyneuropathy.
VAR_007567
Natural variant731G → E in AMYL-TTR. Ref.117
VAR_038975
Natural variant741E → G in AMYL-TTR; amyloid polyneuropathy.
VAR_007568
Natural variant741E → K in AMYL-TTR; early-onset amyloid polyneuropathy. Ref.123
VAR_038976
Natural variant751L → P in AMYL-TTR; amyloid polyneuropathy. Ref.40 Ref.56 Ref.81 Ref.95
VAR_007569
Natural variant751L → Q in AMYL-TTR. Ref.118
VAR_038977
Natural variant781L → H in AMYL-TTR; amyloid polyneuropathy. Ref.125
VAR_007570
Natural variant781L → R in AMYL-TTR; amyloid polyneuropathy. Ref.73
VAR_007571
Natural variant791T → K in AMYL-TTR; amyloid cardiomyopathy. Ref.98
VAR_007572
Natural variant801T → A in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. Ref.97 Ref.120 Ref.125 Ref.128
VAR_007573
Natural variant811E → G in AMYL-TTR. Ref.126
VAR_038978
Natural variant811E → K in AMYL-TTR; amyloid polyneuropathy. Ref.85
VAR_007574
Natural variant841F → L in AMYL-TTR; amyloid polyneuropathy. Ref.75 Ref.119 Ref.128
VAR_007575
Natural variant881I → L in AMYL-TTR; amyloid cardiomyopathy. Ref.86 Ref.128
VAR_007576
Natural variant891Y → H in AMYL-TTR; leptomeningeal amyloidosis; vitreous amyloid in some patients. Ref.121
VAR_007577
Natural variant901K → N in AMYL-TTR; amyloid polyneuropathy. Ref.84
VAR_007578
Natural variant911V → A in AMYL-TTR; amyloid polyneuropathy. Ref.87 Ref.88 Ref.128
VAR_007579
Natural variant931I → V in AMYL-TTR; amyloid polyneuropathy. Ref.105
VAR_007580
Natural variant941D → H.
VAR_007581
Natural variant971S → Y in AMYL-TTR; amyloid polyneuropathy. Ref.69 Ref.97 Ref.125 Ref.128
VAR_007582
Natural variant981Y → F in AMYL-TTR. Ref.51 Ref.56 Ref.128
VAR_038979
Natural variant1041I → N in AMYL-TTR; vitrous amyloid. Ref.128
VAR_007583
Natural variant1041I → S in AMYL-TTR; amyloid polyneuropathy; almost no RBP binding. Ref.67 Ref.92 Ref.128
VAR_007584
Natural variant1041I → T in AMYL-TTR. Ref.128
VAR_038980
Natural variant1091E → K in AMYL-TTR; amyloid polyneuropathy. Ref.114
VAR_010659
Natural variant1091E → Q in AMYL-TTR; amyloid polyneuropathy and cardiomyopathy. Ref.82 Ref.97
VAR_007585
Natural variant1101H → N. Ref.23 Ref.74
VAR_007586
Natural variant1111A → S in AMYL-TTR; amyloid polyneuropathy. Ref.104
VAR_007587
Natural variant1141V → A in a patient with amyloidosis. Ref.125 Ref.128
VAR_038981
Natural variant1171A → G in AMYL-TTR; amyloid polyneuropathy. Ref.94 Ref.110 Ref.128
VAR_007588
Natural variant1171A → S in AMYL-TTR. Ref.110
VAR_038982
Natural variant1211G → S. Ref.106 Ref.128
VAR_007589
Natural variant1221P → R.
VAR_007590
Natural variant1241R → C.
VAR_007591
Natural variant1241R → H. Ref.51 Ref.111
Corresponds to variant rs121918095 [ dbSNP | Ensembl ].
VAR_038983
Natural variant1261T → N in AMYL-TTR. Ref.128
VAR_038984
Natural variant1271I → M in AMYL-TTR. Ref.128
VAR_038985
Natural variant1271I → V in AMYL-TTR; amyloid polyneuropathy. Ref.91 Ref.93 Ref.128
VAR_007592
Natural variant1291A → T in HTDE; increased affinity for thyroxine. Ref.26 Ref.128
VAR_007593
Natural variant1311L → M in AMYL-TTR. Ref.128
VAR_007594
Natural variant1341Y → C in AMYL-TTR; amyloid polyneuropathy. Ref.47 Ref.53 Ref.70
VAR_007595
Natural variant1341Y → H in CTS1; amyloid deposit on carpal tunnel; patients show no other abnormalities. Ref.96
VAR_007598
Natural variant1361Y → S in AMYL-TTR; amyloid polyneuropathy. Ref.104
VAR_007596
Natural variant1361Y → V Requires 2 nucleotide substitutions. Ref.68
VAR_007597
Natural variant1391T → M in Chicago variant. Ref.46 Ref.72 Ref.119 Ref.128
Corresponds to variant rs28933981 [ dbSNP | Ensembl ].
VAR_007599
Natural variant1401A → S in AMYL-TTR. Ref.120
VAR_038986
Natural variant1421V → A in AMYL-TTR. Ref.108
VAR_038987
Natural variant1421V → I in AMYL-TTR. Ref.19 Ref.120 Ref.128
Corresponds to variant rs28933980 [ dbSNP | Ensembl ].
VAR_007600
Natural variant1441N → S in AMYL-TTR. Ref.127
VAR_038988

Experimental info

Mutagenesis1071F → M: Loss of tetramerization; when associated with M-130. Ref.45
Mutagenesis1301L → M: Loss of tetramerization; when associated with M-107. Ref.45
Sequence conflict411R → P in AAA98771. Ref.3
Sequence conflict1471E → D in CAG33189. Ref.12

Secondary structure

............................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02766 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: 3A6AEBCBBA56BC44

FASTA14715,887
        10         20         30         40         50         60 
MASHRLLLLC LAGLVFVSEA GPTGTGESKC PLMVKVLDAV RGSPAINVAV HVFRKAADDT 

        70         80         90        100        110        120 
WEPFASGKTS ESGELHGLTT EEEFVEGIYK VEIDTKSYWK ALGISPFHEH AEVVFTANDS 

       130        140 
GPRRYTIAAL LSPYSYSTTA VVTNPKE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of cDNA for human prealbumin."
Mita S., Maeda S., Shimada K., Araki S.
Biochem. Biophys. Res. Commun. 124:558-564(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Localization of the human prealbumin gene to chromosome 18."
Wallace M.R., Naylor S.L., Kluve-Beckerman B., Long G.L., McDonald L., Shows T.B., Benson M.D.
Biochem. Biophys. Res. Commun. 129:753-758(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the chromosomal gene for human serum prealbumin."
Sasaki H., Yoshioka N., Takagi Y., Sakaki Y.
Gene 37:191-197(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structure of the human prealbumin gene."
Tsuzuki T., Mita S., Maeda S., Araki S., Shimada K.
J. Biol. Chem. 260:12224-12227(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Analyses of prealbumin mRNAs in individuals with familial amyloidotic polyneuropathy."
Mita S., Maeda S., Shimada K., Araki S.
J. Biochem. 100:1215-1222(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AMYL-TTR MET-50.
[6]"Structure and expression of the mutant prealbumin gene associated with familial amyloidotic polyneuropathy."
Maeda S., Mita S., Araki S., Shimada K.
Mol. Biol. Med. 3:329-338(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMYL-TTR MET-50.
Tissue: Liver.
[7]"The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis."
Christmanson L., Betsholtz C., Gustavsson A., Johansson B., Sletten K., Westermark P.
FEBS Lett. 281:177-180(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-28.
Tissue: Liver.
[8]"Transthyretin (prealbumin) gene in human primary hepatic cancer."
Gu J.R., Jiang H.Q., He L.P., Li D.Z., Zhou X.M., Dai W.L., Qian L.F., Chen Y.Q., Schweinfest C., Papas T.
Sci. China, Ser. B, Chem. Life Sci. Earth Sci. 34:1312-1318(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[9]"Transthyretin localization in cultured and native human retinal pigment epithelium."
Getz R.K., Kennedy B.G., Mangini N.J.
Exp. Eye Res. 68:629-636(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Retina.
[10]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Corpus callosum.
[11]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[12]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[13]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[15]"The amino acid sequence of human plasma prealbumin."
Kanda Y., Goodman D.S., Canfield R.E., Morgan F.J.
J. Biol. Chem. 249:6796-6805(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-147.
[16]"Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin."
Pras M., Prelli F., Franklin E.C., Frangione B.
Proc. Natl. Acad. Sci. U.S.A. 80:539-542(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 21-147, VARIANT SER-26.
[17]"Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type)."
Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S.
Biochem. Biophys. Res. Commun. 116:880-888(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[18]"Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin."
Dwulet F.E., Benson M.D.
Proc. Natl. Acad. Sci. U.S.A. 81:694-698(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[19]"Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin."
Cornwell G.G. III, Sletten K., Johansson B., Westermark P.
Biochem. Biophys. Res. Commun. 154:648-653(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR ILE-142.
[20]"Characterization of a transthyretin-related amyloid fibril protein from cerebral amyloid angiopathy in type I familial amyloid polyneuropathy."
Kametani F., Ikeda S., Yanagisawa N., Ishi T., Hanyu N.
J. Neurol. Sci. 108:178-183(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL-TTR MET-50.
[21]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-41.
Tissue: Platelet.
[22]"A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy."
Harding J., Skare J., Skinner M.
Biochim. Biophys. Acta 1097:183-186(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR LEU-53.
[23]"Two transthyretin mutations (Glu42Gly, His90Asn) in an Italian family with amyloidosis."
Skare J.C., Jones L.A., Myles N., Kane K., Milunsky A., Cohen A.S., Skinner M.
Clin. Genet. 45:281-284(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL-TTR GLY-62, VARIANT ASN-110.
[24]"Demonstration of transthyretin mRNA in the brain and other extrahepatic tissues in the rat."
Soprano D.R., Herbert J., Soprano K.J., Schon E.A., Goodman D.S.
J. Biol. Chem. 260:11793-11798(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
[25]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 42-68; 101-123 AND 125-146, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[26]"A point mutation in transthyretin increases affinity for thyroxine and produces euthyroid hyperthyroxinemia."
Moses A.C., Rosen H.N., Moller D.E., Tsuzaki S., Haddow J.E., Lawlor J., Liepnieks J.J., Nichols W.C., Benson M.D.
J. Clin. Invest. 86:2025-2033(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, VARIANT HTDE THR-129.
[27]"Amyloid fibril composition and transthyretin gene structure in senile systemic amyloidosis."
Gustavsson A., Jahr H., Tobiassen R., Jacobson D.R., Sletten K., Westermark P.
Lab. Invest. 73:703-708(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[28]"Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?"
Blake C.C.F., Oatley S.J.
Nature 268:115-120(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING SITES FOR THYROID HORMONES.
[29]"Transthyretin: a choroid plexus-specific transport protein in human brain. The 1986 S. Weir Mitchell award."
Herbert J., Wilcox J.N., Pham K.T., Fremeau R.T. Jr., Zeviani M., Dwork A., Soprano D.R., Makover A., Goodman D.S., Zimmerman E.A., Roberts J.L., Schon E.A.
Neurology 36:900-911(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[30]"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
Tissue: Plasma.
[31]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
Tissue: Plasma.
[32]"Detection of a gamma-carboxy-glutamate as novel post-translational modification of human transthyretin."
Rueggeberg S., Horn P., Li X., Vajkoczy P., Franz T.
Protein Pept. Lett. 15:43-46(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GAMMA-CARBOXYGLUTAMATION AT GLU-62, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cerebrospinal fluid.
[33]"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms."
Ruiz-Canada C., Kelleher D.J., Gilmore R.
Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-118, CHARACTERIZATION OF VARIANT AMYL-TTR GLY-38.
[34]"Structure of human plasma prealbumin at 2.5-A resolution. A preliminary report on the polypeptide chain conformation, quaternary structure and thyroxine binding."
Blake C.C.F., Geisow M.J., Swan I.D.A., Rerat C., Rerat B.
J. Mol. Biol. 88:1-12(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[35]"Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A."
Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C.
J. Mol. Biol. 121:339-356(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[36]"Structure of Met30 variant of transthyretin and its amyloidogenic implications."
Terry C.J., Damas A.M., Oliveira P., Saraiva M.J.M., Alves I.L., Costa P.P., Matias P.M., Sakaki Y., Blake C.C.F.
EMBO J. 12:735-741(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
[37]"The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution."
Hamilton J.A., Steinrauf L.K., Braden B.C., Liepnieks J., Benson M.D., Holmgren G., Sandgren O., Steen L.
J. Biol. Chem. 268:2416-2424(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT AMYL-TTR MET-50.
[38]"Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein."
Monaco H.L., Rizzi M., Coda A.
Science 268:1039-1041(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
[39]"Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation."
Schormann N., Murrell J.R., Benson M.D.
Amyloid 5:175-187(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
[40]"The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils."
Sebastiao M.P., Saraiva M.J., Damas A.M.
J. Biol. Chem. 273:24715-24722(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PRO-75.
[41]"Inhibiting transthyretin conformational changes that lead to amyloid fibril formation."
Peterson S.A., Klabunde T., Lashuel H.A., Purkey H., Sacchettini J.C., Kelly J.W.
Proc. Natl. Acad. Sci. U.S.A. 95:12956-12960(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[42]"The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP."
Naylor H.M., Newcomer M.E.
Biochemistry 38:2647-2653(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP4, SUBUNIT.
[43]"A comparative analysis of 23 structures of the amyloidogenic protein transthyretin."
Hoernberg A., Eneqvist T., Olofsson A., Lundgren E., Sauer-Eriksson A.E.
J. Mol. Biol. 302:649-669(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147.
[44]"Rational design of potent human transthyretin amyloid disease inhibitors."
Klabunde T., Petrassi H.M., Oza V.B., Raman P., Kelly J.W., Sacchettini J.C.
Nat. Struct. Biol. 7:312-321(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[45]"An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured."
Jiang X., Smith C.S., Petrassi H.M., Hammarstroem P., White J.T., Sacchettini J.C., Kelly J.W.
Biochemistry 40:11442-11452(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-147, MUTAGENESIS OF PHE-107 AND LEU-130, IDENTIFICATION BY MASS SPECTROMETRY, FORMATION OF AMYLOID FIBERS AT ACIDIC PH, SUBUNIT.
[46]"Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution."
Sebastiao M.P., Lamzin V., Saraiva M.J., Damas A.M.
J. Mol. Biol. 306:733-744(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 30-144 OF VARIANT AMYL-TTR MET-50 AND VARIANT CHICAGO MET-139 IN COMPLEX WITH L-THYROXINE, SUBUNIT.
[47]"Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro."
Eneqvist T., Olofsson A., Ando Y., Miyakawa T., Katsuragi S., Jass J., Lundgren E., Sauer-Eriksson A.E.
Biochemistry 41:13143-13151(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134.
[48]"Benzoxazoles as transthyretin amyloid fibril inhibitors: synthesis, evaluation, and mechanism of action."
Razavi H., Palaninathan S.K., Powers E.T., Wiseman R.L., Purkey H.E., Mohamedmohaideen N.N., Deechongkit S., Chiang K.P., Dendle M.T.A., Sacchettini J.C., Kelly J.W.
Angew. Chem. Int. Ed. 42:2758-2761(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147IN COMPLEX WITH AMYLOIDOGENESIS INHIBITORS.
[49]"Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization."
Green N.S., Palaninathan S.K., Sacchettini J.C., Kelly J.W.
J. Am. Chem. Soc. 125:13404-13414(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 21-147 IN COMPLEX WITH AMYLOIDOGENESIS INHIBITORS, FIBRIL FORMATION.
[50]"Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis."
Adamski-Werner S.L., Palaninathan S.K., Sacchettini J.C., Kelly J.W.
J. Med. Chem. 47:355-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 21-147 IN COMPLEX WITH DIFLUNISAL ANALOGS, INHIBITION OF AMYLOID FORMATION.
[51]"X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis."
Neto-Silva R.M., Macedo-Ribeiro S., Pereira P.J.B., Coll M., Saraiva M.J., Damas A.M.
Acta Crystallogr. D 61:333-339(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PHE-98 AND VARIANT HIS-124, SUBUNIT.
[52]"The effect of iodide and chloride on transthyretin structure and stability."
Hoernberg A., Hultdin U.W., Olofsson A., Sauer-Eriksson A.E.
Biochemistry 44:9290-9299(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147 IN COMPLEXES WITH CHLORIDE AND IODIDE IONS.
[53]"Cys114-linked dimers of transthyretin are compatible with amyloid formation."
Karlsson A., Olofsson A., Eneqvist T., Sauer-Eriksson A.E.
Biochemistry 44:13063-13070(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134.
[54]"Kinetic stabilization of an oligomeric protein by a single ligand binding event."
Wiseman R.L., Johnson S.M., Kelker M.S., Foss T., Wilson I.A., Kelly J.W.
J. Am. Chem. Soc. 127:5540-5551(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-147 IN COMPLEX WITH THYROID HORMONE ANALOG, SUBUNIT.
[55]"Kinetic stabilization of the native state by protein engineering: implications for inhibition of transthyretin amyloidogenesis."
Foss T.R., Kelker M.S., Wiseman R.L., Wilson I.A., Kelly J.W.
J. Mol. Biol. 347:841-854(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 31-147, SUBUNIT.
[56]"The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin."
Morais-de-Sa E., Neto-Silva R.M., Pereira P.J.B., Saraiva M.J., Damas A.M.
Acta Crystallogr. D 62:512-519(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND VARIANTS AMYL-TTR PRO-75 AND PHE-98.
[57]"Structural basis for the protective role of sulfite against transthyretin amyloid formation."
Gales L., Saraiva M.J., Damas A.M.
Biochim. Biophys. Acta 1774:59-64(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-147.
[58]"Acidic pH-induced conformational changes in amyloidogenic mutant transthyretin."
Pasquato N., Berni R., Folli C., Alfieri B., Cendron L., Zanotti G.
J. Mol. Biol. 366:711-719(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-147.
[59]"Iodination of salicylic acid improves its binding to transthyretin."
Gales L., Almeida M.R., Arsequell G., Valencia G., Saraiva M.J., Damas A.M.
Biochim. Biophys. Acta 1784:512-517(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 IN COMPLEX WITH 3,5-DIIODOSALICYLIC ACID, THYROXINE BINDING.
[60]"Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein."
Zanotti G., Folli C., Cendron L., Alfieri B., Nishida S.K., Gliubich F., Pasquato N., Negro A., Berni R.
FEBS J. 275:5841-5854(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.38 ANGSTROMS) OF 21-147 IN COMPLEX WITH RBP4.
[61]"Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors."
Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.
J. Med. Chem. 51:260-270(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 21-147 IN COMPLEX WITH 2-ARYLBENZOXAZOLE-BASED TRANSTHYRETIN AMYLOIDOGENESIS INHIBITORS.
[62]"Toward optimization of the linker substructure common to transthyretin amyloidogenesis inhibitors using biochemical and structural studies."
Johnson S.M., Connelly S., Wilson I.A., Kelly J.W.
J. Med. Chem. 51:6348-6358(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 21-147 IN COMPLEX WITH BISARYL AMYLOIDOGENESIS INHIBITORS.
[63]"Structural insight into pH-induced conformational changes within the native human transthyretin tetramer."
Palaninathan S.K., Mohamedmohaideen N.N., Snee W.C., Kelly J.W., Sacchettini J.C.
J. Mol. Biol. 382:1157-1167(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 21-147 AT PH 3.5 AND 4.5.
[64]"Crystal structure of the F87M/L110M mutant of human transthyretin at pH 4.6 soaked."
Mycobacterium tuberculosis structural genomics consortium (TB)
Submitted (JUL-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 21-147.
[65]"Transthyretin mutations in health and disease."
Saraiva M.J.M.
Hum. Mutat. 5:191-196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[66]"Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin."
Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S.
Biochem. Biophys. Res. Commun. 123:921-928(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ILE-53.
[67]"Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis."
Wallace M.R., Dwulet F.E., Conneally P.M., Benson M.D.
J. Clin. Invest. 78:6-12(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR SER-104.
[68]"Identification and characterization of a human transthyretin variant."
Strahler J.R., Rosenblum B.B., Hanash S.M.
Biochem. Biophys. Res. Commun. 148:471-477(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-136.
[69]"Identification of a new hereditary amyloidosis prealbumin variant, Tyr-77, and detection of the gene by DNA analysis."
Wallace M.R., Dwulet F.E., Williams E.C., Conneally P.M., Benson M.D.
J. Clin. Invest. 81:189-193(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR TYR-97.
[70]"A novel variant of transthyretin (Tyr114 to Cys) deduced from the nucleotide sequences of gene fragments from familial amyloidotic polyneuropathy in Japanese sibling cases."
Ueno S., Uemichi T., Yorifuji S., Tarui S.
Biochem. Biophys. Res. Commun. 169:143-147(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR CYS-134.
[71]"Two novel variants of transthyretin identified in Japanese cases with familial amyloidotic polyneuropathy: transthyretin (Glu42 to Gly) and transthyretin (Ser50 to Arg)."
Ueno S., Uemichi T., Takahashi N., Soga F., Yorifuji S., Tarui S.
Biochem. Biophys. Res. Commun. 169:1117-1121(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR GLY-62 AND ARG-70.
[72]"Biochemical and clinical characterization of prealbuminCHICAGO: an apparently benign variant of serum prealbumin (transthyretin) discovered with high-resolution two-dimensional electrophoresis."
Harrison H.H., Gordon E.D., Nichols W.C., Benson M.D.
Am. J. Med. Genet. 39:442-452(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CHICAGO MET-139.
[73]"New mutant gene (transthyretin Arg 58) in cases with hereditary polyneuropathy detected by non-isotope method of single-strand conformation polymorphism analysis."
Saeki Y., Ueno S., Yorifuji S., Sugiyama Y., Ide Y., Matsuzawa Y.
Biochem. Biophys. Res. Commun. 180:380-385(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ARG-78.
[74]"A new transthyretin variant from a patient with familial amyloidotic polyneuropathy has asparagine substituted for histidine at position 90."
Skare J.C., Milunsky J.M., Milunsky A., Skare I.B., Cohen A.S., Skinner M.
Clin. Genet. 39:6-12(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-110.
[75]"Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two novel point mutations."
Li S., Minnerath S., Li K., Dyck P.J., Sommer S.S.
Neurology 41:893-898(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR LEU-53 AND LEU-84.
[76]"A new transthyretin mutation associated with amyloid cardiomyopathy."
Saraiva M.J.M., Almeida M.R., Sherman W., Gawinowicz M., Costa P., Costa P.P., Goodman D.S.
Am. J. Hum. Genet. 50:1027-1030(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR THR-65.
[77]"A novel transthyretin mutation associated with familial amyloidotic polyneuropathy."
Murakami T., Maeda S., Yi S., Ikegawa S., Kawashima E., Onodera S., Shimada K., Araki S.
Biochem. Biophys. Res. Commun. 182:520-526(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ARG-67.
[78]"A novel transthyretin mutation at position 30 (Leu for Val) associated with familial amyloidotic polyneuropathy."
Murakami T., Atsumi T., Maeda S., Tanase S., Ishikawa K., Mita S., Kumamoto T., Araki S., Ando M.
Biochem. Biophys. Res. Commun. 187:397-403(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LEU-50.
[79]"Novel variant transthyretin gene (Ser50 to Ile) in familial cardiac amyloidosis."
Nishi H., Kimura A., Harada H., Hayashi Y., Nakamura M., Sasazuki T.
Biochem. Biophys. Res. Commun. 187:460-466(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ILE-70.
[80]"Familial amyloidotic polyneuropathy: a new transthyretin position 30 mutation (alanine for valine) in a family of German descent."
Jones L.A., Skare J.C., Cohen A.S., Harding J.A., Milunsky A., Skinner M.
Clin. Genet. 41:70-73(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ALA-50.
[81]"Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement."
Jacobson D.R., McFarlin D.E., Kane I., Buxbaum J.N.
Hum. Genet. 89:353-356(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR PRO-75.
[82]"Two transthyretin variants (TTR Ala-49 and TTR Gln-89) in two Sicilian kindreds with hereditary amyloidosis."
Almeida M.R., Ferlini A., Forabosco A., Gawinowicz M.A., Costa P.P., Salvi F., Plasmati R., Tassinari C.A., Altland K., Saraiva M.J.
Hum. Mutat. 1:211-215(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR ALA-69 AND GLN-109.
[83]"A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy."
Uemichi T., Murrel J.R., Zeldenrust S., Benson M.D.
J. Med. Genet. 29:888-891(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ARG-30.
[84]"Familial amyloidotic polyneuropathy presenting with carpal tunnel syndrome and a new transthyretin mutation, asparagine 70."
Izumoto S., Younger D., Hays A.P., Martone R.L., Smith R.T., Herbert J.
Neurology 42:2094-2102(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ASN-90.
[85]"A basic transthyretin variant (Glu61-->Lys) causes familial amyloidotic polyneuropathy: protein and DNA sequencing and PCR-induced mutation restriction analysis."
Shiomi K., Nakazato M., Matsukura S., Ohnishi A., Hatanaka H., Tsuji S., Murai Y., Kojima M., Kangawa K., Matsuo H.
Biochem. Biophys. Res. Commun. 194:1090-1096(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LYS-81.
[86]"Cardiac amyloidosis: a review and report of a new transthyretin (prealbumin) variant."
Hesse A., Altland K., Linke R.P., Almeida M.R., Saraiva M.J.M., Steinmetz A., Maisch B.
Br. Heart J. 70:111-115(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LEU-88.
[87]"Transthyretin Ala-71: a new transthyretin variant in a Spanish family with familial amyloidotic polyneuropathy."
Almeida M.R., Lopez-Andreu F., Munar-Ques M., Costa P.P., Saraiva M.J.
Hum. Mutat. 2:420-421(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ALA-91.
[88]"A transthyretin variant (alanine 71) associated with familial amyloidotic polyneuropathy in a French family."
Benson M.D. II, Turpin J.C., Lucotte G., Zeldenrust S., Lechevalier B., Benson M.D.
J. Med. Genet. 30:120-122(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ALA-91.
[89]"Gly47Ala: a new transthyretin gene mutation in hereditary amyloidosis TTR-related."
Ferlini A., Salvi F., Patrosso C., Fini S., Vezzoni P., Forbasco A.
J. Rheumatol. 20:187-187(1993)
Cited for: VARIANT AMYL-TTR ALA-67.
[90]"A double-variant transthyretin allele (Ser 6, Ile 33) in the Israeli patient 'SKO' with familial amyloidotic polyneuropathy."
Jacobson D.R., Buxbaum J.N.
Hum. Mutat. 3:254-260(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-26, VARIANT AMYL-TTR ILE-53.
[91]"Transthyretin VAL107, a new variant associated with familial cardiac and neuropathic amyloidosis."
Jacobson D., Gertz M.A., Buxbaum J.N.
Hum. Mutat. 3:399-401(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR VAL-127.
[92]"The Ile-84-->Ser amino acid substitution in transthyretin interferes with the interaction with plasma retinol-binding protein."
Berni R., Malpeli G., Folli C., Murrell J.R., Liepnieks J.J., Benson M.D.
J. Biol. Chem. 269:23395-23398(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-104, RBP BINDING STUDIES.
[93]"Amyloid polyneuropathy in two German-American families: a new transthyretin variant (Val 107)."
Uemichi T., Gertz M.A., Benson M.D.
J. Med. Genet. 31:416-417(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR VAL-127.
[94]"Familial amyloidotic polyneuropathy with late-onset and well-preserved autonomic function: a Japanese kindred with novel mutant transthyretin (Ala97 to Gly)."
Yasuda T., Sobue G., Doyu M., Nakazato M., Shiomi K., Yanagi T., Mitsuma T.
J. Neurol. Sci. 121:97-102(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLY-117.
[95]"Familial amyloid polyneuropathy in Taiwan: identification of transthyretin variant (Leu55-->Pro)."
Yamamoto K., Hsu S.P., Yoshida K., Ikeda S., Nakazato M., Shiomi K., Cheng S.Y., Furihata K., Ueno I., Yanagisawa N.
Muscle Nerve 17:637-641(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR PRO-75.
[96]"Familial carpal tunnel syndrome due to amyloidogenic transthyretin His 114 variant."
Murakami T., Tachibana S., Endo Y., Kawai R., Hara M., Tanase S., Ando M.
Neurology 44:315-318(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CTS1 HIS-134.
[97]"Transthyretin gene analysis in European patients with suspected familial amyloid polyneuropathy."
Reilly M.M., Adams D., Booth D.R., Davis M.B., Said G., Laubriat-Bianchin M., Pepys M.B., Thomas P.K., Harding A.E.
Brain 118:849-856(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND GLN-109.
[98]"A novel variant of transthyretin, 59Thr-->Lys, associated with autosomal dominant cardiac amyloidosis in an Italian family."
Booth D.R., Tan S.Y., Hawkins P.N., Pepys M.B., Frustaci A.
Circulation 91:962-967(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LYS-79.
[99]"Meningocerebrovascular amyloidosis associated with a novel transthyretin mis-sense mutation at codon 18 (TTRD 18G)."
Vidal R., Garzuly F., Budka H., Lalowski M., Linke R.P., Brittig F., Frangione B., Wisniewski T.
Am. J. Pathol. 148:361-366(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLY-38.
[100]"Transthyretin amyloidosis: a new mutation associated with dementia."
Petersen R.B., Goren H., Cohen M., Richardson S.L., Tresser N., Lynn A., Gali M., Estes M., Gambetti P.
Ann. Neurol. 41:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLY-50.
[101]"Transthyretin ILE20, a new variant associated with late-onset cardiac amyloidosis."
Jacobson D.R., Pan T., Kyle R.A., Buxbaum J.N.
Hum. Mutat. 9:83-85(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ILE-40.
[102]"Novel transthyretin missense mutation (Thr34) in an Italian family with hereditary amyloidosis."
Patrosso M.C., Salvi F., De Grandis D., Vezzoni P., Jacobson D.R., Ferlini A.
Am. J. Med. Genet. 77:135-138(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR THR-54.
[103]"A novel variant of transthyretin (Glu42Asp) associated with sporadic late-onset cardiac amyloidosis."
Dupuy O., Bletry O., Blanc A.S., Droz D., Viemont M., Delpech M., Grateau G.
Amyloid 5:285-287(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ASP-62.
[104]"New transthyretin variants Ser 91 and Ser 116 associated with familial amyloidotic polyneuropathy."
Misrahi A.M., Plante V., Lalu T., Serre I., Adams D., Lacroix D.C., Said G.
Hum. Mutat. 12:71-71(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR SER-111 AND SER-136.
[105]"Transthyretin Ile73Val is associated with familial amyloidotic polyneuropathy in a Bangladeshi family."
Booth D.R., Gillmore J.D., Persey M.R., Booth S.E., Cafferty K.D., Tennent G.A., Madhoo S., Cochrane S.W., Whitehead T.C., Pasvol G., Hawkins P.N.
Hum. Mutat. 12:135-135(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR VAL-93.
[106]"A new nonamyloid transthyretin variant, G101S, detected by electrospray ionization/mass spectrometry."
Kishikawa M., Nakanishi T., Miyazaki A., Hatanaka M., Shimizu A., Tamoto S., Ohsawa N., Hayashi H., Kanai M.
Hum. Mutat. 12:363-363(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-121, IDENTIFICATION BY MASS SPECTROMETRY.
[107]"Transthyretin amyloidosis (serine 44) with headache, hearing loss, and peripheral neuropathy."
Klein C.J., Nakumura M., Jacobson D.R., Lacy M.Q., Benson M.D., Petersen R.C.
Neurology 51:1462-1464(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-64.
[108]"A new amyloidogenic transthyretin variant (Val122Ala) found in a compound heterozygous patient."
Theberge R., Connors L., Skare J., Skinner M., Falk R.H., Costello C.E.
Amyloid 6:54-58(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ALA-142, VARIANT SER-26, IDENTIFICATION BY MASS SPECTROMETRY.
[109]"A new transthyretin variant (Ser23Asn) associated with familial amyloidosis in a Portuguese patient."
Connors L.H., Theberge R., Skare J., Costello C.E., Falk R.H., Skinner M.
Amyloid 6:114-118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ASN-43, IDENTIFICATION BY MASS SPECTROMETRY.
[110]"Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum variant transthyretin in the diagnosis of familial amyloid polyneuropathy."
Tachibana N., Tokuda T., Yoshida K., Taketomi T., Nakazato M., Li Y.F., Masuda Y., Ikeda S.
Amyloid 6:282-288(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117, IDENTIFICATION BY MASS SPECTROMETRY.
[111]"A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with high serum transthyretin (TTR) and retinol binding protein (RBP) levels."
Terazaki H., Ando Y., Misumi S., Nakamura M., Ando E., Matsunaga N., Shoji S., Okuyama M., Ideta H., Nakagawa K., Ishizaki T., Ando M., Saraiva M.J.
Biochem. Biophys. Res. Commun. 264:365-370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-124, IDENTIFICATION BY MASS SPECTROMETRY.
[112]"Transthyretin Leu12Pro is associated with systemic, neuropathic and leptomeningeal amyloidosis."
Brett M., Persey M.R., Reilly M.M., Revesz T., Booth D.R., Booth S.E., Hawkins P.N., Pepys M.B., Morgan-Hughes J.A.
Brain 122:183-190(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR PRO-32.
[113]"Identification of a new transthyretin variant (Ile49) in familial amyloidotic polyneuropathy using electrospray ionization mass spectrometry and nonisotopic RNase cleavage assay."
Nakamura M., Yamashita T., Ando Y., Hamidi Asl K., Tashima K., Ohlsson P., Kususe Y., Benson M.D.
Hum. Hered. 49:186-189(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ILE-69, IDENTIFICATION BY MASS SPECTROMETRY.
[114]"A novel variant of transthyretin (Glu89Lys) associated with familial amyloidotic polyneuropathy."
Nakamura M., Hamidi Asl K., Benson M.D.
Amyloid 7:46-50(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LYS-109.
[115]"Heart failure caused by a novel amyloidogenic mutation of the transthyretin gene: ATTR Ala45Ser."
Janunger T., Anan I., Holmgren G., Lovheim O., Ohlsson P.I., Suhr O.B., Tashima K.
Amyloid 7:137-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR SER-65, IDENTIFICATION BY MASS SPECTROMETRY.
[116]"New transthyretin mutation V28M in a Portuguese kindred with amyloid polyneuropathy."
de Carvalho M., Moreira P., Evangelista T., Ducla-Soares J.L., Bento M., Fernandes R., Saraiva M.J.
Muscle Nerve 23:1016-1021(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR MET-48.
[117]"Recurrent subarachnoid hemorrhage associated with a new transthyretin variant (Gly53Glu)."
Ellie E., Camou F., Vital A., Rummens C., Grateau G., Delpech M., Valleix S.
Neurology 57:135-137(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLU-73.
[118]"A new transthyretin variant Leu55Gln in a patient with systemic amyloidosis."
Yazaki M., Varga J., Dyck P.J., Benson M.D.
Amyloid 9:268-271(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLN-75.
[119]"Characterization of transthyretin variants in familial transthyretin amyloidosis by mass spectrometric peptide mapping and DNA sequence analysis."
Lim A., Prokaeva T., McComb M.E., O'Connor P.B., Theberge R., Connors L.H., Skinner M., Costello C.E.
Anal. Chem. 74:741-751(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-26 AND MET-139, VARIANTS AMYL-TTR ALA-58; LEU-61; SER-64 AND LEU-84, IDENTIFICATION BY MASS SPECTROMETRY.
[120]"Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis."
Lachmann H.J., Booth D.R., Booth S.E., Bybee A., Gilbertson J.A., Gillmore J.D., Pepys M.B., Hawkins P.N.
N. Engl. J. Med. 346:1786-1791(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140 AND ILE-142.
[121]"Oculoleptomeningeal amyloidosis in a large kindred with a new transthyretin variant Tyr69His."
Blevins G., Macaulay R., Harder S., Fladeland D., Yamashita T., Yazaki M., Hamidi Asl K., Benson M.D., Donat J.R.
Neurology 60:1625-1630(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR HIS-89.
[122]"Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosis."
Lim A., Prokaeva T., McComb M.E., Connors L.H., Skinner M., Costello C.E.
Protein Sci. 12:1775-1785(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-53, IDENTIFICATION BY MASS SPECTROMETRY.
[123]"A severe form of amyloidotic polyneuropathy in a Costa Rican family with a rare transthyretin mutation (Glu54Lys)."
Busse A., Sanchez M.A., Monterroso V., Alvarado M.V., Leon P.
Am. J. Med. Genet. A 128:190-194(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR LYS-74.
[124]"An unusual transthyretin gene missense mutation (TTR Phe33Val) linked to familial amyloidotic polyneuropathy."
Frigerio R., Fabrizi G.M., Ferrarini M., Cavallaro T., Brighina L., Santoro P., Agostoni E., Cavaletti G., Rizzuto N., Ferrarese C.
Amyloid 11:121-124(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR VAL-53.
[125]"Identification of transthyretin variants by sequential proteomic and genomic analysis."
Bergen H.R. III, Zeldenrust S.R., Butz M.L., Snow D.S., Dyck P.J., Dyck P.J.B., Klein C.J., O'Brien J.F., Thibodeau S.N., Muddiman D.C.
Clin. Chem. 50:1544-1552(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL-TTR GLU-67; HIS-78; ALA-80 AND TYR-97, IDENTIFICATION BY MASS SPECTROMETRY.
[126]"A new transthyretin variant (Glu61Gly) associated with cardiomyopathy."
Rosenzweig M., Skinner M., Prokaeva T., Theberge R., Costello C., Drachman B.M., Connors L.H.
Amyloid 14:65-71(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR GLY-81.
[127]"A novel type of familial transthyretin amyloidosis, ATTR Asn124Ser, with co-localization of kappa light chains."
Bergstroem J., Patrosso M.C., Colussi G., Salvadore M., Penco S., Lando G., Marocchi A., Ueda A., Nakamura M., Ando Y.
Amyloid 14:141-145(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR SER-144.
[128]"Genetic microheterogeneity of human transthyretin detected by IEF."
Altland K., Benson M.D., Costello C.E., Ferlini A., Hazenberg B.P.C., Hund E., Kristen A.V., Linke R.P., Merlini G., Salvi F., Saraiva M.J., Singer R., Skinner M., Winter P.
Electrophoresis 28:2053-2064(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53; VAL-53; PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84; LEU-88; ALA-91; TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114; GLY-117; ASN-126; MET-127; VAL-127; MET-131 AND ILE-142, VARIANTS ILE-33; SER-121 AND THR-129, VARIANT CHICAGO MET-139.
[129]"Familial amyloidosis in a large Spanish kindred resulting from a D38V mutation in the transthyretin gene."
Augustin S., Llige D., Andreu A., Gonzalez A., Genesca J.
Eur. J. Clin. Invest. 37:673-678(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR VAL-58.
[130]"Delayed diagnosis of transthyretin amyloidosis with a novel mutation (c.210T>A) in the transthyretin gene."
Dekmezian M.S., Tschen J.A., Cho-Vega J.H.
J. Am. Acad. Dermatol. 68:E49-E51(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AMYL-TTR ARG-70.
+Additional computationally mapped references.

Web resources

GeneReviews
Wikipedia

Transthyretin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02091 mRNA. Translation: AAA60011.1.
M10605 mRNA. Translation: AAA60012.1.
M11518 Genomic DNA. Translation: AAA98771.1.
M11844 Genomic DNA. Translation: AAA60013.1.
X59498 mRNA. Translation: CAA42087.1.
D00096 mRNA. Translation: BAA00059.1.
M15517, M15515, M15516 Genomic DNA. Translation: AAA60018.1.
U19780 mRNA. Translation: AAA73473.1.
AF162690 mRNA. Translation: AAD45014.1.
AK312051 mRNA. Translation: BAG34987.1.
BT007189 mRNA. Translation: AAP35853.1.
CR456908 mRNA. Translation: CAG33189.1.
CH471088 Genomic DNA. Translation: EAX01264.1.
BC005310 mRNA. Translation: AAH05310.1.
BC020791 mRNA. Translation: AAH20791.1.
S63185 Genomic DNA. Translation: AAD14937.2.
S72385 Genomic DNA. Translation: AAD14098.1.
M11714 mRNA. Translation: AAA61181.1.
M63285 Genomic DNA. Translation: AAA36784.1.
PIRVBHU. A91532.
RefSeqNP_000362.1. NM_000371.3.
UniGeneHs.427202.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BM7X-ray2.00A/B21-147[»]
1BMZX-ray2.00A/B21-147[»]
1BZ8X-ray2.00A/B21-141[»]
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/B21-145[»]
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[»]
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[»]
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[»]
5TTRX-ray2.70A/B/C/D/E/F/G/H21-147[»]
ProteinModelPortalP02766.
SMRP02766. Positions 30-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113127. 43 interactions.
DIPDIP-1083N.
IntActP02766. 45 interactions.
MINTMINT-1374623.
STRING9606.ENSP00000237014.

Chemistry

BindingDBP02766.
ChEMBLCHEMBL3194.
DrugBankDB00586. Diclofenac.
DB00255. Diethylstilbestrol.
DB00861. Diflunisal.
DB01093. Dimethyl sulfoxide.
DB00451. Levothyroxine.
DB00279. Liothyronine.

PTM databases

PhosphoSiteP02766.

Polymorphism databases

DMDM136464.

2D gel databases

DOSAC-COBS-2DPAGEP02766.
REPRODUCTION-2DPAGEP02766.
SWISS-2DPAGEP02766.
UCD-2DPAGEP02766.

Proteomic databases

PaxDbP02766.
PeptideAtlasP02766.
PRIDEP02766.

Protocols and materials databases

DNASU7276.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000237014; ENSP00000237014; ENSG00000118271.
GeneID7276.
KEGGhsa:7276.
UCSCuc002kwx.4. human.

Organism-specific databases

CTD7276.
GeneCardsGC18P029194.
HGNCHGNC:12405. TTR.
HPACAB002517.
CAB062567.
HPA002550.
MIM105210. phenotype.
115430. phenotype.
145680. phenotype.
176300. gene.
neXtProtNX_P02766.
Orphanet85447. Familial amyloid polyneuropathy.
85451. Transthyretin-related familial amyloid cardiomyopathy.
PharmGKBPA37069.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321124.
HOGENOMHOG000251776.
HOVERGENHBG000285.
InParanoidP02766.
OMATKSYWKA.
OrthoDBEOG7S4X7V.
PhylomeDBP02766.
TreeFamTF300210.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP02766.
BgeeP02766.
CleanExHS_TTR.
GenevestigatorP02766.

Family and domain databases

Gene3D2.60.40.180. 1 hit.
InterProIPR023418. Thyroxine_BS.
IPR000895. Transthyretin/HIU_hydrolase.
IPR023416. Transthyretin/HIU_hydrolase_SF.
IPR023419. Transthyretin_CS.
[Graphical view]
PfamPF00576. Transthyretin. 1 hit.
[Graphical view]
PRINTSPR00189. TRNSTHYRETIN.
SMARTSM00095. TR_THY. 1 hit.
[Graphical view]
SUPFAMSSF49472. SSF49472. 1 hit.
PROSITEPS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTTR. human.
EvolutionaryTraceP02766.
GeneWikiTransthyretin.
GenomeRNAi7276.
NextBio28455.
PMAP-CutDBP02766.
PROP02766.
SOURCESearch...

Entry information

Entry nameTTHY_HUMAN
AccessionPrimary (citable) accession number: P02766
Secondary accession number(s): Q549C7 expand/collapse secondary AC list , Q6IB96, Q9UBZ6, Q9UCM9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 20, 1987
Last modified: April 16, 2014
This is version 182 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM