Reviewed, UniProtKB/Swiss-Prot P02766 (TTHY_HUMAN)

Names and origin

Protein names

Recommended name:
    Transthyretin
Alternative name(s):
    Prealbumin
    TBPA
    TTR
    ATTR

Gene names

Name:	TTR
Synonyms:	PALB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subunit structure	Homotetramer.
Subcellular location	Secreted.
Tissue specificity	Most abundant in the choroid plexus. Also present in the liver.
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.
Involvement in disease	Defects in TTR are the cause of amyloidosis type 1 (AMYL1) [MIM:176300]. AMYL1 is 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. Ref.5 Ref.6 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.39 Ref.40 Ref.42 Ref.43 Ref.44 Ref.46 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.81 Ref.82 Ref.83 Ref.85 Ref.86 Ref.87 Ref.88 Ref.89 Ref.90 Ref.91 Ref.92 Ref.93 Ref.96 Ref.97 Ref.98 Ref.99 Ref.100 Ref.101 Ref.102 Defects in TTR are the cause of amyloidosis type 7 (AMYL7) [MIM:105210]; also known as leptomeningeal amyloidosis or meningocerebrovascular amyloidosis. AMYL7 is a form of hereditary transthyretin amyloidosis 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. Mild systemic amyloidosis may occurr. Ref.72 Ref.94 Defects in TTR are a cause of hyperthyroxinemia [MIM:176300].
Miscellaneous	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.

Ontologies

Keywords
Biological process	Transport
Cellular component	Amyloid Secreted
Coding sequence diversity	Polymorphism
Disease	Amyloidosis Disease mutation Neuropathy
Domain	Signal
Ligand	Retinol-binding Vitamin A
Molecular function	Hormone Thyroid hormone
PTM	Gamma-carboxyglutamic acid Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	thyroid hormone generation Inferred from electronic annotation. Source: UniProtKB-KW transport Non-traceable author statement. Source: ProtInc
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW retinal binding Inferred from electronic annotation. Source: UniProtKB-KW retinol binding Inferred from electronic annotation. Source: UniProtKB-KW steroid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Ref.14 Ref.15 Ref.16 Ref.17 Ref.12 Ref.13 Ref.18

Chain

21 – 147

127

Transthyretin

PRO_0000035755

Sites

Binding site

35

1

Thyroid hormones

Binding site

74

1

Thyroid hormones

Amino acid modifications

Modified residue

62

1

4-carboxyglutamate; in a patient with Moyamoya disease Ref.28

Glycosylation

118

1

N-linked (GlcNAc...) Ref.27

Natural variations

Natural variant

26

1

G → S Common polymorphism. dbSNP rs1800458. Ref.63 Ref.81 Ref.92 Ref.98 Ref.13

VAR_007546

Natural variant

30

1

C → R in AMYL1; amyloid polyneuropathy. Ref.56

VAR_007547

Natural variant

32

1

L → P in AMYL1. Ref.85 Ref.101

VAR_038959

Natural variant

33

1

M → I Ref.101

VAR_038960

Natural variant

38

1

D → E in AMYL1; amyloid polyneuropathy.

VAR_007548

Natural variant

38

1

D → G in AMYL7. Ref.72

VAR_007549

Natural variant

40

1

V → I in AMYL1; late-onset amyloid polyneuropathy with carpal tunnel syndrome. Ref.74 Ref.101

VAR_007550

Natural variant

43

1

S → N in AMYL1. Ref.82

VAR_038961

Natural variant

44

1

P → S in AMYL1; amyloid polyneuropathy. dbSNP rs11541790. Ref.101

VAR_007551

Natural variant

48

1

V → M in AMYL1; amyloid polyneuropathy. Ref.89

VAR_010658

Natural variant

50

1

V → A in AMYL1; amyloid polyneuropathy. Ref.5 Ref.6 Ref.14 Ref.15 Ref.17 Ref.51 Ref.53 Ref.70 Ref.73 Ref.83 Ref.93 Ref.101

VAR_007552

Natural variant

50

1

V → G in AMYL1. Ref.5 Ref.6 Ref.14 Ref.15 Ref.17 Ref.51 Ref.53 Ref.70 Ref.73 Ref.83 Ref.93 Ref.101

VAR_038962

Natural variant

50

1

V → L in AMYL1; amyloid polyneuropathy. Ref.5 Ref.6 Ref.14 Ref.15 Ref.17 Ref.51 Ref.53 Ref.70 Ref.73 Ref.83 Ref.93 Ref.101

VAR_007553

Natural variant

50

1

V → M in AMYL1; amyloid polyneuropathy; by far the most frequent mutation. Ref.5 Ref.6 Ref.14 Ref.15 Ref.17 Ref.51 Ref.53 Ref.70 Ref.73 Ref.83 Ref.93 Ref.101

VAR_007554

Natural variant

53

1

F → C in a patient with amyloidosis. Ref.19 Ref.39 Ref.48 Ref.63 Ref.83 Ref.93 Ref.97 Ref.98 Ref.101 Ref.95

VAR_038963

Natural variant

53

1

F → I in AMYL1; Jewish 'SKO' amyloid polyneuropathy. Ref.19 Ref.39 Ref.48 Ref.63 Ref.83 Ref.93 Ref.97 Ref.101

VAR_007555

Natural variant

53

1

F → L in AMYL1; amyloid polyneuropathy. Ref.19 Ref.39 Ref.48 Ref.63 Ref.83 Ref.93 Ref.97 Ref.101

VAR_007556

Natural variant

53

1

F → V in AMYL1; amyloid polyneuropathy. Ref.19 Ref.39 Ref.48 Ref.63 Ref.83 Ref.93 Ref.97 Ref.101

VAR_038964

Natural variant

54

1

R → T in AMYL1. Ref.75

VAR_038965

Natural variant

55

1

K → N in AMYL1; amyloid polyneuropathy. Ref.70

VAR_038966

Natural variant

56

1

A → P in AMYL1; amyloid polyneuropathy. Ref.101

VAR_007557

Natural variant

58

1

D → A in AMYL1. Ref.83 Ref.92 Ref.93 Ref.102

VAR_038967

Natural variant

58

1

D → V in AMYL1. Ref.83 Ref.92 Ref.93 Ref.102

VAR_038968

Natural variant

61

1

W → L in AMYL1. Ref.92

VAR_038969

Natural variant

62

1

E → D in AMYL1. Ref.20 Ref.44 Ref.76

VAR_038970

Natural variant

62

1

E → G in AMYL1; amyloid polyneuropathy. Ref.20 Ref.44 Ref.76

VAR_007558

Natural variant

64

1

F → S in AMYL1. Ref.92

VAR_038971

Natural variant

65

1

A → D in AMYL1; amyloid cardiomyopathy. Ref.49 Ref.88 Ref.101

VAR_007559

Natural variant

65

1

A → S in AMYL1. Ref.49 Ref.88 Ref.101

VAR_038972

Natural variant

65

1

A → T in AMYL1; amyloid cardiomyopathy. Ref.49 Ref.88 Ref.101

VAR_007560

Natural variant

67

1

G → A in AMYL1; amyloid polyneuropathy. Ref.50 Ref.62 Ref.93 Ref.98 Ref.101

VAR_007561

Natural variant

67

1

G → E in AMYL1. Ref.50 Ref.62 Ref.93 Ref.98 Ref.101

VAR_038973

Natural variant

67

1

G → R in AMYL1; amyloid polyneuropathy. Ref.50 Ref.62 Ref.93 Ref.98 Ref.101

VAR_007562

Natural variant

67

1

G → V in AMYL1; amyloid polyneuropathy with carpal tunnel syndrome. Ref.50 Ref.62 Ref.93 Ref.98 Ref.101

VAR_007563

Natural variant

69

1

T → A in AMYL1; amyloid polyneuropathy. Ref.55 Ref.70 Ref.86 Ref.101

VAR_007564

Natural variant

69

1

T → I in AMYL1. Ref.55 Ref.70 Ref.86 Ref.101

VAR_038974

Natural variant

70

1

S → I in AMYL1; amyloid cardiomyopathy. Ref.44 Ref.52 Ref.70 Ref.83

VAR_007565

Natural variant

70

1

S → R in AMYL1; amyloid polyneuropathy. Ref.44 Ref.52 Ref.70 Ref.83

VAR_007566

Natural variant

72

1

S → P in AMYL1; amyloid polyneuropathy.

VAR_007567

Natural variant

73

1

G → E in AMYL1. Ref.90

VAR_038975

Natural variant

74

1

E → G in AMYL1; amyloid polyneuropathy. Ref.96

VAR_007568

Natural variant

74

1

E → K in AMYL1; early-onset amyloid polyneuropathy. Ref.96

VAR_038976

Natural variant

75

1

L → P in AMYL1; amyloid polyneuropathy. Ref.54 Ref.68 Ref.91

VAR_007569

Natural variant

75

1

L → Q in AMYL1. Ref.54 Ref.68 Ref.91

VAR_038977

Natural variant

78

1

L → H in AMYL1; amyloid polyneuropathy and carpal tunnel syndrome. Ref.46 Ref.98

VAR_007570

Natural variant

78

1

L → R in AMYL1; amyloid polyneuropathy and carpal tunnel syndrome. Ref.46 Ref.98

VAR_007571

Natural variant

79

1

T → K in AMYL1; amyloid cardiomyopathy. Ref.71

VAR_007572

Natural variant

80

1

T → A in AMYL1; amyloid polyneuropathy and cardiomyopathy. Ref.70 Ref.93 Ref.98 Ref.101

VAR_007573

Natural variant

81

1

E → G in AMYL1. Ref.58 Ref.99

VAR_038978

Natural variant

81

1

E → K in AMYL1; amyloid polyneuropathy. Ref.58 Ref.99

VAR_007574

Natural variant

84

1

F → L in AMYL1; amyloid polyneuropathy. Ref.48 Ref.92 Ref.101

VAR_007575

Natural variant

88

1

I → L in AMYL1; amyloid cardiomyopathy. Ref.59 Ref.101

VAR_007576

Natural variant

89

1

Y → H in AMYL7; vitreous amyloid in some patients. Ref.94

VAR_007577

Natural variant

90

1

K → N in AMYL1; amyloid polyneuropathy and carpal tunnel syndrome. Ref.57

VAR_007578

Natural variant

91

1

V → A in AMYL1; amyloid polyneuropathy. Ref.60 Ref.61 Ref.101

VAR_007579

Natural variant

93

1

I → V in AMYL1; amyloid polyneuropathy. Ref.78

VAR_007580

Natural variant

94

1

D → H

VAR_007581

Natural variant

97

1

S → Y in AMYL1; amyloid polyneuropathy. Ref.42 Ref.70 Ref.98 Ref.101

VAR_007582

Natural variant

98

1

Y → F in AMYL1. Ref.101

VAR_038979

Natural variant

104

1

I → N in AMYL1; vitrous amyloid. Ref.40 Ref.101

VAR_007583

Natural variant

104

1

I → S in AMYL1; carpal tunnel syndrome; almost no RBP binding. Ref.40 Ref.101

VAR_007584

Natural variant

104

1

I → T in AMYL1. Ref.40 Ref.101

VAR_038980

Natural variant

109

1

E → K in AMYL1; amyloid polyneuropathy. Ref.55 Ref.70 Ref.87

VAR_010659

Natural variant

109

1

E → Q in AMYL1; amyloid polyneuropathy and cardiomyopathy. Ref.55 Ref.70 Ref.87

VAR_007585

Natural variant

110

1

H → N Ref.20 Ref.47

VAR_007586

Natural variant

111

1

A → S in AMYL1; amyloid polyneuropathy. Ref.77

VAR_007587

Natural variant

114

1

V → A in a patient with amyloidosis. Ref.98 Ref.101

VAR_038981

Natural variant

117

1

A → G in AMYL1; amyloid polyneuropathy. Ref.67 Ref.83 Ref.101

VAR_007588

Natural variant

117

1

A → S in AMYL1. Ref.67 Ref.83 Ref.101

VAR_038982

Natural variant

121

1

G → S Ref.101 Ref.79

VAR_007589

Natural variant

122

1

P → R

VAR_007590

Natural variant

124

1

R → C Ref.84

VAR_007591

Natural variant

124

1

R → H Ref.84

VAR_038983

Natural variant

126

1

T → N in AMYL1. Ref.101

VAR_038984

Natural variant

127

1

I → M in AMYL1. Ref.64 Ref.66 Ref.101

VAR_038985

Natural variant

127

1

I → V in AMYL1; amyloid polyneuropathy. Ref.64 Ref.66 Ref.101

VAR_007592

Natural variant

129

1

A → T Increased affinity for thyroxine. Ref.101 Ref.23

VAR_007593

Natural variant

131

1

L → M in AMYL1. Ref.101

VAR_007594

Natural variant

134

1

Y → C in AMYL1; amyloid polyneuropathy. Ref.43 Ref.69

VAR_007595

Natural variant

134

1

Y → H in AMYL1; amyloid polyneuropathy and carpal tunnel syndrome. Ref.43 Ref.69

VAR_007598

Natural variant

136

1

Y → S in AMYL1; amyloid polyneuropathy. Ref.77

VAR_007596

Natural variant

136

1

Y → V Requires 2 nucleotide substitutions. Ref.77 Ref.41

VAR_007597

Natural variant

139

1

T → M in Chicago variant.

VAR_007599

Natural variant

140

1

A → S in AMYL1. Ref.93

VAR_038986

Natural variant

142

1

V → A in AMYL1. Ref.16 Ref.81 Ref.93 Ref.101

VAR_038987

Natural variant

142

1

V → I in AMYL1. Ref.16 Ref.81 Ref.93 Ref.101

VAR_007600

Natural variant

144

1

N → S in AMYL1. Ref.100

VAR_038988

Experimental info

Sequence conflict

41

1

R → P in AAA98771. Ref.3

Sequence conflict

147

1

E → D in CAG33189. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Beta strand

32 – 38

7

Turn

39 – 42

4

Beta strand

49 – 55

7

Beta strand

61 – 68

8

Beta strand

73 – 75

3

Turn

81 – 83

3

Beta strand

86 – 93

8

Helix

95 – 101

7

Beta strand

107 – 118

12

Beta strand

124 – 132

9

Beta strand

135 – 143

9

Sequences

	Sequence		Length	Mass (Da)
	P02766-1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: 3A6AEBCBBA56BC44	FASTA	147	15,887
	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

References

	« Hide 'large scale' referencesShow '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: 6093805] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2990465] [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: 4054629] [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: 2995367] [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: 3818577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT AMYL1 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: 3022108] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AMYL1 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: 2015890] [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: 1666289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[9]	"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].
[10]	"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].
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[12]	"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: 4607556] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147.
[13]	"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: 6300852] [Abstract] Cited for: PRELIMINARY PROTEIN SEQUENCE OF 21-147, VARIANT SER-26.
[14]	"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: 6651852] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL1 MET-50.
[15]	"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: 6583672] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL1 MET-50.
[16]	"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: 3135807] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL1 ILE-142.
[17]	"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: 1517749] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-147, VARIANT AMYL1 MET-50.
[18]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-41. Tissue: Platelet.
[19]	"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: 1932142] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL1 LEU-53.
[20]	"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: 7923855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67, VARIANT AMYL1 GLY-62, VARIANT ASN-110.
[21]	"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: 4044580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-147.
[22]	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, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[23]	"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: 1979335] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-129, VARIANT THR-129.
[24]	"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: 7474944] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[25]	"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: 201845] [Abstract] Cited for: BINDING SITES FOR THYROID HORMONES.
[26]	"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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Plasma.
[27]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118, MASS SPECTROMETRY. Tissue: Plasma.
[28]	"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: 18221012] [Abstract] Cited for: GAMMA-CARBOXYGLUTAMATION AT GLU-62, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[29]	"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: 671542] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[30]	"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: 4216640] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[31]	"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: 8382610] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF VARIANT MET-50.
[32]	"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: 8428915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF VARIANT MET-50.
[33]	"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: 7754382] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF COMPLEX WITH RBP.
[34]	"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: 10052934] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH RBP.
[35]	"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: 9789022] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[36]	"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: 9818054] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANTS.
[37]	"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: 10742177] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[38]	"Transthyretin mutations in health and disease." Saraiva M.J.M. Hum. Mutat. 5:191-196(1995) [PubMed: 7599630] [Abstract] Cited for: REVIEW ON VARIANTS.
[39]	"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: 6487335] [Abstract] Cited for: VARIANT AMYL1 ILE-53.
[40]	"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: 3722385] [Abstract] Cited for: VARIANT AMYL1 SER-104.
[41]	"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: 3675594] [Abstract] Cited for: VARIANT VAL-136.
[42]	"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: 2891727] [Abstract] Cited for: VARIANT AMYL1 TYR-97.
[43]	"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: 2161654] [Abstract] Cited for: VARIANT AMYL1 CYS-134.
[44]	"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: 2363717] [Abstract] Cited for: VARIANTS AMYL1 GLY-62 AND ARG-70.
[45]	"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: 1877623] [Abstract] Cited for: VARIANT CHICAGO MET-139.
[46]	"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: 1656975] [Abstract] Cited for: VARIANT AMYL1 ARG-78.
[47]	"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: 1997217] [Abstract] Cited for: VARIANT ASN-110.
[48]	"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: 2046936] [Abstract] Cited for: VARIANTS AMYL1 LEU-53 AND LEU-84.
[49]	"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: 1570831] [Abstract] Cited for: VARIANT AMYL1 THR-65.
[50]	"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: 1734866] [Abstract] Cited for: VARIANT AMYL1 ARG-67.
[51]	"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: 1520326] [Abstract] Cited for: VARIANT AMYL1 LEU-50.
[52]	"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: 1520336] [Abstract] Cited for: VARIANT AMYL1 ILE-70.
[53]	"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: 1544214] [Abstract] Cited for: VARIANT AMYL1 ALA-50.
[54]	"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: 1351039] [Abstract] Cited for: VARIANT AMYL1 PRO-75.
[55]	"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: 1301926] [Abstract] Cited for: VARIANTS AMYL1 ALA-69 AND GLN-109.
[56]	"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: 1362222] [Abstract] Cited for: VARIANT AMYL1 ARG-30.
[57]	"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: 1436517] [Abstract] Cited for: VARIANT AMYL1 ASN-90.
[58]	"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: 8352764] [Abstract] Cited for: VARIANT AMYL1 LYS-81.
[59]	"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: 8038017] [Abstract] Cited for: VARIANT AMYL1 LEU-88.
[60]	"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: 8257997] [Abstract] Cited for: VARIANT AMYL1 ALA-91.
[61]	"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: 8095302] [Abstract] Cited for: VARIANT AMYL1 ALA-91.
[62]	"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 AMYL1 ALA-67.
[63]	"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: 8019560] [Abstract] Cited for: VARIANT SER-26, VARIANT AMYL1 ILE-53.
[64]	"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: 8081397] [Abstract] Cited for: VARIANT AMYL1 VAL-127.
[65]	"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: 8089102] [Abstract] Cited for: VARIANT SER-104, RBP BINDING STUDIES.
[66]	"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: 7914929] [Abstract] Cited for: VARIANT AMYL1 VAL-127.
[67]	"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: 8133316] [Abstract] Cited for: VARIANT AMYL1 GLY-117.
[68]	"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: 7910950] [Abstract] Cited for: VARIANT AMYL1 PRO-75.
[69]	"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: 8309582] [Abstract] Cited for: VARIANT AMYL1 HIS-134.
[70]	"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: 7655883] [Abstract] Cited for: VARIANTS AMYL1 MET-50; ASN-55; ALA-69; ARG-70; ALA-80; TYR-97 AND GLN-109.
[71]	"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: 7850982] [Abstract] Cited for: VARIANT AMYL1 LYS-79.
[72]	"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: 8579098] [Abstract] Cited for: VARIANT AMYL7 GLY-38.
[73]	"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: 9066351] [Abstract] Cited for: VARIANT AMYL1 GLY-50.
[74]	"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: 8990019] [Abstract] Cited for: VARIANT AMYL1 ILE-40.
[75]	"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: 9605286] [Abstract] Cited for: VARIANT AMYL1 THR-54.
[76]	"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: 10036587] [Abstract] Cited for: VARIANT AMYL1 ASP-62.
[77]	"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: 10627135] [Abstract] Cited for: VARIANTS AMYL1 SER-111 AND SER-136.
[78]	"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: 10694917] [Abstract] Cited for: VARIANT AMYL1 VAL-93.
[79]	"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: 10671063] [Abstract] Cited for: VARIANT SER-121, MASS SPECTROMETRY.
[80]	"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: 9818883] [Abstract] Cited for: VARIANT SER-64.
[81]	"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: 10211412] [Abstract] Cited for: VARIANT AMYL1 ALA-142, VARIANT SER-26, MASS SPECTROMETRY.
[82]	"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: 10439117] [Abstract] Cited for: VARIANT AMYL1 ASN-43, MASS SPECTROMETRY.
[83]	"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: 10611950] [Abstract] Cited for: VARIANTS AMYL1 LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117, MASS SPECTROMETRY.
[84]	"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: 10529370] [Abstract] Cited for: VARIANT HIS-124, MASS SPECTROMETRY.
[85]	"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: 10071047] [Abstract] Cited for: VARIANT AMYL1 PRO-32.
[86]	"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: 10436378] [Abstract] Cited for: VARIANT AMYL1 ILE-69, MASS SPECTROMETRY.
[87]	"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: 10842705] [Abstract] Cited for: VARIANT AMYL1 LYS-109.
[88]	"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: 10842718] [Abstract] Cited for: VARIANT AMYL1 SER-65, MASS SPECTROMETRY.
[89]	"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: 10882995] [Abstract] Cited for: VARIANT AMYL1 MET-48.
[90]	"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: 11445644] [Abstract] Cited for: VARIANT AMYL1 GLU-73.
[91]	"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: 12557757] [Abstract] Cited for: VARIANT AMYL1 GLN-75.
[92]	"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: 11866053] [Abstract] Cited for: VARIANTS SER-26 AND MET-139, VARIANTS AMYL1 ALA-58; LEU-61; SER-64 AND LEU-84, MASS SPECTROMETRY.
[93]	"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: 12050338] [Abstract] Cited for: VARIANTS AMYL1 MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140 AND ILE-142.
[94]	"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: 12771253] [Abstract] Cited for: VARIANT AMYL7 HIS-89.
[95]	"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: 12876326] [Abstract] Cited for: VARIANT CYS-53, MASS SPECTROMETRY.
[96]	"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: 15214015] [Abstract] Cited for: VARIANT AMYL1 LYS-74.
[97]	"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: 15478468] [Abstract] Cited for: VARIANT AMYL1 VAL-53.
[98]	"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: 15217993] [Abstract] Cited for: VARIANTS SER-26; CYS-53 AND ALA-114, VARIANTS AMYL1 GLU-67; HIS-78; ALA-80 AND TYR-97, MASS SPECTROMETRY.
[99]	"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: 17453626] [Abstract] Cited for: VARIANT AMYL1 GLY-81.
[100]	"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: 17577687] [Abstract] Cited for: VARIANT AMYL1 SER-144.
[101]	"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: 17503405] [Abstract] Cited for: VARIANTS AMYL1 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; THR-129 AND MET-139.
[102]	"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: 17635579] [Abstract] Cited for: VARIANT AMYL1 VAL-58.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Transthyretin entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BT007189 mRNA. Translation: AAP35853.1.
CR456908 mRNA. Translation: CAG33189.1.
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.

IPI

IPI00022432.

PIR

VBHU. A91532.

RefSeq

NP_000362.1.

UniGene

Hs.427202

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BM7	X-ray	2.00	A/B	21-147	[»]
1BMZ	X-ray	2.00	A/B	21-147	[»]
1BZ8	X-ray	2.00	A/B	21-141	[»]
1BZD	X-ray	1.90	A/B	21-147	[»]
1BZE	X-ray	1.80	A/B	21-147	[»]
1DVQ	X-ray	2.00	A/B	21-144	[»]
1DVS	X-ray	2.00	A/B	21-144	[»]
1DVT	X-ray	1.90	A/B	21-144	[»]
1DVU	X-ray	1.90	A/B	21-144	[»]
1DVX	X-ray	2.00	A/B	21-144	[»]
1DVY	X-ray	1.90	A/B	21-144	[»]
1DVZ	X-ray	1.90	A/B	21-144	[»]
1E3F	X-ray	1.90	A/B	21-145	[»]
1E4H	X-ray	1.80	A/B	21-147	[»]
1E5A	X-ray	1.80	A/B	21-147	[»]
1ETA	X-ray	1.70	1/2	21-147	[»]
1ETB	X-ray	1.70	1/2	21-147	[»]
1F41	X-ray	1.30	A/B	21-147	[»]
1F64	model	-	A	21-147	[»]
1F86	X-ray	1.10	A/B	30-144	[»]
1FH2	X-ray	1.80	A/B	21-147	[»]
1FHN	X-ray	1.75	A/B	21-147	[»]
1G1O	X-ray	2.30	A/B/C/D	21-147	[»]
1GKO	X-ray	2.10	A/B/C/D	21-147	[»]
1ICT	X-ray	3.00	A/B/C/D/E/F/G/H	21-147	[»]
1III	X-ray	2.00	A/B	21-147	[»]
1IIK	X-ray	2.00	A/B	21-147	[»]
1IJN	X-ray	1.70	A/B	21-147	[»]
1QAB	X-ray	3.20	A/B/C/D	21-147	[»]
1QWH	X-ray	1.36	A/B	31-147	[»]
1RLB	X-ray	3.10	A/B/C/D	21-147	[»]
1SOK	X-ray	1.60	A/B	21-147	[»]
1SOQ	X-ray	2.10	A/B/C/D	21-147	[»]
1THA	X-ray	2.00	A/B	21-147	[»]
1THC	X-ray	2.30	A/B	21-147	[»]
1TLM	X-ray	1.90	A/B	21-147	[»]
1TSH	X-ray	1.70	A/B	21-147	[»]
1TT6	X-ray	1.80	A/B	21-147	[»]
1TTA	X-ray	1.70	A/B	21-147	[»]
1TTB	X-ray	1.70	A/B	21-147	[»]
1TTC	X-ray	1.70	A/B	21-147	[»]
1TTR	X-ray	1.90	A/B	21-147	[»]
1TYR	X-ray	1.80	A/B	21-147	[»]
1TZ8	X-ray	1.85	A/B/C/D	21-147	[»]
1U21	X-ray	1.69	A/B	21-147	[»]
1X7S	X-ray	1.55	A/B	21-147	[»]
1X7T	X-ray	1.60	A/B	21-147	[»]
1Y1D	X-ray	1.70	A/B	21-147	[»]
1Z7J	X-ray	2.20	A/B	21-147	[»]
1ZCR	X-ray	1.80	A/B	21-147	[»]
1ZD6	X-ray	1.90	A/B	21-147	[»]
2B14	X-ray	2.00	A/B	21-147	[»]
2B15	X-ray	1.70	A/B	21-147	[»]
2B16	X-ray	1.75	A/B	21-147	[»]
2B77	X-ray	1.70	A/B	21-147	[»]
2B9A	X-ray	1.54	A/B	21-147	[»]
2F7I	X-ray	1.60	A/B	21-147	[»]
2F8I	X-ray	1.54	A/B	21-147	[»]
2FBR	X-ray	1.46	A/B	21-147	[»]
2FLM	X-ray	1.65	A/B	21-147	[»]
2G3X	X-ray	1.58	A/B	21-147	[»]
2G3Z	X-ray	1.90	A/B	21-147	[»]
2G4E	X-ray	2.17	A/B	21-147	[»]
2G4G	X-ray	1.85	A/B	21-147	[»]
2G5U	X-ray	1.80	A/B	21-147	[»]
2G9K	X-ray	1.85	A/B	21-147	[»]
2GAB	X-ray	1.85	A/B	21-147	[»]
2H4E	X-ray	1.45	A/B	21-147	[»]
2NOY	X-ray	1.80	A/B	21-147	[»]
2PAB	X-ray	1.80	A/B	21-147	[»]
2QEL	X-ray	2.29	A/B/C/D	21-147	[»]
2QGB	X-ray	1.40	A/B	21-147	[»]
2QGC	X-ray	1.30	A/B	21-147	[»]
2QGD	X-ray	1.50	A/B	21-147	[»]
2QGE	X-ray	1.45	A/B	21-147	[»]
2ROX	X-ray	2.00	A/B	21-147	[»]
2ROY	X-ray	2.20	A/B	21-147	[»]
2TRH	X-ray	1.90	A/B	21-147	[»]
2TRY	X-ray	2.00	A/B	21-147	[»]
3B56	X-ray	1.55	A/B	21-147	[»]
3BSZ	X-ray	3.38	A/B/C/D	21-147	[»]
3BT0	X-ray	1.59	A/B	21-147	[»]
3CBR	X-ray	1.70	A/B	21-147	[»]
3CFM	X-ray	1.60	A/B	30-147	[»]
3CFN	X-ray	1.87	A/B	30-147	[»]
3CFQ	X-ray	2.09	A/B	30-147	[»]
3CFT	X-ray	1.87	A/B	30-147	[»]
3CN0	X-ray	1.52	A/B	21-147	[»]
3CN1	X-ray	1.52	A/B	21-147	[»]
3CN2	X-ray	1.52	A/B	21-147	[»]
3CN3	X-ray	1.80	A/B	21-147	[»]
3CN4	X-ray	1.40	A/B	21-147	[»]
3CXF	X-ray	2.30	A/B	21-147	[»]
3CYK	X-ray	1.38	A/B/C/D	30-145	[»]
3D2T	X-ray	1.85	A/B	21-147	[»]
3D7P	X-ray	1.72	A/B	21-147	[»]
3DGD	X-ray	1.38	A/B/C/D	21-147	[»]
3DID	X-ray	1.78	A/B/C/D	21-147	[»]
3ESN	X-ray	1.35	A/B	31-145	[»]
3ESO	X-ray	1.31	A/B	31-145	[»]
3ESP	X-ray	1.31	A/B	31-145	[»]
3FC8	X-ray	1.85	A/B	21-144	[»]
3FCB	X-ray	1.80	A/B	21-144	[»]
5TTR	X-ray	2.70	A/B/C/D/E/F/G/H	21-147	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1083N.

IntAct

P02766. 19 interactions.

2-D gel databases

SWISS-2DPAGE

P02766.

Cornea-2DPAGE

P02766.

DOSAC-COBS-2DPAGE

P02766.

HSC-2DPAGE

P02766.

REPRODUCTION-2DPAGE

P02766.

Siena-2DPAGE

P02766.

Proteomic databases

PeptideAtlas

P02766.

PRIDE

P02766.

Genome annotation databases

Ensembl

ENSG00000118271. Homo sapiens. [Contig view]

GeneID

7276.

KEGG

hsa:7276.

UCSC

uc002kwx.2. human.

Organism-specific databases

GeneCards

GC18P027425.

H-InvDB

HIX0014380.

HGNC

HGNC:12405. TTR.

HPA

CAB002517.
HPA002550.

MIM

105210. phenotype.
176300. gene+phenotype.

Orphanet

69. Amyloidosis.
85447. Familial amyloid polyneuropathy.
85451. Transthyretin-related familial amyloid cardiomyopathy.

PharmGKB

PA37069.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P02766.

HOVERGEN

P02766.

OMA

P02766. HHLLLLC.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway. FOXA2 and FOXA3 transcription factor networks.

Gene expression databases

ArrayExpress

P02766.

Bgee

P02766.

CleanEx

HS_TTR.

GermOnline

ENSG00000118271. Homo sapiens.

Family and domain databases

InterPro

IPR000895. Transthyretin/HIU_hydrolase.
[Graphical view]

Gene3D

G3DSA:2.60.40.180. Transthyretin. 1 hit.

Pfam

PF00576. Transthyretin. 1 hit.
[Graphical view]

PRINTS

PR00189. TRNSTHYRETIN.

ProDom

PD003457. Transthyretin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00095. TR_THY. 1 hit.
[Graphical view]

PROSITE

PS00768. TRANSTHYRETIN_1. 1 hit.
PS00769. TRANSTHYRETIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00586. Diclofenac.
DB00255. Diethylstilbestrol.
DB00861. Diflunisal.
DB01093. Dimethyl sulfoxide.
DB00451. Levothyroxine.
DB00279. Liothyronine.

NextBio

28455.

PMAP-CutDB

P02766.

SOURCE

Search...

Entry information

Entry name

TTHY_HUMAN

Accession

Primary (citable) accession number: P02766
Secondary accession number(s): Q6IB96, Q9UBZ6, Q9UCM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 20, 1987
Last modified:	July 7, 2009
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)