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Protein

Thyroxine-binding globulin

Gene

SERPINA7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major thyroid hormone transport protein in serum.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei293 – 2931Thyroxine1 Publication
Binding sitei398 – 3981Thyroxine1 Publication

GO - Molecular functioni

  • hormone binding Source: Ensembl
  • serine-type endopeptidase inhibitor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Protein family/group databases

MEROPSiI04.955.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroxine-binding globulin
Alternative name(s):
Serpin A7
T4-binding globulin
Gene namesi
Name:SERPINA7
Synonyms:TBG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11583. SERPINA7.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Thyroxine-binding globulin deficiency (TBG deficiency)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMutations in the SERPINA7 gene can result as a whole spectrum of deficiencies, characterized by either reduced or increased TBG levels in the serum. Patients show, respectively, reduced or elevated protein-bound iodine but are euthyroid.

See also OMIM:314200
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431S → T in TBG deficiency; San Diego; partial TBG deficiency. 1 Publication
VAR_007102
Natural varianti116 – 1161I → N in TBG deficiency; Gary; severe TBG deficiency. 1 Publication
Corresponds to variant rs28933689 [ dbSNP | Ensembl ].
VAR_007103
Natural varianti133 – 1331A → P in TBG deficiency; Montreal/TBG-M; partial TBG deficiency. 1 Publication
Corresponds to variant rs28933688 [ dbSNP | Ensembl ].
VAR_007104
Natural varianti247 – 2471L → P in TBG deficiency; CD5; complete TBG deficiency. 1 Publication
Corresponds to variant rs28937312 [ dbSNP | Ensembl ].
VAR_007107
Natural varianti351 – 3511H → Y in TBG deficiency; Quebec; partial TBG deficiency. 1 Publication
VAR_007109
Natural varianti383 – 3831P → L in TBG deficiency; Kumamoto. 1 Publication
VAR_007110

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi314200. gene+phenotype.
Orphaneti209893. Congenital isolated thyroxine-binding globulin deficiency.
PharmGKBiPA36347.

Chemistry

DrugBankiDB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.

Polymorphism and mutation databases

BioMutaiSERPINA7.
DMDMi1351236.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 415395Thyroxine-binding globulinPRO_0000032436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi99 – 991N-linked (GlcNAc...)
Glycosylationi116 – 1161N-linked (GlcNAc...); in variant GaryCurated
Glycosylationi165 – 1651N-linked (GlcNAc...)1 Publication
Glycosylationi253 – 2531N-linked (GlcNAc...)

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP05543.
PaxDbiP05543.
PeptideAtlasiP05543.
PRIDEiP05543.

PTM databases

PhosphoSiteiP05543.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiP05543.
CleanExiHS_SERPINA7.
GenevisibleiP05543. HS.

Organism-specific databases

HPAiHPA002803.

Interactioni

Protein-protein interaction databases

BioGridi112769. 5 interactions.
STRINGi9606.ENSP00000329374.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 6021Combined sources
Beta strandi66 – 683Combined sources
Helixi70 – 8213Combined sources
Helixi86 – 9510Combined sources
Turni100 – 1023Combined sources
Helixi105 – 12016Combined sources
Beta strandi126 – 13712Combined sources
Helixi144 – 15310Combined sources
Beta strandi156 – 1616Combined sources
Helixi166 – 18015Combined sources
Turni181 – 1833Combined sources
Beta strandi198 – 21215Combined sources
Helixi216 – 2183Combined sources
Beta strandi220 – 2289Combined sources
Beta strandi231 – 24919Combined sources
Turni250 – 2534Combined sources
Beta strandi254 – 27219Combined sources
Helixi277 – 2837Combined sources
Helixi286 – 29510Combined sources
Beta strandi297 – 30610Combined sources
Beta strandi308 – 3158Combined sources
Helixi317 – 3237Combined sources
Helixi327 – 3293Combined sources
Turni336 – 3383Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi344 – 35714Combined sources
Beta strandi359 – 37416Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi391 – 3977Combined sources
Turni398 – 4014Combined sources
Beta strandi402 – 4109Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CEOX-ray2.80A/B39-415[»]
2RIVX-ray1.50A33-386[»]
B376-415[»]
2RIWX-ray2.04A39-386[»]
B376-415[»]
2XN3X-ray2.09A33-386[»]
B377-415[»]
2XN5X-ray1.70A32-380[»]
B381-415[»]
2XN6X-ray1.29A32-380[»]
B381-415[»]
2XN7X-ray1.43A32-380[»]
B381-415[»]
ProteinModelPortaliP05543.
SMRiP05543. Positions 37-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05543.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP05543.
OMAiFNLTDTP.
OrthoDBiEOG7QC7W9.
PhylomeDBiP05543.
TreeFamiTF343201.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05543-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPFLYLVLL VLGLHATIHC ASPEGKVTAC HSSQPNATLY KMSSINADFA
60 70 80 90 100
FNLYRRFTVE TPDKNIFFSP VSISAALVML SFGACCSTQT EIVETLGFNL
110 120 130 140 150
TDTPMVEIQH GFQHLICSLN FPKKELELQI GNALFIGKHL KPLAKFLNDV
160 170 180 190 200
KTLYETEVFS TDFSNISAAK QEINSHVEMQ TKGKVVGLIQ DLKPNTIMVL
210 220 230 240 250
VNYIHFKAQW ANPFDPSKTE DSSSFLIDKT TTVQVPMMHQ MEQYYHLVDM
260 270 280 290 300
ELNCTVLQMD YSKNALALFV LPKEGQMESV EAAMSSKTLK KWNRLLQKGW
310 320 330 340 350
VDLFVPKFSI SATYDLGATL LKMGIQHAYS ENADFSGLTE DNGLKLSNAA
360 370 380 390 400
HKAVLHIGEK GTEAAAVPEV ELSDQPENTF LHPIIQIDRS FMLLILERST
410
RSILFLGKVV NPTEA
Length:415
Mass (Da):46,325
Last modified:February 1, 1996 - v2
Checksum:i8B24EF8C7CEF8F0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 312CH → DS AA sequence (PubMed:414747).Curated
Sequence conflicti38 – 381T → S AA sequence (PubMed:414747).Curated
Sequence conflicti197 – 1971I → T in AAA60616 (PubMed:3094014).Curated

Polymorphismi

Two qualitative TBG variants occur in particular populations. TBG-A is found in 40% of Australian aborigines, it has reduced affinity for thyroxine and triiodothyroxine and increased susceptibility to inactivation by heat or acid. TBG-S ('s' for slow shift on isoelectic focusing) is found in blacks, Eskimos, Melanesians, Polynesians and Indonesians, but not in Caucasians; TBG-S is slightly more thermolabile.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431S → T in TBG deficiency; San Diego; partial TBG deficiency. 1 Publication
VAR_007102
Natural varianti116 – 1161I → N in TBG deficiency; Gary; severe TBG deficiency. 1 Publication
Corresponds to variant rs28933689 [ dbSNP | Ensembl ].
VAR_007103
Natural varianti133 – 1331A → P in TBG deficiency; Montreal/TBG-M; partial TBG deficiency. 1 Publication
Corresponds to variant rs28933688 [ dbSNP | Ensembl ].
VAR_007104
Natural varianti191 – 1911D → N in TBG-S/Slow. 1 Publication
Corresponds to variant rs1050086 [ dbSNP | Ensembl ].
VAR_007105
Natural varianti211 – 2111A → T in TBG-A/Aborigine. 1 Publication
Corresponds to variant rs2234036 [ dbSNP | Ensembl ].
VAR_007106
Natural varianti247 – 2471L → P in TBG deficiency; CD5; complete TBG deficiency. 1 Publication
Corresponds to variant rs28937312 [ dbSNP | Ensembl ].
VAR_007107
Natural varianti303 – 3031L → F Common polymorphism.
Corresponds to variant rs1804495 [ dbSNP | Ensembl ].
VAR_007108
Natural varianti351 – 3511H → Y in TBG deficiency; Quebec; partial TBG deficiency. 1 Publication
VAR_007109
Natural varianti383 – 3831P → L in TBG deficiency; Kumamoto. 1 Publication
VAR_007110

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14091 mRNA. Translation: AAA60616.1.
X64171 Genomic DNA. Translation: CAA45509.1.
L13470 Genomic DNA. Translation: AAA16067.1.
Z83850 Genomic DNA. Translation: CAB06092.1.
CH471120 Genomic DNA. Translation: EAX02747.1.
CH471120 Genomic DNA. Translation: EAX02748.1.
BC020747 mRNA. Translation: AAH20747.1.
CCDSiCCDS14518.1.
PIRiA47224.
RefSeqiNP_000345.2. NM_000354.5.
UniGeneiHs.76838.

Genome annotation databases

EnsembliENST00000327674; ENSP00000329374; ENSG00000123561.
ENST00000372563; ENSP00000361644; ENSG00000123561.
GeneIDi6906.
KEGGihsa:6906.
UCSCiuc004eme.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14091 mRNA. Translation: AAA60616.1.
X64171 Genomic DNA. Translation: CAA45509.1.
L13470 Genomic DNA. Translation: AAA16067.1.
Z83850 Genomic DNA. Translation: CAB06092.1.
CH471120 Genomic DNA. Translation: EAX02747.1.
CH471120 Genomic DNA. Translation: EAX02748.1.
BC020747 mRNA. Translation: AAH20747.1.
CCDSiCCDS14518.1.
PIRiA47224.
RefSeqiNP_000345.2. NM_000354.5.
UniGeneiHs.76838.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CEOX-ray2.80A/B39-415[»]
2RIVX-ray1.50A33-386[»]
B376-415[»]
2RIWX-ray2.04A39-386[»]
B376-415[»]
2XN3X-ray2.09A33-386[»]
B377-415[»]
2XN5X-ray1.70A32-380[»]
B381-415[»]
2XN6X-ray1.29A32-380[»]
B381-415[»]
2XN7X-ray1.43A32-380[»]
B381-415[»]
ProteinModelPortaliP05543.
SMRiP05543. Positions 37-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112769. 5 interactions.
STRINGi9606.ENSP00000329374.

Chemistry

ChEMBLiCHEMBL3843.
DrugBankiDB00451. Levothyroxine.
DB00279. Liothyronine.
DB01583. Liotrix.

Protein family/group databases

MEROPSiI04.955.

PTM databases

PhosphoSiteiP05543.

Polymorphism and mutation databases

BioMutaiSERPINA7.
DMDMi1351236.

Proteomic databases

MaxQBiP05543.
PaxDbiP05543.
PeptideAtlasiP05543.
PRIDEiP05543.

Protocols and materials databases

DNASUi6906.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327674; ENSP00000329374; ENSG00000123561.
ENST00000372563; ENSP00000361644; ENSG00000123561.
GeneIDi6906.
KEGGihsa:6906.
UCSCiuc004eme.2. human.

Organism-specific databases

CTDi6906.
GeneCardsiGC0XM105277.
HGNCiHGNC:11583. SERPINA7.
HPAiHPA002803.
MIMi314200. gene+phenotype.
neXtProtiNX_P05543.
Orphaneti209893. Congenital isolated thyroxine-binding globulin deficiency.
PharmGKBiPA36347.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238521.
HOVERGENiHBG005957.
InParanoidiP05543.
OMAiFNLTDTP.
OrthoDBiEOG7QC7W9.
PhylomeDBiP05543.
TreeFamiTF343201.

Miscellaneous databases

EvolutionaryTraceiP05543.
GenomeRNAii6906.
NextBioi27007.
PROiP05543.
SOURCEiSearch...

Gene expression databases

BgeeiP05543.
CleanExiHS_SERPINA7.
GenevisibleiP05543. HS.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete amino acid sequence of human thyroxine-binding globulin deduced from cloned DNA: close homology to the serine antiproteases."
    Flink I.L., Bayley T.J., Gustafson T.A., Markham B.E., Morkin E.
    Proc. Natl. Acad. Sci. U.S.A. 83:7708-7712(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Human thyroxine-binding globulin gene: complete sequence and transcriptional regulation."
    Hayashi Y., Mori Y., Janssen O.E., Sunthornthepvarakul T., Weiss R.E., Takeda K., Weinberg M., Seo H., Bell G.I., Refetoff S.
    Mol. Endocrinol. 7:1049-1060(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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.
  7. "Partial amino acid sequence of human thyroxine-binding globulin. Further evidence for a single polypeptide chain."
    Cheng S.-Y.
    Biochem. Biophys. Res. Commun. 79:1212-1218(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-40.
  8. "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-36 AND ASN-165.
    Tissue: Plasma.
  9. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural mechanism for the carriage and release of thyroxine in the blood."
    Zhou A., Wei Z., Read R.J., Carrell R.W.
    Proc. Natl. Acad. Sci. U.S.A. 103:13321-13326(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 39-415 IN COMPLEX WITH THYROXINE.
  12. "Molecular basis of inherited thyroxine-binding globulin defects."
    Janssen O.E., Bertenshaw R., Takeda K., Weiss R., Refetoff S.
    Trends Endocrinol. Metab. 3:49-53(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  13. "Replacement of Leu227 by Pro in thyroxine-binding globulin (TBG) is associated with complete TBG deficiency in three of eight families with this inherited defect."
    Mori Y., Takeda K., Charbonneau M., Refetoff S.
    J. Clin. Endocrinol. Metab. 70:804-809(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY PRO-247.
  14. "A mutation causing reduced biological activity and stability of thyroxine-binding globulin probably as a result of abnormal glycosylation of the molecule."
    Mori Y., Seino S., Takeda K., Flink I.L., Murata Y., Bell G.I., Refetoff S.
    Mol. Endocrinol. 3:575-579(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY ASN-116.
  15. "Thyroxine-binding globulin variant (TBG-Kumamoto): identification of a point mutation and genotype analysis of its family."
    Shirotani T., Kishikawa H., Wake N., Miyamura N., Hashimoto Y., Motoyoshi S., Yamaguchi K., Shichiri M.
    Endocrinol. Jpn. 39:577-584(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY LEU-383.
  16. "Sequence of the variant thyroxine-binding globulin (TBG) in a Montreal family with partial TBG deficiency."
    Janssen O.E., Takeda K., Refetoff S.
    Hum. Genet. 87:119-122(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY PRO-133.
  17. "Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec reveals two nucleotide substitutions."
    Bertenshaw R., Takeda K., Refetoff S.
    Am. J. Hum. Genet. 48:741-744(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY TYR-351.
  18. "Sequencing of the variant thyroxine-binding globulin (TBG)-San Diego reveals two nucleotide substitutions."
    Bertenshaw R., Sarne D., Tornari J., Weinberg M., Refetoff S.
    Biochim. Biophys. Acta 1139:307-310(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG DEFICIENCY THR-43.
  19. "Sequence of the variant thyroxine-binding globulin of Australian aborigines. Only one of two amino acid replacements is responsible for its altered properties."
    Takeda K., Mori Y., Sobieszczyk S., Seo H., Dick M., Watson F., Flink I.L., Seino S., Bell G.I., Refetoff S.
    J. Clin. Invest. 83:1344-1348(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG-A THR-211.
  20. "Molecular basis for the properties of the thyroxine-binding globulin-slow variant in American blacks."
    Waltz M.R., Pullman T.N., Takeda K., Sobieszczyk P., Refetoff S.
    J. Endocrinol. Invest. 13:343-349(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT TBG-S ASN-191.

Entry informationi

Entry nameiTHBG_HUMAN
AccessioniPrimary (citable) accession number: P05543
Secondary accession number(s): D3DUX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.