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P05543

- THBG_HUMAN

UniProt

P05543 - THBG_HUMAN

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Protein
Thyroxine-binding globulin
Gene
SERPINA7, TBG
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 2931Thyroxine
Binding sitei398 – 3981Thyroxine

GO - Molecular functioni

  1. hormone binding Source: Ensembl
  2. serine-type endopeptidase inhibitor activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. aging Source: Ensembl
  2. negative regulation of endopeptidase activity Source: RefGenome
  3. post-embryonic development Source: Ensembl
  4. regulation of proteolysis Source: RefGenome
  5. response to corticosterone Source: Ensembl
  6. response to drug Source: Ensembl
  7. response to peptide hormone Source: Ensembl
  8. response to prostaglandin E Source: Ensembl
  9. response to vitamin A Source: Ensembl
  10. thyroid hormone transport Source: UniProt
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
Synonyms:TBG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11583. SERPINA7.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: ProtInc
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Thyroxine-binding globulin deficiency (TBG deficiency) [MIM:314200]: Mutations 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 Publication
Add
BLAST
Chaini21 – 415395Thyroxine-binding globulin
PRO_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 Gary Inferred
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.
GenevestigatoriP05543.

Organism-specific databases

HPAiHPA002803.

Interactioni

Protein-protein interaction databases

BioGridi112769. 1 interaction.
STRINGi9606.ENSP00000329374.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP05543.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
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

MSPFLYLVLL VLGLHATIHC ASPEGKVTAC HSSQPNATLY KMSSINADFA    50
FNLYRRFTVE TPDKNIFFSP VSISAALVML SFGACCSTQT EIVETLGFNL 100
TDTPMVEIQH GFQHLICSLN FPKKELELQI GNALFIGKHL KPLAKFLNDV 150
KTLYETEVFS TDFSNISAAK QEINSHVEMQ TKGKVVGLIQ DLKPNTIMVL 200
VNYIHFKAQW ANPFDPSKTE DSSSFLIDKT TTVQVPMMHQ MEQYYHLVDM 250
ELNCTVLQMD YSKNALALFV LPKEGQMESV EAAMSSKTLK KWNRLLQKGW 300
VDLFVPKFSI SATYDLGATL LKMGIQHAYS ENADFSGLTE DNGLKLSNAA 350
HKAVLHIGEK GTEAAAVPEV ELSDQPENTF LHPIIQIDRS FMLLILERST 400
RSILFLGKVV NPTEA 415
Length:415
Mass (Da):46,325
Last modified:February 1, 1996 - v2
Checksum:i8B24EF8C7CEF8F0A
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 312CH → DS AA sequence 1 Publication
Sequence conflicti38 – 381T → S AA sequence 1 Publication
Sequence conflicti197 – 1971I → T in AAA60616. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi1351236.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14518.1.
PIRi A47224.
RefSeqi NP_000345.2. NM_000354.5.
UniGenei Hs.76838.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CEO X-ray 2.80 A/B 39-415 [» ]
2RIV X-ray 1.50 A 33-386 [» ]
B 376-415 [» ]
2RIW X-ray 2.04 A 39-386 [» ]
B 376-415 [» ]
2XN3 X-ray 2.09 A 33-386 [» ]
B 377-415 [» ]
2XN5 X-ray 1.70 A 32-380 [» ]
B 381-415 [» ]
2XN6 X-ray 1.29 A 32-380 [» ]
B 381-415 [» ]
2XN7 X-ray 1.43 A 32-380 [» ]
B 381-415 [» ]
ProteinModelPortali P05543.
SMRi P05543. Positions 37-415.
ModBasei Search...

Protein-protein interaction databases

BioGridi 112769. 1 interaction.
STRINGi 9606.ENSP00000329374.

Chemistry

ChEMBLi CHEMBL3843.
DrugBanki DB00451. Levothyroxine.
DB00279. Liothyronine.

Protein family/group databases

MEROPSi I04.955.

PTM databases

PhosphoSitei P05543.

Polymorphism databases

DMDMi 1351236.

Proteomic databases

MaxQBi P05543.
PaxDbi P05543.
PeptideAtlasi P05543.
PRIDEi P05543.

Protocols and materials databases

DNASUi 6906.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327674 ; ENSP00000329374 ; ENSG00000123561 .
ENST00000372563 ; ENSP00000361644 ; ENSG00000123561 .
GeneIDi 6906.
KEGGi hsa:6906.
UCSCi uc004eme.2. human.

Organism-specific databases

CTDi 6906.
GeneCardsi GC0XM105277.
HGNCi HGNC:11583. SERPINA7.
HPAi HPA002803.
MIMi 314200. gene+phenotype.
neXtProti NX_P05543.
Orphaneti 209893. Congenital isolated thyroxine-binding globulin deficiency.
PharmGKBi PA36347.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4826.
HOGENOMi HOG000238521.
HOVERGENi HBG005957.
InParanoidi P05543.
OMAi FNLTDTP.
OrthoDBi EOG7QC7W9.
PhylomeDBi P05543.
TreeFami TF343201.

Miscellaneous databases

EvolutionaryTracei P05543.
GenomeRNAii 6906.
NextBioi 27007.
PROi P05543.
SOURCEi Search...

Gene expression databases

Bgeei P05543.
CleanExi HS_SERPINA7.
Genevestigatori P05543.

Family and domain databases

InterProi IPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view ]
PANTHERi PTHR11461. PTHR11461. 1 hit.
Pfami PF00079. Serpin. 1 hit.
[Graphical view ]
SMARTi SM00093. SERPIN. 1 hit.
[Graphical view ]
SUPFAMi SSF56574. SSF56574. 1 hit.
PROSITEi PS00284. SERPIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 158 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

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