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P05543

- THBG_HUMAN

UniProt

P05543 - THBG_HUMAN

Protein

Thyroxine-binding globulin

Gene

SERPINA7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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

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

    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

    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: 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

    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.6 Publications
    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 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.
    GenevestigatoriP05543.

    Organism-specific databases

    HPAiHPA002803.

    Interactioni

    Protein-protein interaction databases

    BioGridi112769. 1 interaction.
    STRINGi9606.ENSP00000329374.

    Structurei

    Secondary structure

    1
    415
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05543.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    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

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 159 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