Reviewed,
UniProtKB/Swiss-Prot P01266 (THYG_HUMAN)
Last modified
November 25, 2008.
Version 108.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Thyroglobulin Short name=Tg | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 2768 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 | Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Thyroid gland specific. |
| Post-translational modification | Sulfated. |
| Involvement in disease | Defects in TG are a cause of some forms of goiter [MIM:188450]. Goiter is an enlargement of the thyroid gland. This is sometimes linked to hypothyroidism. Variations in TG are associated with susceptibility to autoimmune thyroid disease type 3 (AITD3) [MIM:608175]. AITDs including Graves disease (GD) and Hashimoto thyroiditis (HT), are among the most common human autoimmune diseases. They are complex diseases, which are caused by an interaction between susceptibility genes and nongenetic factors, such as infection. |
| Sequence similarities | Belongs to the type-B carboxylesterase/lipase family. Contains 11 thyroglobulin type-1 domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Thyroid hormones biosynthesis |
| Cellular component | Secreted |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Disease mutation |
| Domain | Repeat Signal |
| Molecular function | Hormone Thyroid hormone |
| PTM | Glycoprotein Iodination Sulfation |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW signal transductionNon-traceable author statement. Source: ProtInc thyroid hormone generationInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Non-traceable author statement. Source: UniProtKB |
| Molecular function | hormone activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P01266-1) Also known as: Major; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: P01266-2) Also known as: Minor; The sequence of this isoform differs from the canonical sequence as follows: 1510-1567: CVTDCQRNEAGLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWWETEAPLEDSQCLM → L |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | |||||||||
| Chain | 20 – 2768 | 2749 | Thyroglobulin | PRO_0000008636 | |||||||
Regions | |||||||||||
| Domain | 31 – 92 | 62 | Thyroglobulin type-1 1 | ||||||||
| Domain | 93 – 160 | 68 | Thyroglobulin type-1 2 | ||||||||
| Domain | 161 – 297 | 137 | Thyroglobulin type-1 3 | ||||||||
| Domain | 298 – 358 | 61 | Thyroglobulin type-1 4 | ||||||||
| Domain | 605 – 658 | 54 | Thyroglobulin type-1 5 | ||||||||
| Domain | 659 – 726 | 68 | Thyroglobulin type-1 6 | ||||||||
| Domain | 727 – 921 | 195 | Thyroglobulin type-1 7 | ||||||||
| Domain | 922 – 1073 | 152 | Thyroglobulin type-1 8 | ||||||||
| Domain | 1074 – 1145 | 72 | Thyroglobulin type-1 9 | ||||||||
| Domain | 1146 – 1210 | 65 | Thyroglobulin type-1 10 | ||||||||
| Repeat | 1456 – 1469 | 14 | Type II | ||||||||
| Repeat | 1470 – 1486 | 17 | Type II | ||||||||
| Repeat | 1487 – 1503 | 17 | Type II | ||||||||
| Domain | 1511 – 1565 | 55 | Thyroglobulin type-1 11 | ||||||||
| Repeat | 1603 – 1723 | 121 | Type IIIA | ||||||||
| Repeat | 1724 – 1892 | 169 | Type IIIB | ||||||||
| Repeat | 1893 – 1995 | 103 | Type IIIA | ||||||||
| Repeat | 1996 – 2129 | 134 | Type IIIB | ||||||||
| Repeat | 2130 – 2187 | 58 | Type IIIA | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 24 | 1 | Sulfotyrosine | ||||||||
| Modified residue | 24 | 1 | Thyroxine | ||||||||
| Modified residue | 1310 | 1 | Thyroxine | ||||||||
| Modified residue | 2573 | 1 | Thyroxine | ||||||||
| Modified residue | 2587 | 1 | Thyroxine | ||||||||
| Modified residue | 2766 | 1 | Triiodothyronine | ||||||||
| Glycosylation | 76 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 110 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 198 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 484 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 496 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 529 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 748 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 816 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 947 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1220 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1348 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1349 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1365 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1716 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1774 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1869 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2013 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2122 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2250 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2295 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2582 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 34 ↔ 52 | By similarity | |||||||||
| Disulfide bond | 63 ↔ 70 | By similarity | |||||||||
| Disulfide bond | 72 ↔ 92 | By similarity | |||||||||
| Disulfide bond | 96 ↔ 120 | By similarity | |||||||||
| Disulfide bond | 131 ↔ 138 | By similarity | |||||||||
| Disulfide bond | 140 ↔ 160 | By similarity | |||||||||
| Disulfide bond | 164 ↔ 183 | By similarity | |||||||||
| Disulfide bond | 194 ↔ 235 | By similarity | |||||||||
| Disulfide bond | 301 ↔ 319 | By similarity | |||||||||
| Disulfide bond | 330 ↔ 336 | By similarity | |||||||||
| Disulfide bond | 338 ↔ 358 | By similarity | |||||||||
| Disulfide bond | 608 ↔ 620 | By similarity | |||||||||
| Disulfide bond | 631 ↔ 636 | By similarity | |||||||||
| Disulfide bond | 638 ↔ 658 | By similarity | |||||||||
| Disulfide bond | 662 ↔ 687 | By similarity | |||||||||
| Disulfide bond | 698 ↔ 703 | By similarity | |||||||||
| Disulfide bond | 705 ↔ 726 | By similarity | |||||||||
| Disulfide bond | 730 ↔ 763 | By similarity | |||||||||
| Disulfide bond | 774 ↔ 898 | By similarity | |||||||||
| Disulfide bond | 900 ↔ 921 | By similarity | |||||||||
| Disulfide bond | 1042 ↔ 1049 | By similarity | |||||||||
| Disulfide bond | 1051 ↔ 1073 | By similarity | |||||||||
| Disulfide bond | 1077 ↔ 1108 | By similarity | |||||||||
| Disulfide bond | 1126 ↔ 1145 | By similarity | |||||||||
| Disulfide bond | 1149 ↔ 1169 | By similarity | |||||||||
| Disulfide bond | 1181 ↔ 1188 | By similarity | |||||||||
| Disulfide bond | 1190 ↔ 1210 | By similarity | |||||||||
| Disulfide bond | 1514 ↔ 1523 | By similarity | |||||||||
| Disulfide bond | 1543 ↔ 1565 | By similarity | |||||||||
| Disulfide bond | 2264 ↔ 2281 | Potential | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1510 – 1567 | 58 | CVTDC…SQCLM → L in isoform 2. | VSP_012655 | |||||||
| Natural variant | 135 | 1 | Q → H: dbSNP rs2069546. | VAR_010212 | |||||||
| Natural variant | 515 | 1 | Q → E: dbSNP rs180222. | VAR_016190 | |||||||
| Natural variant | 604 | 1 | S → D Requires 2 nucleotide substitutions. | VAR_016852 | |||||||
| Natural variant | 653 | 1 | G → D: dbSNP rs2069548. | VAR_016853 | |||||||
| Natural variant | 734 | 1 | S → A Polymorphism associated with AITD3. dbSNP rs180223. | VAR_010213 | |||||||
| Natural variant | 830 | 1 | Q → E: dbSNP rs2076737. | VAR_010214 | |||||||
| Natural variant | 870 | 1 | Q → H in goiter; simple. dbSNP rs2229843. | VAR_002365 | |||||||
| Natural variant | 985 | 1 | Missing | VAR_016854 | |||||||
| Natural variant | 1028 | 1 | M → V Polymorphism associated with AITD3. dbSNP rs853326. | VAR_010215 | |||||||
| Natural variant | 1043 | 1 | H → Y | VAR_016855 | |||||||
| Natural variant | 1059 | 1 | I → T | ||||||||

Clusters with