P16473 · TSHR_HUMAN
- ProteinThyrotropin receptor
- GeneTSHR
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids764 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin (PubMed:12045258).
The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:11847099).
Plays a central role in controlling thyroid cell metabolism (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameThyrotropin receptor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP16473
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-413 | Extracellular | ||||
Sequence: GMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMG | ||||||
Transmembrane | 414-441 | Helical; Name=1 | ||||
Sequence: YKFLRIVVWFVSLLALLGNVFVLLILLT | ||||||
Topological domain | 442-450 | Cytoplasmic | ||||
Sequence: SHYKLNVPR | ||||||
Transmembrane | 451-473 | Helical; Name=2 | ||||
Sequence: FLMCNLAFADFCMGMYLLLIASV | ||||||
Topological domain | 474-494 | Extracellular | ||||
Sequence: DLYTHSEYYNHAIDWQTGPGC | ||||||
Transmembrane | 495-517 | Helical; Name=3 | ||||
Sequence: NTAGFFTVFASELSVYTLTVITL | ||||||
Topological domain | 518-537 | Cytoplasmic | ||||
Sequence: ERWYAITFAMRLDRKIRLRH | ||||||
Transmembrane | 538-560 | Helical; Name=4 | ||||
Sequence: ACAIMVGGWVCCFLLALLPLVGI | ||||||
Topological domain | 561-580 | Extracellular | ||||
Sequence: SSYAKVSICLPMDTETPLAL | ||||||
Transmembrane | 581-602 | Helical; Name=5 | ||||
Sequence: AYIVFVLTLNIVAFVIVCCCYV | ||||||
Topological domain | 603-625 | Cytoplasmic | ||||
Sequence: KIYITVRNPQYNPGDKDTKIAKR | ||||||
Transmembrane | 626-649 | Helical; Name=6 | ||||
Sequence: MAVLIFTDFICMAPISFYALSAIL | ||||||
Topological domain | 650-660 | Extracellular | ||||
Sequence: NKPLITVSNSK | ||||||
Transmembrane | 661-682 | Helical; Name=7 | ||||
Sequence: ILLVLFYPLNSCANPFLYAIFT | ||||||
Topological domain | 683-764 | Cytoplasmic | ||||
Sequence: KAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHEMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Hypothyroidism, congenital, non-goitrous, 1 (CHNG1)
- Note
- DescriptionA non-autoimmune condition characterized by resistance to thyroid-stimulating hormone (TSH) leading to increased levels of plasma TSH and low levels of thyroid hormone. It presents variable severity depending on the completeness of the defect. Most patients are euthyroid and asymptomatic, with a normal sized thyroid gland. Only a subset of patients develop hypothyroidism and present a hypoplastic thyroid gland.
- See alsoMIM:275200
Natural variants in CHNG1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_011519 | 41 | C>S | in CHNG1 | |
VAR_011520 | 109 | R>Q | in CHNG1 | |
VAR_011521 | 162 | P>A | in CHNG1; dbSNP:rs121908863 | |
VAR_011522 | 167 | I>N | in CHNG1 | |
VAR_021495 | 252 | L>P | in CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production | |
VAR_011524 | 310 | R>C | in CHNG1 | |
VAR_011525 | 390 | C>W | in CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding | |
VAR_011526 | 410 | D>N | in CHNG1; lack of adenylate cyclase activation | |
VAR_075585 | 432 | N>D | in CHNG1; abolishes cell membrane location; abolishes adenylate cyclase-activating G-protein coupled receptor signaling pathway; abolishes phospholipase C-activating G-protein coupled receptor signaling pathway | |
VAR_075586 | 449 | P>L | in CHNG1; no effect on cell membrane location; upon TSH stimulation decreases more phospholipase C-activating G-protein coupled receptor signaling pathway than adenylate cyclase-activating G-protein coupled receptor signaling pathway | |
VAR_011528 | 450 | R>H | in CHNG1 | |
VAR_017295 | 467 | L>P | in CHNG1 | |
VAR_017296 | 477 | T>I | in CHNG1; severe hypothyroidism | |
VAR_011533 | 498 | G>S | in CHNG1 | |
VAR_011537 | 525 | F>L | in CHNG1; impairs adenylate cyclase activation | |
VAR_011538 | 553 | A>T | in CHNG1; severe hypothyroidism | |
VAR_017297 | 600 | C>R | in CHNG1 |
Familial gestational hyperthyroidism (HTFG)
- Note
- DescriptionA condition characterized by abnormally high levels of serum thyroid hormones occurring during early pregnancy.
- See alsoMIM:603373
Natural variants in HTFG
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003566 | 183 | K>R | in HTFG; enhances receptor response to chorionic gonadotropin |
Hyperthyroidism, non-autoimmune (HTNA)
- Note
- DescriptionA condition characterized by abnormally high levels of serum thyroid hormones, thyroid hyperplasia, goiter and lack of anti-thyroid antibodies. Typical features of Graves disease such as exophthalmia, myxedema, antibodies anti-TSH receptor and lymphocytic infiltration of the thyroid gland are absent.
- See alsoMIM:609152
Natural variants in HTNA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003570 | 281 | S>N | in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |
VAR_011527 | 431 | G>S | in HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system | |
VAR_011529 | 453 | M>T | in HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |
VAR_011530 | 463 | M>V | in HTNA; gain of function | |
VAR_011531 | 486 | I>F | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma | |
VAR_011532 | 486 | I>M | in HTNA; found in hyperfunctioning thyroid adenomas | |
VAR_003571 | 505 | S>N | in HTNA; found in toxic thyroid nodules | |
VAR_011534 | 505 | S>R | in HTNA; gain of function | |
VAR_011535 | 509 | V>A | in HTNA; gain of function | |
VAR_011539 | 568 | I>T | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |
VAR_021499 | 597 | V>F | in HTNA; 11-fold increase in specific constitutive activity; decreased receptor protein expression | |
VAR_003575 | 629 | L>F | in HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules | |
VAR_011545 | 631 | F>L | in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |
VAR_011546 | 632 | T>A | in HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules | |
VAR_011547 | 632 | T>I | in HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |
VAR_011549 | 633 | D>E | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |
VAR_011552 | 639 | P>S | in HTNA; gain of function | |
VAR_011553 | 647 | A>V | in HTNA; found in non-adenomatous hyperfunctioning nodules | |
VAR_011554 | 650 | N>Y | in HTNA; gain of function | |
VAR_011556 | 670 | N>S | in HTNA; gain of function | |
VAR_011557 | 672 | C>Y | in HTNA; gain of function |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055925 | 34 | in dbSNP:rs45499704 | |||
Sequence: E → K | ||||||
Natural variant | VAR_003564 | 36 | in a patient with Graves disease; dbSNP:rs61747482 | |||
Sequence: D → H | ||||||
Natural variant | VAR_011519 | 41 | in CHNG1 | |||
Sequence: C → S | ||||||
Natural variant | VAR_003565 | 52 | does not contribute to the genetic susceptibility to Graves disease; dbSNP:rs2234919 | |||
Sequence: P → T | ||||||
Natural variant | VAR_011520 | 109 | in CHNG1 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_011521 | 162 | in CHNG1; dbSNP:rs121908863 | |||
Sequence: P → A | ||||||
Natural variant | VAR_011522 | 167 | in CHNG1 | |||
Sequence: I → N | ||||||
Natural variant | VAR_003566 | 183 | in HTFG; enhances receptor response to chorionic gonadotropin | |||
Sequence: K → R | ||||||
Natural variant | VAR_003567 | 197 | in papillary cancer | |||
Sequence: F → I | ||||||
Natural variant | VAR_003568 | 219 | in papillary cancer | |||
Sequence: D → E | ||||||
Natural variant | VAR_021495 | 252 | in CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production | |||
Sequence: L → P | ||||||
Natural variant | VAR_003569 | 281 | in hyperthyroidism; congenital; due to a toxic adenoma | |||
Sequence: S → I | ||||||
Natural variant | VAR_003570 | 281 | in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |||
Sequence: S → N | ||||||
Natural variant | VAR_011523 | 281 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas | |||
Sequence: S → T | ||||||
Mutagenesis | 283 | Abolishes cell surface expression. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_011524 | 310 | in CHNG1 | |||
Sequence: R → C | ||||||
Mutagenesis | 385 | Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 385 | Reduces sulfation. Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 385-387 | Inhibits intracellular cAMP accumulation. | ||||
Sequence: YDY → EDE | ||||||
Mutagenesis | 385-387 | Abolishes sulfation. Inhibits intracellular cAMP accumulation. | ||||
Sequence: YDY → FDF | ||||||
Mutagenesis | 387 | No change in intracellular cAMP accumulation. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 387 | Reduces sulfation. No change in intracellular cAMP accumulation. | ||||
Sequence: Y → F | ||||||
Natural variant | VAR_011525 | 390 | in CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding | |||
Sequence: C → W | ||||||
Natural variant | VAR_011526 | 410 | in CHNG1; lack of adenylate cyclase activation | |||
Sequence: D → N | ||||||
Natural variant | VAR_021496 | 425 | found in toxic thyroid nodules; 8 to 9 times higher levels of basal cAMP than wild-type TSHR and similar response to maximal TSH stimulation | |||
Sequence: S → I | ||||||
Natural variant | VAR_011527 | 431 | in HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system | |||
Sequence: G → S | ||||||
Natural variant | VAR_075585 | 432 | in CHNG1; abolishes cell membrane location; abolishes adenylate cyclase-activating G-protein coupled receptor signaling pathway; abolishes phospholipase C-activating G-protein coupled receptor signaling pathway | |||
Sequence: N → D | ||||||
Natural variant | VAR_075586 | 449 | in CHNG1; no effect on cell membrane location; upon TSH stimulation decreases more phospholipase C-activating G-protein coupled receptor signaling pathway than adenylate cyclase-activating G-protein coupled receptor signaling pathway | |||
Sequence: P → L | ||||||
Natural variant | VAR_011528 | 450 | in CHNG1 | |||
Sequence: R → H | ||||||
Natural variant | VAR_011529 | 453 | in HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |||
Sequence: M → T | ||||||
Natural variant | VAR_011530 | 463 | in HTNA; gain of function | |||
Sequence: M → V | ||||||
Natural variant | VAR_017295 | 467 | in CHNG1 | |||
Sequence: L → P | ||||||
Natural variant | VAR_017296 | 477 | in CHNG1; severe hypothyroidism | |||
Sequence: T → I | ||||||
Natural variant | VAR_011531 | 486 | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma | |||
Sequence: I → F | ||||||
Natural variant | VAR_011532 | 486 | in HTNA; found in hyperfunctioning thyroid adenomas | |||
Sequence: I → M | ||||||
Natural variant | VAR_011533 | 498 | in CHNG1 | |||
Sequence: G → S | ||||||
Natural variant | VAR_003571 | 505 | in HTNA; found in toxic thyroid nodules | |||
Sequence: S → N | ||||||
Natural variant | VAR_011534 | 505 | in HTNA; gain of function | |||
Sequence: S → R | ||||||
Natural variant | VAR_011535 | 509 | in HTNA; gain of function | |||
Sequence: V → A | ||||||
Natural variant | VAR_021497 | 512 | found in toxic thyroid nodules; 5 times higher levels of basal cAMP than wild-type TSHR and slightly less response to maximal TSH stimulation | |||
Sequence: L → Q | ||||||
Natural variant | VAR_011536 | 512 | in hyperthyroidism; found in autonomously functioning thyroid nodules; 3.3-fold increase in basal cAMP level | |||
Sequence: L → R | ||||||
Natural variant | VAR_011537 | 525 | in CHNG1; impairs adenylate cyclase activation | |||
Sequence: F → L | ||||||
Natural variant | VAR_003572 | 528 | ||||
Sequence: R → H | ||||||
Natural variant | VAR_011538 | 553 | in CHNG1; severe hypothyroidism | |||
Sequence: A → T | ||||||
Natural variant | VAR_011539 | 568 | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |||
Sequence: I → T | ||||||
Natural variant | VAR_021498 | 593 | in toxic thyroid adenoma; somatic mutation; constitutively activates the cAMP cascade; requires 2 nucleotide substitutions | |||
Sequence: A → N | ||||||
Natural variant | VAR_021499 | 597 | in HTNA; 11-fold increase in specific constitutive activity; decreased receptor protein expression | |||
Sequence: V → F | ||||||
Natural variant | VAR_011540 | 597 | in hyperthyroidism; congenital with severe thyrotoxicosis | |||
Sequence: V → L | ||||||
Natural variant | VAR_017297 | 600 | in CHNG1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_011541 | 606 | ||||
Sequence: I → M | ||||||
Natural variant | VAR_003573 | 619 | in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |||
Sequence: D → G | ||||||
Natural variant | VAR_003574 | 623 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas; gain of function; requires 2 nucleotide substitutions | |||
Sequence: A → I | ||||||
Natural variant | VAR_011542 | 623 | in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas; gain of function | |||
Sequence: A → V | ||||||
Natural variant | VAR_003575 | 629 | in HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules | |||
Sequence: L → F | ||||||
Natural variant | VAR_011543 | 630 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas | |||
Sequence: I → L | ||||||
Natural variant | VAR_011544 | 631 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas | |||
Sequence: F → C | ||||||
Natural variant | VAR_011545 | 631 | in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |||
Sequence: F → L | ||||||
Natural variant | VAR_011546 | 632 | in HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules | |||
Sequence: T → A | ||||||
Natural variant | VAR_011547 | 632 | in HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |||
Sequence: T → I | ||||||
Natural variant | VAR_011548 | 633 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas | |||
Sequence: D → A | ||||||
Natural variant | VAR_011549 | 633 | in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas | |||
Sequence: D → E | ||||||
Natural variant | VAR_011550 | 633 | in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas; also found in hyperfunctioning insular carcinoma; gain of function; dbSNP:rs28937584 | |||
Sequence: D → H | ||||||
Natural variant | VAR_011551 | 633 | in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas | |||
Sequence: D → Y | ||||||
Natural variant | VAR_021500 | 639 | found in toxic thyroid nodules | |||
Sequence: P → A | ||||||
Natural variant | VAR_011552 | 639 | in HTNA; gain of function | |||
Sequence: P → S | ||||||
Natural variant | VAR_011553 | 647 | in HTNA; found in non-adenomatous hyperfunctioning nodules | |||
Sequence: A → V | ||||||
Natural variant | VAR_011554 | 650 | in HTNA; gain of function | |||
Sequence: N → Y | ||||||
Natural variant | VAR_021501 | 656 | found in toxic thyroid nodules | |||
Sequence: V → F | ||||||
Natural variant | VAR_011555 | 658-661 | in hyperthyroidism; found in hyperfunctioning thyroid adenomas | |||
Sequence: Missing | ||||||
Natural variant | VAR_011556 | 670 | in HTNA; gain of function | |||
Sequence: N → S | ||||||
Natural variant | VAR_011557 | 672 | in HTNA; gain of function | |||
Sequence: C → Y | ||||||
Natural variant | VAR_011558 | 677 | in thyroid carcinoma; with thyrotoxicosis; gain of function | |||
Sequence: L → V | ||||||
Natural variant | VAR_011559 | 703 | ||||
Sequence: A → G | ||||||
Natural variant | VAR_003576 | 715 | in papillary cancer | |||
Sequence: N → D | ||||||
Natural variant | VAR_011560 | 720 | ||||
Sequence: Q → E | ||||||
Natural variant | VAR_003577 | 723 | in papillary cancer | |||
Sequence: K → M | ||||||
Natural variant | VAR_003578 | 727 | no effect on thyroid-stimulating hormone receptor activity; dbSNP:rs1991517 | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 70 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MRPADLLQLVLLLDLPRDLG | ||||||
Chain | PRO_0000012786 | 21-764 | Thyrotropin receptor | |||
Sequence: GMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHEMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL | ||||||
Disulfide bond | 31↔41 | |||||
Sequence: CHQEEDFRVTC | ||||||
Glycosylation | 77 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 177 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 385 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Disulfide bond | 494↔569 | |||||
Sequence: CNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSIC |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via the PDZ-binding motif) with SCRIB; regulates TSHR trafficking and function (PubMed:15775968).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P16473 | ADORA1 P30542 | 2 | EBI-13939599, EBI-2903663 | |
BINARY | P16473 | MID1IP1 Q9NPA3 | 2 | EBI-13939599, EBI-750096 | |
BINARY | P16473 | SCRIB Q14160 | 3 | EBI-13939599, EBI-357345 | |
BINARY | P16473 | SYT1 P21579 | 2 | EBI-13939599, EBI-524909 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 100-124 | LRR 1 | ||||
Sequence: LSKVTHIEIRNTRNLTYIDPDALKE | ||||||
Repeat | 125-150 | LRR 2 | ||||
Sequence: LPLLKFLGIFNTGLKMFPDLTKVYST | ||||||
Repeat | 152-174 | LRR 3 | ||||
Sequence: IFFILEITDNPYMTSIPVNAFQG | ||||||
Repeat | 176-199 | LRR 4 | ||||
Sequence: CNETLTLKLYNNGFTSVQGYAFNG | ||||||
Repeat | 200-223 | LRR 5 | ||||
Sequence: TKLDAVYLNKNKYLTVIDKDAFGG | ||||||
Repeat | 227-248 | LRR 6 | ||||
Sequence: GPSLLDVSQTSVTALPSKGLEH | ||||||
Repeat | 250-271 | LRR 7 | ||||
Sequence: KELIARNTWTLKKLPLSLSFLH | ||||||
Motif | 762-764 | PDZ-binding | ||||
Sequence: TVL |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing. Additional isoforms seem to exist.
P16473-1
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.
- NameLong
- Length764
- Mass (Da)86,844
- Last updated2024-10-02 v3
- Checksum27EE9CEBFD650D45
P16473-2
- NameShort
P16473-3
- Name3
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y709 | A0A2R8Y709_HUMAN | TSHR | 89 | ||
A0A1B0GUJ5 | A0A1B0GUJ5_HUMAN | TSHR | 399 | ||
G3V381 | G3V381_HUMAN | TSHR | 112 | ||
Q0VAP8 | Q0VAP8_HUMAN | TSHR | 231 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 87 | in Ref. 2; no nucleotide entry | ||||
Sequence: V → L | ||||||
Sequence conflict | 196-198 | in Ref. 4; AAA70232 | ||||
Sequence: AFN → DFF | ||||||
Alternative sequence | VSP_001981 | 232-253 | in isoform Short | |||
Sequence: DVSQTSVTALPSKGLEHLKELI → LPLGRKSLSFETQKAPRSSMPS | ||||||
Alternative sequence | VSP_044643 | 232-274 | in isoform 3 | |||
Sequence: DVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTR → VENVAVSGKGFCKSLFSWLYRLPLGRKSLSFETQKAPRSSMPS | ||||||
Sequence conflict | 239 | In isoform P16473-2; in Ref. 6; AAB24246 | ||||
Sequence: L → F | ||||||
Sequence conflict | 248 | In isoform P16473-2; in Ref. 5; AAB23390 and 9; AAH09237/AAI20974 | ||||
Sequence: R → S | ||||||
Sequence conflict | 251 | In isoform P16473-2; in Ref. 5; AAB23390 | ||||
Sequence: M → T | ||||||
Alternative sequence | VSP_001982 | 254-764 | in isoform Short | |||
Sequence: Missing | ||||||
Sequence conflict | 257 | in Ref. 4; AAA70232 | ||||
Sequence: T → S | ||||||
Sequence conflict | 264 | in Ref. 4; AAA70232 | ||||
Sequence: P → A | ||||||
Sequence conflict | 269 | In isoform P16473-3; in Ref. 9; AAI27629 | ||||
Sequence: R → S | ||||||
Alternative sequence | VSP_044644 | 275-764 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 306-308 | in Ref. 4; AAA70232 | ||||
Sequence: MQS → IET | ||||||
Sequence conflict | 528 | in Ref. 4; AAA70232 | ||||
Sequence: R → A | ||||||
Sequence conflict | 601 | in Ref. 1; AAA36783 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 635 | in Ref. 4; AAA70232 | ||||
Sequence: I → T | ||||||
Sequence conflict | 645 | in Ref. 4; AAA70232 | ||||
Sequence: L → V | ||||||
Sequence conflict | 669 | in Ref. 4; AAA70232 | ||||
Sequence: L → I | ||||||
Sequence conflict | 744 | in Ref. 3; AAA61236 | ||||
Sequence: N → K |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M31774 EMBL· GenBank· DDBJ | AAA36783.1 EMBL· GenBank· DDBJ | mRNA | ||
M32215 EMBL· GenBank· DDBJ | AAA61236.1 EMBL· GenBank· DDBJ | mRNA | ||
M73747 EMBL· GenBank· DDBJ | AAA70232.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
S45272 EMBL· GenBank· DDBJ | AAB23390.2 EMBL· GenBank· DDBJ | mRNA | ||
S49816 EMBL· GenBank· DDBJ | AAB24246.1 EMBL· GenBank· DDBJ | mRNA | ||
AY429111 EMBL· GenBank· DDBJ | AAR07906.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007262 EMBL· GenBank· DDBJ | AAD31568.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC010072 EMBL· GenBank· DDBJ | AAF09032.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC010582 EMBL· GenBank· DDBJ | AAF26775.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL136040 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC009237 EMBL· GenBank· DDBJ | AAH09237.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024205 EMBL· GenBank· DDBJ | AAH24205.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063613 EMBL· GenBank· DDBJ | AAH63613.1 EMBL· GenBank· DDBJ | mRNA | ||
BC108653 EMBL· GenBank· DDBJ | AAI08654.1 EMBL· GenBank· DDBJ | mRNA | ||
BC120973 EMBL· GenBank· DDBJ | AAI20974.1 EMBL· GenBank· DDBJ | mRNA | ||
BC127628 EMBL· GenBank· DDBJ | AAI27629.1 EMBL· GenBank· DDBJ | mRNA | ||
BC141970 EMBL· GenBank· DDBJ | AAI41971.1 EMBL· GenBank· DDBJ | mRNA |