P16473 · TSHR_HUMAN

  • Protein
    Thyrotropin receptor
  • Gene
    TSHR
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin (PubMed:11847099, PubMed:12045258).
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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentbasolateral plasma membrane
Cellular Componentcell surface
Cellular Componentplasma membrane
Cellular Componentreceptor complex
Molecular FunctionG protein-coupled peptide receptor activity
Molecular Functionprotein-containing complex binding
Molecular Functionsignaling receptor activity
Molecular Functionthyroid-stimulating hormone receptor activity
Biological Processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Biological Processcell surface receptor signaling pathway
Biological Processcell-cell signaling
Biological Processcellular response to glycoprotein
Biological Processcellular response to thyrotropin-releasing hormone
Biological ProcessG protein-coupled receptor signaling pathway
Biological ProcessG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
Biological Processhormone-mediated signaling pathway
Biological Processpositive regulation of cell population proliferation
Biological Processpositive regulation of cold-induced thermogenesis
Biological Processthyroid-stimulating hormone signaling pathway

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Thyrotropin receptor
  • Alternative names
    • Thyroid-stimulating hormone receptor (TSH-R)

Gene names

    • Name
      TSHR
    • Synonyms
      LGR3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P16473
  • Secondary accessions
    • A0A0A0MTJ0
    • A0PJU7
    • F5GYU5
    • G3V2A9
    • Q16503

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Basolateral cell membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain21-413Extracellular
Transmembrane414-441Helical; Name=1
Topological domain442-450Cytoplasmic
Transmembrane451-473Helical; Name=2
Topological domain474-494Extracellular
Transmembrane495-517Helical; Name=3
Topological domain518-537Cytoplasmic
Transmembrane538-560Helical; Name=4
Topological domain561-580Extracellular
Transmembrane581-602Helical; Name=5
Topological domain603-625Cytoplasmic
Transmembrane626-649Helical; Name=6
Topological domain650-660Extracellular
Transmembrane661-682Helical; Name=7
Topological domain683-764Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

  • Defects in TSHR are found in patients affected by hyperthyroidism with different etiologies. Somatic, constitutively activating TSHR mutations and/or constitutively activating G(s)alpha mutations have been identified in toxic thyroid nodules (TTNs) that are the predominant cause of hyperthyroidism in iodine deficient areas. These mutations lead to TSH independent activation of the cAMP cascade resulting in thyroid growth and hormone production. TSHR mutations are found in autonomously functioning thyroid nodules (AFTN), toxic multinodular goiter (TMNG) and hyperfunctioning thyroid adenomas (HTA). TMNG encompasses a spectrum of different clinical entities, ranging from a single hyperfunctioning nodule within an enlarged thyroid, to multiple hyperfunctioning areas scattered throughout the gland. HTA are discrete encapsulated neoplasms characterized by TSH-independent autonomous growth, hypersecretion of thyroid hormones, and TSH suppression. Defects in TSHR are also a cause of thyroid neoplasms (papillary and follicular cancers)
  • Autoantibodies against TSHR are directly responsible for the pathogenesis and hyperthyroidism of Graves disease. Antibody interaction with TSHR results in an uncontrolled receptor stimulation

Hypothyroidism, congenital, non-goitrous, 1 (CHNG1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A 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 also
    MIM:275200
Natural variants in CHNG1
Variant IDPosition(s)ChangeDescription
VAR_01151941C>Sin CHNG1
VAR_011520109R>Qin CHNG1
VAR_011521162P>Ain CHNG1; dbSNP:rs121908863
VAR_011522167I>Nin CHNG1
VAR_021495252L>Pin CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production
VAR_011524310R>Cin CHNG1
VAR_011525390C>Win CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding
VAR_011526410D>Nin CHNG1; lack of adenylate cyclase activation
VAR_075585432N>Din 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_075586449P>Lin 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_011528450R>Hin CHNG1
VAR_017295467L>Pin CHNG1
VAR_017296477T>Iin CHNG1; severe hypothyroidism
VAR_011533498G>Sin CHNG1
VAR_011537525F>Lin CHNG1; impairs adenylate cyclase activation
VAR_011538553A>Tin CHNG1; severe hypothyroidism
VAR_017297600C>Rin CHNG1

Familial gestational hyperthyroidism (HTFG)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A condition characterized by abnormally high levels of serum thyroid hormones occurring during early pregnancy.
  • See also
    MIM:603373
Natural variants in HTFG
Variant IDPosition(s)ChangeDescription
VAR_003566183K>Rin HTFG; enhances receptor response to chorionic gonadotropin

Hyperthyroidism, non-autoimmune (HTNA)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A 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 also
    MIM:609152
Natural variants in HTNA
Variant IDPosition(s)ChangeDescription
VAR_003570281S>Nin HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
VAR_011527431G>Sin HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system
VAR_011529453M>Tin HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
VAR_011530463M>Vin HTNA; gain of function
VAR_011531486I>Fin HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma
VAR_011532486I>Min HTNA; found in hyperfunctioning thyroid adenomas
VAR_003571505S>Nin HTNA; found in toxic thyroid nodules
VAR_011534505S>Rin HTNA; gain of function
VAR_011535509V>Ain HTNA; gain of function
VAR_011539568I>Tin HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
VAR_021499597V>Fin HTNA; 11-fold increase in specific constitutive activity; decreased receptor protein expression
VAR_003575629L>Fin HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules
VAR_011545631F>Lin HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
VAR_011546632T>Ain HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules
VAR_011547632T>Iin HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
VAR_011549633D>Ein HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
VAR_011552639P>Sin HTNA; gain of function
VAR_011553647A>Vin HTNA; found in non-adenomatous hyperfunctioning nodules
VAR_011554650N>Yin HTNA; gain of function
VAR_011556670N>Sin HTNA; gain of function
VAR_011557672C>Yin HTNA; gain of function

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_05592534in dbSNP:rs45499704
Natural variantVAR_00356436in a patient with Graves disease; dbSNP:rs61747482
Natural variantVAR_01151941in CHNG1
Natural variantVAR_00356552does not contribute to the genetic susceptibility to Graves disease; dbSNP:rs2234919
Natural variantVAR_011520109in CHNG1
Natural variantVAR_011521162in CHNG1; dbSNP:rs121908863
Natural variantVAR_011522167in CHNG1
Natural variantVAR_003566183in HTFG; enhances receptor response to chorionic gonadotropin
Natural variantVAR_003567197in papillary cancer
Natural variantVAR_003568219in papillary cancer
Natural variantVAR_021495252in CHNG1; displays a low expression at the cell surface and a reduced response to bovine TSH in terms of cAMP production
Natural variantVAR_003569281in hyperthyroidism; congenital; due to a toxic adenoma
Natural variantVAR_003570281in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_011523281in hyperthyroidism; found in hyperfunctioning thyroid adenomas
Mutagenesis283Abolishes cell surface expression.
Natural variantVAR_011524310in CHNG1
Mutagenesis385Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation.
Mutagenesis385Reduces sulfation. Reduces binding with thyrotropin. Inhibits intracellular cAMP accumulation.
Mutagenesis385-387Inhibits intracellular cAMP accumulation.
Mutagenesis385-387Abolishes sulfation. Inhibits intracellular cAMP accumulation.
Mutagenesis387No change in intracellular cAMP accumulation.
Mutagenesis387Reduces sulfation. No change in intracellular cAMP accumulation.
Natural variantVAR_011525390in CHNG1; persistent hypothyroidism and defective thyroid development; abolishes high affinity hormone binding
Natural variantVAR_011526410in CHNG1; lack of adenylate cyclase activation
Natural variantVAR_021496425found in toxic thyroid nodules; 8 to 9 times higher levels of basal cAMP than wild-type TSHR and similar response to maximal TSH stimulation
Natural variantVAR_011527431in HTNA; gain of function; constitutive activation of the G(s)/adenylyl cyclase system
Natural variantVAR_075585432in 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
Natural variantVAR_075586449in 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
Natural variantVAR_011528450in CHNG1
Natural variantVAR_011529453in HTNA; sporadic; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_011530463in HTNA; gain of function
Natural variantVAR_017295467in CHNG1
Natural variantVAR_017296477in CHNG1; severe hypothyroidism
Natural variantVAR_011531486in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas; also in hyperfunctioning follicular carcinoma
Natural variantVAR_011532486in HTNA; found in hyperfunctioning thyroid adenomas
Natural variantVAR_011533498in CHNG1
Natural variantVAR_003571505in HTNA; found in toxic thyroid nodules
Natural variantVAR_011534505in HTNA; gain of function
Natural variantVAR_011535509in HTNA; gain of function
Natural variantVAR_021497512found in toxic thyroid nodules; 5 times higher levels of basal cAMP than wild-type TSHR and slightly less response to maximal TSH stimulation
Natural variantVAR_011536512in hyperthyroidism; found in autonomously functioning thyroid nodules; 3.3-fold increase in basal cAMP level
Natural variantVAR_011537525in CHNG1; impairs adenylate cyclase activation
Natural variantVAR_003572528
Natural variantVAR_011538553in CHNG1; severe hypothyroidism
Natural variantVAR_011539568in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_021498593in toxic thyroid adenoma; somatic mutation; constitutively activates the cAMP cascade; requires 2 nucleotide substitutions
Natural variantVAR_021499597in HTNA; 11-fold increase in specific constitutive activity; decreased receptor protein expression
Natural variantVAR_011540597in hyperthyroidism; congenital with severe thyrotoxicosis
Natural variantVAR_017297600in CHNG1
Natural variantVAR_011541606
Natural variantVAR_003573619in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_003574623in hyperthyroidism; found in hyperfunctioning thyroid adenomas; gain of function; requires 2 nucleotide substitutions
Natural variantVAR_011542623in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas; gain of function
Natural variantVAR_003575629in HTNA; also in hyperfunctioning thyroid adenomas and non-adenomatous nodules
Natural variantVAR_011543630in hyperthyroidism; found in hyperfunctioning thyroid adenomas
Natural variantVAR_011544631in hyperthyroidism; found in hyperfunctioning thyroid adenomas
Natural variantVAR_011545631in HTNA; gain of function; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_011546632in HTNA; found in toxic thyroid nodules and hyperfunctioning non-adenomatous nodules
Natural variantVAR_011547632in HTNA; gain of function; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_011548633in hyperthyroidism; found in hyperfunctioning thyroid adenomas
Natural variantVAR_011549633in HTNA; found in thyroid toxic nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_011550633in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas; also found in hyperfunctioning insular carcinoma; gain of function; dbSNP:rs28937584
Natural variantVAR_011551633in hyperthyroidism; found in toxic thyroid nodules and hyperfunctioning thyroid adenomas
Natural variantVAR_021500639found in toxic thyroid nodules
Natural variantVAR_011552639in HTNA; gain of function
Natural variantVAR_011553647in HTNA; found in non-adenomatous hyperfunctioning nodules
Natural variantVAR_011554650in HTNA; gain of function
Natural variantVAR_021501656found in toxic thyroid nodules
Natural variantVAR_011555658-661in hyperthyroidism; found in hyperfunctioning thyroid adenomas
Natural variantVAR_011556670in HTNA; gain of function
Natural variantVAR_011557672in HTNA; gain of function
Natural variantVAR_011558677in thyroid carcinoma; with thyrotoxicosis; gain of function
Natural variantVAR_011559703
Natural variantVAR_003576715in papillary cancer
Natural variantVAR_011560720
Natural variantVAR_003577723in papillary cancer
Natural variantVAR_003578727no effect on thyroid-stimulating hormone receptor activity; dbSNP:rs1991517

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000001278621-764Thyrotropin receptor
Disulfide bond31↔41
Glycosylation77N-linked (GlcNAc...) asparagine
Glycosylation99N-linked (GlcNAc...) asparagine
Glycosylation113N-linked (GlcNAc...) asparagine
Glycosylation177N-linked (GlcNAc...) asparagine
Glycosylation198N-linked (GlcNAc...) asparagine
Glycosylation302N-linked (GlcNAc...) asparagine
Modified residue385Sulfotyrosine
Disulfide bond494↔569

Post-translational modification

Glycosylated.
Sulfated. Sulfation on Tyr-385 plays a role in thyrotropin receptor binding and activation.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in thyroide cells (at protein level) (PubMed:11847099).
Expressed in the thyroid (PubMed:2610690).

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with heterodimer GPHA2:GPHB5; this interaction stimulates cAMP production (PubMed:12045258).
Interacts (via the PDZ-binding motif) with SCRIB; regulates TSHR trafficking and function (PubMed:15775968).

Binary interactions

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for repeat, motif.

TypeIDPosition(s)Description
Repeat100-124LRR 1
Repeat125-150LRR 2
Repeat152-174LRR 3
Repeat176-199LRR 4
Repeat200-223LRR 5
Repeat227-248LRR 6
Repeat250-271LRR 7
Motif762-764PDZ-binding

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Protein family/group databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Name
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    764
  • Mass (Da)
    86,844
  • Last updated
    2024-10-02 v3
  • Checksum
    27EE9CEBFD650D45
MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHEMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL

P16473-2

  • Name
    Short
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 232-253: DVSQTSVTALPSKGLEHLKELI → LPLGRKSLSFETQKAPRSSMPS
    • 254-764: Missing

P16473-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 232-274: DVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTR → VENVAVSGKGFCKSLFSWLYRLPLGRKSLSFETQKAPRSSMPS
    • 275-764: Missing

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8Y709A0A2R8Y709_HUMANTSHR89
A0A1B0GUJ5A0A1B0GUJ5_HUMANTSHR399
G3V381G3V381_HUMANTSHR112
Q0VAP8Q0VAP8_HUMANTSHR231

Sequence caution

The sequence AAA70232.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict87in Ref. 2; no nucleotide entry
Sequence conflict196-198in Ref. 4; AAA70232
Alternative sequenceVSP_001981232-253in isoform Short
Alternative sequenceVSP_044643232-274in isoform 3
Sequence conflict239In isoform P16473-2; in Ref. 6; AAB24246
Sequence conflict248In isoform P16473-2; in Ref. 5; AAB23390 and 9; AAH09237/AAI20974
Sequence conflict251In isoform P16473-2; in Ref. 5; AAB23390
Alternative sequenceVSP_001982254-764in isoform Short
Sequence conflict257in Ref. 4; AAA70232
Sequence conflict264in Ref. 4; AAA70232
Sequence conflict269In isoform P16473-3; in Ref. 9; AAI27629
Alternative sequenceVSP_044644275-764in isoform 3
Sequence conflict306-308in Ref. 4; AAA70232
Sequence conflict528in Ref. 4; AAA70232
Sequence conflict601in Ref. 1; AAA36783
Sequence conflict635in Ref. 4; AAA70232
Sequence conflict645in Ref. 4; AAA70232
Sequence conflict669in Ref. 4; AAA70232
Sequence conflict744in Ref. 3; AAA61236

Polymorphism

Polymorphism at position 727 could be associated with Graves disease.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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