TSHR_HUMAN - dbPTM
TSHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSHR_HUMAN
UniProt AC P16473
Protein Name Thyrotropin receptor
Gene Name TSHR
Organism Homo sapiens (Human).
Sequence Length 764
Subcellular Localization Cell membrane
Multi-pass membrane protein . Basolateral cell membrane
Multi-pass membrane protein .
Protein Description Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin. [PubMed: 11847099]
Protein Sequence MRPADLLQLVLLLDLPRDLGGMGCSSPPCECHQEEDFRVTCKDIQRIPSLPPSTQTLKLIETHLRTIPSHAFSNLPNISRIYVSIDVTLQQLESHSFYNLSKVTHIEIRNTRNLTYIDPDALKELPLLKFLGIFNTGLKMFPDLTKVYSTDIFFILEITDNPYMTSIPVNAFQGLCNETLTLKLYNNGFTSVQGYAFNGTKLDAVYLNKNKYLTVIDKDAFGGVYSGPSLLDVSQTSVTALPSKGLEHLKELIARNTWTLKKLPLSLSFLHLTRADLSYPSHCCAFKNQKKIRGILESLMCNESSMQSLRQRKSVNALNSPLHQEYEENLGDSIVGYKEKSKFQDTHNNAHYYVFFEEQEDEIIGFGQELKNPQEETLQAFDSHYDYTICGDSEDMVCTPKSDEFNPCEDIMGYKFLRIVVWFVSLLALLGNVFVLLILLTSHYKLNVPRFLMCNLAFADFCMGMYLLLIASVDLYTHSEYYNHAIDWQTGPGCNTAGFFTVFASELSVYTLTVITLERWYAITFAMRLDRKIRLRHACAIMVGGWVCCFLLALLPLVGISSYAKVSICLPMDTETPLALAYIVFVLTLNIVAFVIVCCCYVKIYITVRNPQYNPGDKDTKIAKRMAVLIFTDFICMAPISFYALSAILNKPLITVSNSKILLVLFYPLNSCANPFLYAIFTKAFQRDVFILLSKFGICKRQAQAYRGQRVPPKNSTDIQVQKVTHDMRQGLHNMEDVYELIENSHLTPKKQGQISEEYMQTVL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
42UbiquitinationEDFRVTCKDIQRIPS
CCCEEEHHHHHCCCC		48.80-
42UbiquitinationEDFRVTCKDIQRIPS
CCCEEEHHHHHCCCC		48.80-
58UbiquitinationPPSTQTLKLIETHLR
CCCHHHHHHHHHHHH		51.29-
58UbiquitinationPPSTQTLKLIETHLR
CCCHHHHHHHHHHHH		51.29-
77N-linked_GlycosylationHAFSNLPNISRIYVS
HHHCCCCCCEEEEEE		48.2917542669
77N-linked_GlycosylationHAFSNLPNISRIYVS
HHHCCCCCCEEEEEE		48.2917542669
99N-linked_GlycosylationLESHSFYNLSKVTHI
HHHCCCEECCCCEEE		35.5117542669
113N-linked_GlycosylationIEIRNTRNLTYIDPD
EEEECCCCCEEECHH		34.4017542669
113N-linked_GlycosylationIEIRNTRNLTYIDPD
EEEECCCCCEEECHH		34.4017542669
177N-linked_GlycosylationNAFQGLCNETLTLKL
HHHHCCCCCCEEEEE		50.7817542669
198N-linked_GlycosylationSVQGYAFNGTKLDAV
CEEEEEECCCEEEEE		49.4017542669
198N-linked_GlycosylationSVQGYAFNGTKLDAV
CEEEEEECCCEEEEE		49.4017542669
226 (in isoform 2)Phosphorylation-41.65-
229 (in isoform 2)Phosphorylation-45.12-
243PhosphorylationTSVTALPSKGLEHLK
CCCCCCCCCCHHHHH		39.9624719451
268PhosphorylationKKLPLSLSFLHLTRA
CCCCCCCHHHHCCCC		23.53-
298PhosphorylationKIRGILESLMCNESS
HHHHHHHHHHCCHHH		20.25-
302N-linked_GlycosylationILESLMCNESSMQSL
HHHHHHCCHHHHHHH		37.9111502179
302N-linked_GlycosylationILESLMCNESSMQSL
HHHHHHCCHHHHHHH		37.9111502179
308PhosphorylationCNESSMQSLRQRKSV
CCHHHHHHHHHHHHH		19.51-
385SulfationLQAFDSHYDYTICGD
HHHHHHCCCEEEECC		18.0111847099
385SulfationLQAFDSHYDYTICGD
HHHHHHCCCEEEECC		18.01-
387SulfationAFDSHYDYTICGDSE
HHHHCCCEEEECCCC		7.28-
425PhosphorylationRIVVWFVSLLALLGN
HHHHHHHHHHHHHHH		14.27-
613PhosphorylationITVRNPQYNPGDKDT
EEECCCCCCCCCCCH		25.2823403867
632PhosphorylationRMAVLIFTDFICMAP
HHHHHHHHCCHHHHH		24.0122210691
641PhosphorylationFICMAPISFYALSAI
CHHHHHHHHHHHHHH		15.9022210691
699S-palmitoylationLLSKFGICKRQAQAY
HHHHHCCHHHHHHHH		2.809449658
706PhosphorylationCKRQAQAYRGQRVPP
HHHHHHHHCCCCCCC		11.82-
739PhosphorylationLHNMEDVYELIENSH
HCCHHHHHHHHHCCC		19.8328796482
745PhosphorylationVYELIENSHLTPKKQ
HHHHHHCCCCCCCCC		13.69-
748PhosphorylationLIENSHLTPKKQGQI
HHHCCCCCCCCCCCC		27.8628122231
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TSHR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSHR_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TSHR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FLNB_HUMANFLNBphysical
8327473
STAT3_HUMANSTAT3physical
10809230
SCRIB_HUMANSCRIBphysical
15775968
IQGA2_HUMANIQGAP2physical
26186194
SALL2_HUMANSALL2physical
26186194
KCC2D_HUMANCAMK2Dphysical
26186194
POTEF_HUMANPOTEFphysical
26186194
PYC_HUMANPCphysical
26186194
PTK7_HUMANPTK7physical
26186194
TBA1A_HUMANTUBA1Aphysical
26186194
CBWD1_HUMANCBWD1physical
26186194
MOCOS_HUMANMOCOSphysical
26186194
ITPA_HUMANITPAphysical
26186194
STIL_HUMANSTILphysical
26186194
SAMD1_HUMANSAMD1physical
26186194
LAMA3_HUMANLAMA3physical
26186194
BORA_HUMANBORAphysical
26186194
FBX7_HUMANFBXO7physical
26186194
TRM44_HUMANTRMT44physical
26186194
GOGA2_HUMANGOLGA2physical
26186194
LAMA3_HUMANLAMA3physical
28514442
POTEF_HUMANPOTEFphysical
28514442
ITPA_HUMANITPAphysical
28514442
MOCOS_HUMANMOCOSphysical
28514442
BORA_HUMANBORAphysical
28514442
PYC_HUMANPCphysical
28514442
MLF1_HUMANMLF1physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
Drug and Disease Associations
Kegg Disease
H00082 Graves' disease
H00250 Congenital nongoitrous hypothyroidism (CHNG)
H01269 Congenital hyperthyroidism, including: Familial gestational hyperthyroidism (HTFG); Hyperthyroidism
OMIM Disease
Note=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).
275200
603373Familial gestational hyperthyroidism (HTFG)
609152Hyperthyroidism, non-autoimmune (HTNA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TSHR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the TSH receptor in complex with a thyroid-stimulating autoantibody.";
Sanders J., Chirgadze D.Y., Sanders P., Baker S., Sullivan A.,Bhardwaja A., Bolton J., Reeve M., Nakatake N., Evans M., Richards T.,Powell M., Miguel R.N., Blundell T.L., Furmaniak J., Smith B.R.;
Thyroid 17:395-410(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 22-260 IN COMPLEX WITHANTIBODY, GLYCOSYLATION AT ASN-77; ASN-99; ASN-113; ASN-177 ANDASN-198, AND N-TERMINAL DISULFIDE BOND.
"Purification and characterization of a soluble bioactive amino-terminal extracellular domain of the human thyrotropin receptor.";
Cornelis S., Uttenweiler-Joseph S., Panneels V., Vassart G.,Costagliola S.;
Biochemistry 40:9860-9869(2001).
Cited for: PROTEIN SEQUENCE OF 66-80; 113-123; 184-210 AND 294-310, ANDGLYCOSYLATION AT ASN-77; ASN-113; ASN-198 AND ASN-302.

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