LSHR_HUMAN - dbPTM
LSHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSHR_HUMAN
UniProt AC P22888
Protein Name Lutropin-choriogonadotropic hormone receptor
Gene Name LHCGR
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Receptor for lutropin-choriogonadotropic hormone. [PubMed: 11847099 The activity of this receptor is mediated by G proteins which activate adenylate cyclase]
Protein Sequence MKQRFSALQLLKLLLLLQPPLPRALREALCPEPCNCVPDGALRCPGPTAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQIDSLERIEANAFDNLLNLSEILIQNTKNLRYIEPGAFINLPRLKYLSICNTGIRKFPDVTKVFSSESNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLTSLELKENVHLEKMHNGAFRGATGPKTLDISSTKLQALPSYGLESIQRLIATSSYSLKKLPSRETFVNLLEATLTYPSHCCAFRNLPTKEQNFSHSISENFSKQCESTVRKVNNKTLYSSMLAESELSGWDYEYGFCLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQVYILTILILNVVAFFIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFQRDFFLLLSKFGCCKRRAELYRRKDFSAYTSNCKNGFTGSNKPSQSTLKLSTLHCQGTALLDKTRYTEC
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
99N-linked_GlycosylationNAFDNLLNLSEILIQ
HHHHHHHCHHHHHHH		44.69UniProtKB CARBOHYD
174N-linked_GlycosylationNAFQGMNNESVTLKL
CCCCCCCCCCEEEEE		33.75UniProtKB CARBOHYD
195N-linked_GlycosylationEVQSHAFNGTTLTSL
HHHHHCCCCCCCEEE		47.92UniProtKB CARBOHYD
240PhosphorylationKLQALPSYGLESIQR
CHHCCCCCCHHHHHH		24.6423403867
244PhosphorylationLPSYGLESIQRLIAT
CCCCCHHHHHHHHHC		29.1223403867
255PhosphorylationLIATSSYSLKKLPSR
HHHCCCCCCCCCCCH		35.3424719451
287PhosphorylationCAFRNLPTKEQNFSH
CHHCCCCCCCHHCCC		50.8329449344
291N-linked_GlycosylationNLPTKEQNFSHSISE
CCCCCCHHCCCHHCH		41.29UniProtKB CARBOHYD
293PhosphorylationPTKEQNFSHSISENF
CCCCHHCCCHHCHHH		24.7129449344
295PhosphorylationKEQNFSHSISENFSK
CCHHCCCHHCHHHHH		26.9829449344
297PhosphorylationQNFSHSISENFSKQC
HHCCCHHCHHHHHHH		29.5129449344
299N-linked_GlycosylationFSHSISENFSKQCES
CCCHHCHHHHHHHHH		39.44UniProtKB CARBOHYD
301PhosphorylationHSISENFSKQCESTV
CHHCHHHHHHHHHHH		33.1429449344
313N-linked_GlycosylationSTVRKVNNKTLYSSM
HHHHHHCCHHHHHHH		41.50UniProtKB CARBOHYD
331SulfationSELSGWDYEYGFCLP
HHHCCCCCCCCEECC		12.4411847099
386PhosphorylationTVLFVLLTSRYKLTV
HHHHHHHHCCCCCCC		13.6524719451
392PhosphorylationLTSRYKLTVPRFLMC
HHCCCCCCCCCHHHC		25.0624719451
417PhosphorylationLYLLLIASVDSQTKG
HHHHHHHCCCCCCCC		21.3325332170
420PhosphorylationLLIASVDSQTKGQYY
HHHHCCCCCCCCCCE		37.2825332170
494PhosphorylationMLGGWLFSSLIAMLP
HHHHHHHHHHHHHHH		23.2824719451
506PhosphorylationMLPLVGVSNYMKVSI
HHHHHCCCCCEEEEE		19.1324719451
561PhosphorylationRNPELMATNKDTKIA
HCHHHHHCCCCHHHH		28.9228674151
643S-palmitoylationLLLSKFGCCKRRAEL
HHHHHHCCHHHHHHH		2.5215539429
644S-palmitoylationLLSKFGCCKRRAELY
HHHHHCCHHHHHHHH		3.8215539429
681PhosphorylationSQSTLKLSTLHCQGT
CCCEEEEEEEECCCE		27.60-
688PhosphorylationSTLHCQGTALLDKTR
EEEECCCEEEECCCC		6.56-
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 LSHR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSHR_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 LSHR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIPC1_HUMANGIPC1physical
14507927
GLHA_HUMANCGAphysical
10342833
ARRB2_HUMANARRB2physical
11867621
Drug and Disease Associations
Kegg Disease
H00608 46,XY disorders of sex development (Disorders in androgen synthesis or action), including: Congenita
H00627 Premature ovarian failure
H00937 Precocious puberty, including: Central precocious puberty (CEPREPU); Familial male precocious pubert
OMIM Disease
176410Familial male precocious puberty (FMPP)
238320Luteinizing hormone resistance (LHR)
Kegg Drug
D02692 Human menopausal gonadotrophin (JP16); Menotropins (USP); Humegon (TN)
D03334 Gonadotrophin, chorionic (JAN); Gonadotropin, chorionic (USP); A.P.L. (TN)
D03478 Choriogonadotropin alfa (USAN/INN); Ovidrel (TN)
D04824 Lutropin alfa (USAN/INN); Luveris (TN)
D05258 Serum gonadotrophin (JP16)
D06457 Chorionic gonadotrophin (JP16); HCG (TN)
D06459 Purified human menopausal gonadotrophin (JAN); Human menopausal gonadotrophin, purified
D06477 Serum gonadotrophin for injection (JP16)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LSHR_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Evidence that palmitoylation of carboxyl terminus cysteine residuesof the human luteinizing hormone receptor regulates postendocyticprocessing.";
Munshi U.M., Clouser C.L., Peegel H., Menon K.M.;
Mol. Endocrinol. 19:749-758(2005).
Cited for: PALMITOYLATION AT CYS-643 AND CYS-644, AND MUTAGENESIS OF CYS-643 ANDCYS-644.

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