FSHR_HUMAN - dbPTM
FSHR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FSHR_HUMAN
UniProt AC P23945
Protein Name Follicle-stimulating hormone receptor
Gene Name FSHR
Organism Homo sapiens (Human).
Sequence Length 695
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Receptor for follicle-stimulating hormone or follitropin. [PubMed: 11847099]
Protein Sequence MALLLVSLLAFLSLGSGCHHRICHCSNRVFLCQESKVTEIPSDLPRNAIELRFVLTKLRVIQKGAFSGFGDLEKIEISQNDVLEVIEADVFSNLPKLHEIRIEKANNLLYINPEAFQNLPNLQYLLISNTGIKHLPDVHKIHSLQKVLLDIQDNINIHTIERNSFVGLSFESVILWLNKNGIQEIHNCAFNGTQLDELNLSDNNNLEELPNDVFHGASGPVILDISRTRIHSLPSYGLENLKKLRARSTYNLKKLPTLEKLVALMEASLTYPSHCCAFANWRRQISELHPICNKSILRQEVDYMTQARGQRSSLAEDNESSYSRGFDMTYTEFDYDLCNEVVDVTCSPKPDAFNPCEDIMGYNILRVLIWFISILAITGNIIVLVILTTSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDIHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLDCKVQLRHAASVMVMGWIFAFAAALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYIHIYLTVRNPNIVSSSSDTRIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKAKILLVLFHPINSCANPFLYAIFTKNFRRDFFILLSKCGCYEMQAQIYRTETSSTVHNTHPRNGHCSSAPRVTNGSTYILVPLSHLAQN
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
35PhosphorylationRVFLCQESKVTEIPS
CEEEECCCCCCCCCC		13.4230631047
140AcetylationKHLPDVHKIHSLQKV
CCCCCHHHHHCHHHH		41.807675179
143PhosphorylationPDVHKIHSLQKVLLD
CCHHHHHCHHHHHHH		35.6521857030
191N-linked_GlycosylationEIHNCAFNGTQLDEL
HHHHCCCCCCCCEEC		33.7915662415
199N-linked_GlycosylationGTQLDELNLSDNNNL
CCCCEECCCCCCCCH		35.14UniProtKB CARBOHYD
218PhosphorylationNDVFHGASGPVILDI
CCCCCCCCCCEEEEE		48.50-
226PhosphorylationGPVILDISRTRIHSL
CCEEEEEECCCCCCC		27.54-
228PhosphorylationVILDISRTRIHSLPS
EEEEEECCCCCCCCC		27.47-
250PhosphorylationKLRARSTYNLKKLPT
HHHHHCCCCCCCCCC		21.5317384208
257PhosphorylationYNLKKLPTLEKLVAL
CCCCCCCCHHHHHHH		58.9724173317
293N-linked_GlycosylationSELHPICNKSILRQE
HHHCHHCCHHHHHHH		41.66UniProtKB CARBOHYD
295PhosphorylationLHPICNKSILRQEVD
HCHHCCHHHHHHHHH		16.9224719451
318N-linked_GlycosylationRSSLAEDNESSYSRG
CCCCCCCCCCCCCCC		42.42UniProtKB CARBOHYD
335SulfationMTYTEFDYDLCNEVV
CCCCEECHHHCCCEE		19.0111847099
390PhosphorylationVLVILTTSQYKLTVP
EEEEECCCCCCCCCC		26.69-
395PhosphorylationTTSQYKLTVPRFLMC
CCCCCCCCCCHHHHC		25.0624719451
563PhosphorylationVRNPNIVSSSSDTRI
ECCCCCCCCCCCHHH		22.2430206219
564PhosphorylationRNPNIVSSSSDTRIA
CCCCCCCCCCCHHHH		23.9830206219
565PhosphorylationNPNIVSSSSDTRIAK
CCCCCCCCCCHHHHH		25.4030206219
566PhosphorylationPNIVSSSSDTRIAKR
CCCCCCCCCHHHHHH		44.9730206219
568PhosphorylationIVSSSSDTRIAKRMA
CCCCCCCHHHHHHHH		26.3930206219
596PhosphorylationSFFAISASLKVPLIT
HHHHHCCCCCCCEEE		23.1823312004
660PhosphorylationIYRTETSSTVHNTHP
EEECCCCCCCCCCCC		41.70-
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 FSHR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FSHR_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 FSHR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX5_HUMANCBX5physical
15196694
S10AA_HUMANS100A10physical
15196694
1433T_HUMANYWHAQphysical
15196694
ZBT16_HUMANZBTB16physical
15196694
DP13A_HUMANAPPL1physical
15196694
DP13A_HUMANAPPL1physical
15070827
AKT2_HUMANAKT2physical
15070827
DP13B_HUMANAPPL2physical
17030088
FOXO1_HUMANFOXO1physical
17030088
TOP1_HUMANTOP1physical
15196694
DJC18_HUMANDNAJC18physical
28514442
DAD1_HUMANDAD1physical
28514442
EDA_HUMANEDAphysical
28514442
ABCD4_HUMANABCD4physical
28514442
UPK3L_HUMANUPK3BLphysical
28514442
C2C2L_HUMANC2CD2Lphysical
28514442
NAGPA_HUMANNAGPAphysical
28514442
F189B_HUMANFAM189Bphysical
28514442
BMR1A_HUMANBMPR1Aphysical
28514442
ABHD6_HUMANABHD6physical
28514442
PDZD8_HUMANPDZD8physical
28514442
SNX14_HUMANSNX14physical
28514442
CJ035_HUMANC10orf35physical
28514442
CXA1_HUMANGJA1physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
S12A7_HUMANSLC12A7physical
28514442
YIPF4_HUMANYIPF4physical
28514442
GLHA_HUMANCGAphysical
12374801
Drug and Disease Associations
Kegg Disease
H00598 46,XX disorders of sex development (Disorders of gonadal development), including: Ovotesticular DSD;
H00627 Premature ovarian failure
H01039 Ovarian hyperstimulation syndrome (OHSS)
OMIM Disease
233300Ovarian dysgenesis 1 (ODG1)
608115Ovarian hyperstimulation syndrome (OHSS)
Kegg Drug
D02692 Human menopausal gonadotrophin (JP16); Menotropins (USP); Humegon (TN)
D04429 Follitropin alfa (genetical recombination) (JAN); Follitropin alfa; Gonale-F (TN)
D04430 Follitropin beta (genetical recombination) (JAN); Follistim (TN)
D05258 Serum gonadotrophin (JP16)
D06269 Urofollitropin (USAN/INN); Bravelle (TN)
D06400 Follitropin alfa/beta; Follistim (TN); Gonal-F (TN)
D06457 Chorionic gonadotrophin (JP16); HCG (TN)
D06459 Purified human menopausal gonadotrophin (JAN); Human menopausal gonadotrophin, purified
D06477 Serum gonadotrophin for injection (JP16)
D08895 Corifollitropin alfa (INN/USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FSHR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of human follicle-stimulating hormone in complex with itsreceptor.";
Fan Q.R., Hendrickson W.A.;
Nature 433:269-277(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 17-268 IN COMPLEX WITH FSHAAND FSHB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-191.

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