LEPR_HUMAN - dbPTM
LEPR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LEPR_HUMAN
UniProt AC P48357
Protein Name Leptin receptor
Gene Name LEPR
Organism Homo sapiens (Human).
Sequence Length 1165
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Basolateral cell membrane .
Isoform E: Secreted .
Protein Description Receptor for hormone LEP/leptin (Probable). [PubMed: 22405007 On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (By similarity)]
Protein Sequence MICQKFCVVLLHWEFIYVITAFNLSYPITPWRFKLSCMPPNSTYDYFLLPAGLSKNTSNSNGHYETAVEPKFNSSGTHFSNLSKTTFHCCFRSEQDRNCSLCADNIEGKTFVSTVNSLVFQQIDANWNIQCWLKGDLKLFICYVESLFKNLFRNYNYKVHLLYVLPEVLEDSPLVPQKGSFQMVHCNCSVHECCECLVPVPTAKLNDTLLMCLKITSGGVIFQSPLMSVQPINMVKPDPPLGLHMEITDDGNLKISWSSPPLVPFPLQYQVKYSENSTTVIREADKIVSATSLLVDSILPGSSYEVQVRGKRLDGPGIWSDWSTPRVFTTQDVIYFPPKILTSVGSNVSFHCIYKKENKIVPSKEIVWWMNLAEKIPQSQYDVVSDHVSKVTFFNLNETKPRGKFTYDAVYCCNEHECHHRYAELYVIDVNINISCETDGYLTKMTCRWSTSTIQSLAESTLQLRYHRSSLYCSDIPSIHPISEPKDCYLQSDGFYECIFQPIFLLSGYTMWIRINHSLGSLDSPPTCVLPDSVVKPLPPSSVKAEITINIGLLKISWEKPVFPENNLQFQIRYGLSGKEVQWKMYEVYDAKSKSVSLPVPDLCAVYAVQVRCKRLDGLGYWSNWSNPAYTVVMDIKVPMRGPEFWRIINGDTMKKEKNVTLLWKPLMKNDSLCSVQRYVINHHTSCNGTWSEDVGNHTKFTFLWTEQAHTVTVLAINSIGASVANFNLTFSWPMSKVNIVQSLSAYPLNSSCVIVSWILSPSDYKLMYFIIEWKNLNEDGEIKWLRISSSVKKYYIHDHFIPIEKYQFSLYPIFMEGVGKPKIINSFTQDDIEKHQSDAGLYVIVPVIISSSILLLGTLLISHQRMKKLFWEDVPNPKNCSWAQGLNFQKPETFEHLFIKHTASVTCGPLLLEPETISEDISVDTSWKNKDEMMPTTVVSLLSTTDLEKGSVCISDQFNSVNFSEAEGTEVTYEDESQRQPFVKYATLISNSKPSETGEEQGLINSSVTKCFSSKNSPLKDSFSNSSWEIEAQAFFILSDQHPNIISPHLTFSEGLDELLKLEGNFPEENNDKKSIYYLGVTSIKKRESGVLLTDKSRVSCPFPAPCLFTDIRVLQDSCSHFVENNINLGTSSKKTFASYMPQFQTCSTQTHKIMENKMCDLTV
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
23N-linked_GlycosylationIYVITAFNLSYPITP
HHHHHHHCCCCCCCC		26.139786864
36PhosphorylationTPWRFKLSCMPPNST
CCCEEEEECCCCCCC		14.68-
41N-linked_GlycosylationKLSCMPPNSTYDYFL
EEECCCCCCCCCEEE		40.909786864
41N-linked_GlycosylationKLSCMPPNSTYDYFL
EEECCCCCCCCCEEE		40.909786864
42PhosphorylationLSCMPPNSTYDYFLL
EECCCCCCCCCEEEE		33.83-
56N-linked_GlycosylationLPAGLSKNTSNSNGH
EEECCCCCCCCCCCC		45.429786864
57PhosphorylationPAGLSKNTSNSNGHY
EECCCCCCCCCCCCC		32.7829083192
58PhosphorylationAGLSKNTSNSNGHYE
ECCCCCCCCCCCCCE		47.8829083192
60PhosphorylationLSKNTSNSNGHYETA
CCCCCCCCCCCCEEC		43.9129083192
64PhosphorylationTSNSNGHYETAVEPK
CCCCCCCCEECEECC		19.1729083192
66PhosphorylationNSNGHYETAVEPKFN
CCCCCCEECEECCCC		28.9229083192
73N-linked_GlycosylationTAVEPKFNSSGTHFS
ECEECCCCCCCCCCC		41.209786864
81N-linked_GlycosylationSSGTHFSNLSKTTFH
CCCCCCCCCCCCEEE		47.609786864
81N-linked_GlycosylationSSGTHFSNLSKTTFH
CCCCCCCCCCCCEEE		47.609786864
98N-linked_GlycosylationFRSEQDRNCSLCADN
CCCCCCCCCCCEEEC		28.199786864
98N-linked_GlycosylationFRSEQDRNCSLCADN
CCCCCCCCCCCEEEC		28.199786864
146PhosphorylationLFICYVESLFKNLFR
HHHHHHHHHHHHHHH		29.1224719451
172PhosphorylationLPEVLEDSPLVPQKG
CHHHHCCCCCCCCCC		15.68-
187N-linked_GlycosylationSFQMVHCNCSVHECC
CEEEEECCCCHHHHH		13.259786864
187N-linked_GlycosylationSFQMVHCNCSVHECC
CEEEEECCCCHHHHH		13.259786864
206N-linked_GlycosylationPVPTAKLNDTLLMCL
ECCCCCCCCEEEEEE		39.249786864
208PhosphorylationPTAKLNDTLLMCLKI
CCCCCCCEEEEEEEE		22.2520058876
276N-linked_GlycosylationYQVKYSENSTTVIRE
EEEEECCCCCEEEEH		38.4216335952
347N-linked_GlycosylationILTSVGSNVSFHCIY
HHCCCCCCCEEEEEE		27.769786864
363PhosphorylationKENKIVPSKEIVWWM
CCCCEECCHHHHHHH		31.8423401153
397N-linked_GlycosylationKVTFFNLNETKPRGK
EEEEEECCCCCCCCC		56.879786864
397N-linked_GlycosylationKVTFFNLNETKPRGK
EEEEEECCCCCCCCC		56.8719159218
516N-linked_GlycosylationYTMWIRINHSLGSLD
CEEEEEECCCCCCCC		14.629786864
621PhosphorylationKRLDGLGYWSNWSNP
EECCCCCCCCCCCCC		15.65-
623PhosphorylationLDGLGYWSNWSNPAY
CCCCCCCCCCCCCCE		21.67-
624N-linked_GlycosylationDGLGYWSNWSNPAYT
CCCCCCCCCCCCCEE		31.869786864
624N-linked_GlycosylationDGLGYWSNWSNPAYT
CCCCCCCCCCCCCEE		31.869786864
626PhosphorylationLGYWSNWSNPAYTVV
CCCCCCCCCCCEEEE		36.87-
658 (in isoform 4)Ubiquitination-66.65-
658UbiquitinationGDTMKKEKNVTLLWK
CCCCCCCCCEEEEEC		66.65-
659N-linked_GlycosylationDTMKKEKNVTLLWKP
CCCCCCCCEEEEECC		32.859786864
688N-linked_GlycosylationINHHTSCNGTWSEDV
EECCCCCCCCCCCCC		51.189786864
697N-linked_GlycosylationTWSEDVGNHTKFTFL
CCCCCCCCCEEEEEE		39.239786864
728N-linked_GlycosylationGASVANFNLTFSWPM
CCEEEEEEEEEECCH		37.679786864
750N-linked_GlycosylationSLSAYPLNSSCVIVS
HHCCCCCCCCEEEEE		27.639786864
795PhosphorylationISSSVKKYYIHDHFI
ECCCEEEEEECCCEE		11.2622817900
796PhosphorylationSSSVKKYYIHDHFIP
CCCEEEEEECCCEEE		10.72-
838PhosphorylationDDIEKHQSDAGLYVI
HHHHHHHHCCCEEEE		29.1922210691
853PhosphorylationVPVIISSSILLLGTL
HHHHHHHHHHHHHHH		15.5122210691
863PhosphorylationLLGTLLISHQRMKKL
HHHHHHHHHHHHHHH		17.3422210691
879UbiquitinationWEDVPNPKNCSWAQG
HCCCCCCCCCCCCCC		76.7816482222
882 (in isoform 2)Phosphorylation-34.5429485707
882PhosphorylationVPNPKNCSWAQGLNF
CCCCCCCCCCCCCCC		34.5427732954
891UbiquitinationAQGLNFQKPETFEHL
CCCCCCCCCCCEEEE		40.4616482222
937PhosphorylationNKDEMMPTTVVSLLS
CCCCCCCHHHHHHHC		17.8330631047
938PhosphorylationKDEMMPTTVVSLLST
CCCCCCHHHHHHHCC		17.0330631047
944PhosphorylationTTVVSLLSTTDLEKG
HHHHHHHCCCCCCCC		34.2622210691
945PhosphorylationTVVSLLSTTDLEKGS
HHHHHHCCCCCCCCC		25.0522210691
946PhosphorylationVVSLLSTTDLEKGSV
HHHHHCCCCCCCCCE		34.90-
986PhosphorylationQRQPFVKYATLISNS
HCCCEEEEEEEEECC		10.2617726024
1076PhosphorylationEENNDKKSIYYLGVT
CCCCCCCCEEEEEEC		22.8926074081
1078PhosphorylationNNDKKSIYYLGVTSI
CCCCCCEEEEEECEE		10.3426074081
1079PhosphorylationNDKKSIYYLGVTSIK
CCCCCEEEEEECEEE		8.7023403867
1083PhosphorylationSIYYLGVTSIKKRES
CEEEEEECEEEECCC		23.9626074081
1084PhosphorylationIYYLGVTSIKKRESG
EEEEEECEEEECCCC		29.9726074081
1090PhosphorylationTSIKKRESGVLLTDK
CEEEECCCCEEECCC		37.93-
1111PhosphorylationFPAPCLFTDIRVLQD
CCCCCEEECHHHHHH		19.9824719451
1137PhosphorylationLGTSSKKTFASYMPQ
CCCCCCHHHHHHCCC		28.3329052541
1140PhosphorylationSSKKTFASYMPQFQT
CCCHHHHHHCCCCCC		20.1329052541
1141PhosphorylationSKKTFASYMPQFQTC
CCHHHHHHCCCCCCC		14.9117726024
1147PhosphorylationSYMPQFQTCSTQTHK
HHCCCCCCCCCHHHH		15.0929052541
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
986YPhosphorylationKinaseJAK2O60674
Uniprot
1141YPhosphorylationKinaseJAK2O60674
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LEPR_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 LEPR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PIN1_HUMANPIN1physical
16169070
JAK3_HUMANJAK3physical
11585385
SOCS3_HUMANSOCS3physical
21239736
NECD_HUMANNDNphysical
28973533
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614963Leptin receptor deficiency (LEPRD)
Kegg Drug
D05014 Mettreleptin (genetical recombination) (JAN); Metreleptin (USAN/INN); Metreleptin (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LEPR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276 AND ASN-397, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276 AND ASN-516, AND MASSSPECTROMETRY.
"Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain.";
Haniu M., Arakawa T., Bures E.J., Young Y., Hui J.O., Rohde M.F.,Welcher A.A., Horan T.;
J. Biol. Chem. 273:28691-28699(1998).
Cited for: GLYCOSYLATION AT ASN-23; ASN-41; ASN-56; ASN-73; ASN-81; ASN-98;ASN-187; ASN-206; ASN-276; ASN-347; ASN-397; ASN-516; ASN-624;ASN-659; ASN-688; ASN-697; ASN-728 AND ASN-750, DISULFIDE BONDS, ANDPARTIAL PROTEIN SEQUENCE.

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