LIFR_HUMAN - dbPTM
LIFR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIFR_HUMAN
UniProt AC P42702
Protein Name Leukemia inhibitory factor receptor
Gene Name LIFR
Organism Homo sapiens (Human).
Sequence Length 1097
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Secreted.
Protein Description Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells..
Protein Sequence MMDIYVCLKRPSWMVDNKRMRTASNFQWLLSTFILLYLMNQVNSQKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLEKTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNISWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDGENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQLLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLVALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPGIRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSSALKTLEMNPCTPNNVEVLETRSAFPKIEDTEIISPVAERPEDRSDAEPENHVVVSYCPPIIEEEIPNPAADEAGGTAQVIYIDVQSMYQPQAKPEEEQENDPVGGAGYKPQMHLPINSTVEDIAAEEDLDKTAGYRPQANVNTWNLVSPDSPRSIDSNSEIVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
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
22PhosphorylationVDNKRMRTASNFQWL
ECCCCCCCHHHHHHH		25.7022210691
64N-linked_GlycosylationTNNLQVWNCSWKAPS
CCCEEEEEEEEECCC		15.87UniProtKB CARBOHYD
85N-linked_GlycosylationDYEVCIENRSRSCYQ
CEEEEEECCCCCEEE		27.58UniProtKB CARBOHYD
131N-linked_GlycosylationKFTLNEQNVSLIPDT
CEEECCCCEEECCCC		21.1118775332
143N-linked_GlycosylationPDTPEILNLSADFST
CCCHHHHCEECCCCC		37.30UniProtKB CARBOHYD
179UbiquitinationWEIKVLRKESMELVK
EEEEEEEHHHHHHEE		50.40-
186UbiquitinationKESMELVKLVTHNTT
HHHHHHEEEEECCCC		50.27-
191N-linked_GlycosylationLVKLVTHNTTLNGKD
HEEEEECCCCCCCCC		25.95UniProtKB CARBOHYD
243N-linked_GlycosylationSDWSPVKNISWIPDS
CCCCCCCCEEECCCC		33.49UniProtKB CARBOHYD
253UbiquitinationWIPDSQTKVFPQDKV
ECCCCCCCEECCCCE		33.95-
303N-linked_GlycosylationNVAIKIRNISVSASS
CEEEEEEEEEEECCC		34.0718775332
367PhosphorylationALVGPRATSYTLVES
EEECCCCCEEEEEEH		24.4425072903
368PhosphorylationLVGPRATSYTLVESF
EECCCCCEEEEEEHH		18.3525072903
369PhosphorylationVGPRATSYTLVESFS
ECCCCCEEEEEEHHC		10.3529759185
370PhosphorylationGPRATSYTLVESFSG
CCCCCEEEEEEHHCC		24.8925072903
374PhosphorylationTSYTLVESFSGKYVR
CEEEEEEHHCCCEEE		19.7525072903
376PhosphorylationYTLVESFSGKYVRLK
EEEEEHHCCCEEEEE		43.5925072903
379PhosphorylationVESFSGKYVRLKRAE
EEHHCCCEEEEEECC		8.3729759185
390N-linked_GlycosylationKRAEAPTNESYQLLF
EECCCCCCHHHHHHH		34.85UniProtKB CARBOHYD
407N-linked_GlycosylationLPNQEIYNFTLNAHN
CCCCEEEEEEECCCC		29.1418775332
426N-linked_GlycosylationSQSTILVNITEKVYP
CCCEEEEECCCCCCC		31.8318775332
445N-linked_GlycosylationSFKVKDINSTAVKLS
EEEEECCCCCEEEEE		43.36UniProtKB CARBOHYD
481N-linked_GlycosylationNSVQEQRNVTIKGVE
CCCCEEECEEEECCC		34.67UniProtKB CARBOHYD
489N-linked_GlycosylationVTIKGVENSSYLVAL
EEEECCCCCEEEEEE		33.57UniProtKB CARBOHYD
490PhosphorylationTIKGVENSSYLVALD
EEECCCCCEEEEEEE		13.57-
491PhosphorylationIKGVENSSYLVALDK
EECCCCCEEEEEEEC		33.78-
492PhosphorylationKGVENSSYLVALDKL
ECCCCCEEEEEEECC		12.67-
526UbiquitinationWSKWSNKKQHLTTEA
HCCCCCCCCCEECCC		47.39-
530PhosphorylationSNKKQHLTTEASPSK
CCCCCCEECCCCCCC		22.0620068231
531PhosphorylationNKKQHLTTEASPSKG
CCCCCEECCCCCCCC		35.5920068231
534PhosphorylationQHLTTEASPSKGPDT
CCEECCCCCCCCCCC		24.3920068231
536PhosphorylationLTTEASPSKGPDTWR
EECCCCCCCCCCCCE		47.9920068231
541PhosphorylationSPSKGPDTWREWSSD
CCCCCCCCCEEECCC		29.5620068231
572N-linked_GlycosylationNGKILSYNVSCSSDE
CCEEEEEEEECCCCH		18.82UniProtKB CARBOHYD
610AcetylationYIISVVAKNSVGSSP
EEEEEEEECCCCCCC		37.847933623
652N-linked_GlycosylationLTWHYDPNMTCDYVI
EEEECCCCCCCCEEE		35.18UniProtKB CARBOHYD
663N-linked_GlycosylationDYVIKWCNSSRSEPC
CEEEECCCCCCCCCC		41.74UniProtKB CARBOHYD
665PhosphorylationVIKWCNSSRSEPCLM
EEECCCCCCCCCCEE		26.3222210691
667PhosphorylationKWCNSSRSEPCLMDW
ECCCCCCCCCCEECC		48.0822210691
680N-linked_GlycosylationDWRKVPSNSTETVIE
CCEECCCCCCCEEEE		47.05UniProtKB CARBOHYD
729N-linked_GlycosylationLAPIVAPNFTVEDTS
HCCEECCCCEECCCC		35.17UniProtKB CARBOHYD
735PhosphorylationPNFTVEDTSADSILV
CCCEECCCCCCEEEE		16.5920068231
736PhosphorylationNFTVEDTSADSILVK
CCEECCCCCCEEEEE		42.2620068231
739PhosphorylationVEDTSADSILVKWED
ECCCCCCEEEEEEEC		19.9620068231
759PhosphorylationLRGFLRGYLFYFGKG
HHHHHHHHHHCCCCC		6.29-
762PhosphorylationFLRGYLFYFGKGERD
HHHHHHHCCCCCCCC		14.61-
787N-linked_GlycosylationRSDIKVKNITDISQK
CCCCEEECCCCCCCC		45.43UniProtKB CARBOHYD
804UbiquitinationRIADLQGKTSYHLVL
EEECCCCCCEEEEEE		22.722063986
807PhosphorylationDLQGKTSYHLVLRAY
CCCCCCEEEEEEEEE		12.3822461510
833PhosphorylationYVVTKENSVGLIIAI
EEEECCCCHHHHHHH		20.75-
866UbiquitinationYRKREWIKETFYPDI
HHHHHHHHHHCCCCC		52.34-
868PhosphorylationKREWIKETFYPDIPN
HHHHHHHHCCCCCCC		24.3830622161
870PhosphorylationEWIKETFYPDIPNPE
HHHHHHCCCCCCCHH		13.8630622161
880UbiquitinationIPNPENCKALQFQKS
CCCHHHCCHHHHHHH		64.81-
880AcetylationIPNPENCKALQFQKS
CCCHHHCCHHHHHHH		64.81125711803
886AcetylationCKALQFQKSVCEGSS
CCHHHHHHHHHCCCC		46.26125711801
886UbiquitinationCKALQFQKSVCEGSS
CCHHHHHHHHHCCCC		46.26-
887PhosphorylationKALQFQKSVCEGSSA
CHHHHHHHHHCCCCC		22.6330576142
896UbiquitinationCEGSSALKTLEMNPC
HCCCCCCCEEECCCC		51.27-
896AcetylationCEGSSALKTLEMNPC
HCCCCCCCEEECCCC		51.27125711799
904PhosphorylationTLEMNPCTPNNVEVL
EEECCCCCCCCEEEE		30.2421815630
923PhosphorylationAFPKIEDTEIISPVA
CCCCCCCCEEECCCC		19.1230266825
927PhosphorylationIEDTEIISPVAERPE
CCCCEEECCCCCCCC		20.9830266825
974PhosphorylationGGTAQVIYIDVQSMY
CCEEEEEEEEEHHCC		7.6922817900
1041PhosphorylationVNTWNLVSPDSPRSI
CCCEEECCCCCCCCC		26.5925159151
1044PhosphorylationWNLVSPDSPRSIDSN
EEECCCCCCCCCCCC		26.1218624908
1047PhosphorylationVSPDSPRSIDSNSEI
CCCCCCCCCCCCCCE		33.8525159151
1050PhosphorylationDSPRSIDSNSEIVSF
CCCCCCCCCCCEEEE		40.3525159151
1052PhosphorylationPRSIDSNSEIVSFGS
CCCCCCCCCEEEECC		32.4330576142
1056PhosphorylationDSNSEIVSFGSPCSI
CCCCCEEEECCCCEE		29.5622210691
1059PhosphorylationSEIVSFGSPCSINSR
CCEEEECCCCEECCC		22.2630576142
1062PhosphorylationVSFGSPCSINSRQFL
EEECCCCEECCCCCC		28.3427307780
1065PhosphorylationGSPCSINSRQFLIPP
CCCCEECCCCCCCCC		26.2827307780
1077PhosphorylationIPPKDEDSPKSNGGG
CCCCCCCCCCCCCCC		31.9830266825
1080PhosphorylationKDEDSPKSNGGGWSF
CCCCCCCCCCCCCCH		44.0522210691
1086PhosphorylationKSNGGGWSFTNFFQN
CCCCCCCCHHHHCCC		26.0122210691
1088PhosphorylationNGGGWSFTNFFQNKP
CCCCCCHHHHCCCCC		26.1222210691
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
1044SPhosphorylationKinaseMK01P28482
PhosphoELM
1044SPhosphorylationKinaseMAPK1P63086
GPS
1044SPhosphorylationKinaseMK03P27361
PhosphoELM
1044SPhosphorylationKinaseMAPK3P21708
GPS
1044SPhosphorylationKinaseMAPK-FAMILY-GPS
1044SPhosphorylationKinaseMAPK_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIFR_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 LIFR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNTFR_HUMANCNTFRphysical
12707266
LIF_HUMANLIFphysical
12601009
ONCM_HUMANOSMphysical
1536831
IL6RB_HUMANIL6STphysical
12047380
PTN6_HUMANPTPN6physical
10800945
Drug and Disease Associations
Kegg Disease
H00462 Stuve-Wiedemann syndrome
OMIM Disease
601559Stueve-Wiedemann syndrome (STWS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIFR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural organization of a full-length gp130/LIF-R cytokinereceptor transmembrane complex.";
Skiniotis G., Lupardus P.J., Martick M., Walz T., Garcia K.C.;
Mol. Cell 31:737-748(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 52-534, IDENTIFICATION IN ACOMPLEX WITH IL6ST; CNTF AND CNTFR, GLYCOSYLATION AT ASN-131; ASN-303;ASN-407 AND ASN-426, DISULFIDE BONDS, ELECTRON MICROSCOPY, ANDSUBUNIT.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND MASSSPECTROMETRY.

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