LIFR_MOUSE - dbPTM
LIFR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIFR_MOUSE
UniProt AC P42703
Protein Name Leukemia inhibitory factor receptor
Gene Name Lifr
Organism Mus musculus (Mouse).
Sequence Length 1092
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 MAAYSWWRQPSWMVDNKRSRMTPNLPWLLSALTLLHLTMHANGLKRGVQDLKCTTNNMRVWDCTWPAPLGVSPGTVKDICIKDRFHSCHPLETTNVKIPALSPGDHEVTINYLNGFQSKFTLNEKDVSLIPETPEILDLSADFFTSSLLLKWNDRGSALPHPSNATWEIKVLQNPRTEPVALVLLNTMLSGKDTVQHWNWTSDLPLQCATHSVSIRWHIDSPHFSGYKEWSDWSPLKNISWIRNTETNVFPQDKVVLAGSNMTICCMSPTKVLSGQIGNTLRPLIHLYGQTVAIHILNIPVSENSGTNIIFITDDDVYGTVVFAGYPPDVPQKLSCETHDLKEIICSWNPGRITGLVGPRNTEYTLFESISGKSAVFHRIEGLTNETYRLGVQMHPGQEIHNFTLTGRNPLGQAQSAVVINVTERVAPHDPTSLKVKDINSTVVTFSWYLPGNFTKINLLCQIEICKANSKKEVRNATIRGAEDSTYHVAVDKLNPYTAYTFRVRCSSKTFWKWSRWSDEKRHLTTEATPSKGPDTWREWSSDGKNLIVYWKPLPINEANGKILSYNVSCSLNEETQSVLEIFDPQHRAEIQLSKNDYIISVVARNSAGSSPPSKIASMEIPNDDITVEQAVGLGNRIFLTWRHDPNMTCDYVIKWCNSSRSEPCLLDWRKVPSNSTETVIESDQFQPGVRYNFYLYGCTNQGYQLLRSIIGYVEELAPIVAPNFTVEDTSADSILVKWDDIPVEELRGFLRGYLFYFQKGERDTPKTRSLEPHHSDIKLKNITDISQKTLRIADLQGKTSYHLVLRAYTHGGLGPEKSMFVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSNALKTLEMNPCTPNNVEVLESRSIVPKIEDTEIISPVAERPGERSEVDPENHVVVSYCPPIIEEEITNPAADEVGGASQVVYIDVQSMYQPQAKAEEEQDVDPVVVAGYKPQMRLPISPAVEDTAAEDEEGKTAGYRPQANVNTWNLVSPDSPRSTDSNNEVVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
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
164N-linked_GlycosylationSALPHPSNATWEIKV
CCCCCCCCCCEEEEE		45.9317652170
177PhosphorylationKVLQNPRTEPVALVL
EEECCCCCCCCEEHH		45.99-
187PhosphorylationVALVLLNTMLSGKDT
CEEHHHHHHHCCCCC		21.32-
199N-linked_GlycosylationKDTVQHWNWTSDLPL
CCCCCCCCCCCCCCC		29.9817652170
214PhosphorylationQCATHSVSIRWHIDS
EEEECEEEEEEEECC		14.9525159016
238N-linked_GlycosylationSDWSPLKNISWIRNT
CCCCCCCCEEEECCC		41.0117652170
261N-linked_GlycosylationKVVLAGSNMTICCMS
CEEEECCCEEEEEEC		30.6017652170
362PhosphorylationGLVGPRNTEYTLFES
EEECCCCCEEEEEEE		31.4825777480
364PhosphorylationVGPRNTEYTLFESIS
ECCCCCEEEEEEECC		13.5025777480
365PhosphorylationGPRNTEYTLFESISG
CCCCCEEEEEEECCC		20.8125777480
369PhosphorylationTEYTLFESISGKSAV
CEEEEEEECCCCCHH		18.0825777480
371PhosphorylationYTLFESISGKSAVFH
EEEEEECCCCCHHHH		49.8225777480
374PhosphorylationFESISGKSAVFHRIE
EEECCCCCHHHHEEE		32.9425777480
385N-linked_GlycosylationHRIEGLTNETYRLGV
HEEECCCCCCEEEEE		44.6617330941
402N-linked_GlycosylationHPGQEIHNFTLTGRN
CCCCEEECEEEECCC		36.9417652170
421N-linked_GlycosylationAQSAVVINVTERVAP
CCEEEEEEECCCCCC		24.0517652170
440N-linked_GlycosylationSLKVKDINSTVVTFS
CCEEECCCCEEEEEE		41.5917652170
453N-linked_GlycosylationFSWYLPGNFTKINLL
EEEECCCCCCCEEEE		39.2017652170
476N-linked_GlycosylationNSKKEVRNATIRGAE
CCCHHHHHCEECCCC		46.76-
505MethylationTAYTFRVRCSSKTFW
CEEEEEEEECCCCCE		15.4418965505
505DimethylationTAYTFRVRCSSKTFW
CEEEEEEEECCCCCE		15.44-
567N-linked_GlycosylationNGKILSYNVSCSLNE
CCEEEEEEEEECCCH		18.82-
611PhosphorylationARNSAGSSPPSKIAS
EECCCCCCCCHHHCC		39.6526026062
647N-linked_GlycosylationLTWRHDPNMTCDYVI
EEECCCCCCCCCEEE		44.44-
658N-linked_GlycosylationDYVIKWCNSSRSEPC
CEEEEECCCCCCCCE		41.7417330941
675N-linked_GlycosylationDWRKVPSNSTETVIE
ECEECCCCCCCEEEE		47.0516944957
724N-linked_GlycosylationLAPIVAPNFTVEDTS
HCCCCCCCCEECCCC		35.17-
782N-linked_GlycosylationHSDIKLKNITDISQK
CCCCCCCCCCCCCCC		53.48-
784PhosphorylationDIKLKNITDISQKTL
CCCCCCCCCCCCCEE		36.3523375375
787PhosphorylationLKNITDISQKTLRIA
CCCCCCCCCCEEEEE		28.5623375375
861UbiquitinationYRKREWIKETFYPDI
HHHHHHHHHHCCCCC		52.34-
881UbiquitinationCKALQFQKSVCEGSN
CCHHHHHHHHHCCCC		46.2622790023
882PhosphorylationKALQFQKSVCEGSNA
CHHHHHHHHHCCCCC		22.6325521595
918PhosphorylationIVPKIEDTEIISPVA
CCCCCCCCEEEECCC		19.1229899451
922PhosphorylationIEDTEIISPVAERPG
CCCCEEEECCCCCCC		20.9822817900
1039PhosphorylationWNLVSPDSPRSTDSN
EEEECCCCCCCCCCC		26.1221082442
1054PhosphorylationNEVVSFGSPCSINSR
CCEEEECCCCEECCC		22.2625162660
1072PhosphorylationIPPKDEDSPKSNGGG
CCCCCCCCCCCCCCC		31.9823140645
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 LIFR_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIFR_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LIFR_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIFR_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"An unusual cytokine:Ig-domain interaction revealed in the crystalstructure of leukemia inhibitory factor (LIF) in complex with the LIFreceptor.";
Huyton T., Zhang J.G., Luo C.S., Lou M.Z., Hilton D.J., Nicola N.A.,Garrett T.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:12737-12742(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 49-529 IN COMPLEX WITH HUMANLIF, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-164; ASN-199; ASN-238;ASN-261; ASN-385; ASN-402; ASN-421; ASN-440 AND ASN-453.
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385, AND MASSSPECTROMETRY.
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385 AND ASN-658, AND MASSSPECTROMETRY.
"Proteome-wide characterization of N-glycosylation events by diagonalchromatography.";
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,Gevaert K.;
J. Proteome Res. 5:2438-2447(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385; ASN-402 AND ASN-675,AND MASS SPECTROMETRY.

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