Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Leukemia inhibitory factor receptor  

UniProtKB / Swiss-Prot ID :  LIFR_MOUSE

Gene Name (Synonyms) : 
Lifr  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. 

Protein Function :  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. 

Transmembrane Topology (topPTM) : LIFR_MOUSE 

Protein Sequence MAAYSWWRQPSWMVDNKRSRMTPNLPWLLSALTLLHLTMHANGLKRGVQDLKCTTNNMRVWDCTWPAPLG...
Predicted Secondary Structure CCEEEEECCCCEEEECCCCEECCCHHHHHHHHHHHHHHHHHCHHHCCCEEEEEEEEEEEEEEEECCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
164N-linked (GlcNAc...).PHPSNATWE
CCCCCEEEE
45.93UniProtKB
Link
199N-linked (GlcNAc...).VQHWNWTSD
CCCCCCHHH
29.98UniProtKB
Link
238N-linked (GlcNAc...).SPLKNISWI
CCCCEEEEC
41.01UniProtKB
Link
261N-linked (GlcNAc...).LAGSNMTIC
EECCEEEEE
30.60UniProtKB
Link
385N-linked (GlcNAc...).EGLTNETYR
CCCCCCEEE
44.66UniProtKB
Link
402N-linked (GlcNAc...).QEIHNFTLT
CCEEEEEEE
36.94UniProtKB
Link
421N-linked (GlcNAc...).AVVINVTER
CEEEEEEEC
24.05UniProtKB
Link
440N-linked (GlcNAc...).VKDINSTVV
EEECCCCEE
41.59UniProtKB
Link
453N-linked (GlcNAc...).YLPGNFTKI
ECCCCCCCE
39.20UniProtKB
Link
658N-linked (GlcNAc...).IKWCNSSRS
EEECCCCCC
41.74UniProtKB
Link-
675N-linked (GlcNAc...).KVPSNSTET
ECCCCCEEE
47.05UniProtKB
Link-
882PhosphoserineQFQKSVCEG
EECCCCCCC
22.63Phosphositeplus
Link-
922PhosphoserineTEIISPVAE
CEEEEEEEE
20.98Phosphositeplus
Link-
1039PhosphoserineVSPDSPRST
ECCCCCCCC
26.12Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures