Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Antigen-presenting glycoprotein CD1d1  

UniProtKB / Swiss-Prot ID :  CD1D1_MOUSE

Gene Name (Synonyms) : 
Cd1d1, Cd1.1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cell membrane; Single-pass type I membrane protein. Endosome membrane. Lysosome membrane. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. 

Protein Function :  Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. 

Transmembrane Topology (topPTM) : CD1D1_MOUSE 

Protein Sequence MRYLPWLLLWAFLQVWGQSEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKP...
Predicted Secondary Structure CHHHHHHHHHHHCCCCCCCCCCCCCEEEEEEEEEEECCCCEEEEEEEEEECCEEEEEEECCCCCEEECCC...
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
38N-linked (GlcNAc...).SSFANRSWS
EEECCCCEE
36.19UniProtKB
Link
60N-linked (GlcNAc...).HRWSNDSAT
EEEECCCCC
40.05UniProtKB
Link
183N-linked (GlcNAc...).QMLLNDTCP
HHHHHCCHH
38.29UniProtKB
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
"Crystal structure of mouse CD1d bound to the self ligandphosphatidylcholine: a molecular basis for NKT cell activation.";
Giabbai B., Sidobre S., Crispin M.D.M., Sanchez-Ruiz Y., Bachi A.,Kronenberg M., Wilson I.A., Degano M.;
J. Immunol. 175:977-984(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-297 IN COMPLEX WITHPHOSPHATIDYLCHOLINE AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 ANDASN-183, AND DISULFIDE BONDS.
"Structure and function of a potent agonist for the semi-invariantnatural killer T cell receptor.";
Zajonc D.M., Cantu C. III, Mattner J., Zhou D., Savage P.B.,Bendelac A., Wilson I.A., Teyton L.;
Nat. Immunol. 6:810-818(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-297 IN COMPLEX WITHGALACTOSYLCERAMIDE AND B2M, FUNCTION, GLYCOSYLATION AT ASN-38; ASN-60AND ASN-183, AND DISULFIDE BONDS.
"Design of natural killer T cell activators: structure and function ofa microbial glycosphingolipid bound to mouse CD1d.";
Wu D., Zajonc D.M., Fujio M., Sullivan B.A., Kinjo Y., Kronenberg M.,Wilson I.A., Wong C.-H.;
Proc. Natl. Acad. Sci. U.S.A. 103:3972-3977(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-297 IN COMPLEX WITHGLYCOSPHINGOLIPID AND B2M, GLYCOSYLATION AT ASN-38; ASN-60 ANDASN-183, AND DISULFIDE BONDS.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures