Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  H-2 class I histocompatibility antigen, K-B alpha chain  

UniProtKB / Swiss-Prot ID :  HA1B_MOUSE

Gene Name (Synonyms) : 
H2-K1, H2-K  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Membrane; Single-pass type I membrane protein. 

Protein Function :  Involved in the presentation of foreign antigens to the immune system. 

Transmembrane Topology (topPTM) : HA1B_MOUSE 

Protein Sequence MVPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRA...
Predicted Secondary Structure CCHHHHHHHHHHHHHCCCCCCCCEEEEEEEEECCCCCCCCCEEEEEEEECCEEEEEEECCCCCCEEEEEE...
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
107N-linked (GlcNAc...).LGYYNQSKG
HHHHCCCCC
31.03UniProtKB
Link
197N-linked (GlcNAc...).LKNGNATLL
HHCCCCCCC
38.86UniProtKB
Link
199PhosphothreonineNGNATLLRT
CCCCCCCCC
30.26Phosphositeplus
Link
348PhosphoserineLAPGSQTSD
CCCCCCCCC
29.26Phosphositeplus
Link-
350PhosphothreoninePGSQTSDLS
CCCCCCCEE
26.38Phosphositeplus
Link-
351PhosphoserineGSQTSDLSL
CCCCCCEEE
28.99Phosphositeplus
Link-
354PhosphoserineTSDLSLPDC
CCCEEECCC
42.73Phosphositeplus
Link-
367PhosphoserineHDPHSLA
ECCCCCC
31.23Phosphositeplus
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
"Amino acid sequence of the carboxyl-terminal hydrophilic region ofthe H-2Kb MHC alloantigen. Completion of the entire primary structureof the H-2Kb molecule.";
Uehara H., Coligan J.E., Nathenson S.G.;
Biochemistry 20:5940-5945(1981).
Cited for: PROTEIN SEQUENCE OF 22-367, AND GLYCOSYLATION AT ASN-107 AND ASN-197.
"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-107, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures