Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Contactin-6  

UniProtKB / Swiss-Prot ID :  CNTN6_HUMAN

Gene Name (Synonyms) : 
CNTN6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor, GPI-anchor (By similarity). 

Protein Function :  Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Involved in motor coordination (By similarity). 

Protein Sequence MRLLWKLVILLPLINSSAGDGLLSRPIFTQEPHDVIFPLDLSKSEVILNCAANGYPSPHYRWKQNGTDID...
Predicted Secondary Structure CHHHHHHHHHHHHHHHHCCCCCCCCCEEEECCCCEEEEEEECCCCEEEEEEEECCCCCEEEEEECCEECC...
Protein Variant
LocationDescription
108T -> A (in a breast cancer sample;somatic mutation).
150F -> S (in dbSNP:rs6808056). VAR_033611
303R -> Q (in dbSNP:rs41293401). VAR_065744
314F -> V. VAR_065745
440A -> S (in dbSNP:rs265771). VAR_019913
585S -> C (in a breast cancer sample;somatic mutation).
954E -> V (in a patient with amyotrophiclateral sclerosis).
- top -

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
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
467PhosphotyrosineSLKIYNITR
EEEEEECCC
10.02Phosphositeplus
Link-
882PhosphotyrosineSVRAYNTAG
EEEEEECCC
11.50Phosphositeplus
Link-
882Phosphotyrosine.SVRAYNTAG
EEEEEECCC
11.50UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-882, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures