Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Chromobox protein homolog 3  

UniProtKB / Swiss-Prot ID :  CBX3_MOUSE

Gene Name (Synonyms) : 
Cbx3  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus. Note=May be associated with microtubules and mitotic poles during mitosis (Potential). Associates with euchromatin and is largely excluded from constitutive heterochromatin. 

Protein Function :  Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin, such as E2F1, MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins (By similarity). 

Protein Sequence MASNKTTLQKMGKKQNGKSKKVEEAEPEEFVVEKVLDRRVVNGKVEYFLKWKGFTDADNTWEPEENLDCP...
Predicted Secondary Structure CCCCHHHHHHHHHHHCCCCCCCCCCCCCEEEHHHHHHCCEECCEEEEEEEECCCCCCCCCCCCHHCCCHH...
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
93PhosphoserineTKRKSLSDS
CCCCCCCCC
36.82Phosphositeplus
Link-
93Phosphoserine.TKRKSLSDS
CCCCCCCCC
36.82UniProtKB
Link-
95PhosphoserineRKSLSDSES
CCCCCCCCC
46.30Phosphositeplus
Link-
95PhosphoserineRKSLSDSES
CCCCCCCCC
46.30SysPTM
Link-
95Phosphoserine.RKSLSDSES
CCCCCCCCC
46.30UniProtKB
Link-
97PhosphoserineSLSDSESDD
CCCCCCCCC
35.31Phosphositeplus
Link-
99PhosphoserineSDSESDDSK
CCCCCCCCC
51.15Phosphositeplus
Link-
102PhosphoserineESDDSKSKK
CCCCCCCCC
43.76Phosphositeplus
Link-
176PhosphoserineLTWHSCPED
HHCCCCCCC
23.95PhosphoELM
Link-
176PhosphoserineLTWHSCPED
HHCCCCCCC
23.95Phosphositeplus
Link-
176Phosphoserine.LTWHSCPED
HHCCCCCCC
23.95UniProtKB
Link-
177S-nitrosocysteineTWHSCPEDE
HCCCCCCCC
2.50dbSNO
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
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures