Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  LisH domain and HEAT repeat-containing protein KIAA1468  

UniProtKB / Swiss-Prot ID :  K1468_MOUSE

Gene Name (Synonyms) : 
Kiaa1468  

Species :  Mus musculus (Mouse). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MAAMAPGGGGSGSGVNPFLSDSDEDDDEVAATEDRRAGLRLGAGVGLDPGSAGSLSPQDPMALGSSARPG...
Predicted Secondary Structure  -
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
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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
4Methionine sulfone-MAAMAPGG
-
6.28SysPTM
Link-
20PhosphoserineNPFLSDSDE
35.13Phosphositeplus
Link-
20PhosphoserineNPFLSDSDE
35.13SysPTM
Link-
20Phosphoserine.NPFLSDSDE
35.13UniProtKB
Link-
22PhosphoserineFLSDSDEDD
39.25Phosphositeplus
Link-
22PhosphoserineFLSDSDEDD
39.25SysPTM
Link-
22Phosphoserine.FLSDSDEDD
39.25UniProtKB
Link-
32PhosphothreonineEVAATEDRR
28.78Phosphositeplus
Link-
32PhosphothreonineEVAATEDRR
28.78SysPTM
Link-
32Phosphothreonine.EVAATEDRR
28.78UniProtKB
Link-
56PhosphoserineAGSLSPQDP
23.39Phosphositeplus
Link-
141PhosphoserineFERQSGTPP
51.35Phosphositeplus
Link-
180PhosphoserineNRAGSISTL
16.63Phosphositeplus
Link-
180PhosphoserineNRAGSISTL
16.63SysPTM
Link-
180Phosphoserine.NRAGSISTL
16.63UniProtKB
Link-
182PhosphoserineAGSISTLDS
25.31Phosphositeplus
Link-
183PhosphothreonineGSISTLDSL
32.68Phosphositeplus
Link-
183PhosphothreonineGSISTLDSL
32.68SysPTM
Link-
183Phosphothreonine.GSISTLDSL
32.68UniProtKB
Link-
186PhosphoserineSTLDSLDFA
32.71Phosphositeplus
Link-
186PhosphoserineSTLDSLDFA
32.71SysPTM
Link-
186Phosphoserine.STLDSLDFA
32.71UniProtKB
Link-
193PhosphoserineFARYSDDGN
24.54Phosphositeplus
Link-
200PhosphothreonineGNRETDERV
39.67Phosphositeplus
Link-
243PhosphoserineKNYKSSPEI
40.54Phosphositeplus
Link-
244PhosphoserineNYKSSPEIQ
23.54Phosphositeplus
Link-
337PhosphothreonineLEALTPILG
18.48Phosphositeplus
Link-
367PhosphoserineEDKISLLNN
32.32Phosphositeplus
Link-
385PhosphoserineRRLESEMDI
42.69Phosphositeplus
Link-
422PhosphoserineDNRQSPAVN
16.16Phosphositeplus
Link-
792PhosphoserinePRPMSPLQD
25.74Phosphositeplus
Link-
1149PhosphoserineMEHLSPEHE
30.10Phosphositeplus
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
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-22; THR-32;SER-180; THR-183 AND SER-186, AND MASS SPECTROMETRY.
"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-186, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures