Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein FAM83G  

UniProtKB / Swiss-Prot ID :  FA83G_HUMAN

Gene Name (Synonyms) : 
FAM83G  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MAFSQVQCLDDNHVNWRSSESKPEFFYSEEQRLALEALVARGRDAFYEVLKRENIRDFLSELELKRILET...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
109I -> T (in dbSNP:rs2074283). VAR_053903
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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
Protein Variant
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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
4Phosphoserine-MAFSQVQC
-
21.65Phosphositeplus
Link-
124PhosphoserineWPQKSDRSI
32.77Phosphositeplus
Link-
127PhosphoserineKSDRSIPQL
43.54HPRD
Link-
127PhosphoserineKSDRSIPQL
43.54Phosphositeplus
Link-
356PhosphoserineVKAKSVDEI
39.39HPRD
Link-
356PhosphoserineVKAKSVDEI
39.39PhosphoELM
Link-
356PhosphoserineVKAKSVDEI
39.39Phosphositeplus
Link-
356PhosphoserineVKAKSVDEI
39.39SysPTM
Link-
356Phosphoserine.VKAKSVDEI
39.39UniProtKB
Link-
634PhosphoserineRRRHSEQVA
28.10Phosphositeplus
Link-
650PhosphoserineRRQLSAPHI
31.26Phosphositeplus
Link-
666PhosphoserinePQGGSPWAQ
24.88HPRD
Link-
666PhosphoserinePQGGSPWAQ
24.88PhosphoELM
Link-
666PhosphoserinePQGGSPWAQ
24.88Phosphositeplus
Link-
666PhosphoserinePQGGSPWAQ
24.88SysPTM
Link-
666Phosphoserine.PQGGSPWAQ
24.88UniProtKB
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
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-666, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures