Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein SGT1  

UniProtKB / Swiss-Prot ID :  SGT1_HUMAN

Gene Name (Synonyms) : 
ECD, SGT1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Novel regulator of p53 stability and function. May also be a transcriptional activator required for the expression of glycolytic genes. 

Protein Sequence MEETMKLATMEDTVEYCLFLIPDESRDSDKHKEILQKYIERIITRFAPMLVPYIWQNQPFNLKYKPGKGG...
Predicted Secondary Structure CCCCCCHHHHHHHHHHHEEECCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHEECCCCEEEEEECCCC...
Protein Variant
LocationDescription
45R -> Q (in dbSNP:rs3812619). VAR_051970
281R -> G (could be a rare polymorphism). VAR_012191
452E -> Q (in dbSNP:rs3736518). VAR_051971
501N -> S (in dbSNP:rs36152134). VAR_051972
634D -> G (in dbSNP:rs2271904). VAR_051973
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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
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
16PhosphotyrosineDTVEYCLFL
HHHHHHEEE
7.07HPRD
Link-
162PhosphothreonineSWLPTTPPT
CCCCCCCCC
50.17HPRD
Link-
186PhosphoserineLASESIRAA
HHHHHHHHH
18.19HPRD
Link-
186PhosphoserineLASESIRAA
HHHHHHHHH
18.19Phosphositeplus
Link-
205PhosphoserineKIQASLHRA
HHCCCCCCE
14.34Phosphositeplus
Link-
325PhosphoserineDCKKSLVTA
CCCCHHHHH
17.36HPRD
Link-
335PhosphoserinePLWASFLES
HHHHHHHHH
20.84HPRD
Link-
339PhosphoserineSFLESLKKN
HHHHHHHHC
47.86HPRD
Link-
339PhosphoserineSFLESLKKN
HHHHHHHHC
47.86Phosphositeplus
Link-
347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NDYFKGLIE
CCHHHHHHC
46.72Phosphositeplus
Link-
458Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SESMKAFIS
HHHHHHHHH
49.80Phosphositeplus
Link-
463Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AFISKVSTH
HHHHHHHCC
35.07Phosphositeplus
Link-
503PhosphoserineRPNESDSDD
CCCCCCCCC
49.40HPRD
Link-
503PhosphoserineRPNESDSDD
CCCCCCCCC
49.40PhosphoELM
Link-
503PhosphoserineRPNESDSDD
CCCCCCCCC
49.40Phosphositeplus
Link-
503PhosphoserineRPNESDSDD
CCCCCCCCC
49.40SysPTM
Link-
503Phosphoserine.RPNESDSDD
CCCCCCCCC
49.40UniProtKB
Link-
505PhosphoserineNESDSDDLD
CCCCCCCCC
42.16HPRD
Link-
505PhosphoserineNESDSDDLD
CCCCCCCCC
42.16PhosphoELM
Link-
505PhosphoserineNESDSDDLD
CCCCCCCCC
42.16Phosphositeplus
Link-
505PhosphoserineNESDSDDLD
CCCCCCCCC
42.16SysPTM
Link-
505Phosphoserine.NESDSDDLD
CCCCCCCCC
42.16UniProtKB
Link-
518PhosphoserineECLDSDDDL
ECCCCCCCC
29.95HPRD
Link-
518PhosphoserineECLDSDDDL
ECCCCCCCC
29.95PhosphoELM
Link-
518PhosphoserineECLDSDDDL
ECCCCCCCC
29.95Phosphositeplus
Link-
518PhosphoserineECLDSDDDL
ECCCCCCCC
29.95SysPTM
Link-
518Phosphoserine.ECLDSDDDL
ECCCCCCCC
29.95UniProtKB
Link-
534PhosphoserineGEEASLKGT
CCHHHHHCC
33.62HPRD
Link-
534PhosphoserineGEEASLKGT
CCHHHHHCC
33.62PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
GCR_HUMANyeast 2-hybridHPRD:11032HPRD9928932
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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
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503; SER-505 ANDSER-518, AND MASS SPECTROMETRY.
"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-503; SER-505 ANDSER-518, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures