Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  WD repeat-containing protein 20  

UniProtKB / Swiss-Prot ID :  WDR20_HUMAN

Gene Name (Synonyms) : 
WDR20  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MATEGGGKEMNEIKTQFTTREGLYKLLPHSEYSRPNRVPFNSQGSNPVRVSFVNLNDQSGNGDRLCFNVG...
Predicted Secondary Structure CCCCCCCCCHHHHCCCCCCCCCEEEECCCCCCCCCCCCCCCCCCCCHHHEEEEEECCCCCCEEEEEEECC...
Protein Variant
LocationDescription
159P -> H (in dbSNP:rs17852545). VAR_031580
444G -> C (in dbSNP:rs12888595). VAR_053425
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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
76PhosphotyrosineELYFYIYKG
CEEEEECCC
6.98Phosphositeplus
Link-
308PhosphoserineKSWVSVVAF
CCCEEEEEE
12.48HPRD
Link-
330PhosphoserineEFSGSDEDF
EEEEECCCE
36.31SysPTM
Link-
347PhosphoserineDRANSTQSR
CCCEEEECC
27.17Phosphositeplus
Link-
348PhosphothreonineRANSTQSRL
CCEEEECCC
30.30Phosphositeplus
Link-
353PhosphoserineQSRLSKRNS
ECCCCCCCE
28.58Phosphositeplus
Link-
357PhosphoserineSKRNSTDSR
CCCCEEEEE
37.31HPRD
Link-
357PhosphoserineSKRNSTDSR
CCCCEEEEE
37.31Phosphositeplus
Link-
357PhosphoserineSKRNSTDSR
CCCCEEEEE
37.31SysPTM
Link-
357Phosphoserine.SKRNSTDSR
CCCCEEEEE
37.31UniProtKB
Link-
360PhosphoserineNSTDSRPVS
CEEEEEECC
38.27HPRD
Link-
360PhosphoserineNSTDSRPVS
CEEEEEECC
38.27Phosphositeplus
Link-
371PhosphoserineYRFGSVGQD
EEEEEECCC
21.99HPRD
Link-
432PhosphoserinePLPRSNSLP
CCCCCCCCC
28.91HPRD
Link-
432PhosphoserinePLPRSNSLP
CCCCCCCCC
28.91PhosphoELM
Link-
432PhosphoserinePLPRSNSLP
CCCCCCCCC
28.91Phosphositeplus
Link-
432PhosphoserinePLPRSNSLP
CCCCCCCCC
28.91SysPTM
Link-
432Phosphoserine.PLPRSNSLP
CCCCCCCCC
28.91UniProtKB
Link-
434PhosphoserinePRSNSLPHS
CCCCCCCCC
44.52HPRD
Link-
434PhosphoserinePRSNSLPHS
CCCCCCCCC
44.52PhosphoELM
Link-
434PhosphoserinePRSNSLPHS
CCCCCCCCC
44.52Phosphositeplus
Link-
434PhosphoserinePRSNSLPHS
CCCCCCCCC
44.52SysPTM
Link-
434Phosphoserine.PRSNSLPHS
CCCCCCCCC
44.52UniProtKB
Link-
441PhosphoserineHSAVSNAGS
CCCCCCCCC
22.22Phosphositeplus
Link-
445PhosphoserineSNAGSKSSV
CCCCCCCEE
27.27Phosphositeplus
Link-
483PhosphoserineKRNHSMGHI
CCCCCCCEE
29.97Phosphositeplus
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
"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-357, 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-432 AND SER-434, ANDMASS SPECTROMETRY.
"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 SER-434, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures