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 44  

UniProtKB / Swiss-Prot ID :  WDR44_MOUSE

Gene Name (Synonyms) : 
Wdr44  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network. Note=Colocalized with RAB11 along microtubules oriented toward lamellipodia (By similarity). 

Protein Function :  Downstream effector for RAB11. May be involved in vesicle recycling (By similarity). 

Protein Sequence MASESDTEEFYDAPEDVHLGTGYPVGSPGKVGLLSFKEAENTANQAGNESPVQELRQDVSKKIIESIIEE...
Predicted Secondary Structure CCCCCCCHHHHCCCCCEECCCCCCCCCCCCEEEEEEEECHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHH...
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
5PhosphoserineMASESDTEE
CCCCCCCHH
47.54SysPTM
Link-
11PhosphotyrosineTEEFYDAPE
CHHHHCCCC
17.93SysPTM
Link-
27PhosphoserineYPVGSPGKV
CCCCCCCCE
30.61Phosphositeplus
Link-
35PhosphoserineVGLLSFKEA
EEEEEEEEC
39.04Phosphositeplus
Link-
50PhosphoserineAGNESPVQE
CCCCCHHHH
34.08Phosphositeplus
Link-
164PhosphoserineLTEVSSGEQ
HHHHCCCCC
26.79Phosphositeplus
Link-
165PhosphoserineTEVSSGEQL
HHHCCCCCC
52.07Phosphositeplus
Link-
221PhosphothreoninePRHLTPEPD
CCCCCCCCC
21.34Phosphositeplus
Link-
264PhosphoserineRKKKSELEF
CCCCCCCCE
57.18Phosphositeplus
Link-
264Phosphoserine.RKKKSELEF
CCCCCCCCE
57.18UniProtKB
Link-
305PhosphoserineDSLPSLDLA
CCCCCCCCC
39.55Phosphositeplus
Link-
344PhosphoserineQRPRSNSGR
CCCCCCCCC
37.72Phosphositeplus
Link-
346PhosphoserinePRSNSGREL
CCCCCCCCC
40.24PhosphoELM
Link-
346PhosphoserinePRSNSGREL
CCCCCCCCC
40.24Phosphositeplus
Link-
346PhosphoserinePRSNSGREL
CCCCCCCCC
40.24SysPTM
Link-
346Phosphoserine.PRSNSGREL
CCCCCCCCC
40.24UniProtKB
Link-
351PhosphothreonineGRELTDEEI
CCCCCCCCE
36.29PhosphoELM
Link-
351PhosphothreonineGRELTDEEI
CCCCCCCCE
36.29Phosphositeplus
Link-
351PhosphothreonineGRELTDEEI
CCCCCCCCE
36.29SysPTM
Link-
351Phosphothreonine.GRELTDEEI
CCCCCCCCE
36.29UniProtKB
Link-
403PhosphothreonineSNDATQSDD
CCCCCCCCC
31.31Phosphositeplus
Link-
403PhosphothreonineSNDATQSDD
CCCCCCCCC
31.31SysPTM
Link-
405PhosphoserineDATQSDDEE
CCCCCCCCC
42.55PhosphoELM
Link-
405PhosphoserineDATQSDDEE
CCCCCCCCC
42.55Phosphositeplus
Link-
405PhosphoserineDATQSDDEE
CCCCCCCCC
42.55SysPTM
Link-
405Phosphoserine.DATQSDDEE
CCCCCCCCC
42.55UniProtKB
Link-
472PhosphoserineQDDPSSSDD
CCCCCCCCC
49.85PhosphoELM
Link-
472PhosphoserineQDDPSSSDD
CCCCCCCCC
49.85Phosphositeplus
Link-
472PhosphoserineQDDPSSSDD
CCCCCCCCC
49.85SysPTM
Link-
472Phosphoserine.QDDPSSSDD
CCCCCCCCC
49.85UniProtKB
Link-
473PhosphoserineDDPSSSDDE
CCCCCCCCC
43.08PhosphoELM
Link-
473PhosphoserineDDPSSSDDE
CCCCCCCCC
43.08Phosphositeplus
Link-
473PhosphoserineDDPSSSDDE
CCCCCCCCC
43.08SysPTM
Link-
473Phosphoserine.DDPSSSDDE
CCCCCCCCC
43.08UniProtKB
Link-
474PhosphoserineDPSSSDDEG
CCCCCCCCC
54.11PhosphoELM
Link-
474PhosphoserineDPSSSDDEG
CCCCCCCCC
54.11Phosphositeplus
Link-
474PhosphoserineDPSSSDDEG
CCCCCCCCC
54.11SysPTM
Link-
474Phosphoserine.DPSSSDDEG
CCCCCCCCC
54.11UniProtKB
Link-
481PhosphotyrosineEGMPYTRPV
CCCCCEEEE
13.39Phosphositeplus
Link-
497PhosphotyrosineFKGPYDFDQ
CCEEEECCC
37.60Phosphositeplus
Link-
509PhosphoserineVQDLSGEHM
EEEEECCCC
50.88Phosphositeplus
Link-
563PhosphoserineEGRVSPSPS
EEEEEECCC
20.49Phosphositeplus
Link-
565PhosphoserineRVSPSPSQE
EEEECCCCC
29.67SysPTM
Link-
567PhosphoserineSPSPSQESL
EECCCCCEE
51.41Phosphositeplus
Link-
567PhosphoserineSPSPSQESL
EECCCCCEE
51.41SysPTM
Link-
570PhosphoserinePSQESLSSS
CCCCEEEEE
26.39Phosphositeplus
Link-
570PhosphoserinePSQESLSSS
CCCCEEEEE
26.39SysPTM
Link-
576PhosphoserineSSSKSDTDM
EEEECCCEE
47.92Phosphositeplus
Link-
576PhosphoserineSSSKSDTDM
EEEECCCEE
47.92SysPTM
Link-
578PhosphothreonineSKSDTDMGV
EECCCEEEE
34.67Phosphositeplus
Link-
578PhosphothreonineSKSDTDMGV
EECCCEEEE
34.67SysPTM
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-405, AND MASSSPECTROMETRY.
"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-346; THR-351; SER-472;SER-473 AND SER-474, 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-264; SER-472; SER-473AND SER-474, 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