WDR26_MOUSE - dbPTM
WDR26_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WDR26_MOUSE
UniProt AC Q8C6G8
Protein Name WD repeat-containing protein 26
Gene Name Wdr26
Organism Mus musculus (Mouse).
Sequence Length 641
Subcellular Localization Cytoplasm . Mitochondrion .
Protein Description G-beta-like protein involved in cell signal transduction (By similarity). Acts as a negative regulator in MAPK signaling pathway (By similarity). Functions as a scaffolding protein to promote G beta:gamma-mediated PLCB2 plasma membrane translocation and subsequent activation in leukocytes (By similarity). Acts as a negative regulator of the canonical Wnt signaling pathway through preventing ubiquitination of beta-catenin CTNNB1 by the beta-catenin destruction complex, thus negatively regulating CTNNB1 degradation (By similarity). Serves as a scaffold to coordinate PI3K/AKT pathway-driven cell growth and migration (By similarity). Protects cells from oxidative stress-induced apoptosis via the down-regulation of AP-1 transcriptional activity as well as by inhibiting cytochrome c release from mitochondria (By similarity). Protects also cells by promoting hypoxia-mediated autophagy and mitophagy (By similarity)..
Protein Sequence MQANGAGGGGGGGGGGQGQTPELACLSAQNGESSPSATSAGDLAHANGLLPAAPSAAGNNSNSLSVNNGVPGGAAAASATAAAAQATPELGSSLKKKKRLSQSDEDVIRLIGQHLNGLGLNQTVDLLMQESGCRLEHPSATKFRNHVMEGDWDKAENDLNELKPLVHSPHAIVVRGALEISQTLLGIIVRMKFLLLQQKYLEYLEDGKVLEALQVLRCELTPLKYNTERIHVLSGYLMCSHAEDLRAKAEWEGKGTASRSKLLDKLQTYLPPSVMLPPRRLQTLLRQAVELQRDRCLYHNTKLDNNLDSVSLLIDHVCSRRQFPCYTQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPDTHLLKLLKTLEGHAYGVSYIAWSPDDSYLVACGPDDCSELWLWNVQTGELRTKMSQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLDGNLLDSWEGVRVQCLWCLSDGKTVLASDTHQRVRGYNFEDLTDRNIVQEDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIHSCFGGHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIWGPAPFIDHQNIEEECSSMDS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
101PhosphorylationLKKKKRLSQSDEDVI
HHHCHHCCCCHHHHH
31.5027087446
103PhosphorylationKKKRLSQSDEDVIRL
HCHHCCCCHHHHHHH
39.3227087446
181PhosphorylationVRGALEISQTLLGII
EECHHHHHHHHHHHH
14.0326745281
183PhosphorylationGALEISQTLLGIIVR
CHHHHHHHHHHHHHH
19.7026745281
192UbiquitinationLGIIVRMKFLLLQQK
HHHHHHHHHHHHHHH
23.4622790023
221PhosphorylationQVLRCELTPLKYNTE
HHHHCCCCCCCCCHH
12.3219367708
318GlutathionylationSLLIDHVCSRRQFPC
HHHHHHHHHHCCCCC
2.0524333276
318S-palmitoylationSLLIDHVCSRRQFPC
HHHHHHHHHHCCCCC
2.0528680068
349UbiquitinationKFSNDGTKLATGSKD
EECCCCCEECCCCCC
41.4722790023
439UbiquitinationVAWNPDGKRFVTGGQ
EEECCCCCCCCCCCC
50.4722790023
516UbiquitinationIMSFTISKNGRLALL
EEEEEECCCCEEEEE
60.6222790023
638PhosphorylationNIEEECSSMDS----
CHHHHHHCCCC----
37.9629899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of WDR26_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WDR26_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of WDR26_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WDR26_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WDR26_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASSSPECTROMETRY.

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