LRRF2_MOUSE - dbPTM
LRRF2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRRF2_MOUSE
UniProt AC Q91WK0
Protein Name Leucine-rich repeat flightless-interacting protein 2
Gene Name Lrrfip2
Organism Mus musculus (Mouse).
Sequence Length 415
Subcellular Localization
Protein Description May function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding (By similarity)..
Protein Sequence MGTPGSGRKRTPVKDRFSAEDEALSNIAREAEARLAAKRAARAEARDIRMRELERQQREGVEDTLSLRSLGSHRLDEKSDKQYAENYTRPSSRNSASATTPLSGQSSRRGSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMDELKEGLRQRDELIEKHGLVIIPDSTPNGDVHHEPVVGAITAVSQEAAQVLESAGEGPLDVRLRKLAGEKDELLSQIRKLKLQLEEERQKCSRNDGMSGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDIATLEQSISRLEGQVLRYKTAAENAEKIEDELKAERRKLQRELRTAQDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ
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
11PhosphorylationPGSGRKRTPVKDRFS
CCCCCCCCCCCCCCC
35.15-
18PhosphorylationTPVKDRFSAEDEALS
CCCCCCCCHHHHHHH
31.4826824392
68 (in isoform 2)Phosphorylation-26.8529514104
79PhosphorylationSHRLDEKSDKQYAEN
CCCCCHHHHHHHHHH
48.2525777480
83PhosphorylationDEKSDKQYAENYTRP
CHHHHHHHHHHCCCC
22.9425777480
87PhosphorylationDKQYAENYTRPSSRN
HHHHHHHCCCCCCCC
8.8125777480
88PhosphorylationKQYAENYTRPSSRNS
HHHHHHCCCCCCCCC
47.9224899341
91PhosphorylationAENYTRPSSRNSASA
HHHCCCCCCCCCCCC
38.3425266776
92PhosphorylationENYTRPSSRNSASAT
HHCCCCCCCCCCCCC
37.8627742792
95PhosphorylationTRPSSRNSASATTPL
CCCCCCCCCCCCCCC
23.6121183079
100PhosphorylationRNSASATTPLSGQSS
CCCCCCCCCCCCCCC
23.19-
103PhosphorylationASATTPLSGQSSRRG
CCCCCCCCCCCCCCC
35.67-
106PhosphorylationTTPLSGQSSRRGSGD
CCCCCCCCCCCCCCC
29.36-
107PhosphorylationTPLSGQSSRRGSGDT
CCCCCCCCCCCCCCH
20.36-
111PhosphorylationGQSSRRGSGDTSSLI
CCCCCCCCCCHHHCC
31.5124925903
114PhosphorylationSRRGSGDTSSLIDPD
CCCCCCCHHHCCCCC
24.6024925903
115PhosphorylationRRGSGDTSSLIDPDT
CCCCCCHHHCCCCCC
28.0824925903
116PhosphorylationRGSGDTSSLIDPDTS
CCCCCHHHCCCCCCC
31.2824925903
122PhosphorylationSSLIDPDTSLSELRE
HHCCCCCCCHHHHHH
36.6325619855
123PhosphorylationSLIDPDTSLSELRES
HCCCCCCCHHHHHHH
36.9625619855
125PhosphorylationIDPDTSLSELRESLS
CCCCCCHHHHHHHHH
34.0625619855
299PhosphorylationCSRNDGMSGDLAGLQ
HHCCCCCCHHCCCCC
34.3822802335
375AcetylationELKAERRKLQRELRT
HHHHHHHHHHHHHHH
56.018440431

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 LRRF2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRRF2_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 LRRF2_MOUSE !!

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

Oops, there are no PPI records of LRRF2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRRF2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-111, 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 THR-114 AND SER-116, ANDMASS SPECTROMETRY.

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