AXIN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AXIN2_MOUSE
• UniProt AC: O88566
• Protein Name: Axin-2
• Gene Name: Axin2
• Organism: Mus musculus (Mouse).
• Sequence Length: 840
• Subcellular Localization: Cytoplasm.
• Protein Description: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (By similarity)..
• Protein Sequence: MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSDPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGVPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHQHHHHQQCHTLLPTGGKLPPVAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHPKAPEPLPGEQFCGSRGGTLPKRNAKGTEPGLALSARDGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSAQSIRKSYPLESACAAPGERVSRHHLLGASGHSRSVARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHSAAGQAGASPFANPSLAPEDHKEPKKLASVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID

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
70	Phosphorylation	GEPEGRASPDSPLTR CCCCCCCCCCCCHHH	28.07	28066266
73	Phosphorylation	EGRASPDSPLTRWTK CCCCCCCCCHHHHHH	25.78	28066266
202	Phosphorylation	IYLEYVRSGGENTAY EEEEEHHHCCCCEEE	40.90	28576409
207	Phosphorylation	VRSGGENTAYMSNGG HHHCCCCEEEECCCC	18.18	28576409
209	Phosphorylation	SGGENTAYMSNGGLG HCCCCEEEECCCCHH	10.07	28576409
211	Phosphorylation	GENTAYMSNGGLGSL CCCEEEECCCCHHHH	21.46	28576409
217	Phosphorylation	MSNGGLGSLKVLCGY ECCCCHHHHHHHHHC	30.02	28576409
244	Phosphorylation	ADLKCKLSPTVVGLS HHCCCCCCCCEEECC	12.20	23984901
246	Phosphorylation	LKCKLSPTVVGLSSK CCCCCCCCEEECCCC	25.17	23984901
430	Phosphorylation	LALLPSGSYEEDPQT EEECCCCCCCCCCCH	33.44	29899451
431	Phosphorylation	ALLPSGSYEEDPQTI EECCCCCCCCCCCHH	27.19	29899451
449	Phosphorylation	HLSRVLKTPGCQSPG HHHHHHCCCCCCCCC	22.28	28066266
454	Phosphorylation	LKTPGCQSPGVGRYS HCCCCCCCCCCCCCC	27.91	28066266
460	Phosphorylation	QSPGVGRYSPRSRSP CCCCCCCCCCCCCCC	19.66	22817900
461	Phosphorylation	SPGVGRYSPRSRSPD CCCCCCCCCCCCCCC	16.69	21743459
464	Phosphorylation	VGRYSPRSRSPDHHH CCCCCCCCCCCCCCC	40.26	22817900
485	Phosphorylation	QCHTLLPTGGKLPPV HHEEECCCCCCCCCC	59.54	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AXIN2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AXIN2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AXIN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RNF11_MOUSE	Rnf11	physical	16601693
SMAD7_MOUSE	Smad7	physical	16601693
CTNB1_MOUSE	Ctnnb1	physical	9554852
GSK3B_MOUSE	Gsk3b	physical	9554852
LEF1_MOUSE	Lef1	genetic	9554852

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 TYR-460 AND SER-464, ANDMASS SPECTROMETRY.
PubMed: 19367708