SNX9_MOUSE - dbPTM
SNX9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX9_MOUSE
UniProt AC Q91VH2
Protein Name Sorting nexin-9
Gene Name Snx9
Organism Mus musculus (Mouse).
Sequence Length 595
Subcellular Localization Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network. Cell projection, ruffle. Cytopla
Protein Description Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate (By similarity)..
Protein Sequence MATKARVMYDFAAEPGNNELTVTEGEIITVTNPNVGGGWLEGKNNKGEQGLVPTDYVEILPNDGKDPFSCGNSVADQAFLDSLTASTAQTNSSSANSNNQVGGGNDPWTAWNAPKPGNWDSSDAWGSRTDGTSAQRNSSANNWDTGFGHPQAYQGPATGDDDEWDEDWDDPKSSSPYFKDSEPAEAGGIQRGNSRAGASSMKLPLNKFPGFAKPGMEQYLLAKQLAKPKEKIAIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVVSESEVFQQFLNFRDEKEWKTGKRKAEKDELVGVMIFSTMEPEAPDLDLIEIEQKCDAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLAAVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGAHKGAIEKVKESDKLVATSKITPQDKQTMVKRVGTMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
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
121PhosphorylationPKPGNWDSSDAWGSR
CCCCCCCCCCCCCCC		23.0228066266
122PhosphorylationKPGNWDSSDAWGSRT
CCCCCCCCCCCCCCC		28.9528066266
127PhosphorylationDSSDAWGSRTDGTSA
CCCCCCCCCCCCCCC		22.7028066266
129PhosphorylationSDAWGSRTDGTSAQR
CCCCCCCCCCCCCCC		40.2423684622
132PhosphorylationWGSRTDGTSAQRNSS
CCCCCCCCCCCCCCC		24.5725338131
133PhosphorylationGSRTDGTSAQRNSSA
CCCCCCCCCCCCCCC		28.1225338131
138PhosphorylationGTSAQRNSSANNWDT
CCCCCCCCCCCCCCC		32.7725338131
139PhosphorylationTSAQRNSSANNWDTG
CCCCCCCCCCCCCCC		38.2725338131
158PhosphorylationQAYQGPATGDDDEWD
HHHCCCCCCCCCCCC		44.2525338131
173PhosphorylationEDWDDPKSSSPYFKD
CCCCCCCCCCCCCCC		41.2425619855
174PhosphorylationDWDDPKSSSPYFKDS
CCCCCCCCCCCCCCC		41.2725619855
175PhosphorylationWDDPKSSSPYFKDSE
CCCCCCCCCCCCCCC		30.6122942356
177PhosphorylationDPKSSSPYFKDSEPA
CCCCCCCCCCCCCHH		25.8025619855
179UbiquitinationKSSSPYFKDSEPAEA
CCCCCCCCCCCHHHC		55.27-
181PhosphorylationSSPYFKDSEPAEAGG
CCCCCCCCCHHHCCC		46.1825619855
194PhosphorylationGGIQRGNSRAGASSM
CCCCCCCCCCCCCCC		26.7425266776
199PhosphorylationGNSRAGASSMKLPLN
CCCCCCCCCCCCCCC		30.0126643407
200PhosphorylationNSRAGASSMKLPLNK
CCCCCCCCCCCCCCC		21.2826824392
207UbiquitinationSMKLPLNKFPGFAKP
CCCCCCCCCCCCCCC		61.70-
219PhosphorylationAKPGMEQYLLAKQLA
CCCHHHHHHHHHHHC		7.1429514104
223UbiquitinationMEQYLLAKQLAKPKE
HHHHHHHHHHCCCHH		45.90-
239PhosphorylationIAIIVGDYGPMWVYP
EEEEECCCCCEEECC		19.7322817900
261PhosphorylationVADPRKGSKMYGLKS
EECCCCCCCEECCCC		19.79-
264PhosphorylationPRKGSKMYGLKSYIE
CCCCCCEECCCCEEE		24.0425367039
267UbiquitinationGSKMYGLKSYIEYQL
CCCEECCCCEEEEEE		36.53-
269PhosphorylationKMYGLKSYIEYQLTP
CEECCCCEEEEEECC		9.0029514104
272PhosphorylationGLKSYIEYQLTPTNT
CCCCEEEEEECCCCC		10.1629514104
288AcetylationRSVNHRYKHFDWLYE
CCCCHHHHCHHHHHH		37.4423236377
407AcetylationDAVGKFTKAMDDGVK
CCCHHHHHHCCHHHH		44.8622826441
425UbiquitinationTVGQEHWKRCTGPLP
HHCHHHHHHCCCCCC		39.23-
428PhosphorylationQEHWKRCTGPLPKEY
HHHHHHCCCCCCHHH		45.9627149854
511UbiquitinationPDIIGAHKGAIEKVK
HHHHHHCHHHHHHHH		49.88-
528UbiquitinationDKLVATSKITPQDKQ
CCEEEECCCCHHHHH		46.36-
536PhosphorylationITPQDKQTMVKRVGT
CCHHHHHHHHHHHHH		29.6719144319
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
-KUbiquitinationE3 ubiquitin ligaseItchQ8C863
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX9_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 SNX9_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INSR_MOUSEInsrphysical
12917015
IGF1R_MOUSEIgf1rphysical
12917015
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNX9_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-175, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-536, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory