SNX2_MOUSE - dbPTM
SNX2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX2_MOUSE
UniProt AC Q9CWK8
Protein Name Sorting nexin-2
Gene Name Snx2
Organism Mus musculus (Mouse).
Sequence Length 519
Subcellular Localization Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, lamellipodium. Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early end
Protein Description Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity. Required for retrograde endosome-to-TGN transport of TGN38. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN (By similarity)..
Protein Sequence MAAEREPPPLGDVKPTDFEELEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGSKPVEVVLDDDREDLFAEATEEVSLDSPERELILSSEPSPAVTPVTPTTLIAPRIESKSISAPVIFDRSRDEIEEEANGDIFDIEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHASVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKRETEAKMMVANKPDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKAVIIKYLESLVQTQQQLIKYWEAFLPEAKAIA
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
85PhosphorylationTEEVSLDSPERELIL
HEECCCCCCCCEEEC		33.67-
93PhosphorylationPERELILSSEPSPAV
CCCEEECCCCCCCCC		26.1725168779
94PhosphorylationERELILSSEPSPAVT
CCEEECCCCCCCCCC		50.5122942356
97PhosphorylationLILSSEPSPAVTPVT
EECCCCCCCCCCCCC		22.8026824392
101PhosphorylationSEPSPAVTPVTPTTL
CCCCCCCCCCCCCEE		17.7225521595
104PhosphorylationSPAVTPVTPTTLIAP
CCCCCCCCCCEEECC		19.0025521595
106PhosphorylationAVTPVTPTTLIAPRI
CCCCCCCCEEECCCC		25.5224723360
107PhosphorylationVTPVTPTTLIAPRIE
CCCCCCCEEECCCCC		19.8525521595
115PhosphorylationLIAPRIESKSISAPV
EECCCCCCCCCCCCE		29.3624719451
116AcetylationIAPRIESKSISAPVI
ECCCCCCCCCCCCEE		38.7323806337
116UbiquitinationIAPRIESKSISAPVI
ECCCCCCCCCCCCEE		38.7327667366
117PhosphorylationAPRIESKSISAPVIF
CCCCCCCCCCCCEEE		30.9325521595
119PhosphorylationRIESKSISAPVIFDR
CCCCCCCCCCEEEEC		33.3425521595
165PhosphorylationAYMAYRVTTKTSLSM
HEEEEEEECCCCHHH		17.3629472430
166PhosphorylationYMAYRVTTKTSLSMF
EEEEEEECCCCHHHC		29.4829472430
167UbiquitinationMAYRVTTKTSLSMFS
EEEEEECCCCHHHCC		27.10-
168PhosphorylationAYRVTTKTSLSMFSK
EEEEECCCCHHHCCC		32.5728576409
169PhosphorylationYRVTTKTSLSMFSKS
EEEECCCCHHHCCCC		21.7229472430
171PhosphorylationVTTKTSLSMFSKSEF
EECCCCHHHCCCCCH		19.9724759943
174PhosphorylationKTSLSMFSKSEFSVK
CCCHHHCCCCCHHHH		26.9929472430
175AcetylationTSLSMFSKSEFSVKR
CCHHHCCCCCHHHHH		42.627718691
181UbiquitinationSKSEFSVKRRFSDFL
CCCCHHHHHHHHHHH		36.3427667366
181AcetylationSKSEFSVKRRFSDFL
CCCCHHHHHHHHHHH		36.347718701
185PhosphorylationFSVKRRFSDFLGLHS
HHHHHHHHHHHHHHH		26.1625521595
192PhosphorylationSDFLGLHSKLASKYL
HHHHHHHHHHHHHHC		34.1125266776
193UbiquitinationDFLGLHSKLASKYLH
HHHHHHHHHHHHHCC		37.01-
203PhosphorylationSKYLHVGYIVPPAPE
HHHCCEEEECCCCCC		9.54-
212PhosphorylationVPPAPEKSIVGMTKV
CCCCCCCCEECEEEE		22.3525521595
218UbiquitinationKSIVGMTKVKVGKED
CCEECEEEEEECCCC		31.03-
220UbiquitinationIVGMTKVKVGKEDSS
EECEEEEEECCCCCC		46.99-
223UbiquitinationMTKVKVGKEDSSSTE
EEEEEECCCCCCCHH		62.43-
226PhosphorylationVKVGKEDSSSTEFVE
EEECCCCCCCHHHHH		27.5526824392
227PhosphorylationKVGKEDSSSTEFVEK
EECCCCCCCHHHHHH		54.3118779572
228PhosphorylationVGKEDSSSTEFVEKR
ECCCCCCCHHHHHHH		35.5918779572
229PhosphorylationGKEDSSSTEFVEKRR
CCCCCCCHHHHHHHH		35.0818779572
234SuccinylationSSTEFVEKRRAALER
CCHHHHHHHHHHHHH		41.7123954790
273PhosphorylationELPRAVNTQALSGAG
CCCCCCCHHHHCHHH		14.5022324799
277PhosphorylationAVNTQALSGAGILRM
CCCHHHHCHHHHHHH		29.6122942356
287UbiquitinationGILRMVNKAADAVNK
HHHHHHHHHHHHHHH		33.2827667366
309AcetylationSDAWFEEKQQQFENL
HHHHHHHHHHHHHCH		46.3223954790
341PhosphorylationRKELSANTAAFAKSA
HHHCCHHHHHHHHHH		21.0520139300
346UbiquitinationANTAAFAKSAAMLGN
HHHHHHHHHHHHHCC		33.89-
354PhosphorylationSAAMLGNSEDHTALS
HHHHHCCCHHHHHHH		42.4729514104
365PhosphorylationTALSRALSQLAEVEE
HHHHHHHHHHHHHHH		23.3526824392
447MalonylationPDKIQQAKNEIREWE
HHHHHHHHHHHHHHH		51.2626320211
468PhosphorylationERDFEQISKTIRKEV
CCCHHHHHHHHHHHH		24.3621454597
469AcetylationRDFEQISKTIRKEVG
CCHHHHHHHHHHHHC		49.99-
487UbiquitinationKERVKDFKAVIIKYL
HHHHHHHHHHHHHHH		52.45-
487AcetylationKERVKDFKAVIIKYL
HHHHHHHHHHHHHHH		52.4523236377
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
104TPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX2_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 SNX2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SNX2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNX2_MOUSE

loading...

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-185, 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-119, AND MASSSPECTROMETRY.

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