SNX1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNX1_MOUSE
• UniProt AC: Q9WV80
• Protein Name: Sorting nexin-1
• Gene Name: Snx1
• Organism: Mus musculus (Mouse).
• Sequence Length: 522
• Subcellular Localization: Endosome membrane ; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane ; Peripheral membrane protein ; Cytoplasmic side . Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, la
• 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. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (By similarity)..
• Protein Sequence: MASGGGGCSASERLPPPFPGMDPESEGAAGASEPEAGDSDTEGEDIFTGAAAATKPQSPKKTTSLFPIKNGSKENGIHEDQDQEPQDLFADATVELSLDSTQNNQKTMPGKTLTSHSPQEATNSPKPQPSYEELEEEEQEDQFDLTVGITDPEKIGDGMNAYVAYKVTTQTSLPMFRSRQFAVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKVGKEDSSSAEFLEKRRAALERYLQRIVNHPTMLQDPDVREFLEKEELPRAVGTQALSGAGLLKMFNKATDAVSKMTIKMNESDIWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTALFAKSLAMLGSSEDNTALSRALSQLAEVEEKIEQLHQEQANNDSFLLAELLSDYIRLLAIVRAAFDQRMKTWQRWQDAQATLQKKRESEARLLWANKPDKLQQAKDEITEWESRVTQYERDFERISTVVRKEVTRFEKEKSKDFKNHVMKYLETLLHSQQQLAKYWEAFLPEAKAIS

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
25	Phosphorylation	FPGMDPESEGAAGAS CCCCCHHCCCCCCCC	46.87	21082442
32	Phosphorylation	SEGAAGASEPEAGDS CCCCCCCCCCCCCCC	53.41	21743459
39	Phosphorylation	SEPEAGDSDTEGEDI CCCCCCCCCCCCCCC	45.58	21743459
41	Phosphorylation	PEAGDSDTEGEDIFT CCCCCCCCCCCCCCC	50.25	21743459
48	Phosphorylation	TEGEDIFTGAAAATK CCCCCCCCCCHHCCC	26.67	22817900
54	Phosphorylation	FTGAAAATKPQSPKK CCCCHHCCCCCCCCC	38.23	22817900
58	Phosphorylation	AAATKPQSPKKTTSL HHCCCCCCCCCCCCC	47.41	21743459
72	Phosphorylation	LFPIKNGSKENGIHE CEECCCCCCCCCCCC	46.30	29514104
117	Phosphorylation	GKTLTSHSPQEATNS CCCCCCCCCCHHHCC	28.22	28507225
122	Phosphorylation	SHSPQEATNSPKPQP CCCCCHHHCCCCCCC	35.16	22807455
124	Phosphorylation	SPQEATNSPKPQPSY CCCHHHCCCCCCCCH	29.91	22807455
188	Phosphorylation	FAVKRRFSDFLGLYE HHHHHHHHHHHHHHH	26.16	26824392
196	Ubiquitination	DFLGLYEKLSEKHSQ HHHHHHHHHHHHHHC	43.70	-
229	Phosphorylation	VKVGKEDSSSAEFLE EEECCCCCCHHHHHH	27.55	19367708
230	Phosphorylation	KVGKEDSSSAEFLEK EECCCCCCHHHHHHH	45.98	29176673
231	Phosphorylation	VGKEDSSSAEFLEKR ECCCCCCHHHHHHHH	35.45	29176673
237	Acetylation	SSAEFLEKRRAALER CHHHHHHHHHHHHHH	49.70	90447
280	Phosphorylation	AVGTQALSGAGLLKM HHHHHHHCHHHHHHH	29.61	27180971
286	Ubiquitination	LSGAGLLKMFNKATD HCHHHHHHHHHHHHH	46.63	-
318	S-palmitoylation	EKLQEVECEEQRLRK HHHHHCCCHHHHHHH	9.36	28680068
368	Phosphorylation	TALSRALSQLAEVEE HHHHHHHHHHHHHHH	23.35	26824392
450	Ubiquitination	PDKLQQAKDEITEWE CHHHHHHHHHHHHHH	52.10	-
463	Phosphorylation	WESRVTQYERDFERI HHHHHHHHHHHHHHH	11.99	-
495	Ubiquitination	DFKNHVMKYLETLLH HHHHHHHHHHHHHHH	45.66	-

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

Oops, there are no upstream regulatory protein records of SNX1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNX1_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 SNX1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SNX1_MOUSE !!

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 SER-188, AND MASSSPECTROMETRY.
PubMed: 19367708