dbPTM

SNX27_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNX27_MOUSE
UniProt AC	Q3UHD6
Protein Name	Sorting nexin-27
Gene Name	Snx27
Organism	Mus musculus (Mouse).
Sequence Length	539
Subcellular Localization	Early endosome membrane Peripheral membrane protein. Cytoplasm, cytosol. Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products (By similarity)..
Protein Description	Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes..
Protein Sequence	MADEDGEGIHPSAPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVINHSFVRKLAPNEFPHKLYVQNYTSAVPGTCLTIRKWLFTTEEEVLLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLHEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Phosphorylation	NGGGGGGSGLHCAGN CCCCCCCCCCCCCCC	41.26	25367039
36	Ubiquitination	AGNGGGGGGGPRVVR CCCCCCCCCCCCEEE	40.95	27667366
47	Phosphorylation	RVVRIVKSESGYGFN CEEEEEECCCCCCEE	26.54	28833060
49	Phosphorylation	VRIVKSESGYGFNVR EEEEECCCCCCEEEE	44.39	25521595
51	Phosphorylation	IVKSESGYGFNVRGQ EEECCCCCCEEEEEE	28.02	28833060
60	Phosphorylation	FNVRGQVSEGGQLRS EEEEEEECCCCCEEE	23.72	24719451
156	Phosphorylation	GQSFYDYTEKQAVPI CHHHCCCCCCCCCCC	33.53	-
213	Phosphorylation	KREFANFTFPRLPGK HHHHHCCCCCCCCCC	32.32	22817900
218	Ubiquitination	NFTFPRLPGKWPFSL CCCCCCCCCCCCCCC	43.53	27667366
220	Ubiquitination	TFPRLPGKWPFSLSE CCCCCCCCCCCCCCH	50.16	22790023
267	Phosphorylation	LSESDENYNGVSDVE HCCCCCCCCCCCCEE	15.96	24224561
315	Phosphorylation	MDSTTVNYFALFEVI CCCCCCCHHHHHHHH	5.96	-
402	Ubiquitination	EKSYQLQKLHEQRKM HHHHHHHHHHHHHHH	61.47	27667366

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 SNX27_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SNX27_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 SNX27_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of SNX27_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASSSPECTROMETRY.	17114649 [Abstract]