SNX16_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNX16_HUMAN
• UniProt AC: P57768
• Protein Name: Sorting nexin-16
• Gene Name: SNX16
• Organism: Homo sapiens (Human).
• Sequence Length: 344
• Subcellular Localization: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Lysosome.
• Protein Description: May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling. Plays a role in intracellular transport of vesicular stomatitis virus nucleocapsids from the endosome to the cytoplasm..
• Protein Sequence: MATPYVPVPMPIGNSASSFTTNRNQRSSSFGSVSTSSNSSKGQLEDSNMGNFKQTSVPDQMDNTSSVCSSPLIRTKFTGTASSIEYSTRPRDTEEQNPETVNWEDRPSTPTILGYEVMEERAKFTVYKILVKKTPEESWVVFRRYTDFSRLNDKLKEMFPGFRLALPPKRWFKDNYNADFLEDRQLGLQAFLQNLVAHKDIANCLAVREFLCLDDPPGPFDSLEESRAFCETLEETNYRLQKELLEKQKEMESLKKLLSEKQLHIDTLENRIRTLSLEPEESLDVSETEGEQILKVESSALEVDQDVLDEESRADNKPCLSFSEPENAVSEIEVAEVAYDAEED

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
3	Phosphorylation	-----MATPYVPVPM -----CCCCCCCCCC	17.54	23401153
15	Phosphorylation	VPMPIGNSASSFTTN CCCCCCCCCCCCCCC	25.06	23401153
17	Phosphorylation	MPIGNSASSFTTNRN CCCCCCCCCCCCCCC	26.30	23401153
18	Phosphorylation	PIGNSASSFTTNRNQ CCCCCCCCCCCCCCC	26.74	23401153
21	Phosphorylation	NSASSFTTNRNQRSS CCCCCCCCCCCCCCC	30.12	23401153
27	Phosphorylation	TTNRNQRSSSFGSVS CCCCCCCCCCCCCEE	22.14	23401153
28	Phosphorylation	TNRNQRSSSFGSVST CCCCCCCCCCCCEEC	31.69	30278072
29	Phosphorylation	NRNQRSSSFGSVSTS CCCCCCCCCCCEECC	34.57	30278072
32	Phosphorylation	QRSSSFGSVSTSSNS CCCCCCCCEECCCCC	15.75	23403867
34	Phosphorylation	SSSFGSVSTSSNSSK CCCCCCEECCCCCCC	25.03	23403867
35	Phosphorylation	SSFGSVSTSSNSSKG CCCCCEECCCCCCCC	33.74	23403867
36	Phosphorylation	SFGSVSTSSNSSKGQ CCCCEECCCCCCCCC	21.73	23403867
37	Phosphorylation	FGSVSTSSNSSKGQL CCCEECCCCCCCCCC	40.60	23403867
39	Phosphorylation	SVSTSSNSSKGQLED CEECCCCCCCCCCCC	35.06	23403867
40	Phosphorylation	VSTSSNSSKGQLEDS EECCCCCCCCCCCCC	45.09	23403867
55	Phosphorylation	NMGNFKQTSVPDQMD CCCCCCCCCCCCCCC	32.08	25850435
56	Phosphorylation	MGNFKQTSVPDQMDN CCCCCCCCCCCCCCC	29.20	25850435
64	Phosphorylation	VPDQMDNTSSVCSSP CCCCCCCCCCCCCCC	20.36	25850435
65	Phosphorylation	PDQMDNTSSVCSSPL CCCCCCCCCCCCCCE	27.33	25850435
66	Phosphorylation	DQMDNTSSVCSSPLI CCCCCCCCCCCCCEE	25.71	25850435
69	Phosphorylation	DNTSSVCSSPLIRTK CCCCCCCCCCEEEEE	32.60	25850435
70	Phosphorylation	NTSSVCSSPLIRTKF CCCCCCCCCEEEEEE	20.71	30278072
75	O-linked_Glycosylation	CSSPLIRTKFTGTAS CCCCEEEEEEEECCC	24.42	30379171
75	Phosphorylation	CSSPLIRTKFTGTAS CCCCEEEEEEEECCC	24.42	26074081
78	Phosphorylation	PLIRTKFTGTASSIE CEEEEEEEECCCCEE	34.87	28348404
80	Phosphorylation	IRTKFTGTASSIEYS EEEEEEECCCCEEEE	21.95	28857561
82	Phosphorylation	TKFTGTASSIEYSTR EEEEECCCCEEEECC	31.52	23312004
83	Phosphorylation	KFTGTASSIEYSTRP EEEECCCCEEEECCC	19.58	25159151
86	Phosphorylation	GTASSIEYSTRPRDT ECCCCEEEECCCCCC	17.42	23312004
87	Phosphorylation	TASSIEYSTRPRDTE CCCCEEEECCCCCCC	12.73	23312004
88	Phosphorylation	ASSIEYSTRPRDTEE CCCEEEECCCCCCCC	43.73	23312004
93	Phosphorylation	YSTRPRDTEEQNPET EECCCCCCCCCCCCC	42.58	26074081
100	Phosphorylation	TEEQNPETVNWEDRP CCCCCCCCCCCCCCC	22.01	26657352
108	Phosphorylation	VNWEDRPSTPTILGY CCCCCCCCCCCCCCH	48.16	25159151
109	Phosphorylation	NWEDRPSTPTILGYE CCCCCCCCCCCCCHH	27.43	27273156
111	Phosphorylation	EDRPSTPTILGYEVM CCCCCCCCCCCHHHC	28.99	23401153
115	Phosphorylation	STPTILGYEVMEERA CCCCCCCHHHCHHHH	11.25	28450419
222	Phosphorylation	DPPGPFDSLEESRAF CCCCCCCCHHHHHHH	37.75	27251275
232	Ubiquitination	ESRAFCETLEETNYR HHHHHHHHHHHHHHH	40.42	29967540
236	Phosphorylation	FCETLEETNYRLQKE HHHHHHHHHHHHHHH	28.33	22468782
238	Phosphorylation	ETLEETNYRLQKELL HHHHHHHHHHHHHHH	21.81	22468782
253	Phosphorylation	EKQKEMESLKKLLSE HHHHHHHHHHHHHHH	44.15	28270605
255	Acetylation	QKEMESLKKLLSEKQ HHHHHHHHHHHHHCC	51.13	7822247
259	Phosphorylation	ESLKKLLSEKQLHID HHHHHHHHHCCCCHH	53.86	24719451
261	Ubiquitination	LKKLLSEKQLHIDTL HHHHHHHCCCCHHHH	55.58	29967540
274	Phosphorylation	TLENRIRTLSLEPEE HHHHHHHHCCCCCCC	20.51	26074081
276	Phosphorylation	ENRIRTLSLEPEESL HHHHHHCCCCCCCCC	30.03	26074081
282	Phosphorylation	LSLEPEESLDVSETE CCCCCCCCCCCCCCC	28.36	30278072
286	Phosphorylation	PEESLDVSETEGEQI CCCCCCCCCCCCCEE	38.17	30266825
288	Phosphorylation	ESLDVSETEGEQILK CCCCCCCCCCCEEEE	41.61	30266825
298	Phosphorylation	EQILKVESSALEVDQ CEEEEEECCCEEECH	24.73	28985074
299	Phosphorylation	QILKVESSALEVDQD EEEEEECCCEEECHH	24.30	28985074

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

Oops, there are no upstream regulatory protein records of SNX16_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNX16_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SNX16_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of SNX16_HUMAN !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
PubMed: 19413330