SNX6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNX6_HUMAN
• UniProt AC: Q9UNH7
• Protein Name: Sorting nexin-6
• Gene Name: SNX6
• Organism: Homo sapiens (Human).
• Sequence Length: 406
• Subcellular Localization: Early endosome . Early endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasmic vesicle . Cytoplasm . Nucleus . Interaction with SNX1 or SNX2 promotes location at endosome membranes (PubMed:19935774). Only a minor proportion i
• Protein Description: Involved in several stages of intracellular trafficking. Interacts with membranes phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate (Probable). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. [PubMed: 19935774 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) (Probable Does not have in vitro vesicle-to-membrane remodeling activity]
• Protein Sequence: MMEGLDDGPDFLSEEDRGLKAINVDLQSDAALQVDISDALSERDKVKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFVENEDYAGYIIPPAPPRPDFDASREKLQKLGEGEGSMTKEEFTKMKQELEAEYLAIFKKTVAMHEVFLCRVAAHPILRRDLNFHVFLEYNQDLSVRGKNKKEKLEDFFKNMVKSADGVIVSGVKDVDDFFEHERTFLLEYHNRVKDASAKSDRMTRSHKSAADDYNRIGSSLYALGTQDSTDICKFFLKVSELFDKTRKIEARVSADEDLKLSDLLKYYLRESQAAKDLLYRRSRSLVDYENANKALDKARAKNKDVLQAETSQQLCCQKFEKISESAKQELIDFKTRRVAAFRKNLVELAELELKHAKGNLQLLQNCLAVLNGDT

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
1	Acetylation	-------MMEGLDDG -------CCCCCCCC	5.07	19413330
2	Acetylation	------MMEGLDDGP ------CCCCCCCCC	5.86	19413330
13	Phosphorylation	DDGPDFLSEEDRGLK CCCCCCCCHHHCCCC	38.64	24850871
17	Methylation	DFLSEEDRGLKAINV CCCCHHHCCCCEECC	56.47	115917461
22	Ubiquitination	EDRGLKAINVDLQSD HHCCCCEECCCCCCC	5.02	21890473
25	Phosphorylation	GLKAINVDLQSDAAL CCCEECCCCCCCCEE	34.21	-
29	Methylation	INVDLQSDAALQVDI ECCCCCCCCEEEECH	23.93	-
47	Acetylation	LSERDKVKFTVHTKS CCCCCCEEEEEECCC	40.85	25953088
53	Ubiquitination	VKFTVHTKSSLPNFK EEEEEECCCCCCCCC	24.14	-
54	Phosphorylation	KFTVHTKSSLPNFKQ EEEEECCCCCCCCCC	37.96	30622161
55	Phosphorylation	FTVHTKSSLPNFKQN EEEECCCCCCCCCCC	49.77	23312004
59	Ubiquitination	TKSSLPNFKQNEFSV CCCCCCCCCCCCCCH	8.99	-
60	Acetylation	KSSLPNFKQNEFSVV CCCCCCCCCCCCCHH	59.87	27452117
60	Malonylation	KSSLPNFKQNEFSVV CCCCCCCCCCCCCHH	59.87	26320211
60	Ubiquitination	KSSLPNFKQNEFSVV CCCCCCCCCCCCCHH	59.87	21890473
65	Ubiquitination	NFKQNEFSVVRQHEE CCCCCCCCHHHCCCE	17.33	-
67	Phosphorylation	KQNEFSVVRQHEEFI CCCCCCHHHCCCEEE	4.77	27251275
72	Ubiquitination	SVVRQHEEFIWLHDS CHHHCCCEEEEEEHH	40.06	-
73	Ubiquitination	VVRQHEEFIWLHDSF HHHCCCEEEEEEHHH	4.41	21890473
109	Ubiquitination	ASREKLQKLGEGEGS HHHHHHHHHCCCCCC	69.74	21906983
116	Phosphorylation	KLGEGEGSMTKEEFT HHCCCCCCCCHHHHH	20.98	28857561
117	Sulfoxidation	LGEGEGSMTKEEFTK HCCCCCCCCHHHHHH	10.24	21406390
118	Phosphorylation	GEGEGSMTKEEFTKM CCCCCCCCHHHHHHH	36.68	30622161
119	Acetylation	EGEGSMTKEEFTKMK CCCCCCCHHHHHHHH	46.75	7682057
119	Ubiquitination	EGEGSMTKEEFTKMK CCCCCCCHHHHHHHH	46.75	21906983
121	Ubiquitination	EGSMTKEEFTKMKQE CCCCCHHHHHHHHHH	61.24	-
124	Acetylation	MTKEEFTKMKQELEA CCHHHHHHHHHHHHH	49.79	7682067
126	Ubiquitination	KEEFTKMKQELEAEY HHHHHHHHHHHHHHH	42.02	-
128	Phosphorylation	EFTKMKQELEAEYLA HHHHHHHHHHHHHHH	42.96	-
131	Ubiquitination	KMKQELEAEYLAIFK HHHHHHHHHHHHHHH	24.29	-
133	Phosphorylation	KQELEAEYLAIFKKT HHHHHHHHHHHHHHH	14.42	-
138	2-Hydroxyisobutyrylation	AEYLAIFKKTVAMHE HHHHHHHHHHHHHHH	41.23	-
138	Ubiquitination	AEYLAIFKKTVAMHE HHHHHHHHHHHHHHH	41.23	21890473
140	Phosphorylation	YLAIFKKTVAMHEVF HHHHHHHHHHHHHHH	17.68	24719451
143	Sulfoxidation	IFKKTVAMHEVFLCR HHHHHHHHHHHHHHH	2.11	30846556
145	Phosphorylation	KKTVAMHEVFLCRVA HHHHHHHHHHHHHHH	23.14	-
149	Glutathionylation	AMHEVFLCRVAAHPI HHHHHHHHHHHHCHH	1.92	22555962
150	Ubiquitination	MHEVFLCRVAAHPIL HHHHHHHHHHHCHHH	24.21	-
152	Phosphorylation	EVFLCRVAAHPILRR HHHHHHHHHCHHHCC	4.82	24719451
183	Malonylation	RGKNKKEKLEDFFKN CCCCHHHHHHHHHHH	67.09	26320211
183	Ubiquitination	RGKNKKEKLEDFFKN CCCCHHHHHHHHHHH	67.09	-
189	Ubiquitination	EKLEDFFKNMVKSAD HHHHHHHHHHHHCCC	44.09	21890473
193	Ubiquitination	DFFKNMVKSADGVIV HHHHHHHHCCCCEEE	29.20	21890473
194	Phosphorylation	FFKNMVKSADGVIVS HHHHHHHCCCCEEEC	21.85	30266825
195	Ubiquitination	FKNMVKSADGVIVSG HHHHHHCCCCEEECC	16.32	-
201	Ubiquitination	SADGVIVSGVKDVDD CCCCEEECCCCCHHH	27.09	-
204	Ubiquitination	GVIVSGVKDVDDFFE CEEECCCCCHHHHHH	56.40	21890473
205	Ubiquitination	VIVSGVKDVDDFFEH EEECCCCCHHHHHHH	46.82	-
206	Phosphorylation	IVSGVKDVDDFFEHE EECCCCCHHHHHHHH	6.70	27251275
216	Ubiquitination	FFEHERTFLLEYHNR HHHHHHHHHHHCHHH	10.31	-
220	Phosphorylation	ERTFLLEYHNRVKDA HHHHHHHCHHHHHHC	12.36	27642862
231	Phosphorylation	VKDASAKSDRMTRSH HHHCCCCHHHHCCCC	30.11	20068231
235	Phosphorylation	SAKSDRMTRSHKSAA CCCHHHHCCCCHHHH	29.88	20068231
239	Ubiquitination	DRMTRSHKSAADDYN HHHCCCCHHHHHHHH	42.93	21890473
243	Phosphorylation	RSHKSAADDYNRIGS CCCHHHHHHHHHHHH	59.65	20068231
247	Phosphorylation	SAADDYNRIGSSLYA HHHHHHHHHHHHHHH	28.54	20068231
250	Phosphorylation	DDYNRIGSSLYALGT HHHHHHHHHHHHCCC	18.13	28152594
251	Phosphorylation	DYNRIGSSLYALGTQ HHHHHHHHHHHCCCC	21.86	28152594
251	Ubiquitination	DYNRIGSSLYALGTQ HHHHHHHHHHHCCCC	21.86	-
253	Phosphorylation	NRIGSSLYALGTQDS HHHHHHHHHCCCCCH	11.17	28152594
259	Ubiquitination	LYALGTQDSTDICKF HHHCCCCCHHHHHHH	54.03	21890473
264	Glutathionylation	TQDSTDICKFFLKVS CCCHHHHHHHHHHHH	3.32	22555962
265	Ubiquitination	QDSTDICKFFLKVSE CCHHHHHHHHHHHHH	39.21	-
269	Acetylation	DICKFFLKVSELFDK HHHHHHHHHHHHHHH	38.26	26051181
269	Ubiquitination	DICKFFLKVSELFDK HHHHHHHHHHHHHHH	38.26	21890473
276	2-Hydroxyisobutyrylation	KVSELFDKTRKIEAR HHHHHHHHHCCEEEE	42.78	-
276	Acetylation	KVSELFDKTRKIEAR HHHHHHHHHCCEEEE	42.78	25953088
276	Ubiquitination	KVSELFDKTRKIEAR HHHHHHHHHCCEEEE	42.78	21890473
277	Ubiquitination	VSELFDKTRKIEARV HHHHHHHHCCEEEEC	38.75	-
281	Ubiquitination	FDKTRKIEARVSADE HHHHCCEEEECCCCC	33.20	-
288	Ubiquitination	EARVSADEDLKLSDL EEECCCCCCCCHHHH	66.03	-
291	Acetylation	VSADEDLKLSDLLKY CCCCCCCCHHHHHHH	59.26	25953088
291	Ubiquitination	VSADEDLKLSDLLKY CCCCCCCCHHHHHHH	59.26	21890473
297	Ubiquitination	LKLSDLLKYYLRESQ CCHHHHHHHHHHHCH	38.86	-
303	Ubiquitination	LKYYLRESQAAKDLL HHHHHHHCHHHHHHH	20.77	-
307	Malonylation	LRESQAAKDLLYRRS HHHCHHHHHHHHHHH	52.50	26320211
307	Ubiquitination	LRESQAAKDLLYRRS HHHCHHHHHHHHHHH	52.50	-
309	Ubiquitination	ESQAAKDLLYRRSRS HCHHHHHHHHHHHHH	4.45	-
314	Phosphorylation	KDLLYRRSRSLVDYE HHHHHHHHHHHCCHH	19.75	28796482
316	Phosphorylation	LLYRRSRSLVDYENA HHHHHHHHHCCHHHH	33.71	23898821
319	Ubiquitination	RRSRSLVDYENANKA HHHHHHCCHHHHHHH	50.77	-
320	Phosphorylation	RSRSLVDYENANKAL HHHHHCCHHHHHHHH	12.01	28796482
325	Malonylation	VDYENANKALDKARA CCHHHHHHHHHHHHH	48.17	26320211
325	Ubiquitination	VDYENANKALDKARA CCHHHHHHHHHHHHH	48.17	-
326	Phosphorylation	DYENANKALDKARAK CHHHHHHHHHHHHHC	22.32	24719451
328	Phosphorylation	ENANKALDKARAKNK HHHHHHHHHHHHCCH	47.64	27251275
333	Malonylation	ALDKARAKNKDVLQA HHHHHHHCCHHHHHH	60.00	26320211
333	Ubiquitination	ALDKARAKNKDVLQA HHHHHHHCCHHHHHH	60.00	-
335	Ubiquitination	DKARAKNKDVLQAET HHHHHCCHHHHHHHH	48.81	-
337	Ubiquitination	ARAKNKDVLQAETSQ HHHCCHHHHHHHHHH	4.57	-
342	Phosphorylation	KDVLQAETSQQLCCQ HHHHHHHHHHHHHHH	34.55	30622161
343	Phosphorylation	DVLQAETSQQLCCQK HHHHHHHHHHHHHHH	13.87	30622161
347	Ubiquitination	AETSQQLCCQKFEKI HHHHHHHHHHHHHHH	1.69	-
350	Acetylation	SQQLCCQKFEKISES HHHHHHHHHHHHCHH	41.39	26051181
350	Ubiquitination	SQQLCCQKFEKISES HHHHHHHHHHHHCHH	41.39	-
353	Acetylation	LCCQKFEKISESAKQ HHHHHHHHHCHHHHH	55.45	25953088
353	Ubiquitination	LCCQKFEKISESAKQ HHHHHHHHHCHHHHH	55.45	-
359	2-Hydroxyisobutyrylation	EKISESAKQELIDFK HHHCHHHHHHHHHHH	54.29	-
359	Ubiquitination	EKISESAKQELIDFK HHHCHHHHHHHHHHH	54.29	21890473
362	Ubiquitination	SESAKQELIDFKTRR CHHHHHHHHHHHHHH	4.16	-
365	Ubiquitination	AKQELIDFKTRRVAA HHHHHHHHHHHHHHH	7.44	-
366	2-Hydroxyisobutyrylation	KQELIDFKTRRVAAF HHHHHHHHHHHHHHH	37.06	-
366	Acetylation	KQELIDFKTRRVAAF HHHHHHHHHHHHHHH	37.06	27452117
366	Ubiquitination	KQELIDFKTRRVAAF HHHHHHHHHHHHHHH	37.06	21890473
371	Ubiquitination	DFKTRRVAAFRKNLV HHHHHHHHHHHHHHH	10.08	-
375	Ubiquitination	RRVAAFRKNLVELAE HHHHHHHHHHHHHHH	48.45	21890473
378	Ubiquitination	AAFRKNLVELAELEL HHHHHHHHHHHHHHH	8.72	-
386	Acetylation	ELAELELKHAKGNLQ HHHHHHHHHCCHHHH	31.94	23954790
386	Ubiquitination	ELAELELKHAKGNLQ HHHHHHHHHCCHHHH	31.94	-
387	Ubiquitination	LAELELKHAKGNLQL HHHHHHHHCCHHHHH	45.35	-
389	Ubiquitination	ELELKHAKGNLQLLQ HHHHHHCCHHHHHHH	48.31	-
398	Acetylation	NLQLLQNCLAVLNGD HHHHHHHHHHHHCCC	1.34	-
398	Ubiquitination	NLQLLQNCLAVLNGD HHHHHHHHHHHHCCC	1.34	-
401	Ubiquitination	LLQNCLAVLNGDT-- HHHHHHHHHCCCC--	2.48	-

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

Oops, there are no upstream regulatory protein records of SNX6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNX6_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 SNX6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PIM1_HUMAN	PIM1	physical	11591366
SNX4_HUMAN	SNX4	physical	11279102
SNX2_HUMAN	SNX2	physical	11279102
BMR1B_HUMAN	BMPR1B	physical	11279102
AVR2B_HUMAN	ACVR2B	physical	11279102
ACVL1_HUMAN	ACVRL1	physical	11279102
SNX1_HUMAN	SNX1	physical	11279102
TGFR2_HUMAN	TGFBR2	physical	11279102
TGFR1_HUMAN	TGFBR1	physical	11279102
PGFRA_HUMAN	PDGFRA	physical	11279102
INSR_HUMAN	INSR	physical	11279102
EGFR_HUMAN	EGFR	physical	11279102
LEPR_HUMAN	LEPR	physical	11279102
PIM1_HUMAN	PIM1	physical	11279102
GIT1_HUMAN	GIT1	physical	18523162
TF2AA_HUMAN	GTF2A1	physical	22863883
H33_HUMAN	H3F3A	physical	22863883
RTF1_HUMAN	RTF1	physical	22863883
TSN_HUMAN	TSN	physical	22863883
BRMS1_HUMAN	BRMS1	physical	20830743

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.