SNX2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNX2_HUMAN
• UniProt AC: O60749
• Protein Name: Sorting nexin-2
• Gene Name: SNX2
• Organism: Homo sapiens (Human).
• 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
• 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). [PubMed: 16179610 Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex]
• Protein Sequence: MAAEREPPPLGDGKPTDFEDLEDGEDLFTSTVSTLESSPSSPEPASLPAEDISANSNGPKPTEVVLDDDREDLFAEATEEVSLDSPEREPILSSEPSPAVTPVTPTTLIAPRIESKSMSAPVIFDRSREEIEEEANGDIFDIEIGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSKSEFSVKRRFSDFLGLHSKLASKYLHVGYIVPPAPEKSIVGMTKVKVGKEDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESSELPRAVNTQALSGAGILRMVNKAADAVNKMTIKMNESDAWFEEKQQQFENLDQQLRKLHVSVEALVCHRKELSANTAAFAKSAAMLGNSEDHTALSRALSQLAEVEEKIDQLHQEQAFADFYMFSELLSDYIRLIAAVKGVFDHRMKCWQKWEDAQITLLKKREAEAKMMVANKPDKIQQAKNEIREWEAKVQQGERDFEQISKTIRKEVGRFEKERVKDFKTVIIKYLESLVQTQQQLIKYWEAFLPEAKAIA

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
2	Phosphorylation	------MAAEREPPP ------CCCCCCCCC	20.31	27251275
53	Phosphorylation	SLPAEDISANSNGPK CCCHHHCCCCCCCCC	33.45	26074081
56	Phosphorylation	AEDISANSNGPKPTE HHHCCCCCCCCCCCE	42.77	26074081
62	Phosphorylation	NSNGPKPTEVVLDDD CCCCCCCCEEEECCC	47.76	26074081
64	Ubiquitination	NGPKPTEVVLDDDRE CCCCCCEEEECCCHH	5.95	32015554
68	Phosphorylation	PTEVVLDDDREDLFA CCEEEECCCHHHHHH	53.35	32645325
80	Ubiquitination	LFAEATEEVSLDSPE HHHHHHEECCCCCCC	32.81	-
82	Phosphorylation	AEATEEVSLDSPERE HHHHEECCCCCCCCC	29.73	26074081
85	Phosphorylation	TEEVSLDSPEREPIL HEECCCCCCCCCCCC	33.67	26074081
93	Phosphorylation	PEREPILSSEPSPAV CCCCCCCCCCCCCCC	33.12	29255136
94	Ubiquitination	EREPILSSEPSPAVT CCCCCCCCCCCCCCC	50.51	-
94	Phosphorylation	EREPILSSEPSPAVT CCCCCCCCCCCCCCC	50.51	30206219
97	Phosphorylation	PILSSEPSPAVTPVT CCCCCCCCCCCCCCC	22.80	29255136
101	Ubiquitination	SEPSPAVTPVTPTTL CCCCCCCCCCCCCEE	17.72	-
101	Phosphorylation	SEPSPAVTPVTPTTL CCCCCCCCCCCCCEE	17.72	29255136
101	Ubiquitination	SEPSPAVTPVTPTTL CCCCCCCCCCCCCEE	17.72	32015554
104	Phosphorylation	SPAVTPVTPTTLIAP CCCCCCCCCCEEECC	19.00	29255136
106	Phosphorylation	AVTPVTPTTLIAPRI CCCCCCCCEEECCCC	25.52	29255136
106	Ubiquitination	AVTPVTPTTLIAPRI CCCCCCCCEEECCCC	25.52	33845483
107	Phosphorylation	VTPVTPTTLIAPRIE CCCCCCCEEECCCCC	19.85	29255136
115	Phosphorylation	LIAPRIESKSMSAPV EECCCCCCCCCCCCE	27.88	26074081
116	Ubiquitination	IAPRIESKSMSAPVI ECCCCCCCCCCCCEE	37.07	21890473
116	Ubiquitination	IAPRIESKSMSAPVI ECCCCCCCCCCCCEE	37.07	21890473
116	Acetylation	IAPRIESKSMSAPVI ECCCCCCCCCCCCEE	37.07	25953088
116	Ubiquitination	IAPRIESKSMSAPVI ECCCCCCCCCCCCEE	37.07	23000965
117	Acetylation	APRIESKSMSAPVIF CCCCCCCCCCCCEEE	27.52	-
117	Ubiquitination	APRIESKSMSAPVIF CCCCCCCCCCCCEEE	27.52	-
117	Phosphorylation	APRIESKSMSAPVIF CCCCCCCCCCCCEEE	27.52	23401153
117	Ubiquitination	APRIESKSMSAPVIF CCCCCCCCCCCCEEE	27.52	29967540
118	Sulfoxidation	PRIESKSMSAPVIFD CCCCCCCCCCCEEEC	4.56	21406390
119	Phosphorylation	RIESKSMSAPVIFDR CCCCCCCCCCEEECC	36.19	19664994
127	Phosphorylation	APVIFDRSREEIEEE CCEEECCCHHHHHHH	45.98	23663014
131	Ubiquitination	FDRSREEIEEEANGD ECCCHHHHHHHHCCC	7.46	-
131	Ubiquitination	FDRSREEIEEEANGD ECCCHHHHHHHHCCC	7.46	21890473
159	Phosphorylation	VGDGMNAYMAYRVTT CCCCHHHEEEEEEEC	4.18	27642862
170	Ubiquitination	RVTTKTSLSMFSKSE EEECCCCHHHCCCCC	5.35	-
170	Ubiquitination	RVTTKTSLSMFSKSE EEECCCCHHHCCCCC	5.35	29967540
171	Phosphorylation	VTTKTSLSMFSKSEF EECCCCHHHCCCCCH	19.97	28857561
176	Phosphorylation	SLSMFSKSEFSVKRR CHHHCCCCCHHHHHH	42.55	28857561
177	Ubiquitination	LSMFSKSEFSVKRRF HHHCCCCCHHHHHHH	45.75	32015554
181	Ubiquitination	SKSEFSVKRRFSDFL CCCCHHHHHHHHHHH	36.34	32015554
185	Phosphorylation	FSVKRRFSDFLGLHS HHHHHHHHHHHHHHH	26.16	29255136
192	Ubiquitination	SDFLGLHSKLASKYL HHHHHHHHHHHHHHC	34.11	-
192	Phosphorylation	SDFLGLHSKLASKYL HHHHHHHHHHHHHHC	34.11	29691806
192	Ubiquitination	SDFLGLHSKLASKYL HHHHHHHHHHHHHHC	34.11	21963094
193	Acetylation	DFLGLHSKLASKYLH HHHHHHHHHHHHHCC	37.01	25953088
196	Phosphorylation	GLHSKLASKYLHVGY HHHHHHHHHHCCEEE	32.06	28857561
197	Ubiquitination	LHSKLASKYLHVGYI HHHHHHHHHCCEEEE	46.34	-
198	Phosphorylation	HSKLASKYLHVGYIV HHHHHHHHCCEEEEC	10.27	21082442
203	Phosphorylation	SKYLHVGYIVPPAPE HHHCCEEEECCCCCC	9.54	28152594
211	Acetylation	IVPPAPEKSIVGMTK ECCCCCCCCEECEEE	44.41	25953088
211	Malonylation	IVPPAPEKSIVGMTK ECCCCCCCCEECEEE	44.41	26320211
211	Ubiquitination	IVPPAPEKSIVGMTK ECCCCCCCCEECEEE	44.41	-
212	Phosphorylation	VPPAPEKSIVGMTKV CCCCCCCCEECEEEE	22.35	28857561
216	Sulfoxidation	PEKSIVGMTKVKVGK CCCCEECEEEEEECC	1.96	30846556
217	Phosphorylation	EKSIVGMTKVKVGKE CCCEECEEEEEECCC	27.10	28857561
218	Acetylation	KSIVGMTKVKVGKED CCEECEEEEEECCCC	31.03	25953088
218	Ubiquitination	KSIVGMTKVKVGKED CCEECEEEEEECCCC	31.03	32015554
220	Ubiquitination	IVGMTKVKVGKEDSS EECEEEEEECCCCCC	46.99	-
223	Acetylation	MTKVKVGKEDSSSTE EEEEEECCCCCCCHH	62.43	19828235
223	Ubiquitination	MTKVKVGKEDSSSTE EEEEEECCCCCCCHH	62.43	33845483
226	Phosphorylation	VKVGKEDSSSTEFVE EEECCCCCCCHHHHH	27.55	25159151
227	Phosphorylation	KVGKEDSSSTEFVEK EECCCCCCCHHHHHH	54.31	25159151
228	Phosphorylation	VGKEDSSSTEFVEKR ECCCCCCCHHHHHHH	35.59	28450419
229	Ubiquitination	GKEDSSSTEFVEKRR CCCCCCCHHHHHHHH	35.08	-
229	Phosphorylation	GKEDSSSTEFVEKRR CCCCCCCHHHHHHHH	35.08	30108239
229	Ubiquitination	GKEDSSSTEFVEKRR CCCCCCCHHHHHHHH	35.08	21963094
234	Acetylation	SSTEFVEKRRAALER CCHHHHHHHHHHHHH	41.71	23749302
234	Ubiquitination	SSTEFVEKRRAALER CCHHHHHHHHHHHHH	41.71	29967540
246	Phosphorylation	LERYLQRTVKHPTLL HHHHHHHHCCCCHHH	22.42	28857561
248	Ubiquitination	RYLQRTVKHPTLLQD HHHHHHCCCCHHHCC	43.16	21890473
248	Ubiquitination	RYLQRTVKHPTLLQD HHHHHHCCCCHHHCC	43.16	21890473
248	Ubiquitination	RYLQRTVKHPTLLQD HHHHHHCCCCHHHCC	43.16	21906983
251	Phosphorylation	QRTVKHPTLLQDPDL HHHCCCCHHHCCCCH	39.56	-
259	Methylation	LLQDPDLRQFLESSE HHCCCCHHHHHHCCC	32.36	115917445
273	Phosphorylation	ELPRAVNTQALSGAG CCCCCCCHHHHCHHH	14.50	30266825
277	Phosphorylation	AVNTQALSGAGILRM CCCHHHHCHHHHHHH	29.61	19664994
283	Methylation	LSGAGILRMVNKAAD HCHHHHHHHHHHHHH	25.69	115917449
287	Ubiquitination	GILRMVNKAADAVNK HHHHHHHHHHHHHHH	33.28	29967540
294	Ubiquitination	KAADAVNKMTIKMNE HHHHHHHHHCEECCH	30.71	32015554
296	Phosphorylation	ADAVNKMTIKMNESD HHHHHHHCEECCHHH	21.03	28857561
298	Ubiquitination	AVNKMTIKMNESDAW HHHHHCEECCHHHHH	26.89	32015554
309	Ubiquitination	SDAWFEEKQQQFENL HHHHHHHHHHHHHCH	46.32	21963094
330	Acetylation	LHVSVEALVCHRKEL HHHHHHHHHHCHHHC	2.39	19608861
330	Ubiquitination	LHVSVEALVCHRKEL HHHHHHHHHHCHHHC	2.39	32015554
335	Acetylation	EALVCHRKELSANTA HHHHHCHHHCCCCHH	39.06	11920815
335	Ubiquitination	EALVCHRKELSANTA HHHHHCHHHCCCCHH	39.06	29967540
339	Ubiquitination	CHRKELSANTAAFAK HCHHHCCCCHHHHHH	29.98	32015554
346	Ubiquitination	ANTAAFAKSAAMLGN CCHHHHHHHHHHHCC	33.89	21963094
350	Sulfoxidation	AFAKSAAMLGNSEDH HHHHHHHHHCCCHHH	5.01	21406390
352	Acetylation	AKSAAMLGNSEDHTA HHHHHHHCCCHHHHH	23.64	19608861
352	Ubiquitination	AKSAAMLGNSEDHTA HHHHHHHCCCHHHHH	23.64	33845483
354	Phosphorylation	SAAMLGNSEDHTALS HHHHHCCCHHHHHHH	42.47	30624053
365	Phosphorylation	TALSRALSQLAEVEE HHHHHHHHHHHHHHH	23.35	28355574
370	Acetylation	ALSQLAEVEEKIDQL HHHHHHHHHHHHHHH	10.81	-
399	Ubiquitination	LLSDYIRLIAAVKGV HHHHHHHHHHHHHCH	1.96	-
399	Ubiquitination	LLSDYIRLIAAVKGV HHHHHHHHHHHHHCH	1.96	21963094
416	Acetylation	HRMKCWQKWEDAQIT HCHHHHHHHHHHHEE	28.22	26051181
442	"N6,N6-dimethyllysine"	MVANKPDKIQQAKNE HHHCCHHHHHHHHHH	51.44	-
442	Acetylation	MVANKPDKIQQAKNE HHHCCHHHHHHHHHH	51.44	25953088
442	Methylation	MVANKPDKIQQAKNE HHHCCHHHHHHHHHH	51.44	-
447	Acetylation	PDKIQQAKNEIREWE HHHHHHHHHHHHHHH	51.26	19608861
447	Ubiquitination	PDKIQQAKNEIREWE HHHHHHHHHHHHHHH	51.26	32015554
456	Acetylation	EIREWEAKVQQGERD HHHHHHHHHHHCCCC	29.12	27452117
456	Ubiquitination	EIREWEAKVQQGERD HHHHHHHHHHHCCCC	29.12	32015554
469	Acetylation	RDFEQISKTIRKEVG CCHHHHHHHHHHHHC	49.99	19608861
469	Ubiquitination	RDFEQISKTIRKEVG CCHHHHHHHHHHHHC	49.99	33845483
484	Acetylation	RFEKERVKDFKTVII CCHHHHHHHHHHHHH	64.76	25953088
487	Acetylation	KERVKDFKTVIIKYL HHHHHHHHHHHHHHH	52.60	23236377
492	Ubiquitination	DFKTVIIKYLESLVQ HHHHHHHHHHHHHHH	32.43	-
516	Ubiquitination	EAFLPEAKAIA---- HHHCHHHHHHC----	38.37	21963094

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

Oops, there are no upstream regulatory protein records of SNX2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNX2_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 SNX2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AVR2B_HUMAN	ACVR2B	physical	11279102
ACV1B_HUMAN	ACVR1B	physical	11279102
PGFRA_HUMAN	PDGFRA	physical	9819414
PGFRB_HUMAN	PDGFRB	physical	9819414
SNX4_HUMAN	SNX4	physical	9819414
EGFR_HUMAN	EGFR	physical	9819414
INSR_HUMAN	INSR	physical	9819414
LEPR_HUMAN	LEPR	physical	9819414
SNX6_HUMAN	SNX6	physical	22939629
VPS29_HUMAN	VPS29	physical	22939629
VPS35_HUMAN	VPS35	physical	22939629
SNX5_HUMAN	SNX5	physical	21988832
ZN202_HUMAN	ZNF202	physical	21988832
SNX6_HUMAN	SNX6	physical	21988832
H33_HUMAN	H3F3A	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
SNX6_HUMAN	SNX6	physical	22863883
PYRG1_HUMAN	CTPS1	physical	26344197
DDB1_HUMAN	DDB1	physical	26344197
HGS_HUMAN	HGS	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
PDXK_HUMAN	PDXK	physical	26344197
PUR1_HUMAN	PPAT	physical	26344197
BRE1B_HUMAN	RNF40	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
SNX5_HUMAN	SNX5	physical	26344197
SNX6_HUMAN	SNX6	physical	26344197
TSN_HUMAN	TSN	physical	26344197
VP26A_HUMAN	VPS26A	physical	26344197
VP26B_HUMAN	VPS26B	physical	26344197
VPS29_HUMAN	VPS29	physical	26344197
VPS35_HUMAN	VPS35	physical	26344197

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

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-447 AND LYS-469, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-277, ANDMASS SPECTROMETRY.
PubMed: 19690332

"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-119 AND SER-277, ANDMASS SPECTROMETRY.
PubMed: 19413330

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-185, ANDMASS SPECTROMETRY.
PubMed: 18669648

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
PubMed: 16964243

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND MASSSPECTROMETRY.
PubMed: 15302935