SNX3_HUMAN - dbPTM
SNX3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX3_HUMAN
UniProt AC O60493
Protein Name Sorting nexin-3
Gene Name SNX3
Organism Homo sapiens (Human).
Sequence Length 162
Subcellular Localization Early endosome . Cytoplasmic vesicle, phagosome . Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures (PubMed:21725319) Colocalizes with EEA1 on nascent phagosome
Protein Description Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Also can bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (By similarity). Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC/VPS). May in part act as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. [PubMed: 21725319]
Protein Sequence MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
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 Orthologous
Protein Cluster
2Acetylation------MAETVADTR
------CCCCHHHHH		22.5925944712
8PhosphorylationMAETVADTRRLITKP
CCCCHHHHHHHCCCC		14.1420068231
13PhosphorylationADTRRLITKPQNLND
HHHHHHCCCCCCCCC		41.0626552605
14UbiquitinationDTRRLITKPQNLNDA
HHHHHCCCCCCCCCC		37.30-
22PhosphorylationPQNLNDAYGPPSNFL
CCCCCCCCCCCCCCE		32.7829978859
26PhosphorylationNDAYGPPSNFLEIDV
CCCCCCCCCCEEEEC		43.2625394399
39UbiquitinationDVSNPQTVGVGRGRF
ECCCCCEEEECCCCC		5.0121890473
41UbiquitinationSNPQTVGVGRGRFTT
CCCCEEEECCCCCEE		4.0322817900
43MethylationPQTVGVGRGRFTTYE
CCEEEECCCCCEEEE		30.6124129315
43DimethylationPQTVGVGRGRFTTYE
CCEEEECCCCCEEEE		30.61-
45DimethylationTVGVGRGRFTTYEIR
EEEECCCCCEEEEEE		25.11-
45MethylationTVGVGRGRFTTYEIR
EEEECCCCCEEEEEE		25.1112018303
47PhosphorylationGVGRGRFTTYEIRVK
EECCCCCEEEEEEEE		27.4020860994
48PhosphorylationVGRGRFTTYEIRVKT
ECCCCCEEEEEEEEC		19.2220860994
49PhosphorylationGRGRFTTYEIRVKTN
CCCCCEEEEEEEECC		13.2920860994
50PhosphorylationRGRFTTYEIRVKTNL
CCCCEEEEEEEECCC		23.4032645325
54UbiquitinationTTYEIRVKTNLPIFK
EEEEEEEECCCCEEE		23.1133845483
55PhosphorylationTYEIRVKTNLPIFKL
EEEEEEECCCCEEEC		38.8522817900
61 (in isoform 3)Ubiquitination-60.4121906983
61 (in isoform 1)Ubiquitination-60.4121890473
61AcetylationKTNLPIFKLKESTVR
ECCCCEEECCCCHHH		60.4126051181
61UbiquitinationKTNLPIFKLKESTVR
ECCCCEEECCCCHHH		60.4127667366
61MalonylationKTNLPIFKLKESTVR
ECCCCEEECCCCHHH		60.4132601280
63UbiquitinationNLPIFKLKESTVRRR
CCCEEECCCCHHHHH		50.6523000965
63 (in isoform 2)Ubiquitination-50.6521890473
64UbiquitinationLPIFKLKESTVRRRY
CCEEECCCCHHHHHH		63.1830230243
66PhosphorylationIFKLKESTVRRRYSD
EEECCCCHHHHHHHC		21.08-
71 (in isoform 3)Phosphorylation-15.69-
71PhosphorylationESTVRRRYSDFEWLR
CCHHHHHHHCHHHHH		15.6923927012
72 (in isoform 3)Phosphorylation-33.7329116813
72PhosphorylationSTVRRRYSDFEWLRS
CHHHHHHHCHHHHHH		33.7322167270
73 (in isoform 4)Ubiquitination-36.2321890473
73UbiquitinationTVRRRYSDFEWLRSE
HHHHHHHCHHHHHHH		36.2323000965
79PhosphorylationSDFEWLRSELERESK
HCHHHHHHHHHHHCC		44.3428450419
85PhosphorylationRSELERESKVVVPPL
HHHHHHHCCEECCCC		36.6521406692
86MalonylationSELERESKVVVPPLP
HHHHHHCCEECCCCC		34.0032601280
86SumoylationSELERESKVVVPPLP
HHHHHHCCEECCCCC		34.00-
86UbiquitinationSELERESKVVVPPLP
HHHHHHCCEECCCCC		34.0030230243
86SumoylationSELERESKVVVPPLP
HHHHHHCCEECCCCC		34.00-
87 (in isoform 2)Ubiquitination-7.9521890473
87UbiquitinationELERESKVVVPPLPG
HHHHHCCEECCCCCC		7.9522817900
95SumoylationVVPPLPGKAFLRQLP
ECCCCCCCHHHHCCC		33.74-
95UbiquitinationVVPPLPGKAFLRQLP
ECCCCCCCHHHHCCC		33.7423000965
95 (in isoform 1)Ubiquitination-33.7421890473
95UbiquitinationVVPPLPGKAFLRQLP
ECCCCCCCHHHHCCC		33.7421890473
95SumoylationVVPPLPGKAFLRQLP
ECCCCCCCHHHHCCC		33.7428112733
96UbiquitinationVPPLPGKAFLRQLPF
CCCCCCCHHHHCCCC		18.0230230243
97 (in isoform 4)Ubiquitination-7.0521890473
97UbiquitinationPPLPGKAFLRQLPFR
CCCCCCHHHHCCCCC		7.0522817900
106UbiquitinationRQLPFRGDDGIFDDN
HCCCCCCCCCCCCCC		46.8630230243
119UbiquitinationDNFIEERKQGLEQFI
CCHHHHHHHHHHHHH		52.5821890473
119SumoylationDNFIEERKQGLEQFI
CCHHHHHHHHHHHHH		52.58-
119 (in isoform 1)Ubiquitination-52.5821890473
119SumoylationDNFIEERKQGLEQFI
CCHHHHHHHHHHHHH		52.58-
119UbiquitinationDNFIEERKQGLEQFI
CCHHHHHHHHHHHHH		52.5822817900
120UbiquitinationNFIEERKQGLEQFIN
CHHHHHHHHHHHHHH		68.8529967540
125 (in isoform 2)Phosphorylation-4.92-
126UbiquitinationKQGLEQFINKVAGHP
HHHHHHHHHHHCCCH		4.9522505724
128UbiquitinationGLEQFINKVAGHPLA
HHHHHHHHHCCCHHH		28.7530230243
128SumoylationGLEQFINKVAGHPLA
HHHHHHHHHCCCHHH		28.75-
130UbiquitinationEQFINKVAGHPLAQN
HHHHHHHCCCHHHCC		16.5229967540
136UbiquitinationVAGHPLAQNERCLHM
HCCCHHHCCHHHHHH		61.0622505724
140GlutathionylationPLAQNERCLHMFLQD
HHHCCHHHHHHHHCH		2.2022555962
152UbiquitinationLQDEIIDKSYTPSKI
HCHHHHCCCCCHHHC		34.6529967540
153PhosphorylationQDEIIDKSYTPSKIR
CHHHHCCCCCHHHCC		30.4123927012
154PhosphorylationDEIIDKSYTPSKIRH
HHHHCCCCCHHHCCC		28.5423927012
155PhosphorylationEIIDKSYTPSKIRHA
HHHCCCCCHHHCCCC		28.3323927012
157PhosphorylationIDKSYTPSKIRHA--
HCCCCCHHHCCCC--		32.6820068231
158SumoylationDKSYTPSKIRHA---
CCCCCHHHCCCC---		44.99-
158UbiquitinationDKSYTPSKIRHA---
CCCCCHHHCCCC---		44.9922505724
158SumoylationDKSYTPSKIRHA---
CCCCCHHHCCCC---		44.99-
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 SNX3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX3_HUMAN !!
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 SNX3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP10_HUMANUSP10physical
18632802
SCNNA_HUMANSCNN1Aphysical
18632802
VPS35_HUMANVPS35physical
22673115
SRPRB_HUMANSRPRBphysical
22939629
SSBP_HUMANSSBP1physical
22939629
STX7_HUMANSTX7physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
AR6P1_HUMANARL6IP1physical
25416956
AK1A1_HUMANAKR1A1physical
26344197
AK1C2_HUMANAKR1C2physical
26344197
PIN1_HUMANPIN1physical
26344197
PPIL3_HUMANPPIL3physical
26344197
RBM12_HUMANRBM12physical
26344197
TAGL_HUMANTAGLNphysical
26344197
TAGL2_HUMANTAGLN2physical
26344197
TAGL3_HUMANTAGLN3physical
26344197
PYRG1_HUMANCTPS1physical
26496610
SSFA2_HUMANSSFA2physical
26496610
SMC1A_HUMANSMC1Aphysical
26496610
KCAB2_HUMANKCNAB2physical
26496610
MPDZ_HUMANMPDZphysical
26496610
PYRG2_HUMANCTPS2physical
26496610
ANO3_HUMANANO3physical
26496610
RT05_HUMANMRPS5physical
26496610
Drug and Disease Associations
Kegg Disease
OMIM Disease
601349Microphthalmia, syndromic, 8 (MCOPS8)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNX3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"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-72, AND MASSSPECTROMETRY.
"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-72, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASSSPECTROMETRY.

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