SNX18_HUMAN - dbPTM
SNX18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX18_HUMAN
UniProt AC Q96RF0
Protein Name Sorting nexin-18
Gene Name SNX18
Organism Homo sapiens (Human).
Sequence Length 628
Subcellular Localization Endomembrane system
Peripheral membrane protein
Cytoplasmic side. Endosome membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle membrane
Peripheral membrane protein
Protein Description Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Stimulates the GTPase activity of DNM2. Promotes DNM2 location at the plasma membrane..
Protein Sequence MALRARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVQVIRAPEPGPAGDGGPGAPARYANVPPGGFEPLPVAPPASFKPPPDAFQALLQPQQAPPPSTFQPPGAGFPYGGGALQPSPQQLYGGYQASQGSDDDWDDEWDDSSTVADEPGALGSGAYPDLDGSSSAGVGAAGRYRLSTRSDLSLGSRGGSVPPQHHPSGPKSSATVSRNLNRFSTFVKSGGEAFVLGEASGFVKDGDKLCVVLGPYGPEWQENPYPFQCTIDDPTKQTKFKGMKSYISYKLVPTHTQVPVHRRYKHFDWLYARLAEKFPVISVPHLPEKQATGRFEEDFISKRRKGLIWWMNHMASHPVLAQCDVFQHFLTCPSSTDEKAWKQGKRKAEKDEMVGANFFLTLSTPPAAALDLQEVESKIDGFKCFTKKMDDSALQLNHTANEFARKQVTGFKKEYQKVGQSFRGLSQAFELDQQAFSVGLNQAIAFTGDAYDAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGKAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF
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
20PhosphorylationSENPGEISLREHEVL
CCCCCCCCCCCHHHH		19.6430266825
54PhosphorylationDRGLFPASYVQVIRA
CCCCCCCHHEEEEEC		26.5221945579
55PhosphorylationRGLFPASYVQVIRAP
CCCCCCHHEEEEECC		9.3021945579
78PhosphorylationGPGAPARYANVPPGG
CCCCCCCCCCCCCCC		12.48-
96PhosphorylationLPVAPPASFKPPPDA
CCCCCCCCCCCCCHH		39.3124719451
173PhosphorylationDEPGALGSGAYPDLD
CCCCCCCCCCCCCCC		22.54-
176PhosphorylationGALGSGAYPDLDGSS
CCCCCCCCCCCCCCC		10.78-
193PhosphorylationGVGAAGRYRLSTRSD
CCCCCCCEEECCCCC		18.2628450419
196PhosphorylationAAGRYRLSTRSDLSL
CCCCEEECCCCCCCC		16.8721722762
197PhosphorylationAGRYRLSTRSDLSLG
CCCEEECCCCCCCCC		38.4928450419
199PhosphorylationRYRLSTRSDLSLGSR
CEEECCCCCCCCCCC		42.8822617229
202PhosphorylationLSTRSDLSLGSRGGS
ECCCCCCCCCCCCCC		35.3622617229
205PhosphorylationRSDLSLGSRGGSVPP
CCCCCCCCCCCCCCC		32.8023403867
206MethylationSDLSLGSRGGSVPPQ
CCCCCCCCCCCCCCC		52.25115917441
209PhosphorylationSLGSRGGSVPPQHHP
CCCCCCCCCCCCCCC		33.9821722762
233PhosphorylationSRNLNRFSTFVKSGG
HCCHHHHHHEEECCC		20.0729978859
234PhosphorylationRNLNRFSTFVKSGGE
CCHHHHHHEEECCCE		29.7229978859
253UbiquitinationGEASGFVKDGDKLCV
EECCEECCCCCEEEE		54.4521906983
253 (in isoform 1)Ubiquitination-54.4521906983
253 (in isoform 2)Ubiquitination-54.4521906983
257UbiquitinationGFVKDGDKLCVVLGP
EECCCCCEEEEEECC		49.6822817900
274PhosphorylationPEWQENPYPFQCTID
CCCCCCCCCEECEEC		28.4122817900
294PhosphorylationTKFKGMKSYISYKLV
CCCCCCCCEEEEEEC		20.8526074081
295PhosphorylationKFKGMKSYISYKLVP
CCCCCCCEEEEEECC		6.5926074081
297PhosphorylationKGMKSYISYKLVPTH
CCCCCEEEEEECCCC		14.1626074081
298PhosphorylationGMKSYISYKLVPTHT
CCCCEEEEEECCCCC		9.9726074081
303PhosphorylationISYKLVPTHTQVPVH
EEEEECCCCCCCCCC		30.0326074081
305PhosphorylationYKLVPTHTQVPVHRR
EEECCCCCCCCCCHH		33.4726074081
313PhosphorylationQVPVHRRYKHFDWLY
CCCCCHHHCCHHHHH		14.5826074081
314UbiquitinationVPVHRRYKHFDWLYA
CCCCHHHCCHHHHHH		35.66-
314MalonylationVPVHRRYKHFDWLYA
CCCCHHHCCHHHHHH		35.6626320211
314 (in isoform 2)Ubiquitination-35.66-
326UbiquitinationLYARLAEKFPVISVP
HHHHHHHHCCCEECC		49.7322817900
326 (in isoform 1)Ubiquitination-49.7321906983
326 (in isoform 2)Ubiquitination-49.7321906983
338 (in isoform 2)Ubiquitination-43.2021906983
338MalonylationSVPHLPEKQATGRFE
ECCCCCHHHCCCCCC		43.2026320211
338UbiquitinationSVPHLPEKQATGRFE
ECCCCCHHHCCCCCC		43.2022817900
338 (in isoform 1)Ubiquitination-43.2021906983
351UbiquitinationFEEDFISKRRKGLIW
CCHHHHHHHHHHHHH		51.9429967540
432UbiquitinationESKIDGFKCFTKKMD
HHHHCCEEEEEEECC		33.69-
432MalonylationESKIDGFKCFTKKMD
HHHHCCEEEEEEECC		33.6926320211
432 (in isoform 2)Ubiquitination-33.69-
437UbiquitinationGFKCFTKKMDDSALQ
CEEEEEEECCCHHHH		44.4929967540
437MalonylationGFKCFTKKMDDSALQ
CEEEEEEECCCHHHH		44.4926320211
437 (in isoform 2)Ubiquitination-44.49-
438SulfoxidationFKCFTKKMDDSALQL
EEEEEEECCCHHHHH		8.0430846556
455UbiquitinationTANEFARKQVTGFKK
HHHHHHHHHHHCCHH		45.7729967540
455AcetylationTANEFARKQVTGFKK
HHHHHHHHHHHCCHH		45.7719826923
461AcetylationRKQVTGFKKEYQKVG
HHHHHCCHHHHHHHH		46.1419826933
466 (in isoform 2)Ubiquitination-47.64-
466AcetylationGFKKEYQKVGQSFRG
CCHHHHHHHHHHHHC		47.6419826943
466UbiquitinationGFKKEYQKVGQSFRG
CCHHHHHHHHHHHHC		47.6427667366
544 (in isoform 2)Phosphorylation-11.07-
562 (in isoform 2)Ubiquitination-2.6121906983
611 (in isoform 2)Phosphorylation-40.5327174698
613UbiquitinationLALGNEYSFSKVQRV
HHHCCCCCCCCCCCC		19.5029967540
613 (in isoform 2)Ubiquitination-19.5021906983
613PhosphorylationLALGNEYSFSKVQRV
HHHCCCCCCCCCCCC		19.5024719451
620UbiquitinationSFSKVQRVPLMTVLS
CCCCCCCCCEEEEEC		2.0929967540
623 (in isoform 2)Phosphorylation-1.6728348404
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 SNX18_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX18_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 SNX18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITCH_HUMANITCHphysical
20491914
DYN2_HUMANDNM2physical
26923255
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.
Regulatory Network of SNX18_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193; SER-196; THR-197;SER-199 AND SER-202, AND MASS SPECTROMETRY.

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