SNX8_HUMAN - dbPTM
SNX8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX8_HUMAN
UniProt AC Q9Y5X2
Protein Name Sorting nexin-8
Gene Name SNX8
Organism Homo sapiens (Human).
Sequence Length 465
Subcellular Localization Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Colocalizes with retromer components.
Protein Description May be involved in several stages of intracellular trafficking. May play a role in intracellular protein transport from early endosomes to the trans-Golgi network..
Protein Sequence MTGRAMDPLPAAAVGAAAEAEADEEADPPASDLPTPQAIEPQAIVQQVPAPSRMQMPQGNPLLLSHTLQELLARDTVQVELIPEKKGLFLKHVEYEVSSQRFKSSVYRRYNDFVVFQEMLLHKFPYRMVPALPPKRMLGADREFIEARRRALKRFVNLVARHPLFSEDVVLKLFLSFSGSDVQNKLKESAQCVGDEFLNCKLATRAKDFLPADIQAQFAISRELIRNIYNSFHKLRDRAERIASRAIDNAADLLIFGKELSAIGSDTTPLPSWAALNSSTWGSLKQALKGLSVEFALLADKAAQQGKQEENDVVEKLNLFLDLLQSYKDLCERHEKGVLHKHQRALHKYSLMKRQMMSATAQNREPESVEQLESRIVEQENAIQTMELRNYFSLYCLHQETQLIHVYLPLTSHILRAFVNSQIQGHKEMSKVWNDLRPKLSCLFAGPHSTLTPPCSPPEDGLCPH
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
2Phosphorylation------MTGRAMDPL
------CCCCCCCCH		35.06-
70UbiquitinationLLSHTLQELLARDTV
HHHHHHHHHHCCCCE		49.1923000965
85UbiquitinationQVELIPEKKGLFLKH
EEEECCCCCCEEEEE		46.9529967540
95PhosphorylationLFLKHVEYEVSSQRF
EEEEEEEEEECCHHH		22.12-
103MethylationEVSSQRFKSSVYRRY
EECCHHHHHHHHHHH		43.97115980725
109UbiquitinationFKSSVYRRYNDFVVF
HHHHHHHHHCCHHHH		19.5423000965
115UbiquitinationRRYNDFVVFQEMLLH
HHHCCHHHHHHHHHH		4.0723000965
123UbiquitinationFQEMLLHKFPYRMVP
HHHHHHHHCCCCCCC		48.2623000965
126PhosphorylationMLLHKFPYRMVPALP
HHHHHCCCCCCCCCC		17.93-
148UbiquitinationDREFIEARRRALKRF
CHHHHHHHHHHHHHH		18.8123000965
154UbiquitinationARRRALKRFVNLVAR
HHHHHHHHHHHHHHH		41.4123000965
176PhosphorylationVVLKLFLSFSGSDVQ
HHHHHHHHCCCHHHH		15.2730622161
178PhosphorylationLKLFLSFSGSDVQNK
HHHHHHCCCHHHHHH		33.7330622161
180PhosphorylationLFLSFSGSDVQNKLK
HHHHCCCHHHHHHHH		33.1530622161
185UbiquitinationSGSDVQNKLKESAQC
CCHHHHHHHHHHHHH		43.79-
187UbiquitinationSDVQNKLKESAQCVG
HHHHHHHHHHHHHHC		51.7523000965
193UbiquitinationLKESAQCVGDEFLNC
HHHHHHHHCHHHHCC		7.8223000965
199UbiquitinationCVGDEFLNCKLATRA
HHCHHHHCCHHHHCC		26.6323000965
201UbiquitinationGDEFLNCKLATRAKD
CHHHHCCHHHHCCHH		39.8323000965
207UbiquitinationCKLATRAKDFLPADI
CHHHHCCHHHCCHHH		45.8023000965
254UbiquitinationIDNAADLLIFGKELS
HHHHHHHHHHCCCHH		2.9122817900
278PhosphorylationPSWAALNSSTWGSLK
CCHHHHCCCCHHHHH		29.9627251275
279PhosphorylationSWAALNSSTWGSLKQ
CHHHHCCCCHHHHHH		27.4027251275
280PhosphorylationWAALNSSTWGSLKQA
HHHHCCCCHHHHHHH		33.4027251275
283PhosphorylationLNSSTWGSLKQALKG
HCCCCHHHHHHHHHC		24.7727251275
293UbiquitinationQALKGLSVEFALLAD
HHHHCCCHHHHHHHH		9.3722817900
299UbiquitinationSVEFALLADKAAQQG
CHHHHHHHHHHHHCC		19.6722817900
307UbiquitinationDKAAQQGKQEENDVV
HHHHHCCCHHHCHHH		50.6422817900
341UbiquitinationHEKGVLHKHQRALHK
HHHCHHHHHHHHHHH		36.9529967540
348UbiquitinationKHQRALHKYSLMKRQ
HHHHHHHHHHHHHHH		37.0729967540
348AcetylationKHQRALHKYSLMKRQ
HHHHHHHHHHHHHHH		37.077935127
350PhosphorylationQRALHKYSLMKRQMM
HHHHHHHHHHHHHHH		27.1327251275
353AcetylationLHKYSLMKRQMMSAT
HHHHHHHHHHHHHHH		44.787935137
358PhosphorylationLMKRQMMSATAQNRE
HHHHHHHHHHHCCCC		19.6828555341
368PhosphorylationAQNREPESVEQLESR
HCCCCCHHHHHHHHH		41.4930622161
441PhosphorylationNDLRPKLSCLFAGPH
HHHHHHHHEEECCCC		18.2026657352
449PhosphorylationCLFAGPHSTLTPPCS
EEECCCCCCCCCCCC		28.3930108239
450PhosphorylationLFAGPHSTLTPPCSP
EECCCCCCCCCCCCC		31.4530108239
452PhosphorylationAGPHSTLTPPCSPPE
CCCCCCCCCCCCCCC		25.8525159151
456PhosphorylationSTLTPPCSPPEDGLC
CCCCCCCCCCCCCCC		49.6230278072
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
95YPhosphorylationKinaseJAK1P23458
PSP
126YPhosphorylationKinaseJAK1P23458
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX8_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 SNX8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATD_HUMANATP6V1Dphysical
22939629
TOLIP_HUMANTOLLIPphysical
22939629
ZWILC_HUMANZWILCHphysical
22939629
THUM2_HUMANTHUMPD2physical
22939629
MSH3_HUMANMSH3physical
26344197
FBXW7_HUMANFBXW7physical
28514442
NCPR_HUMANPORphysical
28514442
RUFY1_HUMANRUFY1physical
28514442
LACC1_HUMANLACC1physical
28514442
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 SNX8_HUMAN

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Related Literatures of Post-Translational Modification
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 THR-452 AND SER-456, ANDMASS SPECTROMETRY.

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