SNX17_HUMAN - dbPTM
SNX17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX17_HUMAN
UniProt AC Q15036
Protein Name Sorting nexin-17
Gene Name SNX17
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization Cytoplasm. Early endosome. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P))..
Protein Sequence MHFSIPETESRSGDSGGSAYVAYNIHVNGVLHCRVRYSQLLGLHEQLRKEYGANVLPAFPPKKLFSLTPAEVEQRREQLEKYMQAVRQDPLLGSSETFNSFLRRAQQETQQVPTEEVSLEVLLSNGQKVLVNVLTSDQTEDVLEAVAAKLDLPDDLIGYFSLFLVREKEDGAFSFVRKLQEFELPYVSVTSLRSQEYKIVLRKSYWDSAYDDDVMENRVGLNLLYAQTVSDIERGWILVTKEQHRQLKSLQEKVSKKEFLRLAQTLRHYGYLRFDACVADFPEKDCPVVVSAGNSELSLQLRLPGQQLREGSFRVTRMRCWRVTSSVPLPSGSTSSPGRGRGEVRLELAFEYLMSKDRLQWVTITSPQAIMMSICLQSMVDELMVKKSGGSIRKMLRRRVGGTLRRSDSQQAVKSPPLLESPDATRESMVKLSSKLSAVSLRGIGSPSTDASASDVHGNFAFEGIGDEDL
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
4Phosphorylation----MHFSIPETESR
----CCCCCCCCCCC		23.6628857561
10PhosphorylationFSIPETESRSGDSGG
CCCCCCCCCCCCCCC		38.8828857561
37PhosphorylationVLHCRVRYSQLLGLH
EEEEEEEHHHHHCHH		9.6426657352
38PhosphorylationLHCRVRYSQLLGLHE
EEEEEEHHHHHCHHH		12.0929255136
51PhosphorylationHEQLRKEYGANVLPA
HHHHHHHHCCCCCCC		25.27-
63UbiquitinationLPAFPPKKLFSLTPA
CCCCCCHHHHCCCHH		61.6121890473
63UbiquitinationLPAFPPKKLFSLTPA
CCCCCCHHHHCCCHH		61.6121890473
66PhosphorylationFPPKKLFSLTPAEVE
CCCHHHHCCCHHHHH		41.5928857561
81UbiquitinationQRREQLEKYMQAVRQ
HHHHHHHHHHHHHHH		55.40-
82PhosphorylationRREQLEKYMQAVRQD
HHHHHHHHHHHHHHC		5.7722964224
168UbiquitinationSLFLVREKEDGAFSF
EEEEEEECCCCCCHH		51.01-
178UbiquitinationGAFSFVRKLQEFELP
CCCHHHHHHHCCCCC		49.58-
198UbiquitinationSLRSQEYKIVLRKSY
ECCCCEEEEEEEHHH		26.11-
203UbiquitinationEYKIVLRKSYWDSAY
EEEEEEEHHHHCCCC		43.68-
241UbiquitinationRGWILVTKEQHRQLK
CCEEEEEHHHHHHHH		48.15-
248UbiquitinationKEQHRQLKSLQEKVS
HHHHHHHHHHHHHCC		40.56-
253UbiquitinationQLKSLQEKVSKKEFL
HHHHHHHHCCHHHHH		38.56-
255PhosphorylationKSLQEKVSKKEFLRL
HHHHHHCCHHHHHHH		49.42-
312PhosphorylationGQQLREGSFRVTRMR
CCCCCCCCEEEEEEE		12.7224719451
324PhosphorylationRMRCWRVTSSVPLPS
EEEEEEEEECCCCCC		13.5023927012
325PhosphorylationMRCWRVTSSVPLPSG
EEEEEEEECCCCCCC		26.8723927012
326PhosphorylationRCWRVTSSVPLPSGS
EEEEEEECCCCCCCC		20.5623927012
331PhosphorylationTSSVPLPSGSTSSPG
EECCCCCCCCCCCCC		53.7322167270
333PhosphorylationSVPLPSGSTSSPGRG
CCCCCCCCCCCCCCC		29.4729255136
334PhosphorylationVPLPSGSTSSPGRGR
CCCCCCCCCCCCCCC		36.4329255136
335PhosphorylationPLPSGSTSSPGRGRG
CCCCCCCCCCCCCCC		35.9129255136
336PhosphorylationLPSGSTSSPGRGRGE
CCCCCCCCCCCCCCE		31.3129255136
339MethylationGSTSSPGRGRGEVRL
CCCCCCCCCCCEEEH		34.71115917433
341MethylationTSSPGRGRGEVRLEL
CCCCCCCCCEEEHHH		36.42115917437
356UbiquitinationAFEYLMSKDRLQWVT
HHHHHHCCCCEEEEE		32.66-
388PhosphorylationDELMVKKSGGSIRKM
HHHHHHHCCCHHHHH		42.54-
403PhosphorylationLRRRVGGTLRRSDSQ
HHHHHCCEECCCCHH		15.9130576142
407PhosphorylationVGGTLRRSDSQQAVK
HCCEECCCCHHCCCC		34.8728176443
409PhosphorylationGTLRRSDSQQAVKSP
CEECCCCHHCCCCCC		25.9928176443
414UbiquitinationSDSQQAVKSPPLLES
CCHHCCCCCCCCCCC		61.33-
415PhosphorylationDSQQAVKSPPLLESP
CHHCCCCCCCCCCCC		25.7529255136
421PhosphorylationKSPPLLESPDATRES
CCCCCCCCCCCCHHH		28.2219664994
425PhosphorylationLLESPDATRESMVKL
CCCCCCCCHHHHHHH		42.2030266825
428PhosphorylationSPDATRESMVKLSSK
CCCCCHHHHHHHHHH		26.1126657352
431UbiquitinationATRESMVKLSSKLSA
CCHHHHHHHHHHHHE		33.73-
433PhosphorylationRESMVKLSSKLSAVS
HHHHHHHHHHHHEEE		21.5125867546
434PhosphorylationESMVKLSSKLSAVSL
HHHHHHHHHHHEEEE		48.3125867546
435UbiquitinationSMVKLSSKLSAVSLR
HHHHHHHHHHEEEEC		42.98-
435AcetylationSMVKLSSKLSAVSLR
HHHHHHHHHHEEEEC		42.9825953088
437PhosphorylationVKLSSKLSAVSLRGI
HHHHHHHHEEEECCC		30.2925159151
440PhosphorylationSSKLSAVSLRGIGSP
HHHHHEEEECCCCCC		16.4425159151
446PhosphorylationVSLRGIGSPSTDASA
EEECCCCCCCCCCCH		17.4728450419
448PhosphorylationLRGIGSPSTDASASD
ECCCCCCCCCCCHHH		40.3928450419
449PhosphorylationRGIGSPSTDASASDV
CCCCCCCCCCCHHHC		38.6828450419
452PhosphorylationGSPSTDASASDVHGN
CCCCCCCCHHHCCCC		30.9928450419
454PhosphorylationPSTDASASDVHGNFA
CCCCCCHHHCCCCCC		37.3628450419
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
437SPhosphorylationKinasePRKAA1Q13131
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX17_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 SNX17_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYAM3_HUMANSELPphysical
11237770
LDLR_HUMANLDLRphysical
12169628
LRP8_HUMANLRP8physical
12169628
LYAM3_HUMANSELPphysical
23382219
INSR_HUMANINSRphysical
23382219
NTRK1_HUMANNTRK1physical
23382219
RASH_HUMANHRASphysical
23382219
A4_HUMANAPPphysical
23382219
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNX17_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-407; SER-415 ANDSER-421, AND MASS SPECTROMETRY.
"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-409; SER-415; SER-421;SER-437 AND SER-440, AND MASS SPECTROMETRY.

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