SNX5_HUMAN - dbPTM
SNX5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX5_HUMAN
UniProt AC Q9Y5X3
Protein Name Sorting nexin-5
Gene Name SNX5
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Endosome . Early endosome . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasm. Ce
Protein Description Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). [PubMed: 15561769 Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC) (Probable Does not have in vitro vesicle-to-membrane remodeling activity]
Protein Sequence MAAVPELLQQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLPTFQSPEFSVTRQHEDFVWLHDTLIETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSSHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFTGVKEVDDFFEQEKNFLINYYNRIKDSCVKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAEAHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN
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------MAAVPELLQ
------CCCHHHHHH		19.7122223895
16PhosphorylationQQQEEDRSKLRSVSV
HHHHHHHHHHHHEEE		48.6528857561
20PhosphorylationEDRSKLRSVSVDLNV
HHHHHHHHEEECCCC		29.2230278072
22PhosphorylationRSKLRSVSVDLNVDP
HHHHHHEEECCCCCC		15.9130278072
30PhosphorylationVDLNVDPSLQIDIPD
ECCCCCCCCCCCCCC		28.5728464451
46UbiquitinationLSERDKVKFTVHTKT
CCCCCCCEEEEEECC		40.85-
48PhosphorylationERDKVKFTVHTKTTL
CCCCCEEEEEECCCC		12.9826074081
51PhosphorylationKVKFTVHTKTTLPTF
CCEEEEEECCCCCCC		26.2526074081
53PhosphorylationKFTVHTKTTLPTFQS
EEEEEECCCCCCCCC		34.4229083192
54PhosphorylationFTVHTKTTLPTFQSP
EEEEECCCCCCCCCC		32.0929083192
57PhosphorylationHTKTTLPTFQSPEFS
EECCCCCCCCCCCCC		37.1029083192
60PhosphorylationTTLPTFQSPEFSVTR
CCCCCCCCCCCCCEE		23.3925159151
64PhosphorylationTFQSPEFSVTRQHED
CCCCCCCCCEECCCC		22.4029083192
66PhosphorylationQSPEFSVTRQHEDFV
CCCCCCCEECCCCEE		24.3429083192
115PhosphorylationKLGEGEGSMTKEEFA
HHCCCCCCCCHHHHH		20.9824719451
116SulfoxidationLGEGEGSMTKEEFAK
HCCCCCCCCHHHHHH		10.2421406390
117PhosphorylationGEGEGSMTKEEFAKM
CCCCCCCCHHHHHHH		36.6828857561
118UbiquitinationEGEGSMTKEEFAKMK
CCCCCCCHHHHHHHH		46.7521906983
132PhosphorylationKQELEAEYLAVFKKT
HHHHHHHHHHHHHHH		13.65-
151PhosphorylationEVFLQRLSSHPVLSK
HHHHHHHHCCCCCCC		28.8720068231
152PhosphorylationVFLQRLSSHPVLSKD
HHHHHHHCCCCCCCC		36.0820068231
157PhosphorylationLSSHPVLSKDRNFHV
HHCCCCCCCCCCEEE		32.5120068231
179PhosphorylationLSVRRKNTKEMFGGF
CCHHCCCHHHHHHHH		31.2724719451
180UbiquitinationSVRRKNTKEMFGGFF
CHHCCCHHHHHHHHH		57.4821890473
188UbiquitinationEMFGGFFKSVVKSAD
HHHHHHHHHHHHCHH		39.8321890473
189PhosphorylationMFGGFFKSVVKSADE
HHHHHHHHHHHCHHH		27.3024719451
192UbiquitinationGFFKSVVKSADEVLF
HHHHHHHHCHHHHEE		37.4621906983
193PhosphorylationFFKSVVKSADEVLFT
HHHHHHHCHHHHEEE		29.3725159151
203UbiquitinationEVLFTGVKEVDDFFE
HHEEECCEECHHHHH		54.06-
213UbiquitinationDDFFEQEKNFLINYY
HHHHHHHHHHHHHHH		53.33-
219PhosphorylationEKNFLINYYNRIKDS
HHHHHHHHHHHHHHH		8.6325003641
226O-linked_GlycosylationYYNRIKDSCVKADKM
HHHHHHHHHHHHHHH		18.7930379171
226PhosphorylationYYNRIKDSCVKADKM
HHHHHHHHHHHHHHH		18.79-
229AcetylationRIKDSCVKADKMTRS
HHHHHHHHHHHHCCC		56.0225953088
263UbiquitinationLEEPTVIKKYLLKVA
CCCCHHHHHHHHHHH		30.91-
268UbiquitinationVIKKYLLKVAELFEK
HHHHHHHHHHHHHHH		36.48-
275UbiquitinationKVAELFEKLRKVEGR
HHHHHHHHHHHCCCC		46.3819608861
275MalonylationKVAELFEKLRKVEGR
HHHHHHHHHHHCCCC		46.3826320211
275AcetylationKVAELFEKLRKVEGR
HHHHHHHHHHHCCCC		46.3819608861
277MethylationAELFEKLRKVEGRVS
HHHHHHHHHCCCCCC		52.6324391077
290AcetylationVSSDEDLKLTELLRY
CCCHHHHHHHHHHHH		66.7325953088
290UbiquitinationVSSDEDLKLTELLRY
CCCHHHHHHHHHHHH		66.7321906983
297PhosphorylationKLTELLRYYMLNIEA
HHHHHHHHHHHCHHH		8.0020068231
298PhosphorylationLTELLRYYMLNIEAA
HHHHHHHHHHCHHHH		6.6820068231
310PhosphorylationEAAKDLLYRRTKALI
HHHHHHHHHHHHHHH		12.8322817900
314UbiquitinationDLLYRRTKALIDYEN
HHHHHHHHHHHCCCC		39.1121890473
319PhosphorylationRTKALIDYENSNKAL
HHHHHHCCCCCCHHH		15.2622817900
322PhosphorylationALIDYENSNKALDKA
HHHCCCCCCHHHHHH		27.9722461510
324UbiquitinationIDYENSNKALDKARL
HCCCCCCHHHHHHHH		50.58-
337AcetylationRLKSKDVKLAEAHQQ
HHHHHCHHHHHHHHH		52.7123749302
337UbiquitinationRLKSKDVKLAEAHQQ
HHHHHCHHHHHHHHH		52.71-
349UbiquitinationHQQECCQKFEQLSES
HHHHHHHHHHHHCHH		36.63-
358UbiquitinationEQLSESAKEELINFK
HHHCHHHHHHHHHHH		62.08-
365MethylationKEELINFKRKRVAAF
HHHHHHHHHHHHHHH		53.1524431761
365UbiquitinationKEELINFKRKRVAAF
HHHHHHHHHHHHHHH		53.15-
365AcetylationKEELINFKRKRVAAF
HHHHHHHHHHHHHHH		53.1527452117
367MethylationELINFKRKRVAAFRK
HHHHHHHHHHHHHHH		52.38115980751
385AcetylationEMSELEIKHARNNVS
HHHHHHHHHHHHHHH		23.1025953088
396PhosphorylationNNVSLLQSCIDLFKN
HHHHHHHHHHHHHHC		17.0127050516
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 SNX5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX5_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 SNX5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FANCA_HUMANFANCAphysical
10600472
VP33B_HUMANVPS33Bphysical
22939629
PI51C_HUMANPIP5K1Cphysical
23602387
HGS_HUMANHGSphysical
23602387
ARFP2_HUMANARFIP2physical
22863883
NU155_HUMANNUP155physical
22863883
PI51C_HUMANPIP5K1Cphysical
25588945
LAP4B_HUMANLAPTM4Bphysical
25588945
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 SNX5_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.
"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-275, AND MASS SPECTROMETRY.

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