SNX4_HUMAN - dbPTM
SNX4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX4_HUMAN
UniProt AC O95219
Protein Name Sorting nexin-4
Gene Name SNX4
Organism Homo sapiens (Human).
Sequence Length 450
Subcellular Localization Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Also detected on a juxtanuclear endocytic recycling compartment (ERC).
Protein Description May be involved in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation..
Protein Sequence MEQAPPDPERQLQPAPLEPLGSPDAGLGAAVGKEAEGAGEESSGVDTMTHNNFWLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHTDGQSVLTDSLWRRYSEFELLRSYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRIASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFTDLKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELVTGTVRTFSLKGMTTKLFGQETPEQREARIKVLEEQINEGEQQLKSKNLEGREFVKNAWADIERFKEQKNRDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM
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
1Acetylation-------MEQAPPDP
-------CCCCCCCH		8.5419413330
22PhosphorylationAPLEPLGSPDAGLGA
CCCCCCCCCCCCCCC		27.5630266825
33UbiquitinationGLGAAVGKEAEGAGE
CCCCCCCCCCCCCCC		47.34-
49PhosphorylationSSGVDTMTHNNFWLK
CCCCCCCCCCCEEEE		24.4430622161
54UbiquitinationTMTHNNFWLKKIEIS
CCCCCCEEEEEEEEE		14.92-
56UbiquitinationTHNNFWLKKIEISVS
CCCCEEEEEEEEEHH		42.1529967540
57UbiquitinationHNNFWLKKIEISVSE
CCCEEEEEEEEEHHH		43.3229967540
60UbiquitinationFWLKKIEISVSEAEK
EEEEEEEEEHHHHHH		5.85-
67UbiquitinationISVSEAEKRTGRNAM
EEHHHHHHHHCCCCC		63.41-
79UbiquitinationNAMNMQETYTAYLIE
CCCCHHHHHEEEEEE		14.85-
89PhosphorylationAYLIETRSVEHTDGQ
EEEEEEECEECCCCC		39.0021712546
97PhosphorylationVEHTDGQSVLTDSLW
EECCCCCCCCCHHHH		25.3228857561
102PhosphorylationGQSVLTDSLWRRYSE
CCCCCCHHHHHHHCH		25.2924719451
107PhosphorylationTDSLWRRYSEFELLR
CHHHHHHHCHHHHHH		12.1823927012
108PhosphorylationDSLWRRYSEFELLRS
HHHHHHHCHHHHHHH		33.7228450419
108UbiquitinationDSLWRRYSEFELLRS
HHHHHHHCHHHHHHH		33.72-
132UbiquitinationVVPPLPEKRAEFVWH
ECCCCCHHHHHHHHH		55.77-
140UbiquitinationRAEFVWHKLSADNMD
HHHHHHHHCCCCCCC		28.5521906983
146SulfoxidationHKLSADNMDPDFVER
HHCCCCCCCHHHHHH		9.0030846556
172S-nitrosylationIASHPILCRDKIFYL
HHCCCEECCCCEEEE		5.6819483679
172S-nitrosocysteineIASHPILCRDKIFYL
HHCCCEECCCCEEEE		5.68-
175UbiquitinationHPILCRDKIFYLFLT
CCEECCCCEEEEEEE		18.50-
194UbiquitinationWKETVNETGFQLKAD
CCCCCCCCCCEEECH		37.78-
199UbiquitinationNETGFQLKADSRLKA
CCCCCEEECHHHHHH		39.0921906983
205UbiquitinationLKADSRLKALNATFR
EECHHHHHHHHEEEE		50.1227667366
205MethylationLKADSRLKALNATFR
EECHHHHHHHHEEEE		50.12115980759
210PhosphorylationRLKALNATFRVKNPD
HHHHHHEEEEECCCC		15.76-
211UbiquitinationLKALNATFRVKNPDK
HHHHHEEEEECCCCC		8.64-
216UbiquitinationATFRVKNPDKRFTDL
EEEEECCCCCCCCCH		42.66-
224UbiquitinationDKRFTDLKHYSDELQ
CCCCCCHHHCCHHHH		43.2221906983
226PhosphorylationRFTDLKHYSDELQSV
CCCCHHHCCHHHHHH		19.0729496907
231UbiquitinationKHYSDELQSVISHLL
HHCCHHHHHHHHHHH		33.34-
245UbiquitinationLRVRARVADRLYGVY
HHHHHHHHHHHCCEE		7.22-
247MethylationVRARVADRLYGVYKV
HHHHHHHHHCCEEEE		21.77115917457
249PhosphorylationARVADRLYGVYKVHG
HHHHHHHCCEEEEEC		12.8729496907
253UbiquitinationDRLYGVYKVHGNYGR
HHHCCEEEEECCCCH		25.9121890473
253UbiquitinationDRLYGVYKVHGNYGR
HHHCCEEEEECCCCH		25.9121890473
256UbiquitinationYGVYKVHGNYGRVFS
CCEEEEECCCCHHHH		31.85-
263PhosphorylationGNYGRVFSEWSAIEK
CCCCHHHHCHHHHHH		34.9928857561
266PhosphorylationGRVFSEWSAIEKEMG
CHHHHCHHHHHHHHC		18.4728857561
299UbiquitinationDILEDEEHYADQLKE
HHHCCHHHHHHHHHH		22.49-
304UbiquitinationEEHYADQLKEYLFYA
HHHHHHHHHHHHHHH		4.72-
320UbiquitinationALRAVCRKHELMQYD
HHHHHHHHHHHHHHH		35.98-
338UbiquitinationAAQDLASKKQQCEEL
HHHHHHHHHHHHHHH		49.3329967540
339UbiquitinationAQDLASKKQQCEELV
HHHHHHHHHHHHHHH		43.0129967540
347PhosphorylationQQCEELVTGTVRTFS
HHHHHHHHCCEEEEE		39.50-
352PhosphorylationLVTGTVRTFSLKGMT
HHHCCEEEEECCCCH		17.1526434776
354PhosphorylationTGTVRTFSLKGMTTK
HCCEEEEECCCCHHH		28.6728857561
356MethylationTVRTFSLKGMTTKLF
CEEEEECCCCHHHHC		45.5082991517
356UbiquitinationTVRTFSLKGMTTKLF
CEEEEECCCCHHHHC		45.5022817900
359PhosphorylationTFSLKGMTTKLFGQE
EEECCCCHHHHCCCC		29.4626434776
360PhosphorylationFSLKGMTTKLFGQET
EECCCCHHHHCCCCC		19.5026434776
361UbiquitinationSLKGMTTKLFGQETP
ECCCCHHHHCCCCCH		32.4321906983
367PhosphorylationTKLFGQETPEQREAR
HHHCCCCCHHHHHHH		25.0025159151
376UbiquitinationEQREARIKVLEEQIN
HHHHHHHHHHHHHHH		34.9021906983
388UbiquitinationQINEGEQQLKSKNLE
HHHHHHHHHHHCCCC		46.7022817900
390UbiquitinationNEGEQQLKSKNLEGR
HHHHHHHHHCCCCHH		55.8621906983
391PhosphorylationEGEQQLKSKNLEGRE
HHHHHHHHCCCCHHH		35.0529514088
392UbiquitinationGEQQLKSKNLEGREF
HHHHHHHCCCCHHHH		65.0622817900
393UbiquitinationEQQLKSKNLEGREFV
HHHHHHCCCCHHHHH		50.8722817900
401UbiquitinationLEGREFVKNAWADIE
CCHHHHHHHHHHHHH		46.3921906983
408UbiquitinationKNAWADIERFKEQKN
HHHHHHHHHHHHHCC		53.2422817900
419AcetylationEQKNRDLKEALISYA
HHCCCHHHHHHHHHH		45.277851125
422UbiquitinationNRDLKEALISYAVMQ
CCHHHHHHHHHHHHH		2.5421963094
424UbiquitinationDLKEALISYAVMQIS
HHHHHHHHHHHHHHH		14.1122817900
433UbiquitinationAVMQISMCKKGIQVW
HHHHHHHCHHCCCHH		3.0822817900
444UbiquitinationIQVWTNAKECFSKM-
CCHHCCHHHHHHCC-		58.02-
449UbiquitinationNAKECFSKM------
CHHHHHHCC------		28.51-
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 SNX4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX4_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 SNX4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGFRA_HUMANPDGFRAphysical
9819414
PGFRB_HUMANPDGFRBphysical
9819414
INSR_HUMANINSRphysical
9819414
LEPR_HUMANLEPRphysical
9819414
EGFR_HUMANEGFRphysical
9819414
SPT5H_HUMANSUPT5Hphysical
21988832
AR6P1_HUMANARL6IP1physical
25416956
SNX30_HUMANSNX30physical
28514442
ANKY2_HUMANANKMY2physical
28514442
ABCBA_HUMANABCB10physical
28514442
CYBP_HUMANCACYBPphysical
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 SNX4_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 MET-1, AND MASS SPECTROMETRY.
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-22, AND MASSSPECTROMETRY.

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