SNX9_HUMAN - dbPTM
SNX9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX9_HUMAN
UniProt AC Q9Y5X1
Protein Name Sorting nexin-9
Gene Name SNX9
Organism Homo sapiens (Human).
Sequence Length 595
Subcellular Localization Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network. Cell projection, ruffle. Cytopla
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. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate..
Protein Sequence MATKARVMYDFAAEPGNNELTVNEGEIITITNPDVGGGWLEGRNIKGERGLVPTDYVEILPSDGKDQFSCGNSVADQAFLDSLSASTAQASSSAASNNHQVGSGNDPWSAWSASKSGNWESSEGWGAQPEGAGAQRNTNTPNNWDTAFGHPQAYQGPATGDDDDWDEDWDGPKSSSYFKDSESADAGGAQRGNSRASSSSMKIPLNKFPGFAKPGTEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELAGVMIFSTMEPEAPDLDLVEIEQKCEAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKITLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
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
54PhosphorylationGERGLVPTDYVEILP
CCCCCCCCCEEEECC		32.2721945579
56PhosphorylationRGLVPTDYVEILPSD
CCCCCCCEEEECCCC		11.4921945579
79UbiquitinationNSVADQAFLDSLSAS
CHHHHHHHHHHCCCH		6.9123503661
85UbiquitinationAFLDSLSASTAQASS
HHHHHCCCHHHHHCC		19.0527667366
113UbiquitinationDPWSAWSASKSGNWE
CCHHHHCCCCCCCCC		15.4127667366
116PhosphorylationSAWSASKSGNWESSE
HHHCCCCCCCCCCCC		34.5625159151
121PhosphorylationSKSGNWESSEGWGAQ
CCCCCCCCCCCCCCC		25.8823403867
122PhosphorylationKSGNWESSEGWGAQP
CCCCCCCCCCCCCCC		28.7223403867
129UbiquitinationSEGWGAQPEGAGAQR
CCCCCCCCCCCCCCC		41.2621890473
138PhosphorylationGAGAQRNTNTPNNWD
CCCCCCCCCCCCCHH		42.5328857561
140PhosphorylationGAQRNTNTPNNWDTA
CCCCCCCCCCCHHHC		25.9228857561
146PhosphorylationNTPNNWDTAFGHPQA
CCCCCHHHCCCCCCC		18.5922210691
154PhosphorylationAFGHPQAYQGPATGD
CCCCCCCCCCCCCCC		14.5722210691
159PhosphorylationQAYQGPATGDDDDWD
CCCCCCCCCCCCCCC		44.2530624053
166UbiquitinationTGDDDDWDEDWDGPK
CCCCCCCCCCCCCCC		51.4723503661
172UbiquitinationWDEDWDGPKSSSYFK
CCCCCCCCCCHHHCC		30.7727667366
173UbiquitinationDEDWDGPKSSSYFKD
CCCCCCCCCHHHCCC		69.3823503661
174PhosphorylationEDWDGPKSSSYFKDS
CCCCCCCCHHHCCCC		27.8729978859
175PhosphorylationDWDGPKSSSYFKDSE
CCCCCCCHHHCCCCC		34.8729978859
176PhosphorylationWDGPKSSSYFKDSES
CCCCCCHHHCCCCCC		41.5029978859
177PhosphorylationDGPKSSSYFKDSESA
CCCCCHHHCCCCCCC		19.3228857561
179UbiquitinationPKSSSYFKDSESADA
CCCHHHCCCCCCCCC		52.7021906983
181PhosphorylationSSSYFKDSESADAGG
CHHHCCCCCCCCCCC		33.7629978859
183PhosphorylationSYFKDSESADAGGAQ
HHCCCCCCCCCCCCC		35.0929978859
191MethylationADAGGAQRGNSRASS
CCCCCCCCCCCCCCC		45.81115917465
194PhosphorylationGGAQRGNSRASSSSM
CCCCCCCCCCCCCCC		31.8622496350
197PhosphorylationQRGNSRASSSSMKIP
CCCCCCCCCCCCCCC		29.6422617229
198PhosphorylationRGNSRASSSSMKIPL
CCCCCCCCCCCCCCC		26.0023401153
199PhosphorylationGNSRASSSSMKIPLN
CCCCCCCCCCCCCCC		31.7721712546
200PhosphorylationNSRASSSSMKIPLNK
CCCCCCCCCCCCCCC		26.4926055452
200UbiquitinationNSRASSSSMKIPLNK
CCCCCCCCCCCCCCC		26.4927667366
202UbiquitinationRASSSSMKIPLNKFP
CCCCCCCCCCCCCCC		43.0229967540
206UbiquitinationSSMKIPLNKFPGFAK
CCCCCCCCCCCCCCC		38.2723503661
207MalonylationSMKIPLNKFPGFAKP
CCCCCCCCCCCCCCC		61.7026320211
207UbiquitinationSMKIPLNKFPGFAKP
CCCCCCCCCCCCCCC		61.7027667366
213UbiquitinationNKFPGFAKPGTEQYL
CCCCCCCCCCHHHHH		41.5429967540
213MalonylationNKFPGFAKPGTEQYL
CCCCCCCCCCHHHHH		41.5432601280
216UbiquitinationPGFAKPGTEQYLLAK
CCCCCCCHHHHHHHH		28.5721890473
216PhosphorylationPGFAKPGTEQYLLAK
CCCCCCCHHHHHHHH		28.5721945579
219PhosphorylationAKPGTEQYLLAKQLA
CCCCHHHHHHHHHHC		9.4621945579
219UbiquitinationAKPGTEQYLLAKQLA
CCCCHHHHHHHHHHC		9.4623503661
223UbiquitinationTEQYLLAKQLAKPKE
HHHHHHHHHHCCCHH		45.9027667366
231UbiquitinationQLAKPKEKIPIIVGD
HHCCCHHHCCEEECC		60.9724816145
239PhosphorylationIPIIVGDYGPMWVYP
CCEEECCCCCEEECC		19.7327259358
242SulfoxidationIVGDYGPMWVYPTST
EECCCCCEEECCCCC		3.0830846556
245PhosphorylationDYGPMWVYPTSTFDC
CCCCEEECCCCCCCE		5.8118083107
261PhosphorylationVADPRKGSKMYGLKS
EECCCCCCCEECCCC		19.7924719451
266UbiquitinationKGSKMYGLKSYIEYQ
CCCCEECCCCEEEEE		1.5121963094
267UbiquitinationGSKMYGLKSYIEYQL
CCCEECCCCEEEEEE		36.5321890473
267MethylationGSKMYGLKSYIEYQL
CCCEECCCCEEEEEE		36.5342371073
268PhosphorylationSKMYGLKSYIEYQLT
CCEECCCCEEEEEEC		36.0628152594
269PhosphorylationKMYGLKSYIEYQLTP
CEECCCCEEEEEECC		9.0023822953
269UbiquitinationKMYGLKSYIEYQLTP
CEECCCCEEEEEECC		9.0027667366
272PhosphorylationGLKSYIEYQLTPTNT
CCCCEEEEEECCCCC		10.16-
272UbiquitinationGLKSYIEYQLTPTNT
CCCCEEEEEECCCCC		10.1623503661
275PhosphorylationSYIEYQLTPTNTNRS
CEEEEEECCCCCCCC		16.7325159151
288UbiquitinationRSVNHRYKHFDWLYE
CCCCHHHHCHHHHHH		37.4419608861
288MalonylationRSVNHRYKHFDWLYE
CCCCHHHHCHHHHHH		37.4426320211
288AcetylationRSVNHRYKHFDWLYE
CCCCHHHHCHHHHHH		37.4419608861
293UbiquitinationRYKHFDWLYERLLVK
HHHCHHHHHHHHHHH		3.2423503661
300UbiquitinationLYERLLVKFGSAIPI
HHHHHHHHHCCCCCC		43.9321906983
306UbiquitinationVKFGSAIPIPSLPDK
HHHCCCCCCCCCCCC		31.9623503661
309PhosphorylationGSAIPIPSLPDKQVT
CCCCCCCCCCCCCCC		53.9427251275
310UbiquitinationSAIPIPSLPDKQVTG
CCCCCCCCCCCCCCC		5.5123503661
313UbiquitinationPIPSLPDKQVTGRFE
CCCCCCCCCCCCCCH		44.7327667366
313MalonylationPIPSLPDKQVTGRFE
CCCCCCCCCCCCCCH		44.7326320211
318UbiquitinationPDKQVTGRFEEEFIK
CCCCCCCCCHHHHHH		26.8324816145
320UbiquitinationKQVTGRFEEEFIKMR
CCCCCCCHHHHHHHH		56.0823503661
325UbiquitinationRFEEEFIKMRMERLQ
CCHHHHHHHHHHHHH		26.2721906983
343UbiquitinationTRMCRHPVISESEVF
HHHCCCCCCCHHHHH		6.5027667366
346UbiquitinationCRHPVISESEVFQQF
CCCCCCCHHHHHHHH		39.5323503661
353UbiquitinationESEVFQQFLNFRDEK
HHHHHHHHHCCCCHH		4.1321963094
356UbiquitinationVFQQFLNFRDEKEWK
HHHHHHCCCCHHHHH		13.0127667366
359UbiquitinationQFLNFRDEKEWKTGK
HHHCCCCHHHHHHCC		48.9323503661
360UbiquitinationFLNFRDEKEWKTGKR
HHCCCCHHHHHHCCH		73.4921963094
363UbiquitinationFRDEKEWKTGKRKAE
CCCHHHHHHCCHHHH		48.7927667366
366UbiquitinationEKEWKTGKRKAERDE
HHHHHHCCHHHHHHH		56.8323503661
397UbiquitinationLDLVEIEQKCEAVGK
CCEEEHHHHHHHHHH		62.4523503661
400UbiquitinationVEIEQKCEAVGKFTK
EEHHHHHHHHHHHHH		54.1227667366
404UbiquitinationQKCEAVGKFTKAMDD
HHHHHHHHHHHHCCH		43.1723503661
407UbiquitinationEAVGKFTKAMDDGVK
HHHHHHHHHCCHHHH		44.8621906983
414AcetylationKAMDDGVKELLTVGQ
HHCCHHHHHHHHHCH		48.457662585
414UbiquitinationKAMDDGVKELLTVGQ
HHCCHHHHHHHHHCH		48.4521906983
422UbiquitinationELLTVGQEHWKRCTG
HHHHHCHHHHHHCCC		45.8727667366
425UbiquitinationTVGQEHWKRCTGPLP
HHCHHHHHHCCCCCC		39.2332015554
430UbiquitinationHWKRCTGPLPKEYQK
HHHHCCCCCCHHHHH		27.6027667366
433UbiquitinationRCTGPLPKEYQKIGK
HCCCCCCHHHHHHHH		76.4023503661
437UbiquitinationPLPKEYQKIGKALQS
CCCHHHHHHHHHHHH		53.1527667366
440UbiquitinationKEYQKIGKALQSLAT
HHHHHHHHHHHHHHH		49.7721906983
470PhosphorylationAITEAGKTYEEIASL
HHHHHHHCHHHHHHH		34.9427762562
471PhosphorylationITEAGKTYEEIASLV
HHHHHHCHHHHHHHH		18.3027762562
483UbiquitinationSLVAEQPKKDLHFLM
HHHHCCCCHHHHHHH		59.6221906983
509UbiquitinationCFPDIIGTHKGAIEK
CCHHHHCCCCCHHHH		15.2527667366
511UbiquitinationPDIIGTHKGAIEKVK
HHHHCCCCCHHHHHH		50.2929967540
516UbiquitinationTHKGAIEKVKESDKL
CCCCHHHHHHHHCCE		53.1227667366
527UbiquitinationSDKLVATSKITLQDK
HCCEEEEEEEEHHHH		16.6027667366
528UbiquitinationDKLVATSKITLQDKQ
CCEEEEEEEEHHHHH		35.0421906983
534UbiquitinationSKITLQDKQNMVKRV
EEEEHHHHHHHHHHH		30.5221906983
565PhosphorylationNRIYDYNSVIRLYLE
CCCCCHHHHHHHHHH		16.82-
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
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:20491914
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX9_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 SNX9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADA15_HUMANADAM15physical
10531379
DYN2_HUMANDNM2physical
12952949
CLH1_HUMANCLTCphysical
12952949
ADAM9_HUMANADAM9physical
10531379
ITCH_HUMANITCHphysical
20491914
ACK1_HUMANTNK2physical
16137687
SNX9_HUMANSNX9physical
16316319
ACK1_HUMANTNK2physical
16316319
DYN1_HUMANDNM1physical
15703209
DYN2_HUMANDNM2physical
15703209
DYN2_HUMANDNM2physical
18388313
WASL_HUMANWASLphysical
18388313
ALDOA_RABITALDOAphysical
20129922
SYNJ1_HUMANSYNJ1physical
28514442
DYN1_HUMANDNM1physical
28514442
DYN3_HUMANDNM3physical
28514442
AP2A1_HUMANAP2A1physical
28514442
FCSD1_HUMANFCHSD1physical
28514442
DCMC_HUMANMLYCDphysical
28514442
AP2M1_HUMANAP2M1physical
28514442
AP2A2_HUMANAP2A2physical
28514442
AP1B1_HUMANAP1B1physical
28514442
HNRPK_HUMANHNRNPKphysical
28514442
DYN2_HUMANDNM2physical
28514442
AP2B1_HUMANAP2B1physical
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 SNX9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-288, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND MASSSPECTROMETRY.

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