SNX33_HUMAN - dbPTM
SNX33_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX33_HUMAN
UniProt AC Q8WV41
Protein Name Sorting nexin-33
Gene Name SNX33
Organism Homo sapiens (Human).
Sequence Length 574
Subcellular Localization Cytoplasm, cytosol. Membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Primarily cytosolic, but a minor proportion is membrane-bound (PubMed:18353773). Not associated
Protein Description Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes..
Protein Sequence MALKGRALYDFHSENKEEISIQQDEDLVIFSETSLDGWLQGQNSRGETGLFPASYVEIVRSGISTNHADYSSSPAGSPGAQVSLYNSPSVASPARSGGGSGFLSNQGSFEEDDDDDWDDWDDGCTVVEEPRAGGLGTNGHPPLNLSYPGAYPSQHMAFRPKPPLERQDSLASAKRGSVVGRNLNRFSCFVRSGVEAFILGDVPMMAKIAETYSIEMGPRGPQWKANPHPFACSVEDPTKQTKFKGIKSYISYKLTPTHAASPVYRRYKHFDWLYNRLLHKFTVISVPHLPEKQATGRFEEDFIEKRKRRLILWMDHMTSHPVLSQYEGFQHFLSCLDDKQWKMGKRRAEKDEMVGASFLLTFQIPTEHQDLQDVEDRVDTFKAFSKKMDDSVLQLSTVASELVRKHVGGFRKEFQKLGSAFQAISHSFQMDPPFCSEALNSAISHTGRTYEAIGEMFAEQPKNDLFQMLDTLSLYQGLLSNFPDIIHLQKGAFAKVKESQRMSDEGRMVQDEADGIRRRCRVVGFALQAEMNHFHQRRELDFKHMMQNYLRQQILFYQRVGQQLEKTLRMYDNL
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
9PhosphorylationALKGRALYDFHSENK
CCCCCCEEECCCCCC		18.6428674419
48PhosphorylationGQNSRGETGLFPASY
CCCCCCCCCCCCHHH		41.8521945579
54PhosphorylationETGLFPASYVEIVRS
CCCCCCHHHHHHHHC		29.9221945579
55PhosphorylationTGLFPASYVEIVRSG
CCCCCHHHHHHHHCC		12.2821945579
61PhosphorylationSYVEIVRSGISTNHA
HHHHHHHCCCCCCCC		29.5921945579
64PhosphorylationEIVRSGISTNHADYS
HHHHCCCCCCCCCCC		27.0421945579
65PhosphorylationIVRSGISTNHADYSS
HHHCCCCCCCCCCCC		29.1521945579
70PhosphorylationISTNHADYSSSPAGS
CCCCCCCCCCCCCCC		15.9621945579
71PhosphorylationSTNHADYSSSPAGSP
CCCCCCCCCCCCCCC		25.5321945579
72PhosphorylationTNHADYSSSPAGSPG
CCCCCCCCCCCCCCC		33.8321945579
73PhosphorylationNHADYSSSPAGSPGA
CCCCCCCCCCCCCCC		16.9021945579
77PhosphorylationYSSSPAGSPGAQVSL
CCCCCCCCCCCEEEE		23.4421945579
83PhosphorylationGSPGAQVSLYNSPSV
CCCCCEEEEECCCCC		17.0421945579
85PhosphorylationPGAQVSLYNSPSVAS
CCCEEEEECCCCCCC		13.1921945579
87PhosphorylationAQVSLYNSPSVASPA
CEEEEECCCCCCCCC		12.6621945579
89PhosphorylationVSLYNSPSVASPARS
EEEECCCCCCCCCCC		30.0921945579
92PhosphorylationYNSPSVASPARSGGG
ECCCCCCCCCCCCCC		19.5521945579
96PhosphorylationSVASPARSGGGSGFL
CCCCCCCCCCCCCCC		43.8524144214
100PhosphorylationPARSGGGSGFLSNQG
CCCCCCCCCCCCCCC		29.6424144214
104PhosphorylationGGGSGFLSNQGSFEE
CCCCCCCCCCCCCCC		25.5024144214
108PhosphorylationGFLSNQGSFEEDDDD
CCCCCCCCCCCCCCC		21.5224144214
125PhosphorylationDDWDDGCTVVEEPRA
CCCCCCCEEEECCCC		32.8724144214
146PhosphorylationGHPPLNLSYPGAYPS
CCCCCCCCCCCCCCC		28.3626657352
151PhosphorylationNLSYPGAYPSQHMAF
CCCCCCCCCCCCCCC		14.8827251275
169PhosphorylationPPLERQDSLASAKRG
CCCHHCCCHHHHHCC		19.9329255136
172PhosphorylationERQDSLASAKRGSVV
HHCCCHHHHHCCCHH		39.3529396449
177PhosphorylationLASAKRGSVVGRNLN
HHHHHCCCHHCCCCC		20.0530576142
187PhosphorylationGRNLNRFSCFVRSGV
CCCCCCCCEEEECCC		11.9228555341
224UbiquitinationGPRGPQWKANPHPFA
CCCCCCCCCCCCCCC		32.7929967540
249PhosphorylationKFKGIKSYISYKLTP
CCCCCCCEEEEECCC		6.7322817900
252PhosphorylationGIKSYISYKLTPTHA
CCCCEEEEECCCCCC		10.6422817900
257PhosphorylationISYKLTPTHAASPVY
EEEECCCCCCCCHHH		20.9321253578
261PhosphorylationLTPTHAASPVYRRYK
CCCCCCCCHHHHHHH		18.7123186163
264PhosphorylationTHAASPVYRRYKHFD
CCCCCHHHHHHHHHH		7.8621253578
282PhosphorylationNRLLHKFTVISVPHL
HHHHHHCEEEECCCC		23.02-
285PhosphorylationLHKFTVISVPHLPEK
HHHCEEEECCCCCHH		25.84-
292UbiquitinationSVPHLPEKQATGRFE
ECCCCCHHHCCCCCC		43.2022817900
305UbiquitinationFEEDFIEKRKRRLIL
CCHHHHHHHHHHEEE		59.4029967540
350AcetylationMGKRRAEKDEMVGAS
CCCHHHHHHHCCCCE		58.9920167786
380PhosphorylationDVEDRVDTFKAFSKK
HHHHHHHHHHHHHHH		24.95-
382AcetylationEDRVDTFKAFSKKMD
HHHHHHHHHHHHHCC		51.0920167786
386AcetylationDTFKAFSKKMDDSVL
HHHHHHHHHCCCHHH		45.7420167786
405UbiquitinationVASELVRKHVGGFRK
HHHHHHHHHCCCHHH		34.8529967540
566UbiquitinationRVGQQLEKTLRMYDN
HHHHHHHHHHHHHHC		62.54-
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 SNX33_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX33_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 SNX33_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX33_HUMANSNX33physical
20964629
SNX9_HUMANSNX9physical
20964629
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 SNX33_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-70, AND MASSSPECTROMETRY.

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