SNX1_HUMAN - dbPTM
SNX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX1_HUMAN
UniProt AC Q13596
Protein Name Sorting nexin-1
Gene Name SNX1
Organism Homo sapiens (Human).
Sequence Length 522
Subcellular Localization Endosome membrane
Peripheral membrane protein
Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein
Cytoplasmic side . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side. Cell projection, la
Protein Description Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). [PubMed: 12198132 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 Can sense membrane curvature and has in vitro vesicle-to-membrane remodeling activity]
Protein Sequence MASGGGGCSASERLPPPFPGLEPESEGAAGGSEPEAGDSDTEGEDIFTGAAVVSKHQSPKITTSLLPINNGSKENGIHEEQDQEPQDLFADATVELSLDSTQNNQKKVLAKTLISLPPQEATNSSKPQPTYEELEEEEQEDQFDLTVGITDPEKIGDGMNAYVAYKVTTQTSLPLFRSKQFAVKRRFSDFLGLYEKLSEKHSQNGFIVPPPPEKSLIGMTKVKVGKEDSSSAEFLEKRRAALERYLQRIVNHPTMLQDPDVREFLEKEELPRAVGTQTLSGAGLLKMFNKATDAVSKMTIKMNESDIWFEEKLQEVECEEQRLRKLHAVVETLVNHRKELALNTAQFAKSLAMLGSSEDNTALSRALSQLAEVEEKIEQLHQEQANNDFFLLAELLSDYIRLLAIVRAAFDQRMKTWQRWQDAQATLQKKREAEARLLWANKPDKLQQAKDEILEWESRVTQYERDFERISTVVRKEVIRFEKEKSKDFKNHVIKYLETLLYSQQQLAKYWEAFLPEAKAIS
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
3Phosphorylation-----MASGGGGCSA
-----CCCCCCCCCH		36.3525159151
21UbiquitinationLPPPFPGLEPESEGA
CCCCCCCCCCCCCCC		11.4724816145
25PhosphorylationFPGLEPESEGAAGGS
CCCCCCCCCCCCCCC		52.6323927012
25 (in isoform 2)Phosphorylation-52.63-
32PhosphorylationSEGAAGGSEPEAGDS
CCCCCCCCCCCCCCC		49.4026503892
32 (in isoform 2)Phosphorylation-49.40-
38UbiquitinationGSEPEAGDSDTEGED
CCCCCCCCCCCCCCC		50.8423000965
39PhosphorylationSEPEAGDSDTEGEDI
CCCCCCCCCCCCCCC		45.5826503892
39 (in isoform 2)Phosphorylation-45.58-
39 (in isoform 3)Phosphorylation-45.5827251275
41PhosphorylationPEAGDSDTEGEDIFT
CCCCCCCCCCCCCCC		50.2526503892
41 (in isoform 2)Phosphorylation-50.25-
41 (in isoform 3)Phosphorylation-50.2527251275
42UbiquitinationEAGDSDTEGEDIFTG
CCCCCCCCCCCCCCC		66.6223000965
48PhosphorylationTEGEDIFTGAAVVSK
CCCCCCCCCCEEEEC		26.6730278072
48 (in isoform 2)Phosphorylation-26.67-
54PhosphorylationFTGAAVVSKHQSPKI
CCCCEEEECCCCCCC		20.1623927012
58PhosphorylationAVVSKHQSPKITTSL
EEEECCCCCCCEEEE		28.0726074081
62PhosphorylationKHQSPKITTSLLPIN
CCCCCCCEEEEEECC		19.2323403867
63PhosphorylationHQSPKITTSLLPINN
CCCCCCEEEEEECCC		22.3523403867
64PhosphorylationQSPKITTSLLPINNG
CCCCCEEEEEECCCC		21.1823403867
64 (in isoform 2)Phosphorylation-21.1821406692
64 (in isoform 3)Phosphorylation-21.1827251275
72PhosphorylationLLPINNGSKENGIHE
EEECCCCCCCCCCCC		38.6329255136
72 (in isoform 2)Phosphorylation-38.6321406692
72 (in isoform 3)Phosphorylation-38.6327251275
109UbiquitinationQNNQKKVLAKTLISL
CCHHHHHHHHHHHHC		5.7821890473
114UbiquitinationKVLAKTLISLPPQEA
HHHHHHHHHCCHHHC		4.8733845483
123PhosphorylationLPPQEATNSSKPQPT
CCHHHCCCCCCCCCC		51.8632142685
123 (in isoform 2)Phosphorylation-51.86-
128UbiquitinationATNSSKPQPTYEELE
CCCCCCCCCCHHHHH		46.8621890473
131PhosphorylationSSKPQPTYEELEEEE
CCCCCCCHHHHHHHH		17.6822817900
131UbiquitinationSSKPQPTYEELEEEE
CCCCCCCHHHHHHHH		17.6823000965
132UbiquitinationSKPQPTYEELEEEEQ
CCCCCCHHHHHHHHH		59.5923000965
135UbiquitinationQPTYEELEEEEQEDQ
CCCHHHHHHHHHHHC		67.6423000965
159SulfoxidationPEKIGDGMNAYVAYK
HHHCCCCCEEEEEEE		2.8530846556
161UbiquitinationKIGDGMNAYVAYKVT
HCCCCCEEEEEEEEE		7.4133845483
162PhosphorylationIGDGMNAYVAYKVTT
CCCCCEEEEEEEEEC		4.8027642862
168PhosphorylationAYVAYKVTTQTSLPL
EEEEEEEECCCCCCC		14.7225599653
171PhosphorylationAYKVTTQTSLPLFRS
EEEEECCCCCCCCCC		30.0925599653
172AcetylationYKVTTQTSLPLFRSK
EEEECCCCCCCCCCC		20.4019608861
172PhosphorylationYKVTTQTSLPLFRSK
EEEECCCCCCCCCCC		20.4025599653
172UbiquitinationYKVTTQTSLPLFRSK
EEEECCCCCCCCCCC		20.4029967540
172 (in isoform 2)Acetylation-20.40-
178PhosphorylationTSLPLFRSKQFAVKR
CCCCCCCCCCHHHHH		24.3925599653
179UbiquitinationSLPLFRSKQFAVKRR
CCCCCCCCCHHHHHH		45.2233845483
188PhosphorylationFAVKRRFSDFLGLYE
HHHHHHHHHHHHHHH		26.1629255136
188 (in isoform 3)Phosphorylation-26.1627251275
194PhosphorylationFSDFLGLYEKLSEKH
HHHHHHHHHHHHHHH		14.8224702127
196UbiquitinationDFLGLYEKLSEKHSQ
HHHHHHHHHHHHHHC		43.7023000965
200UbiquitinationLYEKLSEKHSQNGFI
HHHHHHHHHHCCCCC		45.2223000965
202PhosphorylationEKLSEKHSQNGFIVP
HHHHHHHHCCCCCCC		36.0928857561
202UbiquitinationEKLSEKHSQNGFIVP
HHHHHHHHCCCCCCC		36.0921890473
202 (in isoform 2)Ubiquitination-36.0921890473
215PhosphorylationVPPPPEKSLIGMTKV
CCCCCCCCCCCCEEE		24.4521712546
215 (in isoform 3)Phosphorylation-24.4527251275
220PhosphorylationEKSLIGMTKVKVGKE
CCCCCCCEEEEECCC		27.7221712546
220 (in isoform 3)Phosphorylation-27.7227251275
221UbiquitinationKSLIGMTKVKVGKED
CCCCCCEEEEECCCC		31.0321890473
221 (in isoform 2)Ubiquitination-31.0321890473
223UbiquitinationLIGMTKVKVGKEDSS
CCCCEEEEECCCCCC		46.99-
225UbiquitinationGMTKVKVGKEDSSSA
CCEEEEECCCCCCHH		23.1723000965
226UbiquitinationMTKVKVGKEDSSSAE
CEEEEECCCCCCHHH		62.4333845483
229PhosphorylationVKVGKEDSSSAEFLE
EEECCCCCCHHHHHH		27.5526657352
229 (in isoform 3)Phosphorylation-27.5527251275
230PhosphorylationKVGKEDSSSAEFLEK
EECCCCCCHHHHHHH		45.9830108239
231PhosphorylationVGKEDSSSAEFLEKR
ECCCCCCHHHHHHHH		35.4530108239
232UbiquitinationGKEDSSSAEFLEKRR
CCCCCCHHHHHHHHH		17.3229967540
237AcetylationSSAEFLEKRRAALER
CHHHHHHHHHHHHHH		49.7019608861
237UbiquitinationSSAEFLEKRRAALER
CHHHHHHHHHHHHHH		49.7019608861
254PhosphorylationQRIVNHPTMLQDPDV
HHHHCCCHHHCCCCH		23.9828857561
260UbiquitinationPTMLQDPDVREFLEK
CHHHCCCCHHHHHCC		61.4729967540
262MethylationMLQDPDVREFLEKEE
HHCCCCHHHHHCCCC		36.01115917417
267UbiquitinationDVREFLEKEELPRAV
CHHHHHCCCCCCCCC		59.6522817900
267 (in isoform 1)Ubiquitination-59.6521890473
267UbiquitinationDVREFLEKEELPRAV
CHHHHHCCCCCCCCC		59.6521890473
276PhosphorylationELPRAVGTQTLSGAG
CCCCCCCCCCCCHHH		16.2829978859
278PhosphorylationPRAVGTQTLSGAGLL
CCCCCCCCCCHHHHH		23.8025159151
278 (in isoform 3)Phosphorylation-23.8027251275
280PhosphorylationAVGTQTLSGAGLLKM
CCCCCCCCHHHHHHH		29.9515498486
280 (in isoform 3)Phosphorylation-29.9527251275
286UbiquitinationLSGAGLLKMFNKATD
CCHHHHHHHHHHHCH		46.6323000965
286 (in isoform 1)Ubiquitination-46.6321890473
286UbiquitinationLSGAGLLKMFNKATD
CCHHHHHHHHHHHCH		46.6321890473
290UbiquitinationGLLKMFNKATDAVSK
HHHHHHHHHCHHHHH		41.2023000965
297UbiquitinationKATDAVSKMTIKMNE
HHCHHHHHHEEECCH		33.2029967540
299PhosphorylationTDAVSKMTIKMNESD
CHHHHHHEEECCHHH		22.6028857561
302SulfoxidationVSKMTIKMNESDIWF
HHHHEEECCHHHCCH		6.2630846556
325UbiquitinationCEEQRLRKLHAVVET
CHHHHHHHHHHHHHH		49.5729967540
349UbiquitinationLNTAQFAKSLAMLGS
HHHHHHHHHHHHHCC		47.49-
353SulfoxidationQFAKSLAMLGSSEDN
HHHHHHHHHCCCHHH		5.4421406390
368PhosphorylationTALSRALSQLAEVEE
HHHHHHHHHHHHHHH		23.3528355574
368 (in isoform 3)Phosphorylation-23.3527251275
377UbiquitinationLAEVEEKIEQLHQEQ
HHHHHHHHHHHHHHH		4.6329967540
380UbiquitinationVEEKIEQLHQEQANN
HHHHHHHHHHHHHCC		2.6729967540
385UbiquitinationEQLHQEQANNDFFLL
HHHHHHHHCCCHHHH		18.9533845483
425UbiquitinationQRWQDAQATLQKKRE
HHHHHHHHHHHHHHH		16.4029967540
4292-HydroxyisobutyrylationDAQATLQKKREAEAR
HHHHHHHHHHHHHHH		57.84-
442MalonylationARLLWANKPDKLQQA
HHHHHHCCCHHHHHH		47.0126320211
442UbiquitinationARLLWANKPDKLQQA
HHHHHHCCCHHHHHH		47.0129967540
445MalonylationLWANKPDKLQQAKDE
HHHCCCHHHHHHHHH		57.6426320211
445UbiquitinationLWANKPDKLQQAKDE
HHHCCCHHHHHHHHH		57.6429967540
450UbiquitinationPDKLQQAKDEILEWE
CHHHHHHHHHHHHHH		52.1033845483
454UbiquitinationQQAKDEILEWESRVT
HHHHHHHHHHHHHHH		6.1929967540
472PhosphorylationRDFERISTVVRKEVI
HHHHHHHHHHHHHHH		22.2024719451
4902-HydroxyisobutyrylationKEKSKDFKNHVIKYL
HHCCHHHHHHHHHHH		57.17-
490UbiquitinationKEKSKDFKNHVIKYL
HHCCHHHHHHHHHHH		57.1729967540
502PhosphorylationKYLETLLYSQQQLAK
HHHHHHHHCHHHHHH		13.93-
519UbiquitinationEAFLPEAKAIS----
HHHHHHHHHCC----		44.5929967540
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 SNX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX1_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 SNX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAR1_HUMANF2Rphysical
12058063
SNX1_HUMANSNX1physical
11309204
AVR2B_HUMANACVR2Bphysical
11279102
ACV1B_HUMANACVR1Bphysical
11279102
PGFRB_HUMANPDGFRBphysical
9819414
SNX2_HUMANSNX2physical
9819414
EGFR_HUMANEGFRphysical
9819414
INSR_HUMANINSRphysical
9819414
LEPR_HUMANLEPRphysical
9819414
HGS_HUMANHGSphysical
19874558
DJC13_HUMANDNAJC13physical
19874558
A4_HUMANAPPphysical
21832049
SNX6_HUMANSNX6physical
22939629
SNX6_HUMANSNX6physical
21988832
ERF3B_HUMANGSPT2physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
NASP_HUMANNASPphysical
22863883
GLYM_HUMANSHMT2physical
22863883
STAT1_HUMANSTAT1physical
22863883
RTN3_HUMANRTN3physical
25416956
PRAF1_HUMANRABAC1physical
25416956
AR6P1_HUMANARL6IP1physical
25416956
ATRAP_HUMANAGTRAPphysical
25416956
RTN4_HUMANRTN4physical
25416956
REEP6_HUMANREEP6physical
25416956
CKLF5_HUMANCMTM5physical
25416956
FUND1_HUMANFUNDC1physical
25416956
SNX32_HUMANSNX32physical
25416956
ERF3A_HUMANGSPT1physical
26344197
LSM2_HUMANLSM2physical
26344197
RTN4_HUMANRTN4physical
26344197
RUVB2_HUMANRUVBL2physical
26344197
SMYD2_HUMANSMYD2physical
26344197
SNX5_HUMANSNX5physical
26344197
SNX6_HUMANSNX6physical
26344197
VP26A_HUMANVPS26Aphysical
26344197
VP26B_HUMANVPS26Bphysical
26344197
VPS29_HUMANVPS29physical
26344197
VPS35_HUMANVPS35physical
26344197
REEP6_HUMANREEP6physical
21516116
SNX5_HUMANSNX5physical
28514442
SNX6_HUMANSNX6physical
28514442
BIN3_HUMANBIN3physical
28514442
SNX2_HUMANSNX2physical
28514442
TM87A_HUMANTMEM87Aphysical
28514442
S35F2_HUMANSLC35F2physical
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 SNX1_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-237, AND MASS SPECTROMETRY.
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-188, AND MASSSPECTROMETRY.
"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-32; SER-39; THR-41 ANDSER-188, AND MASS SPECTROMETRY.

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