SNX27_HUMAN - dbPTM
SNX27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX27_HUMAN
UniProt AC Q96L92
Protein Name Sorting nexin-27
Gene Name SNX27
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Early endosome membrane
Peripheral membrane protein. Cytoplasm, cytosol. Localizes to immunological synapse in T-cells. In T-cells, recruited from the cytosol to sorting endosomes by phosphoinositide-3-kinase products.
Protein Description Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being degraded in lysosomes. SNX27 specifically binds and directs sorting of a subset of transmembrane proteins containing a PDZ-binding motif at the C-terminus: following interaction with target transmembrane proteins, associates with the retromer complex, preventing entry into the lysosomal pathway, and promotes retromer-tubule based plasma membrane recycling. SNX27 also binds with the WASH complex. Interacts with membranes containing phosphatidylinositol-3-phosphate (PtdIns(3P)). May participate in establishment of natural killer cell polarity. Recruits CYTIP to early endosomes..
Protein Sequence MADEDGEGIHPSAPHRNGGGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNHVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPRYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFEVISHSFVRKLAPNEFPHKLYIQNYTSAVPGTCLTIRKWLFTTEEEILLNDNDLAVTYFFHQAVDDVKKGYIKAEEKSYQLQKLYEQRKMVMYLNMLRTCEGYNEIIFPHCACDSRRKGHVITAISITHFKLHACTEEGQLENQVIAFEWDEMQRWDTDEEGMAFCFEYARGEKKPRWVKIFTPYFNYMHECFERVFCELKWRKENIFQMARSQQRDVAT
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
6 (in isoform 2)Phosphorylation-32.7425690035
26PhosphorylationGGGGGGGSGLHCAGN
CCCCCCCCCCCCCCC		41.2628450419
26 (in isoform 3)Phosphorylation-41.2627251275
33 (in isoform 2)Ubiquitination-27.6621890473
48UbiquitinationPRVVRIVKSESGYGF
CCEEEEEECCCCCCE		46.24-
49PhosphorylationRVVRIVKSESGYGFN
CEEEEEECCCCCCEE		26.5423898821
49 (in isoform 3)Phosphorylation-26.5427251275
51PhosphorylationVRIVKSESGYGFNVR
EEEEECCCCCCEEEE		44.3919664994
51 (in isoform 3)Phosphorylation-44.3927251275
53PhosphorylationIVKSESGYGFNVRGQ
EEECCCCCCEEEEEE		28.0230108239
62PhosphorylationFNVRGQVSEGGQLRS
EEEEEEECCCCCEEE		23.7225159151
69PhosphorylationSEGGQLRSINGELYA
CCCCCEEEECCEEEC		29.0628857561
75PhosphorylationRSINGELYAPLQHVS
EEECCEEECCCEEEE		11.2321253578
82PhosphorylationYAPLQHVSAVLPGGA
ECCCEEEEEECCCCH		15.55-
115UbiquitinationNVEGATHKQVVDLIR
ECCCCCHHHHHHHHH		40.20-
126UbiquitinationDLIRAGEKELILTVL
HHHHCCCCEEEEEEE		57.8321906983
126 (in isoform 1)Ubiquitination-57.8321890473
126 (in isoform 3)Ubiquitination-57.8321890473
129 (in isoform 2)Ubiquitination-2.9621890473
146PhosphorylationEADNLDPSDDSLGQS
HCCCCCCCCCCCCHH		54.4327251275
149PhosphorylationNLDPSDDSLGQSFYD
CCCCCCCCCCHHCCC		39.1127251275
149 (in isoform 3)Phosphorylation-39.1127251275
153PhosphorylationSDDSLGQSFYDYTEK
CCCCCCHHCCCCCCC		24.7927642862
155PhosphorylationDSLGQSFYDYTEKQA
CCCCHHCCCCCCCCC		17.1827642862
160UbiquitinationSFYDYTEKQAVPISV
HCCCCCCCCCCCCCC		35.44-
166PhosphorylationEKQAVPISVPRYKHV
CCCCCCCCCCCCEEE		21.7224719451
186PhosphorylationKFVVYNVYMAGRQLC
EEEEEEEEECHHHHH		4.2425147952
215PhosphorylationKREFANFTFPRLPGK
HHHHHCCCCCCCCCC		32.3225850435
215 (in isoform 3)Phosphorylation-32.3227251275
218MethylationFANFTFPRLPGKWPF
HHCCCCCCCCCCCCC		49.69115917453
222UbiquitinationTFPRLPGKWPFSLSE
CCCCCCCCCCCCCCH		50.1621890473
222 (in isoform 3)Ubiquitination-50.1621890473
222 (in isoform 1)Ubiquitination-50.1621890473
226PhosphorylationLPGKWPFSLSEQQLD
CCCCCCCCCCHHHHH		27.2322199227
228PhosphorylationGKWPFSLSEQQLDAR
CCCCCCCCHHHHHHH		31.9630624053
245UbiquitinationGLEEYLEKVCSIRVI
CHHHHHHHHHCEEEE		46.04-
255PhosphorylationSIRVIGESDIMQEFL
CEEEEECHHHHHHHH		27.5026552605
263PhosphorylationDIMQEFLSESDENYN
HHHHHHHCCCCCCCC		40.1326552605
265PhosphorylationMQEFLSESDENYNGV
HHHHHCCCCCCCCCC		47.0126552605
269PhosphorylationLSESDENYNGVSDVE
HCCCCCCCCCCCCEE		15.9628796482
273PhosphorylationDENYNGVSDVELRVA
CCCCCCCCCEEEEEE		37.0226552605
285PhosphorylationRVALPDGTTVTVRVK
EEECCCCCEEEEEEE		26.0221406692
286PhosphorylationVALPDGTTVTVRVKK
EECCCCCEEEEEEEC		21.5121406692
288PhosphorylationLPDGTTVTVRVKKNS
CCCCCEEEEEEECCC		10.6621406692
295PhosphorylationTVRVKKNSTTDQVYQ
EEEEECCCCHHHHHH		41.38-
296PhosphorylationVRVKKNSTTDQVYQA
EEEECCCCHHHHHHH		43.73-
297PhosphorylationRVKKNSTTDQVYQAI
EEECCCCHHHHHHHH		25.02-
311 (in isoform 2)Ubiquitination-36.5821890473
340UbiquitinationAPNEFPHKLYIQNYT
CCCCCCCCEEEEECC		43.13-
342PhosphorylationNEFPHKLYIQNYTSA
CCCCCCEEEEECCCC		12.7921945579
346PhosphorylationHKLYIQNYTSAVPGT
CCEEEEECCCCCCCC		5.9121945579
347PhosphorylationKLYIQNYTSAVPGTC
CEEEEECCCCCCCCE		20.1221945579
348PhosphorylationLYIQNYTSAVPGTCL
EEEEECCCCCCCCEE		19.5321945579
392PhosphorylationVDDVKKGYIKAEEKS
HHHHHHCCEEHHHHH		14.2317322306
398UbiquitinationGYIKAEEKSYQLQKL
CCEEHHHHHHHHHHH		46.07-
400PhosphorylationIKAEEKSYQLQKLYE
EEHHHHHHHHHHHHH		25.06-
404 (in isoform 1)Ubiquitination-62.7221890473
404UbiquitinationEKSYQLQKLYEQRKM
HHHHHHHHHHHHHHH		62.7221890473
404 (in isoform 3)Ubiquitination-62.7221890473
435 (in isoform 2)Phosphorylation-27.01-
444PhosphorylationRRKGHVITAISITHF
CCCCEEEEEEEEEEE		19.4927134283
504PhosphorylationPRWVKIFTPYFNYMH
CCEEEEECCCCHHHH		22.1320068231
506PhosphorylationWVKIFTPYFNYMHEC
EEEEECCCCHHHHHH		11.0320068231
509PhosphorylationIFTPYFNYMHECFER
EECCCCHHHHHHHHH		7.0220068231
522UbiquitinationERVFCELKWRKENIF
HHHHHHHHHHHHHHH		23.74-
528 (in isoform 3)Phosphorylation-2.38-
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 SNX27_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX27_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 SNX27_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MRP4_HUMANABCC4physical
22411990
INSR_HUMANINSRphysical
23382219
NTRK1_HUMANNTRK1physical
23382219
APOA1_HUMANAPOA1physical
28514442
CERU_HUMANCPphysical
28514442
HPT_HUMANHPphysical
28514442
CO3_HUMANC3physical
28514442
BPIA1_HUMANBPIFA1physical
28514442
CO4A_HUMANC4Aphysical
28514442
TRFL_HUMANLTFphysical
28514442
PROL4_HUMANPRR4physical
28514442
A1AT_HUMANSERPINA1physical
28514442
PIGR_HUMANPIGRphysical
28514442
FIBB_HUMANFGBphysical
28514442
LACRT_HUMANLACRTphysical
28514442
A1AG1_HUMANORM1physical
28514442
FIBA_HUMANFGAphysical
28514442
FIBG_HUMANFGGphysical
28514442
FETUA_HUMANAHSGphysical
28514442
SG2A1_HUMANSCGB2A1physical
28514442
BPIB1_HUMANBPIFB1physical
28514442
TRFE_HUMANTFphysical
28514442
NGAL_HUMANLCN2physical
28514442
LEG1H_HUMANC6orf58physical
28514442
HEMO_HUMANHPXphysical
28514442
AACT_HUMANSERPINA3physical
28514442
CYTN_HUMANCST1physical
28514442
DMBT1_HUMANDMBT1physical
28514442
TTHY_HUMANTTRphysical
28514442
ZG16B_HUMANZG16Bphysical
28514442
IGJ_HUMANIGJphysical
28514442
KNG1_HUMANKNG1physical
28514442
SG1D1_HUMANSCGB1D1physical
28514442
IGLL5_HUMANIGLL5physical
28514442
ALBU_HUMANALBphysical
28514442
LYSC_HUMANLYZphysical
28514442
LCN1_HUMANLCN1physical
28514442
CYTS_HUMANCST4physical
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 SNX27_HUMAN

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Related Literatures of Post-Translational Modification

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