TBC17_HUMAN - dbPTM
TBC17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC17_HUMAN
UniProt AC Q9HA65
Protein Name TBC1 domain family member 17
Gene Name TBC1D17
Organism Homo sapiens (Human).
Sequence Length 648
Subcellular Localization Cytoplasmic vesicle, autophagosome .
Protein Description Probable GTPase-activating protein for Rab8; its transient association with Rab8 is mediated by OPTN. Inhibits Rab8-mediated endocytic trafficking, such as of transferrin receptor (TfR) and reduces Rab8 recruitnment to tubules emanating from the endocytic recycling compartment (ERC). Involved in regulation of autophagy. Mediates inhibition of autophagy caused by the OPTN variant GLC1E LYS-50; the function requires its catalytic activity, however, the involved Rab is not known..
Protein Sequence MEGAGYRVVFEKGGVYLHTSAKKYQDRDSLIAGVIRVVEKDNDVLLHWAPVEEAGDSTQILFSKKDSSGGDSCASEEEPTFDPDYEPDWAVISTVRPQLCHSEPTRGAEPSCPQGSWAFSVSLGELKSIRRSKPGLSWAYLVLVTQAGGSLPALHFHRGGTRALLRVLSRYLLLASSPQDSRLYLVFPHDSSALSNSFHHLQLFDQDSSNVVSRFLQDPYSTTFSSFSRVTNFFRGALQPQPEGAASDLPPPPDDEPEPGFEVISCVELGPRPTVERGPPVTEEEWARHVGPEGRLQQVPELKNRIFSGGLSPSLRREAWKFLLGYLSWEGTAEEHKAHIRKKTDEYFRMKLQWKSVSPEQERRNSLLHGYRSLIERDVSRTDRTNKFYEGPENPGLGLLNDILLTYCMYHFDLGYVQGMSDLLSPILYVIQNEVDAFWCFCGFMELVQGNFEESQETMKRQLGRLLLLLRVLDPLLCDFLDSQDSGSLCFCFRWLLIWFKREFPFPDVLRLWEVLWTGLPGPNLHLLVACAILDMERDTLMLSGFGSNEILKHINELTMKLSVEDVLTRAEALHRQLTACPELPHNVQEILGLAPPAEPHSPSPTASPLPLSPTRAPPTPPPSTDTAPQPDSSLEILPEEEDEGADS
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
16PhosphorylationVFEKGGVYLHTSAKK
EEEECCEEEECCCCH
8.9523312004
19PhosphorylationKGGVYLHTSAKKYQD
ECCEEEECCCCHHCC
27.9920068231
20PhosphorylationGGVYLHTSAKKYQDR
CCEEEECCCCHHCCH
27.6125159151
22UbiquitinationVYLHTSAKKYQDRDS
EEEECCCCHHCCHHH
52.3522817900
23UbiquitinationYLHTSAKKYQDRDSL
EEECCCCHHCCHHHH
48.1121890473
23UbiquitinationYLHTSAKKYQDRDSL
EEECCCCHHCCHHHH
48.1121890473
23UbiquitinationYLHTSAKKYQDRDSL
EEECCCCHHCCHHHH
48.1122817900
24PhosphorylationLHTSAKKYQDRDSLI
EECCCCHHCCHHHHH
18.2324275569
29PhosphorylationKKYQDRDSLIAGVIR
CHHCCHHHHHHEEEE
23.6729214152
31UbiquitinationYQDRDSLIAGVIRVV
HCCHHHHHHEEEEEE
3.4832015554
63PhosphorylationDSTQILFSKKDSSGG
CCCEEEEECCCCCCC
35.0424719451
64UbiquitinationSTQILFSKKDSSGGD
CCEEEEECCCCCCCC
53.9532015554
65UbiquitinationTQILFSKKDSSGGDS
CEEEEECCCCCCCCC
62.74-
191PhosphorylationYLVFPHDSSALSNSF
EEEEECCHHHHHCCC
17.9328857561
192PhosphorylationLVFPHDSSALSNSFH
EEEECCHHHHHCCCE
39.0128857561
197PhosphorylationDSSALSNSFHHLQLF
CHHHHHCCCEEEEEE
23.6828857561
221PhosphorylationRFLQDPYSTTFSSFS
HHHCCCCCCCCHHHH
26.7628348404
222PhosphorylationFLQDPYSTTFSSFSR
HHCCCCCCCCHHHHH
26.4728857561
223PhosphorylationLQDPYSTTFSSFSRV
HCCCCCCCCHHHHHH
18.6428857561
225PhosphorylationDPYSTTFSSFSRVTN
CCCCCCCHHHHHHHH
28.5124719451
226PhosphorylationPYSTTFSSFSRVTNF
CCCCCCHHHHHHHHH
24.0528857561
228PhosphorylationSTTFSSFSRVTNFFR
CCCCHHHHHHHHHHC
27.9928857561
270UbiquitinationVISCVELGPRPTVER
EEEEEEECCCCCCCC
11.5833845483
303UbiquitinationLQQVPELKNRIFSGG
HHCCHHHHHHHHCCC
42.3833845483
308PhosphorylationELKNRIFSGGLSPSL
HHHHHHHCCCCCHHH
29.58-
310UbiquitinationKNRIFSGGLSPSLRR
HHHHHCCCCCHHHHH
23.0629967540
314PhosphorylationFSGGLSPSLRREAWK
HCCCCCHHHHHHHHH
31.00-
343UbiquitinationHKAHIRKKTDEYFRM
HHHHHHHHCHHHHHH
51.8929967540
347PhosphorylationIRKKTDEYFRMKLQW
HHHHCHHHHHHHHEE
10.1722817900
351UbiquitinationTDEYFRMKLQWKSVS
CHHHHHHHHEEECCC
33.02-
366PhosphorylationPEQERRNSLLHGYRS
HHHHHHHHHHHHHHH
30.4229214152
455PhosphorylationVQGNFEESQETMKRQ
HCCCHHHCHHHHHHH
26.56-
569PhosphorylationLSVEDVLTRAEALHR
CCHHHHHHHHHHHHH
27.9020068231
579PhosphorylationEALHRQLTACPELPH
HHHHHHHHCCCCCCC
20.2030278072
602PhosphorylationAPPAEPHSPSPTASP
CCCCCCCCCCCCCCC
37.4830278072
604PhosphorylationPAEPHSPSPTASPLP
CCCCCCCCCCCCCCC
37.5930278072
606PhosphorylationEPHSPSPTASPLPLS
CCCCCCCCCCCCCCC
44.0730278072
608PhosphorylationHSPSPTASPLPLSPT
CCCCCCCCCCCCCCC
29.4630278072
613PhosphorylationTASPLPLSPTRAPPT
CCCCCCCCCCCCCCC
23.4528348404
615PhosphorylationSPLPLSPTRAPPTPP
CCCCCCCCCCCCCCC
35.7722854040
620PhosphorylationSPTRAPPTPPPSTDT
CCCCCCCCCCCCCCC
47.5730576142
624PhosphorylationAPPTPPPSTDTAPQP
CCCCCCCCCCCCCCC
44.6930242111
625PhosphorylationPPTPPPSTDTAPQPD
CCCCCCCCCCCCCCC
43.0430242111
627PhosphorylationTPPPSTDTAPQPDSS
CCCCCCCCCCCCCCC
40.0830242111
633PhosphorylationDTAPQPDSSLEILPE
CCCCCCCCCCCCCCH
43.4328270605
634PhosphorylationTAPQPDSSLEILPEE
CCCCCCCCCCCCCHH
37.0824275569
648PhosphorylationEEDEGADS-------
HCCCCCCC-------
41.4022673903

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 TBC17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC17_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 TBC17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CACO1_HUMANCALCOCO1physical
16169070
TAXB1_HUMANTAX1BP1physical
16169070
TF3C1_HUMANGTF3C1physical
16169070
RAB5A_HUMANRAB5Aphysical
16923123
RAB5B_HUMANRAB5Bphysical
16923123
RAB5C_HUMANRAB5Cphysical
16923123
PARVA_HUMANPARVAphysical
22863883
RAB8A_HUMANRAB8Aphysical
22854040
UBXN8_HUMANUBXN8physical
26389662

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 TBC17_HUMAN

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Related Literatures of Post-Translational Modification

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