TBC13_HUMAN - dbPTM
TBC13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC13_HUMAN
UniProt AC Q9NVG8
Protein Name TBC1 domain family member 13
Gene Name TBC1D13
Organism Homo sapiens (Human).
Sequence Length 400
Subcellular Localization Membrane . Cytoplasm .
Protein Description Acts as a GTPase-activating protein for RAB35. Together with RAB35 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes..
Protein Sequence MSSLHKSRIADFQDVLKEPSIALEKLRELSFSGIPCEGGLRCLCWKILLNYLPLERASWTSILAKQRELYAQFLREMIIQPGIAKANMGVSREDVTFEDHPLNPNPDSRWNTYFKDNEVLLQIDKDVRRLCPDISFFQRATDYPCLLILDPQNEFETLRKRVEQTTLKSQTVARNRSGVTNMSSPHKNSVPSSLNEYEVLPNGCEAHWEVVERILFIYAKLNPGIAYVQGMNEIVGPLYYTFATDPNSEWKEHAEADTFFCFTNLMAEIRDNFIKSLDDSQCGITYKMEKVYSTLKDKDVELYLKLQEQNIKPQFFAFRWLTLLLSQEFLLPDVIRIWDSLFADDNRFDFLLLVCCAMLMLIREQLLEGDFTVNMRLLQDYPITDVCQILQKAKELQDSK
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
6Acetylation--MSSLHKSRIADFQ
--CCCCCHHHCCHHH
46.8825953088
17UbiquitinationADFQDVLKEPSIALE
CHHHHHHHCHHHHHH
68.38-
25UbiquitinationEPSIALEKLRELSFS
CHHHHHHHHHHHCCC
54.41-
58PhosphorylationYLPLERASWTSILAK
CCCCCHHCHHHHHHH
36.79-
91PhosphorylationAKANMGVSREDVTFE
HHCCCCCCHHHCCCC
24.9928348404
96PhosphorylationGVSREDVTFEDHPLN
CCCHHHCCCCCCCCC
33.3617924679
106UbiquitinationDHPLNPNPDSRWNTY
CCCCCCCCCCCCCCC
42.06-
108PhosphorylationPLNPNPDSRWNTYFK
CCCCCCCCCCCCCCC
40.2217924679
112PhosphorylationNPDSRWNTYFKDNEV
CCCCCCCCCCCCCEE
24.31-
113PhosphorylationPDSRWNTYFKDNEVL
CCCCCCCCCCCCEEE
12.86-
115UbiquitinationSRWNTYFKDNEVLLQ
CCCCCCCCCCEEEEE
49.59-
125UbiquitinationEVLLQIDKDVRRLCP
EEEEEECHHHHHHCC
60.80-
131GlutathionylationDKDVRRLCPDISFFQ
CHHHHHHCCCCCHHH
2.4222555962
135PhosphorylationRRLCPDISFFQRATD
HHHCCCCCHHHHHCC
27.6525159151
143PhosphorylationFFQRATDYPCLLILD
HHHHHCCCCEEEEEC
7.47-
145GlutathionylationQRATDYPCLLILDPQ
HHHCCCCEEEEECCC
3.8322555962
165PhosphorylationLRKRVEQTTLKSQTV
HHHHHHHHHHHCHHH
22.1630622161
166PhosphorylationRKRVEQTTLKSQTVA
HHHHHHHHHHCHHHH
31.7030622161
168UbiquitinationRVEQTTLKSQTVARN
HHHHHHHHCHHHHCC
38.12-
177PhosphorylationQTVARNRSGVTNMSS
HHHHCCCCCCCCCCC
40.9623401153
180PhosphorylationARNRSGVTNMSSPHK
HCCCCCCCCCCCCCC
28.8228176443
183PhosphorylationRSGVTNMSSPHKNSV
CCCCCCCCCCCCCCC
42.6723401153
184PhosphorylationSGVTNMSSPHKNSVP
CCCCCCCCCCCCCCC
21.9123401153
189PhosphorylationMSSPHKNSVPSSLNE
CCCCCCCCCCCCCCE
39.9628857561
192PhosphorylationPHKNSVPSSLNEYEV
CCCCCCCCCCCEEEE
45.3528796482
193PhosphorylationHKNSVPSSLNEYEVL
CCCCCCCCCCEEEEC
29.1928796482
197PhosphorylationVPSSLNEYEVLPNGC
CCCCCCEEEECCCCH
15.4028796482
213UbiquitinationAHWEVVERILFIYAK
HHHHHHHHHHHHHHH
21.21-
287UbiquitinationSQCGITYKMEKVYST
CCCCCEEEEEHHHHH
31.75-
290AcetylationGITYKMEKVYSTLKD
CCEEEEEHHHHHHCC
42.8725953088
298UbiquitinationVYSTLKDKDVELYLK
HHHHHCCCCHHHHHH
63.18-
387GlutathionylationDYPITDVCQILQKAK
CCCHHHHHHHHHHHH
2.0122555962
394UbiquitinationCQILQKAKELQDSK-
HHHHHHHHHHHCCC-
67.02-

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 TBC13_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC13_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 TBC13_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WDR12_HUMANWDR12physical
22939629

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 TBC13_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 AND SER-108, AND MASSSPECTROMETRY.

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