TBC19_HUMAN - dbPTM
TBC19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TBC19_HUMAN
UniProt AC Q8N5T2
Protein Name TBC1 domain family member 19
Gene Name TBC1D19
Organism Homo sapiens (Human).
Sequence Length 526
Subcellular Localization
Protein Description May act as a GTPase-activating protein for Rab family protein(s)..
Protein Sequence MLQEESDLSLIIAQIVQKLKGSNLYSQLERQAWASLQRPEIKLESLKEDIKEFFKISGWEKKLQNAVYSELSVFPLPSHPAAPPEHLKEPLVYMRKAQGSWEKRILKSLNSMCTELSIPLARKRPVGEQKELLNKWNEMGTDEPDLSLFRPVYAPKDFLEVLINLRNPNYENGDSLSFRTHLGLIQVPLKVKDIPELKECFVELGLNIGQLGIDDSTQVPPELFENEHVRIGQKVLAEQDSAAAQQYIRQGSPTALRAELWALILNISSQPEDVLYYEQLKTNVIQHDLLVDSLIYKDVKLTASNDDYYFVFEDYLYQVLLCFSRDTSVLSHFAFNSASPPKSYIRGKLGLEEYAVFYPPNGVIPFHGFSMYVAPLCFLYHEPSKLYQIFREMYVRFFFRLHSISSHPSGIVSLCLLFETLLQTYLPQLFYHLREIGAQPLRISFKWMVRAFSGYLATDQLLLLWDRILGYNSLEILAVLAAAVFAFRAVNLMEVTSLAAAEAVLADLSTLKVMPLLQIFLFATVT
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
18AcetylationIIAQIVQKLKGSNLY
HHHHHHHHHCCCCHH
41.0711794941
20AcetylationAQIVQKLKGSNLYSQ
HHHHHHHCCCCHHHH
68.2911794951
25PhosphorylationKLKGSNLYSQLERQA
HHCCCCHHHHHHHHH
9.9122817900
45PhosphorylationRPEIKLESLKEDIKE
CCCCCHHHHHHHHHH
56.0022496350
47UbiquitinationEIKLESLKEDIKEFF
CCCHHHHHHHHHHHH
63.7229967540
65UbiquitinationGWEKKLQNAVYSELS
CHHHHHHHHHHCCCC
41.6422817900
68PhosphorylationKKLQNAVYSELSVFP
HHHHHHHHCCCCCCC
8.26-
70UbiquitinationLQNAVYSELSVFPLP
HHHHHHCCCCCCCCC
27.63-
70UbiquitinationLQNAVYSELSVFPLP
HHHHHHCCCCCCCCC
27.6322817900
93PhosphorylationHLKEPLVYMRKAQGS
HHCCCHHHHHHCCCH
10.0129449344
130UbiquitinationKRPVGEQKELLNKWN
CCCCHHHHHHHHHHH
46.1322817900
135UbiquitinationEQKELLNKWNEMGTD
HHHHHHHHHHHCCCC
51.9022817900
147PhosphorylationGTDEPDLSLFRPVYA
CCCCCCHHHCCCCCC
32.6124719451
169UbiquitinationLINLRNPNYENGDSL
HHHCCCCCCCCCCCC
61.37-
169UbiquitinationLINLRNPNYENGDSL
HHHCCCCCCCCCCCC
61.3722817900
177PhosphorylationYENGDSLSFRTHLGL
CCCCCCCCEEEEEEE
19.3424719451
234UbiquitinationEHVRIGQKVLAEQDS
CCCCCCCHHHHHCCH
33.7222817900
324PhosphorylationYQVLLCFSRDTSVLS
HHHHHHHCCCCHHHH
28.4024719451
327PhosphorylationLLCFSRDTSVLSHFA
HHHHCCCCHHHHHHH
21.45-
328PhosphorylationLCFSRDTSVLSHFAF
HHHCCCCHHHHHHHC
25.91-
337PhosphorylationLSHFAFNSASPPKSY
HHHHHCCCCCCCHHH
24.5424706070
339PhosphorylationHFAFNSASPPKSYIR
HHHCCCCCCCHHHHC
41.3729900121
354PhosphorylationGKLGLEEYAVFYPPN
CCCCCEEEEEEECCC
9.93-
358PhosphorylationLEEYAVFYPPNGVIP
CEEEEEEECCCCCCC
15.92-
387PhosphorylationYHEPSKLYQIFREMY
HCCHHHHHHHHHHHH
11.87-
444PhosphorylationGAQPLRISFKWMVRA
CCCCCEEEHHHHHHH
17.8424719451
509PhosphorylationEAVLADLSTLKVMPL
HHHHHCHHHCCHHHH
32.04-
510PhosphorylationAVLADLSTLKVMPLL
HHHHCHHHCCHHHHH
37.58-

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 TBC19_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TBC19_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 TBC19_HUMAN !!

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

Oops, there are no PPI records of TBC19_HUMAN !!

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 TBC19_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25, AND MASSSPECTROMETRY.

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