TPPC3_HUMAN - dbPTM
TPPC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPPC3_HUMAN
UniProt AC O43617
Protein Name Trafficking protein particle complex subunit 3
Gene Name TRAPPC3
Organism Homo sapiens (Human).
Sequence Length 180
Subcellular Localization Golgi apparatus, cis-Golgi network. Endoplasmic reticulum.
Protein Description May play a role in vesicular transport from endoplasmic reticulum to Golgi..
Protein Sequence MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDKMGFNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSSLIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
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
42UbiquitinationENDEDVNKQLDKMGF
CCCHHHHHHHHHHCC		52.6821906983
46UbiquitinationDVNKQLDKMGFNIGV
HHHHHHHHHCCHHHH		49.9021890473
68S-palmitoylationARSNVGRCHDFRETA
HHCCCCCCCCHHHHH		2.7215692564
156UbiquitinationKFVQDTLKGDGVTEI
HHHHHHHCCCCCCHH		57.982190698
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 TPPC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPPC3_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 TPPC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPC6A_HUMANTRAPPC6Aphysical
16189514
TPC2L_HUMANTRAPPC2Lphysical
16189514
TPC13_HUMANTRAPPC13physical
21453443
TPPC8_HUMANTRAPPC8physical
21453443
TPPC5_HUMANTRAPPC5physical
21525244
TPC6A_HUMANTRAPPC6Aphysical
21525244
TPC6B_HUMANTRAPPC6Bphysical
21525244
TPC2L_HUMANTRAPPC2Lphysical
21525244
TPC2A_HUMANTRAPPC2physical
21525244
TPC2B_HUMANTRAPPC2physical
21525244
TPPC1_HUMANTRAPPC1physical
21525244
A4_HUMANAPPphysical
21832049
TPC2L_HUMANTRAPPC2Lphysical
25416956
TPC6A_HUMANTRAPPC6Aphysical
25416956
PKHF2_HUMANPLEKHF2physical
25416956
TPC10_HUMANTRAPPC10physical
27173435
TPPC4_HUMANTRAPPC4physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
TPC2L_HUMANTRAPPC2Lphysical
27173435
TM102_HUMANTMEM102physical
27173435
M21D2_HUMANMB21D2physical
27173435
PDLI7_HUMANPDLIM7physical
27173435
R3GEF_HUMANRAB3IL1physical
27173435
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 TPPC3_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Structure of palmitoylated BET3: insights into TRAPP complex assemblyand membrane localization.";
Turnbull A.P., Kummel D., Prinz B., Holz C., Schultchen J., Lang C.,Niesen F.H., Hofmann K.P., Delbruck H., Behlke J., Muller E.C.,Jarosch E., Sommer T., Heinemann U.;
EMBO J. 24:875-884(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-180, SUBUNIT, MUTAGENESISOF CYS-68, AND PALMITOYLATION AT CYS-68.

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