TULP3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TULP3_MOUSE
• UniProt AC: O88413
• Protein Name: Tubby-related protein 3
• Gene Name: Tulp3
• Organism: Mus musculus (Mouse).
• Sequence Length: 460
• Subcellular Localization: Nucleus. Cell membrane. Cell projection, cilium. Cytoplasm. Secreted. Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha (By similarity). Does not have a cleavable signal pept
• Protein Description: Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. Not involved in ciliogenesis..
• Protein Sequence: MEAARCAPGPRGDSAFDDETLRLRQLKLDNQRALLEKKQRKKRLEPLMVQPNPEARLRRLKPRGSEEHTPLVDPQMPRSDVILHGIDGPAAFLKPEAQDLESKPQVLSVGSPAPEEGTEGSADGESPEETAPKPDLQEILQKHGILSSVNYDEEPDKEEDEGGNLSSPSARSEESAAASQKAASETGASGVTAQQGDAQLGEVENLEDFAYSPAPRGVTVKCKVTRDKKGMDRGLFPTYYMHLEREENRKIFLLAGRKRKKSKTSNYLVSTDPTDLSREGESYIGKLRSNLMGTKFTVYDHGVNPVKAQGLVEKAHTRQELAAICYETNVLGFKGPRKMSVIIPGMNMNHERIPFRPRNEHESLLSKWQNKSMENLIELHNKAPVWNDDTQSYVLNFHGRVTQASVKNFQIVHGNDPDYIVMQFGRVADDVFTLDYNYPLCALQAFAIGLSSFDSKLACE

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
65	Phosphorylation	RRLKPRGSEEHTPLV HHCCCCCCCCCCCCC	40.88	28507225
69	Phosphorylation	PRGSEEHTPLVDPQM CCCCCCCCCCCCCCC	22.92	26824392
126	Phosphorylation	EGSADGESPEETAPK CCCCCCCCCCCCCCC	43.04	25195567
148	Phosphorylation	QKHGILSSVNYDEEP HHCCCHHCCCCCCCC	15.78	25338131
166	Phosphorylation	EDEGGNLSSPSARSE CCCCCCCCCCCHHCH	44.17	30387612
167	Phosphorylation	DEGGNLSSPSARSEE CCCCCCCCCCHHCHH	26.49	29514104
169	Phosphorylation	GGNLSSPSARSEESA CCCCCCCCHHCHHHH	37.96	30635358
172	Phosphorylation	LSSPSARSEESAAAS CCCCCHHCHHHHHHH	45.49	25338131
184	Phosphorylation	AASQKAASETGASGV HHHHHHHHHHCCCCC	40.32	25338131
186	Phosphorylation	SQKAASETGASGVTA HHHHHHHHCCCCCEE	35.24	25338131
238	Phosphorylation	MDRGLFPTYYMHLER CCCCCCCHHHEEEEH	21.68	-
239	Phosphorylation	DRGLFPTYYMHLERE CCCCCCHHHEEEEHH	10.07	-
240	Phosphorylation	RGLFPTYYMHLEREE CCCCCHHHEEEEHHH	4.78	-
307	Acetylation	DHGVNPVKAQGLVEK ECCCCHHHHCCHHHH	35.93	19849145
372	Phosphorylation	LSKWQNKSMENLIEL HHHHHCHHHHHHHHH	38.59	25521595
393	Phosphorylation	WNDDTQSYVLNFHGR CCCCCCCEEEEECCC	10.11	29514104

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TULP3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TULP3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TULP3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GLI2_MOUSE	Gli2	physical	19286674

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.
PubMed: 19367708