TUB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TUB_HUMAN
• UniProt AC: P50607
• Protein Name: Tubby protein homolog
• Gene Name: TUB
• Organism: Homo sapiens (Human).
• Sequence Length: 506
• Subcellular Localization: Cytoplasm. Nucleus. Secreted. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Binds phospholipid and is anchored to the plasma membrane through binding phosphatidylinositol 4,5-bisphosphate. Is released upon activation of phospholipase
• Protein Description: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages..
• Protein Sequence: MTSKPHSDWIPYSVLDDEGRNLRQQKLDRQRALLEQKQKKKRQEPLMVQANADGRPRSRRARQSEEQAPLVESYLSSSGSTSYQVQEADSLASVQLGATRPTAPASAKRTKAAATAGGQGGAARKEKKGKHKGTSGPAALAEDKSEAQGPVQILTVGQSDHAQDAGETAAGGGERPSGQDLRATMQRKGISSSMSFDEDEEDEEENSSSSSQLNSNTRPSSATSRKSVREAASAPSPTAPEQPVDVEVQDLEEFALRPAPQGITIKCRITRDKKGMDRGMYPTYFLHLDREDGKKVFLLAGRKRKKSKTSNYLISVDPTDLSRGGDSYIGKLRSNLMGTKFTVYDNGVNPQKASSSTLESGTLRQELAAVCYETNVLGFKGPRKMSVIVPGMNMVHERVSIRPRNEHETLLARWQNKNTESIIELQNKTPVWNDDTQSYVLNFHGRVTQASVKNFQIIHGNDPDYIVMQFGRVAEDVFTMDYNYPLCALQAFAIALSSFDSKLACE

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
58	Phosphorylation	NADGRPRSRRARQSE CCCCCCCCHHHHHCH	28.88	-
64	Phosphorylation	RSRRARQSEEQAPLV CCHHHHHCHHHHHHH	37.23	-
115	Phosphorylation	KRTKAAATAGGQGGA HHHHHHHHHCCCCCC	22.55	-
327	Phosphorylation	DLSRGGDSYIGKLRS HHCCCCCCHHHHHHH	23.17	29978859
328	Phosphorylation	LSRGGDSYIGKLRSN HCCCCCCHHHHHHHH	20.59	29978859
340	Ubiquitination	RSNLMGTKFTVYDNG HHHCCCCEEEEEECC	33.05	32015554
352	Ubiquitination	DNGVNPQKASSSTLE ECCCCHHHCCCCCCC	52.04	23000965
354	Phosphorylation	GVNPQKASSSTLESG CCCHHHCCCCCCCCC	31.68	-
364	Ubiquitination	TLESGTLRQELAAVC CCCCCCHHHHHHHHH	27.97	23000965
380	Ubiquitination	ETNVLGFKGPRKMSV HCCCCCCCCCCCCEE	67.23	23000965
384	Ubiquitination	LGFKGPRKMSVIVPG CCCCCCCCCEEEECC	38.36	23000965
386	Phosphorylation	FKGPRKMSVIVPGMN CCCCCCCEEEECCCC	16.24	26552605
392	Ubiquitination	MSVIVPGMNMVHERV CEEEECCCCEEEECE	2.09	23000965
394	Ubiquitination	VIVPGMNMVHERVSI EEECCCCEEEECEEC	2.12	23000965
395	Ubiquitination	IVPGMNMVHERVSIR EECCCCEEEECEECC	3.44	32015554
396	Ubiquitination	VPGMNMVHERVSIRP ECCCCEEEECEECCC	13.33	23000965
407 (in isoform 2)	Ubiquitination	-	36.57	-
407	Ubiquitination	SIRPRNEHETLLARW ECCCCCHHHHHHHHH	36.57	23000965
422	Ubiquitination	QNKNTESIIELQNKT HCCCHHHHEEECCCC	2.00	23000965
426	Ubiquitination	TESIIELQNKTPVWN HHHHEEECCCCCCCC	36.26	23000965
435	Ubiquitination	KTPVWNDDTQSYVLN CCCCCCCCCCEEEEE	43.35	23000965
439	Ubiquitination	WNDDTQSYVLNFHGR CCCCCCEEEEEECCC	10.11	23000965

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of TUB_HUMAN !!

Drug and Disease Associations

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