CC50A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CC50A_RAT
• UniProt AC: Q6AY41
• Protein Name: Cell cycle control protein 50A
• Gene Name: Tmem30a
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 328
• Subcellular Localization: Membrane; Multi-pass membrane protein. Cell membrane. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle membrane. Apical cell membrane.
• Protein Description: Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF). Can also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from ER to other membrane localizations (By similarity)..
• Protein Sequence: MAMNYSAKDEVDGGPTGPPGGAAKTRRPDNTAFKQQRLPAWQPILTAGTVLPTFFIIGLIFIPIGIGIFVTSNNIREIEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDPSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLVANESDPKPVPILLKKKGIAWWTDKNVKFRNPPGKDSLQEKFKDTTKPVNWHKPVYELDPDDESNNGFINEDFIVWMRTAALPTFRKLYRLIERTDDLHPTLPAGQYYLNITYNYPVHFFDGRKRMILSTISWMGGKNPFLGIAYITIGSISFLLGVVLLVINHKYRNSSNTADITI

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
2	Acetylation	------MAMNYSAKD ------CCCCCCCCC	8.57	-
5	Phosphorylation	---MAMNYSAKDEVD ---CCCCCCCCCCCC	9.27	23984901
6	Phosphorylation	--MAMNYSAKDEVDG --CCCCCCCCCCCCC	24.68	23984901
16	Phosphorylation	DEVDGGPTGPPGGAA CCCCCCCCCCCCCCC	66.64	25575281
24	Ubiquitination	GPPGGAAKTRRPDNT CCCCCCCCCCCCCCC	41.87	-
144	N-linked_Glycosylation	AIANSMFNDTLELFL HHHHHHHCCCEEEEE	32.49	-
261	N-linked_Glycosylation	PAGQYYLNITYNYPV CCCCEEEEEEEECEE	14.40	24090084

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

Oops, there are no upstream regulatory protein records of CC50A_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CC50A_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CC50A_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of CC50A_RAT !!

Drug and Disease Associations

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