dbPTM

ATX3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATX3_MOUSE
UniProt AC	Q9CVD2
Protein Name	Ataxin-3
Gene Name	Atxn3
Organism	Mus musculus (Mouse).
Sequence Length	355
Subcellular Localization	Nucleus .
Protein Description	Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (By similarity). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (By similarity). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. [PubMed: 21855799 Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (By similarity Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1]
Protein Sequence	MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERLRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIKVQQMHRPKLIGEELAHLKEQSALKADLERVLEAADGSGIFDEDEDDLQRALAISRQEIDMEDEEADLRRAIQLSMQGSSRSMCENSPQTSSPDLSSEELRRRREAYFEKQQQQQQEVDRPGPLSYPRERPTTSSGGRRSDQGGDAVSEEDMLRAAVTMSLETAKDNLKAERKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	LLQGEYFSPVELSSI HHCCCCCCHHHHHHH	27.43	20347968
54	Phosphorylation	RMAEGGVTSEDYRTF HHHCCCCCHHHHHHH	29.67	30635358
55	Phosphorylation	MAEGGVTSEDYRTFL HHCCCCCHHHHHHHH	26.51	30635358
117	Ubiquitination	RSFICNYKEHWFTVR CCCCCCCHHHEEEHH	29.16	-
200	Ubiquitination	GEELAHLKEQSALKA HHHHHHHHHHHHHHH	43.79	-
203	Phosphorylation	LAHLKEQSALKADLE HHHHHHHHHHHHHHH	36.34	25338131
206	Ubiquitination	LKEQSALKADLERVL HHHHHHHHHHHHHHH	39.30	-
219	Phosphorylation	VLEAADGSGIFDEDE HHHHHCCCCCCCCCH	29.30	21082442
256	Phosphorylation	LRRAIQLSMQGSSRS HHHHHHHHHHCCCHH	7.84	29895711
263	Phosphorylation	SMQGSSRSMCENSPQ HHHCCCHHHHCCCCC	29.72	27087446
264	Oxidation	MQGSSRSMCENSPQT HHCCCHHHHCCCCCC	3.02	17242355
268	Phosphorylation	SRSMCENSPQTSSPD CHHHHCCCCCCCCCC	8.97	22942356
271	Phosphorylation	MCENSPQTSSPDLSS HHCCCCCCCCCCCCH	34.26	27742792
272	Phosphorylation	CENSPQTSSPDLSSE HCCCCCCCCCCCCHH	34.33	27742792
273	Phosphorylation	ENSPQTSSPDLSSEE CCCCCCCCCCCCHHH	26.31	27087446
277	Phosphorylation	QTSSPDLSSEELRRR CCCCCCCCHHHHHHH	42.98	25619855
278	Phosphorylation	TSSPDLSSEELRRRR CCCCCCCHHHHHHHH	42.24	25619855
291	Ubiquitination	RREAYFEKQQQQQQE HHHHHHHHHHHHHHC	43.43	-
313	Phosphorylation	SYPRERPTTSSGGRR CCCCCCCCCCCCCCC	45.60	25338131
321	Phosphorylation	TSSGGRRSDQGGDAV CCCCCCCCCCCCCCC	32.69	21082442
333	Oxidation	DAVSEEDMLRAAVTM CCCCHHHHHHHHHHH	2.86	17242355
346	Ubiquitination	TMSLETAKDNLKAER HHCHHHHHHHHHHHH	55.35	-

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
29	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
29	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
29	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
29	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
268	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
268	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
271	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
272	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
272	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
273	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
273	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
277	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
277	S	Phosphorylation	Kinase	GSK-FAMILY	-	GPS
329	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
341	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ATX3_MOUSE !!

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 ATX3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ITA5_MOUSE	Itga5	physical	20668528
CHIP_MOUSE	Stub1	physical	15664989
TBB2B_RAT	Tubb2b	physical	19666135
TBA1A_RAT	Tuba1a	physical	19666135
MTAP2_RAT	Map2	physical	19666135
TBB4B_RAT	Tubb4b	physical	19666135
CNTFR_RAT	Cntfr	physical	19666135
TERA_RAT	Vcp	physical	19666135
ACTC_RAT	Actc1	physical	19666135
DNJA1_MOUSE	Dnaja1	physical	15639784
HSP7C_MOUSE	Hspa8	physical	15639784
HS71B_MOUSE	Hspa1b	physical	15639784
ATX3_MOUSE	Atxn3	physical	16939621
UBC_MOUSE	Ubc	physical	16432517
NDUA8_MOUSE	Ndufa8	physical	29111377

Drug and Disease Associations

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

Regulatory Network of ATX3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-273, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASSSPECTROMETRY.	15345747 [Abstract]