dbPTM

SIR2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIR2_MOUSE
UniProt AC	Q8VDQ8
Protein Name	NAD-dependent protein deacetylase sirtuin-2
Gene Name	Sirt2
Organism	Mus musculus (Mouse).
Sequence Length	389
Subcellular Localization	Nucleus . Cytoplasm . Cytoplasm, perinuclear region. Perikaryon. Cytoplasm, cytoskeleton. Cell projection. Cell projection, growth cone. Myelin membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
Protein Description	NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors. [PubMed: 17521387]
Protein Sequence	MAEPDPSDPLETQAGKVQEAQDSDSDTEGGATGGEAEMDFLRNLFTQTLGLGSQKERLLDELTLEGVTRYMQSERCRKVICLVGAGISTSAGIPDFRSPSTGLYANLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFIRLLKEKGLLLRCYTQNIDTLERVAGLEPQDLVEAHGTFYTSHCVNTSCRKEYTMGWMKEKIFSEATPRCEQCQSVVKPDIVFFGENLPSRFFSCMQSDFSKVDLLIIMGTSLQVQPFASLISKAPLATPRLLINKEKTGQTDPFLGMMMGLGGGMDFDSKKAYRDVAWLGDCDQGCLALADLLGWKKELEDLVRREHANIDAQSGSQAPNPSTTISPGKSPPPAKEAARTKEKEEQQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEPDPSDP ------CCCCCCCCC	36.71	-
7	Phosphorylation	-MAEPDPSDPLETQA -CCCCCCCCCCCCCC	60.28	25293948
12	Phosphorylation	DPSDPLETQAGKVQE CCCCCCCCCCCCCEE	31.25	25293948
18	Ubiquitination	ETQAGKVQEAQDSDS CCCCCCCEECCCCCC	43.74	27667366
23	Phosphorylation	KVQEAQDSDSDTEGG CCEECCCCCCCCCCC	27.25	25521595
25	Phosphorylation	QEAQDSDSDTEGGAT EECCCCCCCCCCCCC	50.84	25521595
27	Phosphorylation	AQDSDSDTEGGATGG CCCCCCCCCCCCCCH	40.25	25521595
32	Phosphorylation	SDTEGGATGGEAEMD CCCCCCCCCHHHHHH	49.33	25619855
38	Oxidation	ATGGEAEMDFLRNLF CCCHHHHHHHHHHHH	5.94	17242355
46	Phosphorylation	DFLRNLFTQTLGLGS HHHHHHHHHHHCCCC	24.66	20415495
48	Phosphorylation	LRNLFTQTLGLGSQK HHHHHHHHHCCCCHH	21.53	20415495
53	Phosphorylation	TQTLGLGSQKERLLD HHHHCCCCHHHHHHH	43.02	22817900
55	Ubiquitination	TLGLGSQKERLLDEL HHCCCCHHHHHHHHH	46.64	22790023
56	Ubiquitination	LGLGSQKERLLDELT HCCCCHHHHHHHHHC	40.71	-
74	Ubiquitination	VTRYMQSERCRKVIC HHHHHCCHHHCEEEE	38.62	-
75	Methylation	TRYMQSERCRKVICL HHHHCCHHHCEEEEE	30.68	18966039
75	Dimethylation	TRYMQSERCRKVICL HHHHCCHHHCEEEEE	30.68	-
77	Dimethylation	YMQSERCRKVICLVG HHCCHHHCEEEEECC	42.36	-
77	Methylation	YMQSERCRKVICLVG HHCCHHHCEEEEECC	42.36	18966049
89	Phosphorylation	LVGAGISTSAGIPDF ECCCCCCCCCCCCCC	22.22	29899451
90	Phosphorylation	VGAGISTSAGIPDFR CCCCCCCCCCCCCCC	20.08	29899451
96	Ubiquitination	TSAGIPDFRSPSTGL CCCCCCCCCCCCCCC	7.56	27667366
98	Phosphorylation	AGIPDFRSPSTGLYA CCCCCCCCCCCCCCC	24.16	29899451
100	Phosphorylation	IPDFRSPSTGLYANL CCCCCCCCCCCCCCH	36.03	25521595
101	Phosphorylation	PDFRSPSTGLYANLE CCCCCCCCCCCCCHH	34.29	20415495
104	Phosphorylation	RSPSTGLYANLEKYH CCCCCCCCCCHHHCC	8.52	20415495
126	Malonylation	FEISYFKKHPEPFFA HHCCHHHHCCCCCHH	55.27	30639696
126	Acetylation	FEISYFKKHPEPFFA HHCCHHHHCCCCCHH	55.27	19856745
126	Ubiquitination	FEISYFKKHPEPFFA HHCCHHHHCCCCCHH	55.27	22790023
132	Ubiquitination	KKHPEPFFALAKELY HHCCCCCHHHHHHHC	8.78	-
140	Ubiquitination	ALAKELYPGQFKPTI HHHHHHCCCCCCHHH	42.61	27667366
140	Ubiquitination	ALAKELYPGQFKPTI HHHHHHCCCCCCHHH	42.61	-
144	Ubiquitination	ELYPGQFKPTICHYF HHCCCCCCHHHHHHH	33.11	22790023
148	S-palmitoylation	GQFKPTICHYFIRLL CCCCHHHHHHHHHHH	2.04	28680068
166	Phosphorylation	GLLLRCYTQNIDTLE CCEEEEECCCHHHHH	20.83	25338131
173	Ubiquitination	TQNIDTLERVAGLEP CCCHHHHHHHCCCCH	47.40	27667366
181	Ubiquitination	RVAGLEPQDLVEAHG HHCCCCHHHHHHHCC	47.50	27667366
202	Ubiquitination	CVNTSCRKEYTMGWM CCCCCCCCEECHHHH	60.44	22790023
205	Phosphorylation	TSCRKEYTMGWMKEK CCCCCEECHHHHHHH	15.42	29899451
210	Ubiquitination	EYTMGWMKEKIFSEA EECHHHHHHHHHHCC	49.71	22790023
217	Ubiquitination	KEKIFSEATPRCEQC HHHHHHCCCCCHHHH	23.00	-
218	Phosphorylation	EKIFSEATPRCEQCQ HHHHHCCCCCHHHHC	13.76	22324799
249	Phosphorylation	RFFSCMQSDFSKVDL HHHHHHCCCCCCCCE	17.46	25521595
251	Ubiquitination	FSCMQSDFSKVDLLI HHHHCCCCCCCCEEE	10.36	27667366
269	Ubiquitination	TSLQVQPFASLISKA CCCCHHCCHHHHHCC	3.94	27667366
269	Ubiquitination	TSLQVQPFASLISKA CCCCHHCCHHHHHCC	3.94	-
283	Ubiquitination	APLATPRLLINKEKT CCCCCCEEEECHHHC	6.24	27667366
287	Ubiquitination	TPRLLINKEKTGQTD CCEEEECHHHCCCCC	54.30	22790023
301	Ubiquitination	DPFLGMMMGLGGGMD CHHHHHHHCCCCCCC	2.73	27667366
301	Ubiquitination	DPFLGMMMGLGGGMD CHHHHHHHCCCCCCC	2.73	-
302	Ubiquitination	PFLGMMMGLGGGMDF HHHHHHHCCCCCCCC	11.86	27667366
307	Ubiquitination	MMGLGGGMDFDSKKA HHCCCCCCCCCCHHH	5.40	27667366
312	Ubiquitination	GGMDFDSKKAYRDVA CCCCCCCHHHHCCCH	43.18	-
334	Ubiquitination	GCLALADLLGWKKEL HHHHHHHHHCHHHHH	3.86	27667366
338	Ubiquitination	LADLLGWKKELEDLV HHHHHCHHHHHHHHH	34.27	-
338	Acetylation	LADLLGWKKELEDLV HHHHHCHHHHHHHHH	34.27	156105
339	Ubiquitination	ADLLGWKKELEDLVR HHHHCHHHHHHHHHH	62.11	22790023
340	Ubiquitination	DLLGWKKELEDLVRR HHHCHHHHHHHHHHH	54.38	27667366
356	Phosphorylation	HANIDAQSGSQAPNP HCCCCCCCCCCCCCC	41.98	25619855
358	Phosphorylation	NIDAQSGSQAPNPST CCCCCCCCCCCCCCC	28.54	25619855
364	Phosphorylation	GSQAPNPSTTISPGK CCCCCCCCCCCCCCC	44.84	25521595
365	Phosphorylation	SQAPNPSTTISPGKS CCCCCCCCCCCCCCC	29.43	24925903
366	O-linked_Glycosylation	QAPNPSTTISPGKSP CCCCCCCCCCCCCCC	24.64	22517741
366	Ubiquitination	QAPNPSTTISPGKSP CCCCCCCCCCCCCCC	24.64	27667366
366	Phosphorylation	QAPNPSTTISPGKSP CCCCCCCCCCCCCCC	24.64	25521595
368	Phosphorylation	PNPSTTISPGKSPPP CCCCCCCCCCCCCCC	26.05	25521595
371	Ubiquitination	STTISPGKSPPPAKE CCCCCCCCCCCCHHH	64.27	22790023
372	Phosphorylation	TTISPGKSPPPAKEA CCCCCCCCCCCHHHH	48.86	25521595
377	Ubiquitination	GKSPPPAKEAARTKE CCCCCCHHHHHHHHH	54.37	27667366
398	Ubiquitination	---------------- ----------------		27667366
404	Ubiquitination	---------------------- ----------------------		27667366
412	Ubiquitination	------------------------------ ------------------------------		27667366
436	Ubiquitination	------------------------------------------------------ ------------------------------------------------------		27667366
444	Ubiquitination	-------------------------------------------------------------- --------------------------------------------------------------		27667366
450	Ubiquitination	-------------------------------------------------------------------- --------------------------------------------------------------------		27667366
468	Ubiquitination	-------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------		27667366
474	Ubiquitination	-------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------		27667366
500	Ubiquitination	---------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------		27667366
506	Ubiquitination	---------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------		27667366

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 SIR2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
368	S	Acetylation	21183079
Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation.
368	S	Phosphorylation	21183079
Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase (By similarity).
368	S	Phosphorylation	21183079
Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the G2/M transition; phosphorylation regulates the delay in cell-cycle progression.
368	S	Phosphorylation	21183079
Phosphorylated at Ser-368 by a mitotic kinase G1/S-specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-mediated alpha-tubulin deacetylation and thereby negatively regulates cell adhesion, cell migration and neurite outgrowth during neuronal differentiation.

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 SIR2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSBP3_MOUSE	Ssbp3	physical	20211142
ZBTB3_MOUSE	Zbtb3	physical	20211142
AURKA_MOUSE	Aurka	physical	22014574
APC1_HUMAN	ANAPC1	physical	22014574
CDC27_HUMAN	CDC27	physical	22014574
APC4_HUMAN	ANAPC4	physical	22014574
CDC16_HUMAN	CDC16	physical	22014574
CDC23_HUMAN	CDC23	physical	22014574
AURKA_HUMAN	AURKA	physical	22014574
CDC20_HUMAN	CDC20	physical	22014574
FZR1_HUMAN	FZR1	physical	22014574
FZR1_MOUSE	Fzr1	physical	22014574
CDC20_MOUSE	Cdc20	physical	22014574
EP300_HUMAN	EP300	physical	15632193
PA24A_MOUSE	Pla2g4a	physical	26303530
CCNA2_MOUSE	Ccna2	physical	26303530

Drug and Disease Associations

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

Regulatory Network of SIR2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-23, AND MASSSPECTROMETRY.	19367708 [Abstract]

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