dbPTM

SIR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIR2_HUMAN
UniProt AC	Q8IXJ6
Protein Name	NAD-dependent protein deacetylase sirtuin-2
Gene Name	SIRT2
Organism	Homo sapiens (Human).
Sequence Length	389
Subcellular Localization	Nucleus. Cytoplasm, perinuclear region. Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. 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: 24177535]
Protein Sequence	MAEPDPSHPLETQAGKVQEAQDSDSDSEGGAAGGEADMDFLRNLFSQTLSLGSQKERLLDELTLEGVARYMQSERCRRVICLVGAGISTSAGIPDFRSPSTGLYDNLEKYHLPYPEAIFEISYFKKHPEPFFALAKELYPGQFKPTICHYFMRLLKDKGLLLRCYTQNIDTLERIAGLEQEDLVEAHGTFYTSHCVSASCRHEYPLSWMKEKIFSEVTPKCEDCQSLVKPDIVFFGESLPARFFSCMQSDFLKVDLLLVMGTSLQVQPFASLISKAPLSTPRLLINKEKAGQSDPFLGMIMGLGGGMDFDSKKAYRDVAWLGECDQGCLALAELLGWKKELEDLVRREHASIDAQSGAGVPNPSTSASPKKSPPPAKDEARTTEREKPQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEPDPSHP ------CCCCCCCCC	36.71	19413330
18 (in isoform 2)	Ubiquitination	-	43.74	21890473
23	Phosphorylation	KVQEAQDSDSDSEGG CCCCCCCCCCCCCCC	27.25	30278072
25	Phosphorylation	QEAQDSDSDSEGGAA CCCCCCCCCCCCCCC	47.16	30278072
27	Phosphorylation	AQDSDSDSEGGAAGG CCCCCCCCCCCCCCC	41.93	26055452
35 (in isoform 3)	Ubiquitination	-	40.35	21890473
46	Phosphorylation	DFLRNLFSQTLSLGS HHHHHHHHCHHCCCC	25.97	24076635
48	Phosphorylation	LRNLFSQTLSLGSQK HHHHHHCHHCCCCHH	19.67	24076635
50	Phosphorylation	NLFSQTLSLGSQKER HHHHCHHCCCCHHHH	33.79	24076635
53	Phosphorylation	SQTLSLGSQKERLLD HCHHCCCCHHHHHHH	43.29	25307156
55 (in isoform 4)	Ubiquitination	-	46.64	21890473
55 (in isoform 1)	Ubiquitination	-	46.64	21890473
55	Ubiquitination	TLSLGSQKERLLDEL HHCCCCHHHHHHHHH	46.64	2189047
100	Phosphorylation	IPDFRSPSTGLYDNL CCCCCCCCCCCCCCH	36.03	24076635
101	Phosphorylation	PDFRSPSTGLYDNLE CCCCCCCCCCCCCHH	34.29	29978859
104	Phosphorylation	RSPSTGLYDNLEKYH CCCCCCCCCCHHHCC	12.25	28796482
121 (in isoform 2)	Ubiquitination	-	2.55	21890473
126	Ubiquitination	FEISYFKKHPEPFFA HHHHHHHHCCCCCHH	55.27	-
138 (in isoform 3)	Ubiquitination	-	6.52	21890473
158 (in isoform 4)	Ubiquitination	-	50.28	21890473
158 (in isoform 1)	Ubiquitination	-	50.28	21890473
158	Ubiquitination	FMRLLKDKGLLLRCY HHHHHHHCCHHHHHH	50.28	-
189	Phosphorylation	DLVEAHGTFYTSHCV HHHHHCCEEEEHHCC	12.00	23898821
191	Phosphorylation	VEAHGTFYTSHCVSA HHHCCEEEEHHCCCH	13.73	23898821
192	Phosphorylation	EAHGTFYTSHCVSAS HHCCEEEEHHCCCHH	14.06	23898821
193	Phosphorylation	AHGTFYTSHCVSASC HCCEEEEHHCCCHHH	11.96	23898821
197	Phosphorylation	FYTSHCVSASCRHEY EEEHHCCCHHHCCCC	21.62	23898821
199	Phosphorylation	TSHCVSASCRHEYPL EHHCCCHHHCCCCCC	12.27	23898821
204	Phosphorylation	SASCRHEYPLSWMKE CHHHCCCCCCHHHHH	11.89	23898821
207	Phosphorylation	CRHEYPLSWMKEKIF HCCCCCCHHHHHHHH	22.18	23898821
212	Ubiquitination	PLSWMKEKIFSEVTP CCHHHHHHHHHCCCC	43.46	-
215	Phosphorylation	WMKEKIFSEVTPKCE HHHHHHHHCCCCCCH	34.33	26270265
218	Phosphorylation	EKIFSEVTPKCEDCQ HHHHHCCCCCCHHHH	16.99	26270265
226	Phosphorylation	PKCEDCQSLVKPDIV CCCHHHHHHCCCCEE	41.27	26270265
238	Phosphorylation	DIVFFGESLPARFFS CEEEECCCCCHHHHH	39.78	24719451
271	Phosphorylation	LQVQPFASLISKAPL CCHHCCHHHHHCCCC	26.98	24719451
274	Phosphorylation	QPFASLISKAPLSTP HCCHHHHHCCCCCCC	28.23	-
279	Phosphorylation	LISKAPLSTPRLLIN HHHCCCCCCCEEECC	34.99	29449344
280	Phosphorylation	ISKAPLSTPRLLINK HHCCCCCCCEEECCH	21.80	29449344
287	Ubiquitination	TPRLLINKEKAGQSD CCEEECCHHHCCCCC	54.31	-
311	Phosphorylation	GGGMDFDSKKAYRDV CCCCCCCCHHHHCCC	35.73	30387612
316	Methylation	FDSKKAYRDVAWLGE CCCHHHHCCCHHHCC	36.47	24379893
316	Dimethylation	FDSKKAYRDVAWLGE CCCHHHHCCCHHHCC	36.47	-
331	Phosphorylation	CDQGCLALAELLGWK CHHHHHHHHHHHCCH	2.16	-
338	Acetylation	LAELLGWKKELEDLV HHHHHCCHHHHHHHH	34.27	156103
339	Ubiquitination	AELLGWKKELEDLVR HHHHCCHHHHHHHHH	62.11	-
351	Phosphorylation	LVRREHASIDAQSGA HHHHHHHCCCCCCCC	23.94	22167270
356	Phosphorylation	HASIDAQSGAGVPNP HHCCCCCCCCCCCCC	32.12	22167270
364	Phosphorylation	GAGVPNPSTSASPKK CCCCCCCCCCCCCCC	41.45	29255136
365	Phosphorylation	AGVPNPSTSASPKKS CCCCCCCCCCCCCCC	29.57	30266825
366	Phosphorylation	GVPNPSTSASPKKSP CCCCCCCCCCCCCCC	30.96	23401153
368	Phosphorylation	PNPSTSASPKKSPPP CCCCCCCCCCCCCCC	36.70	29255136
372	Phosphorylation	TSASPKKSPPPAKDE CCCCCCCCCCCCCCC	49.09	27512957
382	Phosphorylation	PAKDEARTTEREKPQ CCCCCCCCCCCCCCC	39.80	26074081
383	Phosphorylation	AKDEARTTEREKPQ- CCCCCCCCCCCCCC-	27.73	26074081

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
101	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
104	Y	Phosphorylation	Kinase	SRC	P12931	PSP
331	S	Phosphorylation	Kinase	CDK2	P24941	PSP
368	S	Phosphorylation	Kinase	CDK1	P06493	PSP
368	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
368	S	Phosphorylation	Kinase	CDK5	Q00535	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
368	S	Acetylation	17488717
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	17488717
Dephosphorylated at Ser-368 by CDC14A and CDC14B around early anaphase.
368	S	Phosphorylation	17488717
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	17488717
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PHB2_HUMAN	PHB2	physical	17353931
GYS1_HUMAN	GYS1	physical	17353931
RTN4_HUMAN	RTN4	physical	17353931
K2C78_HUMAN	KRT78	physical	17353931
SYSC_HUMAN	SARS	physical	17353931
DNJB8_HUMAN	DNAJB8	physical	20159555
DNJB6_HUMAN	DNAJB6	physical	20159555
H31_HUMAN	HIST1H3A	physical	19801601
EP300_HUMAN	EP300	physical	18995842
EP300_HUMAN	EP300	physical	18722353
ING1_HUMAN	ING1	physical	14522900
TAT_HV1H2	tat	physical	15719057
FOXO1_HUMAN	FOXO1	physical	15220471
RUNX3_HUMAN	RUNX3	physical	21511279
FZR1_HUMAN	FZR1	physical	22014574
CDC20_HUMAN	CDC20	physical	22014574
FOXO1_HUMAN	FOXO1	physical	24419059
EP300_HUMAN	EP300	physical	23934153
H31_HUMAN	HIST1H3A	physical	19270680
RBGPR_HUMAN	RAB3GAP2	physical	26186194
GPAT1_HUMAN	GPAM	physical	26186194
RB3GP_HUMAN	RAB3GAP1	physical	26186194
SCFD2_HUMAN	SCFD2	physical	26186194
SYSC_HUMAN	SARS	physical	26186194
FADS1_HUMAN	FADS1	physical	26186194
LYRIC_HUMAN	MTDH	physical	26186194
DEGS1_HUMAN	DEGS1	physical	26186194
ORC2_HUMAN	ORC2	physical	26186194
TPC12_HUMAN	TRAPPC12	physical	26186194
VAMP7_HUMAN	VAMP7	physical	26186194
TBA4A_HUMAN	TUBA4A	physical	12620231
SKP2_HUMAN	SKP2	physical	26942878
MDM2_HUMAN	MDM2	physical	28196907
PA24A_HUMAN	PLA2G4A	physical	26303530
SYSC_HUMAN	SARS	physical	28514442
SCFD2_HUMAN	SCFD2	physical	28514442
RB3GP_HUMAN	RAB3GAP1	physical	28514442
GPAT1_HUMAN	GPAM	physical	28514442
ORC2_HUMAN	ORC2	physical	28514442
LYRIC_HUMAN	MTDH	physical	28514442
FADS1_HUMAN	FADS1	physical	28514442
RBGPR_HUMAN	RAB3GAP2	physical	28514442
DEGS1_HUMAN	DEGS1	physical	28514442
VAMP7_HUMAN	VAMP7	physical	28514442
GDIR1_HUMAN	ARHGDIA	physical	26719334

Drug and Disease Associations

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

Regulatory Network of SIR2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-23; SER-27 AND SER-368, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-23; SER-27 AND SER-368, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND MASSSPECTROMETRY.	18088087 [Abstract]

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