dbPTM

SIR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SIR1_HUMAN
UniProt AC	Q96EB6
Protein Name	NAD-dependent protein deacetylase sirtuin-1
Gene Name	SIRT1
Organism	Homo sapiens (Human).
Sequence Length	747
Subcellular Localization	Nucleus, PML body . Cytoplasm . Nucleus . Recruited to the nuclear bodies via its interaction with PML (PubMed:12006491). Colocalized with APEX1 in the nucleus (PubMed:19934257). May be found in nucleolus, nuclear euchromatin, heterochromatin and inn
Protein Description	NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Modulates AP-1 transcription factor activity. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates ACSS2 leading to its activation, and HMGCS1. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis. [PubMed: 11672523]
Protein Sequence	MADEAALALQPGGSPSAAGADREAASSPAGEPLRKRPRRDGPGLERSPGEPGGAAPEREVPAAARGCPGAAAAALWREAEAEAAAAGGEQEAQATAAAGEGDNGPGLQGPSREPPLADNLYDEDDDDEGEEEEEAAAAAIGYRDNLLFGDEIITNGFHSCESDEEDRASHASSSDWTPRPRIGPYTFVQQHLMIGTDPRTILKDLLPETIPPPELDDMTLWQIVINILSEPPKRKKRKDINTIEDAVKLLQECKKIIVLTGAGVSVSCGIPDFRSRDGIYARLAVDFPDLPDPQAMFDIEYFRKDPRPFFKFAKEIYPGQFQPSLCHKFIALSDKEGKLLRNYTQNIDTLEQVAGIQRIIQCHGSFATASCLICKYKVDCEAVRGDIFNQVVPRCPRCPADEPLAIMKPEIVFFGENLPEQFHRAMKYDKDEVDLLIVIGSSLKVRPVALIPSSIPHEVPQILINREPLPHLHFDVELLGDCDVIINELCHRLGGEYAKLCCNPVKLSEITEKPPRTQKELAYLSELPPTPLHVSEDSSSPERTSPPDSSVIVTLLDQAAKSNDDLDVSESKGCMEEKPQEVQTSRNVESIAEQMENPDLKNVGSSTGEKNERTSVAGTVRKCWPNRVAKEQISRRLDGNQYLFLPPNRYIFHGAEVYSDSEDDVLSSSSCGSNSDSGTCQSPSLEEPMEDESEIEEFYNGLEDEPDVPERAGGAGFGTDGDDQEAINEAISVKQEVTDMNYPSNKS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADEAALAL ------CCCHHHHHC	24.29	20068231
14	Phosphorylation	LALQPGGSPSAAGAD HHCCCCCCCCCCCCC	22.92	29255136
16	Phosphorylation	LQPGGSPSAAGADRE CCCCCCCCCCCCCHH	32.23	29255136
26	Phosphorylation	GADREAASSPAGEPL CCCHHHHCCCCCCCC	43.85	29255136
27	Phosphorylation	ADREAASSPAGEPLR CCHHHHCCCCCCCCC	17.65	29255136
47	Phosphorylation	DGPGLERSPGEPGGA CCCCCCCCCCCCCCC	28.07	29255136
67	Glutathionylation	VPAAARGCPGAAAAA CCHHHCCCCHHHHHH	2.04	22833525
154	Phosphorylation	LFGDEIITNGFHSCE ECCCEEECCCCCCCC	34.64	27251275
159	Phosphorylation	IITNGFHSCESDEED EECCCCCCCCCCHHH	19.81	23663014
162	Phosphorylation	NGFHSCESDEEDRAS CCCCCCCCCHHHHHH	55.43	23663014
169	Phosphorylation	SDEEDRASHASSSDW CCHHHHHHHCCCCCC	22.08	23663014
172	Phosphorylation	EDRASHASSSDWTPR HHHHHHCCCCCCCCC	25.58	27794612
173	Phosphorylation	DRASHASSSDWTPRP HHHHHCCCCCCCCCC	32.85	27794612
174	Phosphorylation	RASHASSSDWTPRPR HHHHCCCCCCCCCCC	34.37	23663014
177	Phosphorylation	HASSSDWTPRPRIGP HCCCCCCCCCCCCCC	17.89	20873877
185	Phosphorylation	PRPRIGPYTFVQQHL CCCCCCCCCHHHHHE	13.95	24043423
186	Phosphorylation	RPRIGPYTFVQQHLM CCCCCCCCHHHHHEE	22.06	24043423
196	Phosphorylation	QQHLMIGTDPRTILK HHHEECCCCHHHHHH	31.72	24043423
238	Acetylation	PPKRKKRKDINTIED CCCCCCCCCCCHHHH	72.36	-
238	Ubiquitination	PPKRKKRKDINTIED CCCCCCCCCCCHHHH	72.36	21890473
248	Ubiquitination	NTIEDAVKLLQECKK CHHHHHHHHHHHHCC	45.24	-
280	Phosphorylation	FRSRDGIYARLAVDF HHHCCCEEEEEEECC	7.38	-
301	Phosphorylation	QAMFDIEYFRKDPRP HHHCCHHHHHCCCCC	14.71	-
304	Acetylation	FDIEYFRKDPRPFFK CCHHHHHCCCCCHHH	63.28	25953088
311	Ubiquitination	KDPRPFFKFAKEIYP CCCCCHHHHHHHHCC	44.80	21890473
314	Ubiquitination	RPFFKFAKEIYPGQF CCHHHHHHHHCCCCC	48.02	-
328	Ubiquitination	FQPSLCHKFIALSDK CCHHHHHHHHCCCCC	37.15	-
333	Phosphorylation	CHKFIALSDKEGKLL HHHHHCCCCCCCHHH	37.30	21406692
335	Ubiquitination	KFIALSDKEGKLLRN HHHCCCCCCCHHHHH	66.06	-
338	Ubiquitination	ALSDKEGKLLRNYTQ CCCCCCCHHHHHHHC	45.50	-
344	Phosphorylation	GKLLRNYTQNIDTLE CHHHHHHHCCCHHHH	20.77	22728651
377	Acetylation	SCLICKYKVDCEAVR EEEEEEEEECHHHHC	19.66	-
395	S-nitrosylation	FNQVVPRCPRCPADE HHCCCCCCCCCCCCC	1.72	-
395	S-nitrosocysteine	FNQVVPRCPRCPADE HHCCCCCCCCCCCCC	1.72	-
398	S-nitrosylation	VVPRCPRCPADEPLA CCCCCCCCCCCCCCE	1.65	-
398	S-nitrosocysteine	VVPRCPRCPADEPLA CCCCCCCCCCCCCCE	1.65	-
428	Phosphorylation	QFHRAMKYDKDEVDL HHHHHHCCCHHHCCE	18.36	23312004
430	Acetylation	HRAMKYDKDEVDLLI HHHHCCCHHHCCEEE	53.34	7972685
441	Phosphorylation	DLLIVIGSSLKVRPV CEEEEECCCCCEEEE	22.75	23312004
442	Phosphorylation	LLIVIGSSLKVRPVA EEEEECCCCCEEEEE	27.31	23312004
444	Acetylation	IVIGSSLKVRPVALI EEECCCCCEEEEEEC	37.84	7972695
499	Ubiquitination	RLGGEYAKLCCNPVK HCCHHHHHHHCCCCC	40.95	-
506	Acetylation	KLCCNPVKLSEITEK HHHCCCCCHHHHCCC	47.77	25953088
506	Ubiquitination	KLCCNPVKLSEITEK HHHCCCCCHHHHCCC	47.77	-
513	Ubiquitination	KLSEITEKPPRTQKE CHHHHCCCCCCCHHH	52.23	-
513	Acetylation	KLSEITEKPPRTQKE CHHHHCCCCCCCHHH	52.23	-
523	Phosphorylation	RTQKELAYLSELPPT CCHHHHHHHHCCCCC	24.32	20068231
525	Phosphorylation	QKELAYLSELPPTPL HHHHHHHHCCCCCCC	25.14	20068231
530	Phosphorylation	YLSELPPTPLHVSED HHHCCCCCCCCCCCC	36.22	25159151
535	Phosphorylation	PPTPLHVSEDSSSPE CCCCCCCCCCCCCCC	25.57	25159151
538	Phosphorylation	PLHVSEDSSSPERTS CCCCCCCCCCCCCCC	28.76	25159151
539	Phosphorylation	LHVSEDSSSPERTSP CCCCCCCCCCCCCCC	63.33	25159151
540	Phosphorylation	HVSEDSSSPERTSPP CCCCCCCCCCCCCCC	34.43	25159151
544	Phosphorylation	DSSSPERTSPPDSSV CCCCCCCCCCCCCHH	43.88	25159151
545	Phosphorylation	SSSPERTSPPDSSVI CCCCCCCCCCCCHHH	40.43	28464451
549	Phosphorylation	ERTSPPDSSVIVTLL CCCCCCCCHHHHHHH	32.07	25850435
549	O-linked_Glycosylation	ERTSPPDSSVIVTLL CCCCCCCCHHHHHHH	32.07	23301498
550	Phosphorylation	RTSPPDSSVIVTLLD CCCCCCCHHHHHHHH	24.20	25850435
554	Phosphorylation	PDSSVIVTLLDQAAK CCCHHHHHHHHHHHH	15.52	20068231
561	Ubiquitination	TLLDQAAKSNDDLDV HHHHHHHHCCCCCCH	53.46	-
562	Phosphorylation	LLDQAAKSNDDLDVS HHHHHHHCCCCCCHH	40.54	20873877
569	Phosphorylation	SNDDLDVSESKGCME CCCCCCHHHCCCCCC	35.50	25159151
571	Phosphorylation	DDLDVSESKGCMEEK CCCCHHHCCCCCCCC	27.17	21815630
572	Ubiquitination	DLDVSESKGCMEEKP CCCHHHCCCCCCCCC	52.67	-
575	Sulfoxidation	VSESKGCMEEKPQEV HHHCCCCCCCCCCHH	11.54	21406390
578	Ubiquitination	SKGCMEEKPQEVQTS CCCCCCCCCCHHHCH	38.40	-
578	Acetylation	SKGCMEEKPQEVQTS CCCCCCCCCCHHHCH	38.40	26051181
590	Phosphorylation	QTSRNVESIAEQMEN HCHHHHHHHHHHHCC	23.86	25159151
601	Ubiquitination	QMENPDLKNVGSSTG HHCCCCHHCCCCCCC	57.90	21890473
605	Phosphorylation	PDLKNVGSSTGEKNE CCHHCCCCCCCCCCC	22.05	28985074
606	Phosphorylation	DLKNVGSSTGEKNER CHHCCCCCCCCCCCC	34.21	30624053
607	Phosphorylation	LKNVGSSTGEKNERT HHCCCCCCCCCCCCC	51.57	28985074
610	Acetylation	VGSSTGEKNERTSVA CCCCCCCCCCCCCCC	66.51	-
610	Ubiquitination	VGSSTGEKNERTSVA CCCCCCCCCCCCCCC	66.51	21890473
614	Phosphorylation	TGEKNERTSVAGTVR CCCCCCCCCCCHHHH	22.75	25159151
614	O-linked_Glycosylation	TGEKNERTSVAGTVR CCCCCCCCCCCHHHH	22.75	23301498
615	Phosphorylation	GEKNERTSVAGTVRK CCCCCCCCCCHHHHH	19.05	25159151
619	Phosphorylation	ERTSVAGTVRKCWPN CCCCCCHHHHHHCCC	13.85	25159151
622	Methylation	SVAGTVRKCWPNRVA CCCHHHHHHCCCHHH	35.99	116254479
659	Phosphorylation	FHGAEVYSDSEDDVL ECCEEEECCCCCCCC	39.58	22817900
661	Phosphorylation	GAEVYSDSEDDVLSS CEEEECCCCCCCCCC	36.66	22817900
682	Phosphorylation	SDSGTCQSPSLEEPM CCCCCCCCCCCCCCC	20.71	-
719	Phosphorylation	AGGAGFGTDGDDQEA CCCCCCCCCCCCHHH	34.25	29255136
734	Sumoylation	INEAISVKQEVTDMN HHHHHHHHHHHHCCC	33.67	-
734	Sumoylation	INEAISVKQEVTDMN HHHHHHHHHHHHCCC	33.67	-
742	Phosphorylation	QEVTDMNYPSNKS-- HHHHCCCCCCCCC--	11.03	27732954
744	Phosphorylation	VTDMNYPSNKS---- HHCCCCCCCCC----	46.67	25159151
747	Phosphorylation	MNYPSNKS------- CCCCCCCC-------	50.10	21471201

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
27	S	Phosphorylation	Kinase	JNK1	P45983	PSP
27	S	Phosphorylation	Kinase	CAMKK2	Q96RR4	PSP
27	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP
47	S	Phosphorylation	Kinase	JNK1	P45983	PSP
47	S	Phosphorylation	Kinase	CAMKK2	Q96RR4	PSP
280	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
301	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
344	T	Phosphorylation	Kinase	AURA	O14965	PSP
530	T	Phosphorylation	Kinase	CDK1	P06493	PSP
530	T	Phosphorylation	Kinase	JNK1	P45983	PSP
530	T	Phosphorylation	Kinase	DYRK3	O43781	Uniprot
530	T	Phosphorylation	Kinase	DYRK1A	Q13627	Uniprot
540	S	Phosphorylation	Kinase	CDK1	P06493	PSP
659	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
659	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
661	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
661	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
682	S	Phosphorylation	Kinase	HIPK2	Q9H2X6	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
27	S	Phosphorylation	18838864
Phosphorylation at Ser-27 implicating MAPK9 is linked to protein stability.
27	S	Phosphorylation	18838864
Phosphorylation by MAPK8/JNK1 at Ser-27, Ser-47, and Thr-530 leads to increased nuclear localization and enzymatic activity.
47	S	Acetylation	16964243
Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-47 inhibits deacetylation activity.
47	S	Phosphorylation	16964243
Phosphorylation by MAPK8/JNK1 at Ser-27, Ser-47, and Thr-530 leads to increased nuclear localization and enzymatic activity.
47	S	Phosphorylation	16964243
Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-47 inhibits deacetylation activity.
238	K	Acetylation	21245319
Autodeacetylation at Lys-238 promotes its protein deacetylase activity.
530	T	Acetylation	19107194
Phosphorylation at Thr-530 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival.
530	T	Phosphorylation	19107194
Phosphorylation at Thr-530 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival.
530	T	Phosphorylation	19107194
Phosphorylation by MAPK8/JNK1 at Ser-27, Ser-47, and Thr-530 leads to increased nuclear localization and enzymatic activity.

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 SIR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HES1_HUMAN	HES1	physical	12535671
HEY2_HUMAN	HEY2	physical	12535671
KAT5_HUMAN	KAT5	physical	20100829
SUV91_HUMAN	SUV39H1	physical	19218236
KAT2B_HUMAN	KAT2B	physical	19188449
E2F1_HUMAN	E2F1	physical	19188449
KAT5_HUMAN	KAT5	physical	19895790
MEF2C_HUMAN	MEF2C	physical	19553684
MYOD1_HUMAN	MYOD1	physical	19553684
TF65_HUMAN	RELA	physical	17041012
SRC8_HUMAN	CTTN	physical	18850005
ANDR_HUMAN	AR	physical	16923962
NCOR1_HUMAN	NCOR1	physical	18829436
JUN_HUMAN	JUN	physical	18823944
DOT1L_HUMAN	DOT1L	physical	19491102
CLOCK_HUMAN	CLOCK	physical	18662547
BMAL1_HUMAN	ARNTL	physical	18662547
HDAC4_HUMAN	HDAC4	physical	16166628
TAT_HV1H2	tat	physical	15719057
EZH2_HUMAN	EZH2	physical	15684044
SUZ12_HUMAN	SUZ12	physical	15684044
BC11A_HUMAN	BCL11A	physical	15639232
BRNP1_HUMAN	BRINP1	physical	18235502
P53_HUMAN	TP53	physical	18235502
SIR2_HUMAN	SIRT2	physical	18193082
RET1_HUMAN	RBP1	physical	18193082
ARI4B_HUMAN	ARID4B	physical	18193082
ING2_HUMAN	ING2	physical	18193082
ING1_HUMAN	ING1	physical	18193082
FOXO3_HUMAN	FOXO3	physical	15126506
BHE41_HUMAN	BHLHE41	physical	17487425
TLE1_HUMAN	TLE1	physical	17680780
ERR1_HUMAN	ESRRA	physical	20484414
NBN_HUMAN	NBN	physical	17612497
DVL1_HUMAN	DVL1	physical	20439735
DVL2_HUMAN	DVL2	physical	20439735
CSK21_HUMAN	CSNK2A1	physical	20439735
NR0B2_HUMAN	NR0B2	physical	20375098
SETD7_HUMAN	SETD7	physical	21245319
P53_HUMAN	TP53	physical	21245319
SMAD7_HUMAN	SMAD7	physical	17098745
NR1H4_HUMAN	NR1H4	physical	19883617
FOXO3_HUMAN	FOXO3	physical	20733005
SRBP1_HUMAN	SREBF1	physical	20595232
HNF1A_HUMAN	HNF1A	physical	21176092
BRNP1_HUMAN	BRINP1	physical	21030595
G3P_HUMAN	GAPDH	physical	20972425
ACACA_HUMAN	ACACA	physical	19343720
HSP74_HUMAN	HSPA4	physical	19343720
WRN_HUMAN	WRN	physical	19343720
CH60_HUMAN	HSPD1	physical	19343720
CHCH2_HUMAN	CHCHD2	physical	19343720
DIAP3_HUMAN	DIAPH3	physical	19343720
YBOX1_HUMAN	YBX1	physical	19343720
DYHC1_HUMAN	DYNC1H1	physical	19343720
HS71L_HUMAN	HSPA1L	physical	19343720
GRP78_HUMAN	HSPA5	physical	19343720
H2A2B_HUMAN	HIST2H2AB	physical	19343720
GRP75_HUMAN	HSPA9	physical	19343720
HDAC2_HUMAN	HDAC2	physical	19343720
CMYA5_HUMAN	CMYA5	physical	19343720
IMA1_HUMAN	KPNA2	physical	19343720
IMA4_HUMAN	KPNA3	physical	19343720
LAMA3_HUMAN	LAMA3	physical	19343720
EF1G_HUMAN	EEF1G	physical	19343720
RHG29_HUMAN	ARHGAP29	physical	19343720
MF2L2_HUMAN	MCF2L2	physical	19343720
ELL3_HUMAN	ELL3	physical	19343720
USP9Y_HUMAN	USP9Y	physical	19343720
NAT10_HUMAN	NAT10	physical	19343720
UGDH_HUMAN	UGDH	physical	19343720
CAC1C_HUMAN	CACNA1C	physical	19343720
LANC1_HUMAN	LANCL1	physical	19343720
ZEB1_HUMAN	ZEB1	physical	22249256
EVI1_HUMAN	MECOM	physical	21555002
KAT8_HUMAN	KAT8	physical	21502975
CSK2B_HUMAN	CSNK2B	physical	21968188
DNMT1_HUMAN	DNMT1	physical	21947282
ESR1_HUMAN	ESR1	physical	21920899
STAT3_HUMAN	STAT3	physical	22542455
JAK1_HUMAN	JAK1	physical	22542455
HS90A_HUMAN	HSP90AA1	physical	22542455
TIF1B_HUMAN	TRIM28	physical	22542455
UBP22_HUMAN	USP22	physical	22542455
KAT2A_HUMAN	KAT2A	physical	22542455
HNRPK_HUMAN	HNRNPK	physical	22542455
SATB1_HUMAN	SATB1	physical	22328728
FOXO3_HUMAN	FOXO3	physical	21713995
MYCN_HUMAN	MYCN	physical	21698133
HIC1_HUMAN	HIC1	physical	22510409
P53_HUMAN	TP53	physical	12006491
JUN_HUMAN	JUN	physical	20042607
FOS_HUMAN	FOS	physical	20042607
TF2AA_HUMAN	GTF2A1	physical	22939629
SMRD2_HUMAN	SMARCD2	physical	22939629
AKT1_HUMAN	AKT1	physical	21775285
UBP22_HUMAN	USP22	physical	23382074
KAT2A_HUMAN	KAT2A	physical	23382074
ST65G_HUMAN	SUPT7L	physical	23382074
AT7L3_HUMAN	ATXN7L3	physical	23382074
JUN_HUMAN	JUN	physical	23382074
CREB1_HUMAN	CREB1	physical	23382074
AROS_HUMAN	RPS19BP1	physical	23382074
PUS7_HUMAN	PUS7	physical	23382074
SPDLY_HUMAN	SPDL1	physical	23382074
BRNP1_HUMAN	BRINP1	physical	23382074
TULP3_HUMAN	TULP3	physical	23382074
PI51A_HUMAN	PIP5K1A	physical	23382074
PHLB3_HUMAN	PHLDB3	physical	23382074
AKIR2_HUMAN	AKIRIN2	physical	23382074
IQCB1_HUMAN	IQCB1	physical	23382074
JUND_HUMAN	JUND	physical	23382074
BCD1_HUMAN	ZNHIT6	physical	23382074
K2C79_HUMAN	KRT79	physical	23382074
WDR70_HUMAN	WDR70	physical	23382074
NOP14_HUMAN	NOP14	physical	23382074
PICAL_HUMAN	PICALM	physical	23382074
SPB4_HUMAN	SERPINB4	physical	23382074
ARRB2_HUMAN	ARRB2	physical	23382074
TSYL1_HUMAN	TSPYL1	physical	23382074
RECQ4_HUMAN	RECQL4	physical	23382074
SCNM1_HUMAN	SCNM1	physical	23382074
ZN346_HUMAN	ZNF346	physical	23382074
BRNP1_HUMAN	BRINP1	physical	18235501
NOC4L_HUMAN	NOC4L	physical	18235501
SNUT1_HUMAN	SART1	physical	18235501
TAF2_HUMAN	TAF2	physical	18235501
RAP1A_HUMAN	RAP1A	physical	18235501
CHD3_HUMAN	CHD3	physical	18235501
P53_HUMAN	TP53	physical	18235501
RPTOR_HUMAN	RPTOR	physical	21471201
MTOR_HUMAN	MTOR	physical	21471201
FOXO3_HUMAN	FOXO3	physical	14976264
DNMT1_HUMAN	DNMT1	physical	22094255
EZH2_HUMAN	EZH2	physical	22094255
SUZ12_HUMAN	SUZ12	physical	22094255
EED_HUMAN	EED	physical	22094255
HDAC4_HUMAN	HDAC4	physical	23417673
CAP1_HUMAN	CAP1	physical	22863883
FAS_HUMAN	FASN	physical	22863883
SHOT1_HUMAN	KIAA1598	physical	22863883
TPM4_HUMAN	TPM4	physical	22863883
PPARA_HUMAN	PPARA	physical	19356714
KCNA5_HUMAN	KCNA5	physical	23390957
KCNA4_HUMAN	KCNA4	physical	23390957
KCAB2_HUMAN	KCNAB2	physical	23390957
PSME3_HUMAN	PSME3	physical	23612972
WRN_HUMAN	WRN	physical	18203716
FOXO1_HUMAN	FOXO1	physical	15692560
PRGC1_HUMAN	PPARGC1A	physical	15716268
STK11_HUMAN	STK11	physical	18687677
AROS_HUMAN	RPS19BP1	physical	17964266
P53_HUMAN	TP53	physical	17964266
CDK1_HUMAN	CDK1	physical	19107194
CCNB1_HUMAN	CCNB1	physical	19107194
IRS2_HUMAN	IRS2	physical	17901049
UBC9_HUMAN	UBE2I	physical	23395904
PARP1_HUMAN	PARP1	physical	19470756
H31_HUMAN	HIST1H3A	physical	19270680
RICTR_HUMAN	RICTOR	physical	22084251
EPAS1_HUMAN	EPAS1	physical	22807441
CSK22_HUMAN	CSNK2A2	physical	19680552
CSK21_HUMAN	CSNK2A1	physical	19680552
NMNA1_HUMAN	NMNAT1	physical	19478080
APEX1_HUMAN	APEX1	physical	19934257
SNW1_HUMAN	SNW1	physical	19934264
RARA_HUMAN	RARA	physical	19934264
TSC2_HUMAN	TSC2	physical	20169165
NOS3_HUMAN	NOS3	physical	20479254
SIR1_HUMAN	SIRT1	physical	20479254
E2F1_HUMAN	E2F1	physical	16892051
RB_HUMAN	RB1	physical	16892051
SRBP1_HUMAN	SREBF1	physical	20817729
P73_HUMAN	TP73	physical	16998810
P85A_HUMAN	PIK3R1	physical	21241768
IRS1_HUMAN	IRS1	physical	21241768
IRS2_HUMAN	IRS2	physical	21241768
CCAR2_HUMAN	CCAR2	physical	25361978
CHK2_HUMAN	CHEK2	physical	25361978
EZH2_HUMAN	EZH2	physical	25800736
TIF1B_HUMAN	TRIM28	physical	25905708
MPP8_HUMAN	MPHOSPH8	physical	25870236
MYC_HUMAN	MYC	physical	22190494
CCAR2_HUMAN	CCAR2	physical	22190494
ZYX_HUMAN	ZYX	physical	19173742
P53_HUMAN	TP53	physical	22689577
CHFR_HUMAN	CHFR	physical	27883020
UBP22_HUMAN	USP22	physical	27183383
HERC2_HUMAN	HERC2	physical	27259994
UBP22_HUMAN	USP22	physical	28166203
MDM2_HUMAN	MDM2	physical	28196907
P53_HUMAN	TP53	physical	18753379
NECD_HUMAN	NDN	physical	18753379
MTOR_HUMAN	MTOR	physical	26453307
RICTR_HUMAN	RICTOR	physical	26453307
HXB9_HUMAN	HOXB9	physical	27613418
CCAR2_HUMAN	CCAR2	physical	22735644
P53_HUMAN	TP53	physical	22735644

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 SIR1_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-14; SER-16; SER-27 AND THR-719, AND MASSSPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Cancer cell survival following DNA damage-mediated prematuresenescence is regulated by mammalian target of rapamycin (mTOR)-dependent Inhibition of sirtuin 1."; Back J.H., Rezvani H.R., Zhu Y., Guyonnet-Duperat V., Athar M.,Ratner D., Kim A.L.; J. Biol. Chem. 286:19100-19108(2011). Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-47, AND MUTAGENESIS OFSER-47 AND PHE-474.	21471201 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-530; SER-535 ANDTHR-719, AND MASS SPECTROMETRY.	19690332 [Abstract]
"JNK1 phosphorylates SIRT1 and promotes its enzymatic activity."; Nasrin N., Kaushik V.K., Fortier E., Wall D., Pearson K.J.,de Cabo R., Bordone L.; PLoS ONE 4:E8414-E8414(2009). Cited for: PHOSPHORYLATION AT SER-27; SER-47 AND THR-530, MUTAGENESIS OF SER-27;SER-47 AND THR-530, AND SUBCELLULAR LOCATION.	20027304 [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-14; SER-16; SER-27 AND THR-719, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-719, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Phosphorylation regulates SIRT1 function."; Sasaki T., Maier B., Koclega K.D., Chruszcz M., Gluba W.,Stukenberg P.T., Minor W., Scrable H.; PLoS ONE 3:E4020-E4020(2008). Cited for: PHOSPHORYLATION AT SER-14; SER-26; SER-27; SER-47; SER-159; SER-162;SER-172; SER-173; THR-530; THR-544; SER-545; THR-719 AND SER-747, ANDMUTAGENESIS OF THR-530 AND SER-540.	19107194 [Abstract]
"JNK2-dependent regulation of SIRT1 protein stability."; Ford J., Ahmed S., Allison S., Jiang M., Milner J.; Cell Cycle 7:3091-3097(2008). Cited for: PHOSPHORYLATION AT SER-27 AND SER-47.	18838864 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-47, AND MASSSPECTROMETRY.	15302935 [Abstract]

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