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Protein Page:
SIRT2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SIRT2 NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and non-histone proteins. Deacetylates 'Lys-40' of alpha-tubulin. Involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton. Deacetylates PCK1, opposing proteasomal degradation. Deacetylates 'Lys-310' of RELA. Interacts with HDAC6, suggesting that these proteins belong to a large complex that deacetylate the cytoskeleton. Widely expressed. Highly expressed in heart, brain and skeletal muscle, while it is weakly expressed in placenta and lung. Down-regulated in many gliomas suggesting that it may act as a tumor suppressor gene in human gliomas possibly through the regulation of microtubule network. Inhibited by Sirtinol, A3 and M15 small molecules. Inhibited by nicotinamide. Belongs to the sirtuin family. Class I subfamily. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.5.1.-; Deacetylase
Chromosomal Location of Human Ortholog: 19q13
Cellular Component: centriole; centrosome; chromosome; cytoplasm; cytosol; lateral loop; microtubule; midbody; myelin sheath; nuclear heterochromatin; nucleus; paranode region of axon; perikaryon; perinuclear region of cytoplasm; spindle
Molecular Function: chromatin binding; histone acetyltransferase binding; histone deacetylase activity; histone deacetylase binding; NAD+ ADP-ribosyltransferase activity; NAD-dependent histone deacetylase activity; NAD-dependent histone deacetylase activity (H4-K16 specific); protein binding; protein deacetylase activity; transcription factor binding; tubulin deacetylase activity; ubiquitin binding; zinc ion binding
Biological Process: cellular lipid catabolic process; hepatocyte growth factor receptor signaling pathway; histone deacetylation; myelination in the peripheral nervous system; negative regulation of autophagy; negative regulation of cell proliferation; negative regulation of fat cell differentiation; negative regulation of protein catabolic process; negative regulation of striated muscle development; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; phosphoinositide 3-kinase cascade; positive regulation of attachment of spindle microtubules to kinetochore; positive regulation of cell division; positive regulation of DNA binding; positive regulation of meiosis; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; positive regulation of transcription from RNA polymerase II promoter; proteasomal ubiquitin-dependent protein catabolic process; protein amino acid ADP-ribosylation; protein amino acid deacetylation; protein kinase B signaling cascade; regulation of cell cycle; regulation of myelination; substantia nigra development
Reference #:  Q8IXJ6 (UniProtKB)
Alt. Names/Synonyms: NAD-dependent deacetylase sirtuin-2; silencing information regulator 2-like; silent information regulator 2; SIR2; SIR2-like protein 2; sir2-related protein type 2; SIR2L; SIR2L2; SIRT2; sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae); sirtuin type 2
Gene Symbols: SIRT2
Molecular weight: 43,182 Da
Basal Isoelectric point: 5.22  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Mitochondrial Control of Apoptosis  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SIRT2

Protein Structure Not Found.
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Sites Implicated In
cell adhesion, altered: S368‑p
cell growth, altered: S368‑p
cell motility, altered: S368‑p
enzymatic activity, induced: S372‑p
enzymatic activity, inhibited: S368‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 28 S23‑p KVQEAQDsDsDsEGG
0 23 S25‑p QEAQDsDsDsEGGAA
0 12 S27‑p AQDsDsDsEGGAAGG
0 2 S53 SQTLSLGSQkERLLD
0 1 K55 TLSLGSQKERLLDEL
0 6 K55‑ub TLSLGSQkERLLDEL
0 1 R75 ARYMQSERCRRVICL
0 1 R77 YMQSERCRRVICLVG
0 1 S100 IPDFRSPStGLyDNL
1 0 T101‑p PDFRSPStGLyDNLE
1 3 Y104‑p RSPStGLyDNLEKYH
0 1 K126 FEISYFKKHPEPFFA
0 1 K126 FEISYFKKHPEPFFA
0 1 K144 ELYPGQFKPTICHYF
0 1 K158 FMRLLKDKGLLLRCY
0 1 H202 CVSASCRHEYPLSWM
0 1 S207 CRHEYPLSWMKEKIF
0 1 K210 EYPLSWMKEKIFSEV
0 1 K212 PLSWMKEKIFSEVTP
0 1 K220 IFSEVTPKCEDCQSL
0 1 S271‑p LQVQPFAsLIsKAPL
0 2 S274‑p QPFAsLIsKAPLSTP
0 1 K287 TPRLLINKEKAGQSD
0 1 K287 TPRLLINKEKAGQSD
0 1 K312 GGMDFDSKKAYrDVA
0 1 R316‑m2 FDSKKAYrDVAWLGE
0 7 K338‑ac LAELLGWkKELEDLV
0 1 K338 LAELLGWKKELEDLV
0 1 K339 AELLGWkKELEDLVR
0 2 S356‑p HASIDAQsGAGVPNP
0 1 A358 SIDAQsGAGVPNPsT
0 4 S364‑p GAGVPNPsTsAsPKK
0 3 S366‑p GVPNPsTsAsPKKsP
5 22 S368‑p PNPsTsAsPKKsPPP
0 1 K371 sTsAsPKKsPPPAKD
1 15 S372‑p TsAsPKKsPPPAKDE
  SIRT2 iso2  
- gap
- gap
- gap
S16 SQTLSLGSQKERLLD
K18 TLSLGSQKERLLDEL
K18 TLSLGSQKERLLDEL
R38 ARYMQSERCRRVICL
R40 YMQSERCRRVICLVG
S63 IPDFRSPSTGLYDNL
T64 PDFRSPSTGLYDNLE
Y67 RSPSTGLYDNLEKYH
K89 FEISYFKKHPEPFFA
K89 FEISYFKKHPEPFFA
K107 ELYPGQFKPTICHYF
K121 FMRLLKDKGLLLRCY
H165 CVSASCRHEYPLSWM
S170 CRHEYPLSWMKEKIF
K173 EYPLSWMKEKIFSEV
K175 PLSWMKEKIFSEVTP
K183 IFSEVTPKCEDCQSL
S234 LQVQPFASLISKAPL
S237 QPFASLISKAPLSTP
K250 TPRLLINKEKAGQSD
K250 TPRLLINKEKAGQSD
K275 GGMDFDSKKAYRDVA
R279 FDSKKAYRDVAWLGE
K301 LAELLGWKKELEDLV
K301 LAELLGWKKELEDLV
K302 AELLGWKKELEDLVR
S319 HASIDAQSGAGVPNP
A321 SIDAQSGAGVPNPST
S327 GAGVPNPSTSAsPKK
S329 GVPNPSTSAsPKKSP
S331‑p PNPSTSAsPKKSPPP
K334 STSAsPKKSPPPAKD
S335 TSAsPKKSPPPAKDE
  mouse

► Hide Isoforms
 
S23‑p KVQEAQDsDsDtEGG
S25‑p QEAQDsDsDtEGGAT
T27‑p AQDsDsDtEGGATGG
S53‑p TQTLGLGsQkERLLD
K55 TLGLGsQKERLLDEL
K55‑ub TLGLGsQkERLLDEL
R75‑m2 TRYMQSErCrKVICL
R77‑m2 YMQSErCrKVICLVG
S100 IPDFRSPSTGLYANL
T101 PDFRSPSTGLYANLE
Y104 RSPSTGLYANLEKYH
K126‑ac FEISYFKkHPEPFFA
K126‑ub FEISYFKkHPEPFFA
K144‑ub ELYPGQFkPTICHYF
K158 FIRLLKEKGLLLRCY
K202‑ub CVNTSCRkEYTMGWM
G207 CRkEYTMGWMkEKIF
K210‑ub EYTMGWMkEKIFSEA
K212 TMGWMkEKIFSEATP
R220 IFSEATPRCEQCQSV
S271 LQVQPFASLISKAPL
S274 QPFASLISKAPLATP
K287 TPRLLINKEKTGQTD
K287‑ub TPRLLINkEKTGQTD
K312‑ub GGMDFDSkKAYRDVA
R316 FDSkKAYRDVAWLGD
K338‑ac LADLLGWkkELEDLV
K338‑ub LADLLGWkkELEDLV
K339‑ub ADLLGWkkELEDLVR
S356‑p HANIDAQsGsQAPNP
S358‑p NIDAQsGsQAPNPsT
S364‑p GsQAPNPsTTIsPGk
T366 QAPNPsTTIsPGksP
S368‑p PNPsTTIsPGksPPP
K371‑ub sTTIsPGksPPPAKE
S372‑p TTIsPGksPPPAKEA
  SIRT2 iso2  
- gap
- gap
- gap
S17 TQTLGLGSQKERLLD
K19 TLGLGSQKERLLDEL
K19 TLGLGSQKERLLDEL
R39 TRYMQSERCRKVICL
R41 YMQSERCRKVICLVG
S64 IPDFRSPSTGLYANL
T65 PDFRSPSTGLYANLE
Y68 RSPSTGLYANLEKYH
K90 FEISYFKKHPEPFFA
K90 FEISYFKKHPEPFFA
K108 ELYPGQFKPTICHYF
K122 FIRLLKEKGLLLRCY
K166 CVNTSCRKEYTMGWM
G171 CRKEYTMGWMKEKIF
K174 EYTMGWMKEKIFSEA
K176 TMGWMKEKIFSEATP
R184 IFSEATPRCEQCQSV
S235 LQVQPFASLISKAPL
S238 QPFASLISKAPLATP
K251 TPRLLINKEKTGQTD
K251 TPRLLINKEKTGQTD
K276 GGMDFDSKKAYRDVA
R280 FDSKKAYRDVAWLGD
K302 LADLLGWKKELEDLV
K302 LADLLGWKKELEDLV
K303 ADLLGWKKELEDLVR
S320 HANIDAQSGSQAPNP
S322 NIDAQSGSQAPNPST
S328 GSQAPNPSTTIsPGK
T330 QAPNPSTTIsPGKSP
S332‑p PNPSTTIsPGKSPPP
K335 STTIsPGKSPPPAKE
S336 TTIsPGKSPPPAKEA
  rat

► Hide Isoforms
 
- gap
- gap
- gap
S16‑p TQTLGLGsQkERLLD
K18‑ac TLGLGsQkERLLDEL
K18‑ub TLGLGsQkERLLDEL
R38 TRYMQSERCRRVICL
R40 YMQSERCRRVICLVG
S63‑p IPDFRSPsTGLYANL
T64 PDFRSPsTGLYANLE
Y67 RSPsTGLYANLEKYH
K89 FEISYFKKHPEPFFA
K89 FEISYFKKHPEPFFA
K107 ELYPGQFKPTICHYF
K121‑ac FIRLLKEkGLLLRCY
K165 CVNTSCGKEYTMsWM
S170‑p CGKEYTMsWMKEkIF
K173 EYTMsWMKEkIFSEA
K175‑ac TMsWMKEkIFSEATP
K183‑ac IFSEATPkCEKCQNV
S234 LQVQPFASLISKAPL
S237 QPFASLISKAPLATP
K250‑ac TPRLLINkEKTGQTD
K250 TPRLLINKEKTGQTD
K275 GGMDFDSKKAYRDVA
R279 FDSKKAYRDVAWLGD
K301‑ac LADLLGWkELEDLVR
K301 LADLLGWKELEDLVR
- gap
S318 HANIDAQSGSQASNP
S320 NIDAQSGSQASNPsA
S326‑p GSQASNPsATVsPRK
T328 QASNPsATVsPRKsP
S330‑p SNPsATVsPRKsPPP
K333 sATVsPRKsPPPAKE
S334‑p ATVsPRKsPPPAKEA
  SIRT2 iso2  
S23‑p KVQEAQDsDsDTEGG
S25‑p QEAQDsDsDTEGGAT
T27 AQDsDsDTEGGATGG
S53 TQTLGLGSQKERLLD
K55 TLGLGSQKERLLDEL
K55 TLGLGSQKERLLDEL
R75 TRYMQSERCRRVICL
R77 YMQSERCRRVICLVG
S100 IPDFRSPSTGLYANL
T101 PDFRSPSTGLYANLE
Y104 RSPSTGLYANLEKYH
K126 FEISYFKKHPEPFFA
K126 FEISYFKKHPEPFFA
K144 ELYPGQFKPTICHYF
K158 FIRLLKEKGLLLRCY
K202 CVNTSCGKEYTMSWM
S207 CGKEYTMSWMKEKIF
K210 EYTMSWMKEKIFSEA
K212 TMSWMKEKIFSEATP
K220 IFSEATPKCEKCQNV
S343 LQVQPFASLISKAPL
S346 QPFASLISKAPLATP
K359 TPRLLINKEKTGQTD
K359 TPRLLINKEKTGQTD
K384 GGMDFDSKKAYRDVA
R388 FDSKKAYRDVAWLGD
K410 LADLLGWKKELEDLV
K410 LADLLGWKKELEDLV
K411 ADLLGWKKELEDLVR
S428 HANIDAQSGSQASNP
S430 NIDAQSGSQASNPSA
S436 GSQASNPSATVSPRK
T438 QASNPSATVSPRKSP
S440 SNPSATVSPRKSPPP
K443 SATVSPRKSPPPAKE
S444 ATVSPRKSPPPAKEA
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