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Protein Page:
HDAC2 (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
HDAC2 a transcriptional regulator of the histone deacetylase family, subfamily 1. Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays a role in epigenetic repression and transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Deacetylase; Transcription, coactivator/corepressor; EC 3.5.1.98
Chromosomal Location of Human Ortholog: 6q21
Cellular Component: cytoplasm; ESC/E(Z) complex; nuclear chromatin; nucleoplasm; nucleus; NuRD complex; protein complex; Sin3 complex
Molecular Function: chromatin binding; deacetylase activity; enzyme binding; histone deacetylase activity; NF-kappaB binding; nucleosomal DNA binding; protein binding; protein deacetylase activity; sequence-specific DNA binding; transcription factor binding
Biological Process: ATP-dependent chromatin remodeling; blood coagulation; chromatin remodeling; circadian regulation of gene expression; dendrite development; embryonic digit morphogenesis; epidermal cell differentiation; histone deacetylation; maintenance of chromatin silencing; negative regulation of apoptosis; negative regulation of MHC class II biosynthetic process; negative regulation of transcription factor activity; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; odontogenesis of dentine-containing teeth; positive regulation of cell proliferation; positive regulation of collagen biosynthetic process; positive regulation of proteolysis; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent
Reference #:  Q92769 (UniProtKB)
Alt. Names/Synonyms: HD2; HDAC2; Histone deacetylase 2; RPD3; transcriptional regulator homolog RPD3; YAF1; YY1-associated factor 1
Gene Symbols: HDAC2
Molecular weight: 55,364 Da
Basal Isoelectric point: 5.59  Predict pI for various phosphorylation states
CST Pathways:  G1/S Checkpoint  |  NF-kB Signaling  |  Protein Acetylation  |  Wnt/ß-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HDAC2

Protein Structure Not Found.
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Sites Implicated In
apoptosis, induced: S394‑p
transcription, inhibited: Y222‑p
acetylation: S394‑p, S411‑p, S422‑p, S424‑p
enzymatic activity, induced: S394‑p
enzymatic activity, inhibited: S394‑p, S411‑p, S422‑p, S424‑p
molecular association, regulation: S394‑p, S411‑p, S422‑p, S424‑p
protein stabilization: Y222‑p
ubiquitination: Y222‑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

 
0 1 S4 ____MAYSQGGGKKk
0 1 K11‑ub SQGGGKKkVCYYYDG
0 1 T61‑p IYRPHKAtAEEMTkY
0 3 K67‑ub AtAEEMTkYHSDEyI
0 1 Y73‑p TkYHSDEyIkFLRSI
1 2 K75‑ac YHSDEyIkFLRSIRP
0 4 K75‑ub YHSDEyIkFLRSIRP
0 9 Y88‑p RPDNMSEyskQMQRF
0 1 S89‑p PDNMSEyskQMQRFN
1 3 K90‑ac DNMSEyskQMQRFNV
0 77 K90‑ub DNMSEyskQMQRFNV
0 2 Y205‑p SFHKYGEyFPGTGDL
1 2 Y222‑p IGAGKGKyYAVNFPM
0 16 K243‑ub ESYGQIFkPIISkVM
0 1 K248‑ub IFkPIISkVMEMYQP
0 1 K284‑ub LTVKGHAkCVEVVKT
0 1 S349 FKLHISPSNMTNQNt
0 1 T352 HISPSNMTNQNtPEy
0 2 T356‑p SNMTNQNtPEyMEkI
0 3 Y359‑p TNQNtPEyMEkIKQR
0 1 K362‑ub NtPEyMEkIKQRLFE
6 121 S394‑p EDAVHEDsGDEDGED
0 10 S407‑p EDPDKRIsIRAsDKR
2 2 S411‑p KRIsIRAsDKRIACD
3 99 S422‑p IACDEEFsDsEDEGE
4 96 S424‑p CDEEFsDsEDEGEGG
1 1 K462‑sm EDKKTDVkEEDKSKD
0 1 T477‑p NSGEKTDtKGTkSEQ
0 1 K481‑sm KTDtKGTkSEQLSNP
  mouse

 
S4‑p ____MAYsQGGGKKK
K11 sQGGGKKKVCYYYDG
T61 IYRPHKATAEEMTKY
K67 ATAEEMTKYHSDEYI
Y73 TKYHSDEYIkFLRSI
K75‑ac YHSDEYIkFLRSIRP
K75‑ub YHSDEYIkFLRSIRP
Y88‑p RPDNMSEySkQMQRF
S89 PDNMSEySkQMQRFN
K90 DNMSEySKQMQRFNV
K90‑ub DNMSEySkQMQRFNV
Y205 SFHKYGEYFPGTGDL
Y222 IGAGKGKYYAVNFPM
K243‑ub ESYGQIFkPIISKVM
K248 IFkPIISKVMEMYQP
K284 LTVKGHAKCVEVAKT
S349‑p FKLHISPsNMtNQNt
T352‑p HISPsNMtNQNtPEy
T356‑p sNMtNQNtPEyMEKI
Y359‑p tNQNtPEyMEKIKQR
K362 NtPEyMEKIKQRLFE
S394‑p EDAVHEDsGDEDGED
S407 EDPDKRISIRAsDKR
S411‑p KRISIRAsDKRIACD
S422‑p IACDEEFsDsEDEGE
S424‑p CDEEFsDsEDEGEGG
K462 EDKKTDVKEEDKSKD
P477 NSGEKTDPKGAKSEQ
K481 KTDPKGAKSEQLSNP
  rat

 
S4 ____MAYSQGGGKKK
K11 SQGGGKKKVCYYYDG
T61 IYRPHKATAEEMTKY
K67 ATAEEMTKYHSDEYI
Y73 TKYHSDEYIKFLRSI
K75 YHSDEYIKFLRSIRP
K75 YHSDEYIKFLRSIRP
Y88 RPDNMSEYSkQMQRF
S89 PDNMSEYSkQMQRFN
K90‑ac DNMSEYSkQMQRFNV
K90 DNMSEYSKQMQRFNV
Y205 SFHKYGEYFPGTGDL
Y222 IGAGKGKYYAVNFPM
K243 ESYGQIFKPIISKVM
K248 IFKPIISKVMEMYQP
K284 LTVKGHAKCVEVVKT
S349 FKLHISPSNMTNQNT
T352 HISPSNMTNQNTPEY
T356 SNMTNQNTPEYMEKI
Y359 TNQNTPEYMEKIKQR
K362 NTPEYMEKIKQRLFE
S394‑p EDAVHEDsGDEDGED
S407 EDPDKRISIRASDKR
S411 KRISIRASDKRIACD
S422‑p IACDEEFsDsEDEGE
S424‑p CDEEFsDsEDEGEGG
K462 EDKRTDVKEEDKSKD
T477 NSGEKTDTKGAKSEQ
K481 KTDTKGAKSEQLNNP
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