Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone deacetylase 2  

UniProtKB / Swiss-Prot ID :  HDAC2_HUMAN

Gene Name (Synonyms) : 
HDAC2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. 

Protein Sequence MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHS...
Predicted Secondary Structure CCCCCCCCCCEEEEEECCHHHCCCCCCCCCCCHHHHHHHHHHHHHCCCCCCCEEECCCCCCHHHHHHCCC...
Protein Variant
LocationDescription
230R -> C (in dbSNP:rs1042903). VAR_025311
315Y -> H (in dbSNP:rs17852888). VAR_025312
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGKKKVCYY
CCCCEEEEE
40.81Phosphositeplus
Link
67Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEMTKYHSD
HHHHHCCCH
39.39Phosphositeplus
Link
75Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEYIKFLRS
HHHHHHHHH
37.13Phosphositeplus
Link
75N6-acetyllysineDEYIKFLRS
HHHHHHHHH
37.13Phosphositeplus
Link
75N6-acetyllysine.DEYIKFLRS
HHHHHHHHH
37.13UniProtKB
Link
90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SEYSKQMQR
HHHHHHHCC
49.22Phosphositeplus
Link
90N6-acetyllysine.SEYSKQMQR
HHHHHHHCC
49.22UniProtKB
Link
243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GQIFKPIIS
HHHHHHHHH
36.62Phosphositeplus
Link
262S-nitrosocysteineVVLQCGADS
EEEECCCHH
4.19dbSNO
Link
274S-nitrosocysteineDRLGCFNLT
CCCCEEEEC
2.12dbSNO
Link
304PhosphotyrosineGGGGYTIRN
ECCCCCHHH
11.41SysPTM
Link
362Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EYMEKIKQR
HHHHHHHHH
38.38Phosphositeplus
Link
394PhosphoserineVHEDSGDED
CCCCCHHHH
45.20Phosphositeplus
Link-
394PhosphoserineVHEDSGDED
CCCCCHHHH
45.20SysPTM
Link-
394PhosphoserineVHEDSGDED
CCCCCHHHH
45.20SysPTM
Link-
394Phosphoserine (CK2_group;CK2_alpha)VHEDSGDED
CCCCCHHHH
45.20PhosphoELM
Link-
394Phosphoserine.VHEDSGDED
CCCCCHHHH
45.20UniProtKB
Link-
407PhosphoserineDKRISIRAS
CCCCCHHHC
15.28PhosphoELM
Link-
407PhosphoserineDKRISIRAS
CCCCCHHHC
15.28Phosphositeplus
Link-
407PhosphoserineDKRISIRAS
CCCCCHHHC
15.28SysPTM
Link-
407Phosphoserine.DKRISIRAS
CCCCCHHHC
15.28UniProtKB
Link-
411PhosphoserineSIRASDKRI
CHHHCCCCC
33.54Phosphositeplus
Link-
422PhosphoserineDEEFSDSED
CCCCCCCCC
43.43Phosphositeplus
Link-
422PhosphoserineDEEFSDSED
CCCCCCCCC
43.43SysPTM
Link-
422Phosphoserine (CK2_group)DEEFSDSED
CCCCCCCCC
43.43PhosphoELM
Link-
422Phosphoserine.DEEFSDSED
CCCCCCCCC
43.43UniProtKB
Link-
424PhosphoserineEFSDSEDEG
CCCCCCCCC
45.83Phosphositeplus
Link-
424PhosphoserineEFSDSEDEG
CCCCCCCCC
45.83SysPTM
Link-
424Phosphoserine (CK2_group)EFSDSEDEG
CCCCCCCCC
45.83PhosphoELM
Link-
424Phosphoserine.EFSDSEDEG
CCCCCCCCC
45.83UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SUV91_HUMANphysical interactionMINT-18658MINT11788710
SUV91_HUMANphysical interactionMINT-18659MINT11788710
RB_HUMANphysical interactionMINT-73396MINT10228159
NPM_HUMANphysical interactionMINT-4544944MINT17318229
MYBB_HUMANphysical interactionMINT-4054286MINT17159899
HDAC1_HUMANphysical interactionMINT-16048MINT11287668
BC11B_HUMANphysical interactionMINT-4298980MINT17245431
CIR_HUMANphysical interactionEBI-633387
intact9874765
MBD1_HUMANphysical interaction
physical interaction
EBI-994784
EBI-994861
intact12711603
12711603
SUV91_HUMANphysical interaction
physical interaction
physical interaction
EBI-994754
EBI-994747
EBI-994
intact12711603
12711603
12711603
RFX5_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-937037
EBI-937031
EBI-923
intact16464847
16464847
16464847
16464847
SIN3B_HUMANphysical interactionEBI-923305
intact16464847
BRCA1_HUMANin vitro
in vivo
HPRD:05521HPRD10220405
DNMT1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05521HPRD10888872
TOP2A_HUMANin vivoHPRD:05521HPRD11062478
TF65_HUMANin vitro
in vivo
HPRD:05521HPRD12138131
12419806
TYY1_HUMANin vitro
in vivo
HPRD:05521HPRD11486036
MAD1_HUMANin vivoHPRD:05521HPRD9150134
FKBP3_HUMANin vitro
in vivo
HPRD:05521HPRD11532945
SUV91_HUMANin vitro
in vivo
HPRD:05521HPRD11788710
PTMA_HUMANin vitroHPRD:05521HPRD12634383
SP1_HUMANin vivoHPRD:05521HPRD12151407
ARI4A_HUMANin vivoHPRD:05521HPRD10490602
SP3_HUMANin vivoHPRD:05521HPRD12151407
RUNX3_HUMANin vitro
in vivo
HPRD:05521HPRD15138260
ING1_HUMANin vivoHPRD:05521HPRD15451426
HDAC1_HUMANin vitro
in vivo
HPRD:05521HPRD15451426
9520398
11287668
PPARD_HUMANin vivoHPRD:05521HPRD11867749
IFRD1_HUMANin vitro
in vivo
HPRD:05521HPRD12198164
MTA1_HUMANin vitro
in vivo
HPRD:05521HPRD11146623
MBD2_HUMANin vitro
in vivo
HPRD:05521HPRD10471499
RBBP7_HUMANin vivoHPRD:05521HPRD15451426
RBBP4_HUMANin vitro
in vivo
HPRD:05521HPRD15451426
12943729
12091390
11302704
CDYL1_HUMANin vitro
in vivo
HPRD:05521HPRD12947414
IKZF1_HUMANin vitro
in vivo
HPRD:05521HPRD10357820
SNW1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:05521HPRD10644367
CTBP1_HUMANin vitro
in vivo
HPRD:05521HPRD10766745
11022042
PA2G4_HUMANin vitroHPRD:05521HPRD12682367
PP1R8_HUMANin vitro
in vivo
HPRD:05521HPRD12788942
SALL1_HUMANin vitroHPRD:05521HPRD11836251
SAP30_HUMANin vivoHPRD:05521HPRD15451426
DMAP1_HUMANin vivo
yeast 2-hybrid
HPRD:05521HPRD10888872
STAT3_HUMANin vivoHPRD:05521HPRD15653507
SMCA5_HUMANin vivoHPRD:05521HPRD15775975
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB01223Aminophylline
DB00227Lovastatin
DB01303Oxtriphylline
DB00277Theophylline
DB00313Valproic Acid
DB02546Vorinostat
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75 AND LYS-90, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-394; SER-422 ANDSER-424, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; SER-422 ANDSER-424, AND MASS SPECTROMETRY.
"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-394, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY.
"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-394; SER-407; SER-422AND SER-424, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 ANDSER-424, AND MASS SPECTROMETRY.
"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-394, AND MASSSPECTROMETRY.
"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 SER-394; SER-422 ANDSER-424, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures