HDAC2_HUMAN - dbPTM
HDAC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC2_HUMAN
UniProt AC Q92769
Protein Name Histone deacetylase 2
Gene Name HDAC2
Organism Homo sapiens (Human).
Sequence Length 488
Subcellular Localization Nucleus . Cytoplasm .
Protein Description 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. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A..
Protein Sequence MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MAYSQGGGKKK
----CCCCCCCCCCE
16.8928348404
92-HydroxyisobutyrylationAYSQGGGKKKVCYYY
CCCCCCCCCEEEEEE
53.33-
9UbiquitinationAYSQGGGKKKVCYYY
CCCCCCCCCEEEEEE
53.3333845483
10UbiquitinationYSQGGGKKKVCYYYD
CCCCCCCCEEEEEEC
54.4322817900
11UbiquitinationSQGGGKKKVCYYYDG
CCCCCCCEEEEEECC
40.8121890473
11 (in isoform 1)Ubiquitination-40.8121890473
21UbiquitinationYYYDGDIGNYYYGQG
EEECCCCCCEEECCC
22.34-
21UbiquitinationYYYDGDIGNYYYGQG
EEECCCCCCEEECCC
22.3427667366
29UbiquitinationNYYYGQGHPMKPHRI
CEEECCCCCCCCCEE
16.05-
32AcetylationYGQGHPMKPHRIRMT
ECCCCCCCCCEECCH
41.9727452117
32UbiquitinationYGQGHPMKPHRIRMT
ECCCCCCCCCEECCH
41.9721963094
37AcetylationPMKPHRIRMTHNLLL
CCCCCEECCHHHHHH
24.73-
37UbiquitinationPMKPHRIRMTHNLLL
CCCCCEECCHHHHHH
24.73-
37MethylationPMKPHRIRMTHNLLL
CCCCCEECCHHHHHH
24.73-
37UbiquitinationPMKPHRIRMTHNLLL
CCCCCEECCHHHHHH
24.7321890473
39PhosphorylationKPHRIRMTHNLLLNY
CCCEECCHHHHHHHH
9.5824719451
45UbiquitinationMTHNLLLNYGLYRKM
CHHHHHHHHHHHHCC
28.88-
45UbiquitinationMTHNLLLNYGLYRKM
CHHHHHHHHHHHHCC
28.8823000965
46PhosphorylationTHNLLLNYGLYRKME
HHHHHHHHHHHHCCE
14.4228258704
49PhosphorylationLLLNYGLYRKMEIYR
HHHHHHHHHCCEEEC
12.1124719451
51UbiquitinationLNYGLYRKMEIYRPH
HHHHHHHCCEEECCC
27.5927667366
55PhosphorylationLYRKMEIYRPHKATA
HHHCCEEECCCCCCH
12.5628258704
59UbiquitinationMEIYRPHKATAEEMT
CEEECCCCCCHHHHH
50.5529967540
60AcetylationEIYRPHKATAEEMTK
EEECCCCCCHHHHHH
14.70-
60UbiquitinationEIYRPHKATAEEMTK
EEECCCCCCHHHHHH
14.70-
60UbiquitinationEIYRPHKATAEEMTK
EEECCCCCCHHHHHH
14.7023000965
61PhosphorylationIYRPHKATAEEMTKY
EECCCCCCHHHHHHH
39.13-
65SulfoxidationHKATAEEMTKYHSDE
CCCCHHHHHHHCCHH
2.7030846556
66PhosphorylationKATAEEMTKYHSDEY
CCCHHHHHHHCCHHH
31.5629496907
67AcetylationATAEEMTKYHSDEYI
CCHHHHHHHCCHHHH
39.3923236377
67UbiquitinationATAEEMTKYHSDEYI
CCHHHHHHHCCHHHH
39.3921963094
67 (in isoform 1)Ubiquitination-39.3921890473
68NitrationTAEEMTKYHSDEYIK
CHHHHHHHCCHHHHH
9.44-
68PhosphorylationTAEEMTKYHSDEYIK
CHHHHHHHCCHHHHH
9.4428152594
70PhosphorylationEEMTKYHSDEYIKFL
HHHHHHCCHHHHHHH
29.1028152594
73NitrationTKYHSDEYIKFLRSI
HHHCCHHHHHHHHHH
17.88-
73PhosphorylationTKYHSDEYIKFLRSI
HHHCCHHHHHHHHHH
17.8830576142
75AcetylationYHSDEYIKFLRSIRP
HCCHHHHHHHHHHCC
37.1319608861
75SumoylationYHSDEYIKFLRSIRP
HCCHHHHHHHHHHCC
37.1328112733
75UbiquitinationYHSDEYIKFLRSIRP
HCCHHHHHHHHHHCC
37.1323000965
75 (in isoform 1)Ubiquitination-37.1321890473
86PhosphorylationSIRPDNMSEYSKQMQ
HHCCCCHHHHHHHHH
39.3728450419
88PhosphorylationRPDNMSEYSKQMQRF
CCCCHHHHHHHHHHC
17.54-
89PhosphorylationPDNMSEYSKQMQRFN
CCCHHHHHHHHHHCC
16.6220860994
90SumoylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.22-
90AcetylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.2222641419
90MethylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.2222641419
90NeddylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.2232015554
90SumoylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.22-
90UbiquitinationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC
49.2227667366
90 (in isoform 1)Ubiquitination-49.2221890473
115UbiquitinationFEFCQLSTGGSVAGA
HHHCCCCCCCCHHHE
54.90-
144UbiquitinationAGGLHHAKKSEASGF
CCCCCCCCHHCCCCC
53.1029967540
145UbiquitinationGGLHHAKKSEASGFC
CCCCCCCHHCCCCCH
55.07-
167NitrationAILELLKYHQRVLYI
HHHHHHHHHCCEEEE
11.80-
171UbiquitinationLLKYHQRVLYIDIDI
HHHHHCCEEEEEEEE
3.71-
171UbiquitinationLLKYHQRVLYIDIDI
HHHHHCCEEEEEEEE
3.7121890473
173NitrationKYHQRVLYIDIDIHH
HHHCCEEEEEEEECC
8.16-
189UbiquitinationDGVEEAFYTTDRVMT
CCHHHEEEECCCEEE
18.7722817900
191AcetylationVEEAFYTTDRVMTVS
HHHEEEECCCEEEEE
15.49-
191UbiquitinationVEEAFYTTDRVMTVS
HHHEEEECCCEEEEE
15.49-
191UbiquitinationVEEAFYTTDRVMTVS
HHHEEEECCCEEEEE
15.4921963094
196PhosphorylationYTTDRVMTVSFHKYG
EECCCEEEEEEEECC
15.3320068231
198PhosphorylationTDRVMTVSFHKYGEY
CCCEEEEEEEECCCC
16.6820068231
201UbiquitinationVMTVSFHKYGEYFPG
EEEEEEEECCCCCCC
53.6023000965
201 (in isoform 1)Ubiquitination-53.6021890473
202PhosphorylationMTVSFHKYGEYFPGT
EEEEEEECCCCCCCC
13.4528152594
205PhosphorylationSFHKYGEYFPGTGDL
EEEECCCCCCCCCCC
15.6528152594
213UbiquitinationFPGTGDLRDIGAGKG
CCCCCCCEECCCCCC
37.94-
213UbiquitinationFPGTGDLRDIGAGKG
CCCCCCCEECCCCCC
37.9423000965
218UbiquitinationDLRDIGAGKGKYYAV
CCEECCCCCCCEEEE
33.7523000965
219UbiquitinationLRDIGAGKGKYYAVN
CEECCCCCCCEEEEE
52.2622817900
221AcetylationDIGAGKGKYYAVNFP
ECCCCCCCEEEEEEE
38.2825953088
221UbiquitinationDIGAGKGKYYAVNFP
ECCCCCCCEEEEEEE
38.2821963094
222PhosphorylationIGAGKGKYYAVNFPM
CCCCCCCEEEEEEEC
12.8227811184
237PhosphorylationRDGIDDESYGQIFKP
CCCCCCCCHHHHHHH
41.3720068231
238PhosphorylationDGIDDESYGQIFKPI
CCCCCCCHHHHHHHH
15.8223090842
243AcetylationESYGQIFKPIISKVM
CCHHHHHHHHHHHHH
36.6226051181
243NeddylationESYGQIFKPIISKVM
CCHHHHHHHHHHHHH
36.6232015554
243UbiquitinationESYGQIFKPIISKVM
CCHHHHHHHHHHHHH
36.6223000965
243 (in isoform 1)Ubiquitination-36.6221890473
248UbiquitinationIFKPIISKVMEMYQP
HHHHHHHHHHHHHCC
34.8823000965
250UbiquitinationKPIISKVMEMYQPSA
HHHHHHHHHHHCCCE
2.55-
250UbiquitinationKPIISKVMEMYQPSA
HHHHHHHHHHHCCCE
2.5521963094
253NitrationISKVMEMYQPSAVVL
HHHHHHHHCCCEEEE
12.17-
254UbiquitinationSKVMEMYQPSAVVLQ
HHHHHHHCCCEEEEE
24.94-
254UbiquitinationSKVMEMYQPSAVVLQ
HHHHHHHCCCEEEEE
24.9422817900
262S-nitrosocysteinePSAVVLQCGADSLSG
CCEEEEECCCCCCCC
4.19-
262S-nitrosylationPSAVVLQCGADSLSG
CCEEEEECCCCCCCC
4.1919047631
274S-nitrosocysteineLSGDRLGCFNLTVKG
CCCCCEECEEEEECC
2.12-
274S-nitrosylationLSGDRLGCFNLTVKG
CCCCCEECEEEEECC
2.1219047631
280UbiquitinationGCFNLTVKGHAKCVE
ECEEEEECCCCEEEE
39.4821963094
284UbiquitinationLTVKGHAKCVEVVKT
EEECCCCEEEEEEHH
32.8922817900
291PhosphorylationKCVEVVKTFNLPLLM
EEEEEEHHCCCCEEE
13.2220068231
304PhosphorylationLMLGGGGYTIRNVAR
EEECCCCCHHHCHHH
11.4120068231
305PhosphorylationMLGGGGYTIRNVARC
EECCCCCHHHCHHHC
19.4117081983
332AcetylationIPNELPYNDYFEYFG
CCCCCCCCCCHHHHC
35.25-
332UbiquitinationIPNELPYNDYFEYFG
CCCCCCCCCCHHHHC
35.2521890473
332UbiquitinationIPNELPYNDYFEYFG
CCCCCCCCCCHHHHC
35.2521963094
334UbiquitinationNELPYNDYFEYFGPD
CCCCCCCCHHHHCCC
8.48-
334PhosphorylationNELPYNDYFEYFGPD
CCCCCCCCHHHHCCC
8.48-
334UbiquitinationNELPYNDYFEYFGPD
CCCCCCCCHHHHCCC
8.4822817900
337PhosphorylationPYNDYFEYFGPDFKL
CCCCCHHHHCCCCEE
12.16-
343SumoylationEYFGPDFKLHISPSN
HHHCCCCEEEECCCC
46.68-
347PhosphorylationPDFKLHISPSNMTNQ
CCCEEEECCCCCCCC
16.1327050516
349PhosphorylationFKLHISPSNMTNQNT
CEEEECCCCCCCCCC
32.2329214152
356PhosphorylationSNMTNQNTPEYMEKI
CCCCCCCCHHHHHHH
14.0325159151
359PhosphorylationTNQNTPEYMEKIKQR
CCCCCHHHHHHHHHH
16.2728064214
362AcetylationNTPEYMEKIKQRLFE
CCHHHHHHHHHHHHH
38.3823236377
362NeddylationNTPEYMEKIKQRLFE
CCHHHHHHHHHHHHH
38.3832015554
362UbiquitinationNTPEYMEKIKQRLFE
CCHHHHHHHHHHHHH
38.3821963094
362 (in isoform 1)Ubiquitination-38.3821890473
364UbiquitinationPEYMEKIKQRLFENL
HHHHHHHHHHHHHHH
40.2022817900
366MethylationYMEKIKQRLFENLRM
HHHHHHHHHHHHHCC
36.02-
394PhosphorylationEDAVHEDSGDEDGED
CCCCCCCCCCCCCCC
45.2029255136
407O-linked_GlycosylationEDPDKRISIRASDKR
CCCCCCEEEEECCCE
15.2830379171
407PhosphorylationEDPDKRISIRASDKR
CCCCCCEEEEECCCE
15.2825159151
409UbiquitinationPDKRISIRASDKRIA
CCCCEEEEECCCEEE
22.65-
409UbiquitinationPDKRISIRASDKRIA
CCCCEEEEECCCEEE
22.6522053931
410UbiquitinationDKRISIRASDKRIAC
CCCEEEEECCCEEEC
22.02-
410UbiquitinationDKRISIRASDKRIAC
CCCEEEEECCCEEEC
22.0222053931
411PhosphorylationKRISIRASDKRIACD
CCEEEEECCCEEECC
33.5425159151
422PhosphorylationIACDEEFSDSEDEGE
EECCCCCCCCCCCCC
43.4329255136
424PhosphorylationCDEEFSDSEDEGEGG
CCCCCCCCCCCCCCC
45.8329255136
4392-HydroxyisobutyrylationRRNVADHKKGAKKAR
CCCHHHHHHHHHHHH
54.15-
439UbiquitinationRRNVADHKKGAKKAR
CCCHHHHHHHHHHHH
54.1522053931
440UbiquitinationRNVADHKKGAKKARI
CCHHHHHHHHHHHHH
61.7622053931
452SumoylationARIEEDKKETEDKKT
HHHHHHHHHCCHHCC
80.3928112733
458SumoylationKKETEDKKTDVKEED
HHHCCHHCCCCCHHH
63.3828112733
459O-linked_GlycosylationKETEDKKTDVKEEDK
HHCCHHCCCCCHHHH
52.3330379171
462SumoylationEDKKTDVKEEDKSKD
CHHCCCCCHHHHCCC
59.19-
462SumoylationEDKKTDVKEEDKSKD
CHHCCCCCHHHHCCC
59.1928112733
477PhosphorylationNSGEKTDTKGTKSEQ
CCCCCCCCCCCCHHH
36.28-
478SumoylationSGEKTDTKGTKSEQL
CCCCCCCCCCCHHHC
68.3528112733
481SumoylationKTDTKGTKSEQLSNP
CCCCCCCCHHHCCCC
61.74-
481AcetylationKTDTKGTKSEQLSNP
CCCCCCCCHHHCCCC
61.7426051181
481SumoylationKTDTKGTKSEQLSNP
CCCCCCCCHHHCCCC
61.7428112733
481UbiquitinationKTDTKGTKSEQLSNP
CCCCCCCCHHHCCCC
61.7433845483
486PhosphorylationGTKSEQLSNP-----
CCCHHHCCCC-----
46.9128985074

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
222YPhosphorylationKinaseABL1P00519
GPS
394SPhosphorylationKinaseCSNK2A1P68400
GPS
394SPhosphorylationKinaseCK2-FAMILY-GPS
394SPhosphorylationKinaseCK2_GROUP-PhosphoELM
422SPhosphorylationKinaseCK2-FAMILY-GPS
422SPhosphorylationKinaseCK2_GROUP-PhosphoELM
424SPhosphorylationKinaseCK2-FAMILY-GPS
424SPhosphorylationKinaseCK2_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseHUWE1Q7Z6Z7
PMID:22016339
-KUbiquitinationE3 ubiquitin ligaseRLIMQ9NVW2
PMID:12840003

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
262CAcetylation

-
262CS-nitrosylation

-
274CAcetylation

-
274CS-nitrosylation

-

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 HDAC2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
12032298
HM20B_HUMANHMG20Bphysical
12032298
PF21A_HUMANPHF21Aphysical
15325272
CDYL_HUMANCDYLphysical
12947414
SIN3A_HUMANSIN3Aphysical
12943729
CHD3_HUMANCHD3physical
12493763
CHD4_HUMANCHD4physical
12493763
MTA1_HUMANMTA1physical
12493763
MTA2_HUMANMTA2physical
12493763
RBBP4_HUMANRBBP4physical
12493763
RBBP7_HUMANRBBP7physical
12493763
ZMYM3_HUMANZMYM3physical
12493763
ZMYM2_HUMANZMYM2physical
12493763
GSE1_HUMANGSE1physical
12493763
GTF2I_HUMANGTF2Iphysical
12493763
KDM1A_HUMANKDM1Aphysical
12493763
PF21A_HUMANPHF21Aphysical
12493763
HM20B_HUMANHMG20Bphysical
12493763
HDAC1_HUMANHDAC1physical
12493763
HDAC2_HUMANHDAC2physical
12493763
SIN3A_HUMANSIN3Aphysical
12493763
SETB1_HUMANSETDB1physical
12398767
TYY1_HUMANYY1physical
9346952
GTF2I_HUMANGTF2Iphysical
12393887
HDAC1_HUMANHDAC1physical
11777905
HSP74_HUMANHSPA4physical
11777905
TOP2B_HUMANTOP2Bphysical
11062478
TOP2A_HUMANTOP2Aphysical
11062478
SNW1_HUMANSNW1physical
10644367
DNMT1_HUMANDNMT1physical
10888872
HDAC1_HUMANHDAC1physical
11739383
HDA10_HUMANHDAC10physical
11739383
CHD4_HUMANCHD4physical
10545197
ATR_HUMANATRphysical
10545197
RCOR1_HUMANRCOR1physical
11171972
PML_HUMANPMLphysical
11259576
RB_HUMANRB1physical
10490602
RBL1_HUMANRBL1physical
10490602
FKBP3_HUMANFKBP3physical
11532945
SIN3A_HUMANSIN3Aphysical
9150134
MAD1_HUMANMXD1physical
9150134
PPARD_HUMANPPARDphysical
11867749
MTA1_HUMANMTA1physical
11146623
DAXX_HUMANDAXXphysical
10669754
SIN3A_HUMANSIN3Aphysical
12091390
CHD4_HUMANCHD4physical
9804427
KDM1A_HUMANKDM1Aphysical
9804427
HDAC1_HUMANHDAC1physical
9804427
RBBP4_HUMANRBBP4physical
9804427
CHD3_HUMANCHD3physical
9804427
CABIN_HUMANCABIN1physical
10933397
HDAC1_HUMANHDAC1physical
9520398
VHL_HUMANVHLphysical
11641274
HIF1N_HUMANHIF1ANphysical
11641274
HIF1A_HUMANHIF1Aphysical
11641274
MTG8_HUMANRUNX1T1physical
11533236
MTG16_HUMANCBFA2T3physical
11533236
CHD3_HUMANCHD3physical
12198550
SMC3_HUMANSMC3physical
12198550
SMCA5_HUMANSMARCA5physical
12198550
EED_HUMANEEDphysical
10581039
EZH2_HUMANEZH2physical
10581039
HDAC1_HUMANHDAC1physical
10581039
HAIR_HUMANHRphysical
11641275
TYY1_HUMANYY1physical
9016636
TF65_HUMANRELAphysical
12138131
PRDM1_HUMANPRDM1physical
12626569
FOXP3_HUMANFOXP3physical
19276356
NSD2_HUMANWHSC1physical
18156491
PRDM1_HUMANPRDM1physical
19124609
PADI4_HUMANPADI4physical
20190809
GLI1_HUMANGLI1physical
20081843
MTA1_HUMANMTA1physical
20071335
SMCA4_HUMANSMARCA4physical
19081374
HSF1_HUMANHSF1physical
19793920
HDAC1_HUMANHDAC1physical
19041848
MBD3_HUMANMBD3physical
19041848
C2TA_HUMANCIITAphysical
19041327
SMAD7_HUMANSMAD7physical
15831498
HELLS_HUMANHELLSphysical
19561196
CREST_HUMANSS18L1physical
20211142
PML_HUMANPMLphysical
18644863
SNAI1_HUMANSNAI1physical
14673164
SNAI2_HUMANSNAI2physical
14673164
SNAI3_HUMANSNAI3physical
14673164
LMO4_HUMANLMO4physical
16288053
ESCO2_HUMANESCO2physical
18501190
C2TA_HUMANCIITAphysical
12697811
BC11B_HUMANBCL11Bphysical
16091750
HDAC1_HUMANHDAC1physical
11919195
SP1_HUMANSP1physical
16036112
CTBP1_HUMANCTBP1physical
16036112
SMAD7_HUMANSMAD7physical
15831516
SMCA5_HUMANSMARCA5physical
15775975
CCND1_HUMANCCND1physical
15713663
RB_HUMANRB1physical
11593423
IKBA_HUMANNFKBIAphysical
15536134
MTA2_HUMANMTA2physical
11102443
RCOR1_HUMANRCOR1physical
11102443
KDM1A_HUMANKDM1Aphysical
11102443
HDAC1_HUMANHDAC1physical
15297431
PHB2_HUMANPHB2physical
15140878
SMN_HUMANSMN1physical
14749338
SIN3A_HUMANSIN3Aphysical
14749338
HELLS_HUMANHELLSphysical
17967891
DNMT1_HUMANDNMT1physical
17967891
CTBP1_HUMANCTBP1physical
17967884
RBBP4_HUMANRBBP4physical
17827154
RARA_HUMANRARAphysical
21383775
ESR1_HUMANESR1physical
17312152
SP1_HUMANSP1physical
17312152
OVOL1_HUMANOVOL1physical
17311813
SP3_HUMANSP3physical
17548428
CSK21_HUMANCSNK2A1physical
20388487
P53_HUMANTP53physical
20388487
HDAC1_HUMANHDAC1physical
20388487
SAP30_HUMANSAP30physical
20388487
RBBP7_HUMANRBBP7physical
20388487
RBBP4_HUMANRBBP4physical
20388487
MBD3_HUMANMBD3physical
20388487
TF65_HUMANRELAphysical
20388487
CBP_HUMANCREBBPphysical
20388487
PARP1_HUMANPARP1physical
20596014
SMCA4_HUMANSMARCA4physical
20596014
DEC1_HUMANDEC1physical
21317427
KLF4_HUMANKLF4physical
21252119
ESCO1_HUMANESCO1physical
20331966
SNAI1_HUMANSNAI1physical
20534591
DDX53_HUMANDDX53physical
20534591
TF65_HUMANRELAphysical
20065107
MYCN_HUMANMYCNphysical
20697349
SP1_HUMANSP1physical
20697349
H2AY_HUMANH2AFYphysical
16107708
H2AY_HUMANH2AFYphysical
17474147
CHD4_HUMANCHD4physical
9885572
CHD3_HUMANCHD3physical
9885572
HDAC2_HUMANHDAC2physical
9885572
RBBP4_HUMANRBBP4physical
9885572
MTA1_HUMANMTA1physical
9885572
PP6R3_HUMANPPP6R3physical
9885572
SP130_HUMANSAP130physical
9885572
SIN3A_HUMANSIN3Aphysical
9885572
RBBP7_HUMANRBBP7physical
9885572
SAP30_HUMANSAP30physical
9885572
PAR14_HUMANPARP14physical
21081493
H31T_HUMANHIST3H3physical
12700765
SIN3A_HUMANSIN3Aphysical
12082111
SENP1_HUMANSENP1physical
22493095
SIN3A_HUMANSIN3Aphysical
22493095
RNF12_HUMANRLIMphysical
22493095
UBE2H_HUMANUBE2Hphysical
22493095
TWST1_HUMANTWIST1physical
22457607
KBZIP_HHV8PK8physical
22416134
HDAC1_HUMANHDAC1physical
22416134
VHL_HUMANVHLphysical
22286234
MYC_HUMANMYCphysical
22286234
EZH2_HUMANEZH2physical
21685935
SNAI1_HUMANSNAI1physical
21685935
ZFP1_HUMANZFP1physical
21540836
NFAC1_HUMANNFATC1physical
19218564
RBBP4_HUMANRBBP4physical
22939629
RBBP7_HUMANRBBP7physical
22939629
MBD3_HUMANMBD3physical
22939629
MTA2_HUMANMTA2physical
22939629
SMCA5_HUMANSMARCA5physical
22939629
SNF5_HUMANSMARCB1physical
22939629
P66A_HUMANGATAD2Aphysical
22939629
SUZ12_HUMANSUZ12physical
22939629
SRSF9_HUMANSRSF9physical
22939629
ZMYM2_HUMANZMYM2physical
21258344
RCOR2_HUMANRCOR2physical
21258344
RCOR3_HUMANRCOR3physical
21258344
ZMYM3_HUMANZMYM3physical
21258344
GSE1_HUMANGSE1physical
21258344
HM20B_HUMANHMG20Bphysical
21258344
KDM1A_HUMANKDM1Aphysical
21258344
RCOR1_HUMANRCOR1physical
21258344
HM20A_HUMANHMG20Aphysical
21258344
TDIF1_HUMANDNTTIP1physical
21258344
EMSA1_HUMANELMSAN1physical
21258344
MIER1_HUMANMIER1physical
21258344
MIER2_HUMANMIER2physical
21258344
MIER3_HUMANMIER3physical
21258344
RERE_HUMANREREphysical
21258344
HDAC1_HUMANHDAC1physical
21258344
RBBP7_HUMANRBBP7physical
21258344
RBBP4_HUMANRBBP4physical
21258344
CDKA1_HUMANCDK2AP1physical
21258344
MBD3_HUMANMBD3physical
21258344
MBD2_HUMANMBD2physical
21258344
P66B_HUMANGATAD2Bphysical
21258344
P66A_HUMANGATAD2Aphysical
21258344
MTA3_HUMANMTA3physical
21258344
MTA1_HUMANMTA1physical
21258344
CHD4_HUMANCHD4physical
21258344
MTA2_HUMANMTA2physical
21258344
EHMT1_HUMANEHMT1physical
21258344
BRMS1_HUMANBRMS1physical
21258344
WIZ_HUMANWIZphysical
21258344
RREB1_HUMANRREB1physical
21258344
EHMT2_HUMANEHMT2physical
21258344
CDYL_HUMANCDYLphysical
21258344
SP30L_HUMANSAP30Lphysical
21258344
SAP30_HUMANSAP30physical
21258344
SIN3A_HUMANSIN3Aphysical
21258344
SIN3B_HUMANSIN3Bphysical
21258344
ACL6A_HUMANACTL6Aphysical
23752268
SYNC_HUMANNARSphysical
23752268
ARI4B_HUMANARID4Bphysical
23752268
ARI5B_HUMANARID5Bphysical
23752268
BC11A_HUMANBCL11Aphysical
23752268
BC11B_HUMANBCL11Bphysical
23752268
BRMS1_HUMANBRMS1physical
23752268
CDYL_HUMANCDYLphysical
23752268
CHD3_HUMANCHD3physical
23752268
CHD4_HUMANCHD4physical
23752268
CDKA1_HUMANCDK2AP1physical
23752268
DP13A_HUMANAPPL1physical
23752268
TDIF1_HUMANDNTTIP1physical
23752268
DNJA1_HUMANDNAJA1physical
23752268
GSE1_HUMANGSE1physical
23752268
HM20A_HUMANHMG20Aphysical
23752268
HDAC1_HUMANHDAC1physical
23752268
HDAC2_HUMANHDAC2physical
23752268
SP130_HUMANSAP130physical
23752268
IMA5_HUMANKPNA1physical
23752268
IPO5_HUMANIPO5physical
23752268
KDM1A_HUMANKDM1Aphysical
23752268
MIER1_HUMANMIER1physical
23752268
MTA1_HUMANMTA1physical
23752268
MTA2_HUMANMTA2physical
23752268
MTA3_HUMANMTA3physical
23752268
MBD2_HUMANMBD2physical
23752268
MBD3_HUMANMBD3physical
23752268
SIN3A_HUMANSIN3Aphysical
23752268
PF21A_HUMANPHF21Aphysical
23752268
EMSY_HUMANC11orf30physical
23752268
RREB1_HUMANRREB1physical
23752268
RCOR1_HUMANRCOR1physical
23752268
RCOR2_HUMANRCOR2physical
23752268
RCOR3_HUMANRCOR3physical
23752268
SRRM2_HUMANSRRM2physical
23752268
SDS3_HUMANSUDS3physical
23752268
HM20B_HUMANHMG20Bphysical
23752268
TXND5_HUMANTXNDC5physical
23752268
P66A_HUMANGATAD2Aphysical
23752268
P66B_HUMANGATAD2Bphysical
23752268
RU17_HUMANSNRNP70physical
23752268
EMSA1_HUMANELMSAN1physical
23752268
CP087_HUMANC16orf87physical
23752268
ZMYM2_HUMANZMYM2physical
23752268
ZN217_HUMANZNF217physical
23752268
HDAC1_HUMANHDAC1physical
17894944
SP1_HUMANSP1physical
17894944
H31_HUMANHIST1H3Aphysical
12626569
H2A2C_HUMANHIST2H2ACphysical
12626569
H2B2E_HUMANHIST2H2BEphysical
12626569
NACC2_HUMANNACC2physical
22926524
DNMT1_HUMANDNMT1physical
23708667
CUL4B_HUMANCUL4Bphysical
25189618
DDB1_HUMANDDB1physical
25189618
CHFR_HUMANCHFRphysical
19182791
DDX5_HUMANDDX5physical
20663877
DDX17_HUMANDDX17physical
20663877
BRMS1_HUMANBRMS1physical
14581478
APEX1_HUMANAPEX1physical
14633989
RPC9_HUMANCRCPphysical
26344197
MTA1_HUMANMTA1physical
26344197
MTA2_HUMANMTA2physical
26344197
MTA3_HUMANMTA3physical
26344197
SIN3A_HUMANSIN3Aphysical
26344197
SUZ12_HUMANSUZ12physical
26344197
NRIP1_HUMANNRIP1physical
15060175
HDAC1_HUMANHDAC1physical
25241761
CADH1_HUMANCDH1physical
25241761
HIF1A_HUMANHIF1Aphysical
25241761
STAT3_HUMANSTAT3physical
25241761
PPARD_HUMANPPARDphysical
25241761
TF65_HUMANRELAphysical
25241761
UBP4_HUMANUSP4physical
26411366
DCAF1_HUMANVPRBPphysical
26679995
DDB1_HUMANDDB1physical
26679995
U17L2_HUMANUSP17L2physical
26617781
UBP19_HUMANUSP19physical
27517492
SMCA4_HUMANSMARCA4genetic
28319113
MP2K1_HUMANMAP2K1genetic
28319113
VHL_HUMANVHLgenetic
28319113
BUB1B_HUMANBUB1Bphysical
28985013
ZN827_HUMANZNF827physical
25150861

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
DB01223Aminophylline
DB00227Lovastatin
DB01303Oxtriphylline
DB00277Theophylline
DB00313Valproic Acid
DB02546Vorinostat
Regulatory Network of HDAC2_HUMAN

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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
"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.
"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.
"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.
"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.
"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.
"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.
"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.
"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, 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.

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