HDAC5_HUMAN - dbPTM
HDAC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC5_HUMAN
UniProt AC Q9UQL6
Protein Name Histone deacetylase 5
Gene Name HDAC5
Organism Homo sapiens (Human).
Sequence Length 1122
Subcellular Localization Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its p
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. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer..
Protein Sequence MNSPNESDGMSGREPSLEILPRTSLHSIPVTVEVKPVLPRAMPSSMGGGGGGSPSPVELRGALVGSVDPTLREQQLQQELLALKQQQQLQKQLLFAEFQKQHDHLTRQHEVQLQKHLKQQQEMLAAKQQQEMLAAKRQQELEQQRQREQQRQEELEKQRLEQQLLILRNKEKSKESAIASTEVKLRLQEFLLSKSKEPTPGGLNHSLPQHPKCWGAHHASLDQSSPPQSGPPGTPPSYKLPLPGPYDSRDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGTVISTFKKRAVEITGAGPGASSVCNSAPGSGPSSPNSSHSTIAENGFTGSVPNIPTEMLPQHRALPLDSSPNQFSLYTSPSLPNISLGLQATVTVTNSHLTASPKLSTQQEAERQALQSLRQGGTLTGKFMSTSSIPGCLLGVALEGDGSPHGHASLLQHVLLLEQARQQSTLIAVPLHGQSPLVTGERVATSMRTVGKLPRHRPLSRTQSSPLPQSPQALQQLVMQQQHQQFLEKQKQQQLQLGKILTKTGELPRQPTTHPEETEEELTEQQEVLLGEGALTMPREGSTESESTQEDLEEEDEEDDGEEEEDCIQVKDEEGESGAEEGPDLEEPGAGYKKLFSDAQPLQPLQVYQAPLSLATVPHQALGRTQSSPAAPGGMKSPPDQPVKHLFTTGVVYDTFMLKHQCMCGNTHVHPEHAGRIQSIWSRLQETGLLSKCERIRGRKATLDEIQTVHSEYHTLLYGTSPLNRQKLDSKKLLGPISQKMYAVLPCGGIGVDSDTVWNEMHSSSAVRMAVGCLLELAFKVAAGELKNGFAIIRPPGHHAEESTAMGFCFFNSVAITAKLLQQKLNVGKVLIVDWDIHHGNGTQQAFYNDPSVLYISLHRYDNGNFFPGSGAPEEVGGGPGVGYNVNVAWTGGVDPPIGDVEYLTAFRTVVMPIAHEFSPDVVLVSAGFDAVEGHLSPLGGYSVTARCFGHLTRQLMTLAGGRVVLALEGGHDLTAICDASEACVSALLSVELQPLDEAVLQQKPNINAVATLEKVIEIQSKHWSCVQKFAAGLGRSLREAQAGETEEAETVSAMALLSVGAEQAQAAAAREHSPRPAEEPMEQEPAL
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
3 (in isoform 3)Phosphorylation-40.7522210691
3Phosphorylation-----MNSPNESDGM
-----CCCCCCCCCC
40.7521081666
7 (in isoform 3)Phosphorylation-46.2124043423
7Phosphorylation-MNSPNESDGMSGRE
-CCCCCCCCCCCCCC
46.2121081666
12 (in isoform 3)Phosphorylation-29.1324043423
16PhosphorylationGMSGREPSLEILPRT
CCCCCCCCCEECCCC
33.6022210691
23PhosphorylationSLEILPRTSLHSIPV
CCEECCCCCCCCCCE
33.4327251275
24PhosphorylationLEILPRTSLHSIPVT
CEECCCCCCCCCCEE
25.9328555341
25PhosphorylationEILPRTSLHSIPVTV
EECCCCCCCCCCEEE
3.4827251275
32 (in isoform 3)Phosphorylation-8.9522210691
35SumoylationIPVTVEVKPVLPRAM
CCEEEEEECCCCCCC
18.8628112733
35SumoylationIPVTVEVKPVLPRAM
CCEEEEEECCCCCCC
18.86-
44PhosphorylationVLPRAMPSSMGGGGG
CCCCCCCCCCCCCCC
21.6329214152
45PhosphorylationLPRAMPSSMGGGGGG
CCCCCCCCCCCCCCC
18.6424043423
53PhosphorylationMGGGGGGSPSPVELR
CCCCCCCCCCCHHHH
26.0225850435
54PhosphorylationGGGGGGSPSPVELRG
CCCCCCCCCCHHHHH
46.0224719451
55PhosphorylationGGGGGSPSPVELRGA
CCCCCCCCCHHHHHH
43.1825850435
56PhosphorylationGGGGSPSPVELRGAL
CCCCCCCCHHHHHHH
27.3027251275
66PhosphorylationLRGALVGSVDPTLRE
HHHHHHCCCCHHHHH
18.8321081666
70PhosphorylationLVGSVDPTLREQQLQ
HHCCCCHHHHHHHHH
33.70-
84UbiquitinationQQELLALKQQQQLQK
HHHHHHHHHHHHHHH
40.2229967540
85UbiquitinationQELLALKQQQQLQKQ
HHHHHHHHHHHHHHH
47.3629967540
115UbiquitinationQHEVQLQKHLKQQQE
HHHHHHHHHHHHHHH
60.5429967540
116UbiquitinationHEVQLQKHLKQQQEM
HHHHHHHHHHHHHHH
25.8729967540
136UbiquitinationQQEMLAAKRQQELEQ
HHHHHHHHHHHHHHH
45.1729967540
137UbiquitinationQEMLAAKRQQELEQQ
HHHHHHHHHHHHHHH
38.3929967540
180PhosphorylationSKESAIASTEVKLRL
CHHHHHCHHHHHHHH
20.98-
181PhosphorylationKESAIASTEVKLRLQ
HHHHHCHHHHHHHHH
35.46-
199PhosphorylationLSKSKEPTPGGLNHS
HHCCCCCCCCCCCCC
35.3428787133
206PhosphorylationTPGGLNHSLPQHPKC
CCCCCCCCCCCCCCC
40.4421081666
220PhosphorylationCWGAHHASLDQSSPP
CCCCCCCCCCCCCCC
28.2827080861
221PhosphorylationWGAHHASLDQSSPPQ
CCCCCCCCCCCCCCC
7.8327251275
224PhosphorylationHHASLDQSSPPQSGP
CCCCCCCCCCCCCCC
44.4727080861
225PhosphorylationHASLDQSSPPQSGPP
CCCCCCCCCCCCCCC
34.6627080861
229PhosphorylationDQSSPPQSGPPGTPP
CCCCCCCCCCCCCCC
60.0727080861
234PhosphorylationPQSGPPGTPPSYKLP
CCCCCCCCCCCCCCC
37.4927251275
256UbiquitinationRDDFPLRKTASEPNL
CCCCCCCCCCCCCCH
57.01-
257PhosphorylationDDFPLRKTASEPNLK
CCCCCCCCCCCCCHH
29.0530183078
259PhosphorylationFPLRKTASEPNLKVR
CCCCCCCCCCCHHHH
59.8425159151
260PhosphorylationPLRKTASEPNLKVRS
CCCCCCCCCCHHHHH
35.4324719451
278PhosphorylationQKVAERRSSPLLRRK
HHHHHHCCCCCHHCC
42.3925159151
279PhosphorylationKVAERRSSPLLRRKD
HHHHHCCCCCHHCCC
20.1126846344
288PhosphorylationLLRRKDGTVISTFKK
CHHCCCCCEEECCCC
25.46-
291PhosphorylationRKDGTVISTFKKRAV
CCCCCEEECCCCCEE
24.37-
292PhosphorylationKDGTVISTFKKRAVE
CCCCEEECCCCCEEE
28.4920188095
368PhosphorylationFSLYTSPSLPNISLG
EEEEECCCCCCCEEE
57.1121081666
458PhosphorylationLEQARQQSTLIAVPL
HHHHHHCCCEEEEEC
19.4924043423
459PhosphorylationEQARQQSTLIAVPLH
HHHHHCCCEEEEECC
20.1824043423
469PhosphorylationAVPLHGQSPLVTGER
EEECCCCCCCCCCCH
25.4621712546
473PhosphorylationHGQSPLVTGERVATS
CCCCCCCCCCHHHCC
40.7924043423
479PhosphorylationVTGERVATSMRTVGK
CCCCHHHCCCCCCCC
21.8724043423
480PhosphorylationTGERVATSMRTVGKL
CCCHHHCCCCCCCCC
9.1324043423
496PhosphorylationRHRPLSRTQSSPLPQ
CCCCCCCCCCCCCCC
29.4430266825
498PhosphorylationRPLSRTQSSPLPQSP
CCCCCCCCCCCCCCH
33.0530266825
499PhosphorylationPLSRTQSSPLPQSPQ
CCCCCCCCCCCCCHH
22.1930266825
500PhosphorylationLSRTQSSPLPQSPQA
CCCCCCCCCCCCHHH
53.9927251275
504PhosphorylationQSSPLPQSPQALQQL
CCCCCCCCHHHHHHH
19.6230266825
533SumoylationQQQLQLGKILTKTGE
HHHHHHHHHHHHCCC
43.04-
533AcetylationQQQLQLGKILTKTGE
HHHHHHHHHHHHCCC
43.0419608861
533SumoylationQQQLQLGKILTKTGE
HHHHHHHHHHHHCCC
43.0419608861
534AcetylationQQLQLGKILTKTGEL
HHHHHHHHHHHCCCC
5.8419608861
537UbiquitinationQLGKILTKTGELPRQ
HHHHHHHHCCCCCCC
51.6029967540
538UbiquitinationLGKILTKTGELPRQP
HHHHHHHCCCCCCCC
30.5629967540
546PhosphorylationGELPRQPTTHPEETE
CCCCCCCCCCHHHCH
29.4220736484
547PhosphorylationELPRQPTTHPEETEE
CCCCCCCCCHHHCHH
41.96-
605SumoylationEEDCIQVKDEEGESG
HHCCEEEECCCCCCC
42.94-
611PhosphorylationVKDEEGESGAEEGPD
EECCCCCCCCCCCCC
54.9123927012
612PhosphorylationKDEEGESGAEEGPDL
ECCCCCCCCCCCCCC
32.4824719451
650PhosphorylationQAPLSLATVPHQALG
ECCCCCCCCCHHHCC
39.6029514088
659PhosphorylationPHQALGRTQSSPAAP
CHHHCCCCCCCCCCC
30.8822115753
661PhosphorylationQALGRTQSSPAAPGG
HHCCCCCCCCCCCCC
37.3623401153
662PhosphorylationALGRTQSSPAAPGGM
HCCCCCCCCCCCCCC
14.5622115753
671PhosphorylationAAPGGMKSPPDQPVK
CCCCCCCCCCCCCCC
32.5428985074
713PhosphorylationEHAGRIQSIWSRLQE
HHHHHHHHHHHHHHH
24.5328857561
725PhosphorylationLQETGLLSKCERIRG
HHHHCCHHHHHHHCC
40.0624719451
755PhosphorylationHTLLYGTSPLNRQKL
HHHHHCCCCCCHHHC
24.0321081666
776PhosphorylationGPISQKMYAVLPCGG
HCHHHCEEEEEECCC
10.70-
798PhosphorylationVWNEMHSSSAVRMAV
HHHHHCCHHHHHHHH
13.98-
799PhosphorylationWNEMHSSSAVRMAVG
HHHHCCHHHHHHHHH
33.52-
1046PhosphorylationPNINAVATLEKVIEI
CCCCCEEEHHHHHHH
28.9324719451
1071PhosphorylationFAAGLGRSLREAQAG
HHHHHCHHHHHHHCC
29.94-
1108PhosphorylationAAAAREHSPRPAEEP
HHHHHHCCCCCCCCC
20.1823401153
1109PhosphorylationAAAREHSPRPAEEPM
HHHHHCCCCCCCCCC
48.4524719451

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
259SPhosphorylationKinaseAMPK-FAMILY-GPS
259SPhosphorylationKinaseMAP3K7O43318
GPS
259SPhosphorylationKinaseMARK2Q7KZI7
PSP
259SPhosphorylationKinasePRKD1Q15139
Uniprot
259SPhosphorylationKinasePRKCDQ05655
GPS
259SPhosphorylationKinaseSIK1P57059
Uniprot
259SPhosphorylationKinaseKKCC1Q8N5S9
PhosphoELM
259SPhosphorylationKinaseCAMK4Q16566
PSP
259SPhosphorylationKinaseQIKQ9H0K1
PSP
259SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
259SPhosphorylationKinaseCAMK1AQ14012
PSP
259SPhosphorylationKinaseCAMK1-FAMILY-GPS
259SPhosphorylationKinasePRKAA2P54646
GPS
259SPhosphorylationKinasePRKAA1Q13131
GPS
259SPhosphorylationKinaseAMPKQ9Y478
Uniprot
278SPhosphorylationKinaseAURKBQ96GD4
GPS
279SPhosphorylationKinasePRKACAP17612
GPS
279SPhosphorylationKinaseCDK5Q00535
PSP
279SPhosphorylationKinasePKA-FAMILY-GPS
292TPhosphorylationKinasePKC-Uniprot
292TPhosphorylationKinasePKC-FAMILY-GPS
292TPhosphorylationKinasePKN1Q16512
PSP
498SPhosphorylationKinasePRKD3O94806
PSP
498SPhosphorylationKinasePRKD2Q9BZL6
PSP
498SPhosphorylationKinasePRKD1Q15139
Uniprot
498SPhosphorylationKinaseKKCC1Q8N5S9
PhosphoELM
498SPhosphorylationKinaseSIK1P57059
Uniprot
498SPhosphorylationKinaseCAMK4Q16566
PSP
498SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
498SPhosphorylationKinaseAMPK-FAMILY-GPS
498SPhosphorylationKinaseCAMK1-FAMILY-GPS
498SPhosphorylationKinaseCAMK1AQ14012
PSP
498SPhosphorylationKinasePRKAA2P54646
GPS
498SPhosphorylationKinasePRKAA1Q13131
GPS
498SPhosphorylationKinaseAMPKQ9Y478
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
259SPhosphorylation

11081517
498SPhosphorylation

11081517

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 HDAC5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT16_HUMANZBTB16physical
15467736
1433T_HUMANYWHAQphysical
15367659
KPCD1_HUMANPRKD1physical
15367659
CTBP1_HUMANCTBP1physical
11022042
GATA1_HUMANGATA1physical
14668799
HDAC3_HUMANHDAC3physical
10220385
HDAC3_HUMANHDAC3physical
11804585
NCOR1_HUMANNCOR1physical
11931768
TBL1X_HUMANTBL1Xphysical
11931768
HDAC3_HUMANHDAC3physical
11931768
GPS2_HUMANGPS2physical
11931768
BCL6_HUMANBCL6physical
11929873
ZBT16_HUMANZBTB16physical
11929873
IKZF1_HUMANIKZF1physical
12015313
1433B_HUMANYWHABphysical
10869435
1433E_HUMANYWHAEphysical
10869435
HDAC3_HUMANHDAC3physical
10869435
SUV91_HUMANSUV39H1physical
12242305
EF1G_HUMANEEF1Gphysical
16169070
GBRAP_HUMANGABARAPphysical
16169070
HAIR_HUMANHRphysical
11641275
PKN2_HUMANPKN2physical
20188095
HIF1A_HUMANHIF1Aphysical
19071119
GATA3_HUMANGATA3physical
17075044
SMAD7_HUMANSMAD7physical
15831498
MAFF_HUMANMAFFphysical
20211142
1433G_HUMANYWHAGphysical
18951085
REST_HUMANRESTphysical
17011572
SIN3A_HUMANSIN3Aphysical
17011572
MARK3_HUMANMARK3physical
16980613
KLF4_HUMANKLF4physical
18768922
TYY1_HUMANYY1physical
16822951
KCC1A_HUMANCAMK1physical
16767219
GCM1_HUMANGCM1physical
16528103
NU214_HUMANNUP214physical
16356933
GBB1_HUMANGNB1physical
16221676
UBC9_HUMANUBE2Iphysical
16166628
RUNX2_HUMANRUNX2physical
15990875
RFXK_HUMANRFXANKphysical
15964851
ANRA2_HUMANANKRA2physical
15964851
C2TA_HUMANCIITAphysical
15964851
SMAD7_HUMANSMAD7physical
15831516
KPCD1_HUMANPRKD1physical
15728188
PP2AA_HUMANPPP2CAphysical
18339811
1433E_RATYwhaephysical
15572669
IKBA_HUMANNFKBIAphysical
15536134
HDAC5_HUMANHDAC5physical
18332106
HDAC4_HUMANHDAC4physical
18332106
AAKB1_HUMANPRKAB1physical
18184930
NR2E1_HUMANNR2E1physical
17873065
NFAC1_HUMANNFATC1physical
21413932
1433T_HUMANYWHAQphysical
20716686
HDAC5_HUMANHDAC5physical
21081666
RBM25_HUMANRBM25physical
21081666
NCOR1_HUMANNCOR1physical
21081666
NCOR2_HUMANNCOR2physical
21081666
TBL1X_HUMANTBL1Xphysical
21081666
TBL1R_HUMANTBL1XR1physical
21081666
GPS2_HUMANGPS2physical
21081666
HDAC1_HUMANHDAC1physical
21081666
RBBP7_HUMANRBBP7physical
21081666
RBBP4_HUMANRBBP4physical
21081666
MTA2_HUMANMTA2physical
21081666
KPCD1_HUMANPRKD1physical
21081666
KPCD2_HUMANPRKD2physical
21081666
2AAA_HUMANPPP2R1Aphysical
21081666
2ABA_HUMANPPP2R2Aphysical
21081666
PP2AA_HUMANPPP2CAphysical
21081666
1433B_HUMANYWHABphysical
21081666
1433E_HUMANYWHAEphysical
21081666
1433F_HUMANYWHAHphysical
21081666
1433G_HUMANYWHAGphysical
21081666
1433T_HUMANYWHAQphysical
21081666
1433Z_HUMANYWHAZphysical
21081666
PRKDC_HUMANPRKDCphysical
21081666
P53_HUMANTP53physical
21081666
TBB5_HUMANTUBBphysical
21081666
TBA1A_HUMANTUBA1Aphysical
21081666
HS90B_HUMANHSP90AB1physical
21081666
RBM39_HUMANRBM39physical
21081666
ROA2_HUMANHNRNPA2B1physical
21081666
NUMA1_HUMANNUMA1physical
21081666
H2A2C_HUMANHIST2H2ACphysical
21081666
H2B1K_HUMANHIST1H2BKphysical
21081666
H31T_HUMANHIST3H3physical
21081666
HDAC3_HUMANHDAC3physical
21081666
KPCD3_HUMANPRKD3physical
21081666
RAD50_HUMANRAD50physical
21081666
MAP1B_HUMANMAP1Bphysical
21081666
USP9X_HUMANUSP9Xphysical
21081666
UBP7_HUMANUSP7physical
21081666
SYIC_HUMANIARSphysical
21081666
PSA5_HUMANPSMA5physical
21081666
PRP39_HUMANPRPF39physical
21081666
HCFC1_HUMANHCFC1physical
21081666
RUVB1_HUMANRUVBL1physical
21081666
BAG2_HUMANBAG2physical
21081666
CCAR2_HUMANCCAR2physical
21081666
RENT1_HUMANUPF1physical
21081666
PRS8_HUMANPSMC5physical
21081666
NUDC_HUMANNUDCphysical
21081666
GCN1_HUMANGCN1L1physical
21081666
PSD11_HUMANPSMD11physical
21081666
NEUR1_HUMANNEU1physical
21081666
CDK1_HUMANCDK1physical
21081666
SF3A1_HUMANSF3A1physical
21081666
PRS10_HUMANPSMC6physical
21081666
LKHA4_HUMANLTA4Hphysical
21081666
ETFA_HUMANETFAphysical
21081666
COPB2_HUMANCOPB2physical
21081666
PIMT_HUMANPCMT1physical
21081666
TNPO1_HUMANTNPO1physical
21081666
CSK21_HUMANCSNK2A1physical
21081666
OGT1_HUMANOGTphysical
21081666
PGAM5_HUMANPGAM5physical
21081666
SF3B1_HUMANSF3B1physical
21081666
PSMD1_HUMANPSMD1physical
21081666
WDR5_HUMANWDR5physical
21081666
AATM_HUMANGOT2physical
21081666
XPOT_HUMANXPOTphysical
21081666
RL9_HUMANRPL9physical
21081666
ANM1_HUMANPRMT1physical
21081666
EIF3L_HUMANEIF3Lphysical
21081666
CAND1_HUMANCAND1physical
21081666
DDX20_HUMANDDX20physical
21081666
SAHH_HUMANAHCYphysical
21081666
HCD2_HUMANHSD17B10physical
21081666
PP2AB_HUMANPPP2CBphysical
21081666
LG3BP_HUMANLGALS3BPphysical
21081666
SMC1A_HUMANSMC1Aphysical
21081666
STRAP_HUMANSTRAPphysical
21081666
RPN2_HUMANRPN2physical
21081666
OST48_HUMANDDOSTphysical
21081666
PSMD2_HUMANPSMD2physical
21081666
PRS6B_HUMANPSMC4physical
21081666
SF3B2_HUMANSF3B2physical
21081666
ECH1_HUMANECH1physical
21081666
TPIS_HUMANTPI1physical
21081666
PSMD6_HUMANPSMD6physical
21081666
EFTU_HUMANTUFMphysical
21081666
PSMD3_HUMANPSMD3physical
21081666
PCNA_HUMANPCNAphysical
21081666
CISY_HUMANCSphysical
21081666
M2OM_HUMANSLC25A11physical
21081666
RAN_HUMANRANphysical
21081666
ENPL_HUMANHSP90B1physical
21081666
RL7_HUMANRPL7physical
21081666
QCR2_HUMANUQCRC2physical
21081666
SF3B3_HUMANSF3B3physical
21081666
RL13_HUMANRPL13physical
21081666
ANM5_HUMANPRMT5physical
21081666
PHB_HUMANPHBphysical
21081666
SMC3_HUMANSMC3physical
21081666
RL10A_HUMANRPL10Aphysical
21081666
LDHA_HUMANLDHAphysical
21081666
MDHM_HUMANMDH2physical
21081666
PSB5_HUMANPSMB5physical
21081666
CH60_HUMANHSPD1physical
21081666
HNRPF_HUMANHNRNPFphysical
21081666
DDB1_HUMANDDB1physical
21081666
SFXN1_HUMANSFXN1physical
21081666
ATPA_HUMANATP5A1physical
21081666
FLNA_HUMANFLNAphysical
21081666
OAT_HUMANOATphysical
21081666
VDAC1_HUMANVDAC1physical
21081666
HSP74_HUMANHSPA4physical
21081666
TRAP1_HUMANTRAP1physical
21081666
ATPB_HUMANATP5Bphysical
21081666
2ABD_HUMANPPP2R2Dphysical
21081666
RPN1_HUMANRPN1physical
21081666
C1TC_HUMANMTHFD1physical
21081666
PDIA6_HUMANPDIA6physical
21081666
SERA_HUMANPHGDHphysical
21081666
TCPB_HUMANCCT2physical
21081666
NDKA_HUMANNME1physical
21081666
SYLC_HUMANLARSphysical
21081666
PCBP2_HUMANPCBP2physical
21081666
ALDOA_HUMANALDOAphysical
21081666
TIF1B_HUMANTRIM28physical
21081666
GANAB_HUMANGANABphysical
21081666
ACTN4_HUMANACTN4physical
21081666
HS90A_HUMANHSP90AA1physical
21081666
SYDC_HUMANDARSphysical
21081666
AT1A1_HUMANATP1A1physical
21081666
CALX_HUMANCANXphysical
21081666
PGK1_HUMANPGK1physical
21081666
PDIA1_HUMANP4HBphysical
21081666
RS8_HUMANRPS8physical
21081666
RLA0_HUMANRPLP0physical
21081666
TCPZ_HUMANCCT6Aphysical
21081666
PRP19_HUMANPRPF19physical
21081666
HNRH2_HUMANHNRNPH2physical
21081666
PA2G4_HUMANPA2G4physical
21081666
FXR1_HUMANFXR1physical
21081666
LPPRC_HUMANLRPPRCphysical
21081666
VDAC2_HUMANVDAC2physical
21081666
EF1G_HUMANEEF1Gphysical
21081666
XPO2_HUMANCSE1Lphysical
21081666
KPYM_HUMANPKMphysical
21081666
RL3_HUMANRPL3physical
21081666
PRDX3_HUMANPRDX3physical
21081666
THIL_HUMANACAT1physical
21081666
COPB_HUMANCOPB1physical
21081666
DJB11_HUMANDNAJB11physical
21081666
IF4A3_HUMANEIF4A3physical
21081666
PPIA_HUMANPPIAphysical
21081666
C1QBP_HUMANC1QBPphysical
21081666
MCM3_HUMANMCM3physical
21081666
TCPA_HUMANTCP1physical
21081666
MCM4_HUMANMCM4physical
21081666
IMDH2_HUMANIMPDH2physical
21081666
RSSA_HUMANRPSAphysical
21081666
IF4A1_HUMANEIF4A1physical
21081666
TCPH_HUMANCCT7physical
21081666
DX39B_HUMANDDX39Bphysical
21081666
AT2A2_HUMANATP2A2physical
21081666
MCM2_HUMANMCM2physical
21081666
IRS4_HUMANIRS4physical
21081666
TXTP_HUMANSLC25A1physical
21081666
SYEP_HUMANEPRSphysical
21081666
MPCP_HUMANSLC25A3physical
21081666
PHB2_HUMANPHB2physical
21081666
PRDX4_HUMANPRDX4physical
21081666
EIF3F_HUMANEIF3Fphysical
21081666
EIF3C_HUMANEIF3Cphysical
21081666
XRCC5_HUMANXRCC5physical
21081666
RUVB2_HUMANRUVBL2physical
21081666
NFS1_HUMANNFS1physical
21081666
HNRLL_HUMANHNRNPLLphysical
21081666
PRP8_HUMANPRPF8physical
21081666
CLH1_HUMANCLTCphysical
21081666
TCPD_HUMANCCT4physical
21081666
U5S1_HUMANEFTUD2physical
21081666
TCPE_HUMANCCT5physical
21081666
DHE3_HUMANGLUD1physical
21081666
XRCC6_HUMANXRCC6physical
21081666
SYMC_HUMANMARSphysical
21081666
XPO1_HUMANXPO1physical
21081666
UBA1_HUMANUBA1physical
21081666
SYTC_HUMANTARSphysical
21081666
RS3A_HUMANRPS3Aphysical
21081666
FAS_HUMANFASNphysical
21081666
IMB1_HUMANKPNB1physical
21081666
MCM6_HUMANMCM6physical
21081666
ACLY_HUMANACLYphysical
21081666
SRSF1_HUMANSRSF1physical
21081666
HNRPD_HUMANHNRNPDphysical
21081666
ADT3_HUMANSLC25A6physical
21081666
TCPQ_HUMANCCT8physical
21081666
PYR1_HUMANCADphysical
21081666
PSA_HUMANNPEPPSphysical
21081666
TCPG_HUMANCCT3physical
21081666
TBB4B_HUMANTUBB4Bphysical
21081666
EIF3B_HUMANEIF3Bphysical
21081666
PRDX6_HUMANPRDX6physical
21081666
ILF2_HUMANILF2physical
21081666
CDC5L_HUMANCDC5Lphysical
21081666
GLYM_HUMANSHMT2physical
21081666
DNJA1_HUMANDNAJA1physical
21081666
PTBP1_HUMANPTBP1physical
21081666
GRP75_HUMANHSPA9physical
21081666
RS11_HUMANRPS11physical
21081666
APLP2_HUMANAPLP2physical
21081666
DHX15_HUMANDHX15physical
21081666
RL5_HUMANRPL5physical
21081666
RS3_HUMANRPS3physical
21081666
SYRC_HUMANRARSphysical
21081666
KCRB_HUMANCKBphysical
21081666
P5CS_HUMANALDH18A1physical
21081666
PP1A_HUMANPPP1CAphysical
21081666
NONO_HUMANNONOphysical
21081666
U520_HUMANSNRNP200physical
21081666
DDX1_HUMANDDX1physical
21081666
TERA_HUMANVCPphysical
21081666
GRP78_HUMANHSPA5physical
21081666
DDX17_HUMANDDX17physical
21081666
RL7A_HUMANRPL7Aphysical
21081666
TKT_HUMANTKTphysical
21081666
PABP1_HUMANPABPC1physical
21081666
MCM5_HUMANMCM5physical
21081666
TFR1_HUMANTFRCphysical
21081666
EMD_HUMANEMDphysical
21081666
SYQ_HUMANQARSphysical
21081666
MCM7_HUMANMCM7physical
21081666
RS4X_HUMANRPS4Xphysical
21081666
RL4_HUMANRPL4physical
21081666
KCRU_HUMANCKMT1Bphysical
21081666
NUP93_HUMANNUP93physical
21081666
HNRPL_HUMANHNRNPLphysical
21081666
SFPQ_HUMANSFPQphysical
21081666
RBM14_HUMANRBM14physical
21081666
PARP1_HUMANPARP1physical
21081666
DSRAD_HUMANADARphysical
21081666
ILF3_HUMANILF3physical
21081666
NPM_HUMANNPM1physical
21081666
DHX9_HUMANDHX9physical
21081666
H12_HUMANHIST1H1Cphysical
21081666
IF2B1_HUMANIGF2BP1physical
21081666
DDX3X_HUMANDDX3Xphysical
21081666
MYH9_HUMANMYH9physical
21081666
ROA1_HUMANHNRNPA1physical
21081666
ECHA_HUMANHADHAphysical
21081666
ROA3_HUMANHNRNPA3physical
21081666
DDX47_HUMANDDX47physical
21081666
HNRPR_HUMANHNRNPRphysical
21081666
NOP2_HUMANNOP2physical
21081666
RBMX_HUMANRBMXphysical
21081666
TOP1_HUMANTOP1physical
21081666
NFKB1_HUMANNFKB1physical
12917325
SF01_HUMANSF1physical
12917325
KDM5B_HUMANKDM5Bphysical
17373667
NRIP1_HUMANNRIP1physical
15060175
JDP2_HUMANJDP2physical
22989952
ATF3_HUMANATF3physical
22989952
ZBT7B_HUMANZBTB7Bphysical
22730529
HDAC4_HUMANHDAC4physical
22730529
1433B_HUMANYWHABphysical
23752268
1433E_HUMANYWHAEphysical
23752268
1433F_HUMANYWHAHphysical
23752268
1433G_HUMANYWHAGphysical
23752268
1433S_HUMANSFNphysical
23752268
1433T_HUMANYWHAQphysical
23752268
1433Z_HUMANYWHAZphysical
23752268
DP13A_HUMANAPPL1physical
23752268
TBL1X_HUMANTBL1Xphysical
23752268
TBL1R_HUMANTBL1XR1physical
23752268
HDAC5_HUMANHDAC5physical
23752268
NCOR1_HUMANNCOR1physical
23752268
PHB_HUMANPHBphysical
23752268
2ABA_HUMANPPP2R2Aphysical
23752268
MYCN_HUMANMYCNphysical
23812427
1433T_HUMANYWHAQphysical
23393134
DDIT3_HUMANDDIT3physical
17872950
CBX5_MOUSECbx5physical
12242305
1433E_HUMANYWHAEphysical
24841198
ANRA2_HUMANANKRA2physical
25752541
CUL7_HUMANCUL7physical
25752541
KPCD1_HUMANPRKD1physical
26137861
TFEB_HUMANTFEBphysical
26137861
CING_HUMANCGNphysical
27173435
NR2E1_HUMANNR2E1physical
26965827

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 HDAC5_HUMAN

loading...

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-533, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-661, AND MASSSPECTROMETRY.
"Protein kinase D-dependent phosphorylation and nuclear export ofhistone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis.";
Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K.,McKinsey T.A., Olson E.N., Jin Z.G.;
J. Biol. Chem. 283:14590-14599(2008).
Cited for: PHOSPHORYLATION AT SER-259 AND SER-498.
"AMP-activated protein kinase regulates GLUT4 transcription byphosphorylating histone deacetylase 5.";
McGee S.L., van Denderen B.J., Howlett K.F., Mollica J.,Schertzer J.D., Kemp B.E., Hargreaves M.;
Diabetes 57:860-867(2008).
Cited for: PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-259 AND SER-498.
"Activation of the myocyte enhancer factor-2 transcription factor bycalcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5.";
McKinsey T.A., Zhang C.-L., Olson E.N.;
Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000).
Cited for: INTERACTION WITH 14-3-3, AND PHOSPHORYLATION AT SER-259 AND SER-498.
"Protein kinase C-related kinase targets nuclear localization signalsin a subset of class IIa histone deacetylases.";
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,McKinsey T.A.;
FEBS Lett. 584:1103-1110(2010).
Cited for: PHOSPHORYLATION AT THR-292, AND MUTAGENESIS OF SER-259; SER-291 ANDTHR-292.

TOP