HDAC4_MOUSE - dbPTM
HDAC4_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC4_MOUSE
UniProt AC Q6NZM9
Protein Name Histone deacetylase 4
Gene Name Hdac4
Organism Mus musculus (Mouse).
Sequence Length 1076
Subcellular Localization Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on
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 via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Deacetylates HSPA1A and HSPA1A at 'Lys-77' leading to their preferential binding to co-chaperone STUB1..
Protein Sequence MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPTAVPMDLRLDHQFSLPLEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSASYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVATALKKRPLDVTDSACSSAPGSGPSSPNSSSGNVSTENGIAPTVPSAPAETSLAHRLVTREGSVAPLPLYTSPSLPNITLGLPATGPAAGAAGQQDAERLALPALQQRILFPGTHLTPYLSTSPLERDGAAAHNPLLQHMVLLEQPPTQTPLVTGLGALPLHSQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLHLSKIISKPSEPPRQPESHPEETEEELREHQALLDEPYLDRLPGQKEPSLAGVQVKQEPIESEEEEAEATRETEPGQRPATEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGSHRPLSRAQSSPASATFPMSVQEPPTKPRFTTGLVYDTLMLKHQCTCGNTNSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSSLTSVFVRLPCGGVGVDSDTIWNEVHSSGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLNVSKILIVDWDVHHGNGTQQAFYNDPNVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLEPPMGDAEYLAAFRTVVMPIANEFAPDVVLVSSGFDAVEGHPTPLGGYNLSAKCFGYLTKQLMGLAGGRLVLALEGGHDLTAICDASEACVSALLGNELEPLPEKVLHQRPNANAVHSMEKVMDIHSKYWRCLQRLSSTVGHSLIEAQKCEKEEAETVTAMASLSVGVKPAEKRSEEEPMEEEPPL
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
58PhosphorylationLRLDHQFSLPLEPAL
CCCCCCCCCCCCHHH		23.6229899451
171AcetylationAVASTEVKMKLQEFV
HCCHHHHHHHHHHHH		24.882388415
195PhosphorylationRNLNHCISSDPRYWY
CCCCHHHCCCCCCCC		33.8025266776
205PhosphorylationPRYWYGKTQHSSLDQ
CCCCCCCCCCCCCCC		27.4426643407
208PhosphorylationWYGKTQHSSLDQSSP
CCCCCCCCCCCCCCC		23.8426643407
209PhosphorylationYGKTQHSSLDQSSPP
CCCCCCCCCCCCCCC		33.5626643407
213PhosphorylationQHSSLDQSSPPQSGV
CCCCCCCCCCCCCCC		44.4726643407
214PhosphorylationHSSLDQSSPPQSGVS
CCCCCCCCCCCCCCC		34.6626643407
218PhosphorylationDQSSPPQSGVSASYN
CCCCCCCCCCCCCCC		47.1123984901
221PhosphorylationSPPQSGVSASYNHPV
CCCCCCCCCCCCCCC		18.2829472430
223PhosphorylationPQSGVSASYNHPVLG
CCCCCCCCCCCCCCC		20.9729472430
224PhosphorylationQSGVSASYNHPVLGM
CCCCCCCCCCCCCCC		19.7329472430
243PhosphorylationDDFPLRKTASEPNLK
CCCCCCCCCCCCCHH		29.0528833060
245PhosphorylationFPLRKTASEPNLKLR
CCCCCCCCCCCHHHH		59.8427087446
264PhosphorylationQKVAERRSSPLLRRK
HHHHHHHCCCCHHCC		42.3926824392
265PhosphorylationKVAERRSSPLLRRKD
HHHHHHCCCCHHCCC		20.1126824392
271UbiquitinationSSPLLRRKDGPVATA
CCCCHHCCCCCCHHH		61.68-
280UbiquitinationGPVATALKKRPLDVT
CCCHHHHCCCCCCCC		44.25-
281UbiquitinationPVATALKKRPLDVTD
CCHHHHCCCCCCCCC		61.16-
292PhosphorylationDVTDSACSSAPGSGP
CCCCCCCCCCCCCCC		29.2925338131
297PhosphorylationACSSAPGSGPSSPNS
CCCCCCCCCCCCCCC		46.6129514104
300PhosphorylationSAPGSGPSSPNSSSG
CCCCCCCCCCCCCCC		63.0525338131
301PhosphorylationAPGSGPSSPNSSSGN
CCCCCCCCCCCCCCC		31.1029514104
304PhosphorylationSGPSSPNSSSGNVST
CCCCCCCCCCCCCCC		29.3025338131
305PhosphorylationGPSSPNSSSGNVSTE
CCCCCCCCCCCCCCC		49.2425338131
338PhosphorylationRLVTREGSVAPLPLY
HHHCCCCCCCCCCCC		15.4529514104
345PhosphorylationSVAPLPLYTSPSLPN
CCCCCCCCCCCCCCC		11.8426643407
346PhosphorylationVAPLPLYTSPSLPNI
CCCCCCCCCCCCCCE		41.6726643407
347PhosphorylationAPLPLYTSPSLPNIT
CCCCCCCCCCCCCEE		10.0326643407
349PhosphorylationLPLYTSPSLPNITLG
CCCCCCCCCCCEEEE		57.1130352176
354PhosphorylationSPSLPNITLGLPATG
CCCCCCEEEECCCCC		22.7826643407
360PhosphorylationITLGLPATGPAAGAA
EEEECCCCCCCCCCC		41.5826643407
396PhosphorylationTHLTPYLSTSPLERD
CCCCCCCCCCCCCCC		22.4626643407
397PhosphorylationHLTPYLSTSPLERDG
CCCCCCCCCCCCCCC		31.5924759943
398PhosphorylationLTPYLSTSPLERDGA
CCCCCCCCCCCCCCH		24.9026824392
463PhosphorylationQHRPLGRTQSAPLPQ
HCCCCCCCCCCCCCC		25.6925521595
465PhosphorylationRPLGRTQSAPLPQNA
CCCCCCCCCCCCCHH		31.1025521595
549PhosphorylationLPGQKEPSLAGVQVK
CCCCCCCCCCCCEEE		31.7628285833
562PhosphorylationVKQEPIESEEEEAEA
EECCCCCCHHHHHHH		51.5325521595
570PhosphorylationEEEEAEATRETEPGQ
HHHHHHHHCCCCCCC		22.1225619855
581PhosphorylationEPGQRPATEQELLFR
CCCCCCCCHHHHHHH		40.6728285833
608PhosphorylationQLRNYQASMEAAGIP
HHHHHHHHHHHCCCC		11.1329899451
625PhosphorylationFGSHRPLSRAQSSPA
CCCCCCCCCCCCCCC		28.4029514104
629PhosphorylationRPLSRAQSSPASATF
CCCCCCCCCCCCCCC		36.9926824392
630PhosphorylationPLSRAQSSPASATFP
CCCCCCCCCCCCCCC		16.6527742792
633PhosphorylationRAQSSPASATFPMSV
CCCCCCCCCCCCCCC		31.0925619855
635PhosphorylationQSSPASATFPMSVQE
CCCCCCCCCCCCCCC		26.2725619855
639PhosphorylationASATFPMSVQEPPTK
CCCCCCCCCCCCCCC		22.3825619855
645PhosphorylationMSVQEPPTKPRFTTG
CCCCCCCCCCCCCCC		65.4825619855
733PhosphorylationNRQKLDSSLTSVFVR
CHHHCCCCCEEEEEC		35.02-
736PhosphorylationKLDSSLTSVFVRLPC
HCCCCCEEEEECCCC		20.89-
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
245SPhosphorylationKinaseCAMK4P08414
Uniprot
245SPhosphorylationKinaseSIK1Q60670
Uniprot
465SPhosphorylationKinaseCAMK4P08414
Uniprot
465SPhosphorylationKinaseSIK1Q60670
Uniprot
629SPhosphorylationKinaseCAMK4P08414
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
245SPhosphorylation

17468767
349SPhosphorylation

-
465SPhosphorylation

17468767
556KPhosphorylation

17923476
556KSumoylation

17923476
629SPhosphorylation

-
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 HDAC4_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IFRD1_MOUSEIfrd1physical
15743821
1433B_MOUSEYwhabphysical
10958686
1433B_MOUSEYwhabphysical
17923476
MEF2A_MOUSEMef2aphysical
22466704
CREB1_MOUSECreb1physical
22466704
PP2AA_MOUSEPpp2caphysical
22466704
ATM_MOUSEAtmgenetic
22466704
MYCD_MOUSEMyocdphysical
15601857
RUNX2_MOUSERunx2physical
15537544
DNJB6_MOUSEDnajb6physical
16260608
TNFA_MOUSETnfphysical
16260608
MEF2A_MOUSEMef2aphysical
10737771
MEF2C_MOUSEMef2cphysical
10737771
MEF2D_MOUSEMef2dphysical
10737771
RFXK_MOUSERfxankphysical
16236793
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDAC4_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND MASSSPECTROMETRY.
"SIK1 is a class II HDAC kinase that promotes survival of skeletalmyocytes.";
Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T.,Shelton G.D., Montminy M.;
Nat. Med. 13:597-603(2007).
Cited for: PHOSPHORYLATION AT SER-465 AND SER-465.

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