HDAC6_MOUSE - dbPTM
HDAC6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC6_MOUSE
UniProt AC Q9Z2V5
Protein Name Histone deacetylase 6
Gene Name Hdac6
Organism Mus musculus (Mouse).
Sequence Length 1149
Subcellular Localization Nucleus. Cytoplasm. Perikaryon. Cell projection, dendrite. Cell projection, axon. It is mainly cytoplasmic, where it is associated with microtubules.
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 (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.; In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy (By similarity)..
Protein Sequence MTSTGQDSSTRQRKSRHNPQSPLQESSATLKRGGKKCAVPHSSPNLAEVKKKGKMKKLSQPAEEDLVVGLQGLDLNPETRVPVGTGLVFDEQLNDFHCLWDDSFPESPERLHAIREQLILEGLLGRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAETYDSVYLHPNSYSCACLATGSVLRLVDALMGAEIRNGMAVIRPPGHHAQHNLMDGYCMFNHLAVAARYAQKKHRIQRVLIVDWDVHHGQGTQFIFDQDPSVLYFSIHRYEHGRFWPHLKASNWSTIGFGQGQGYTINVPWNQTGMRDADYIAAFLHILLPVASEFQPQLVLVAAGFDALHGDPKGEMAATPAGFAHLTHLLMGLAGGKLILSLEGGYNLRALAKGVSASLHTLLGDPCPMLESCVVPCASAQTSIYCTLEALEPFWEVLERSVETQEEDEVEEAVLEEEEEEGGWEATALPMDTWPLLQNRTGLVYDEKMMSHCNLWDNHHPETPQRILRIMCHLEEVGLAARCLILPARPALDSELLTCHSAEYVEHLRTTEKMKTRDLHREGANFDSIYICPSTFACAKLATGAACRLVEAVLSGEVLNGIAVVRPPGHHAEPNAACGFCFFNSVAVAARHAQIIAGRALRILIVDWDVHHGNGTQHIFEDDPSVLYVSLHRYDRGTFFPMGDEGASSQVGRDAGIGFTVNVPWNGPRMGDADYLAAWHRLVLPIAYEFNPELVLISAGFDAAQGDPLGGCQVTPEGYAHLTHLLMGLAGGRIILILEGGYNLASISESMAACTHSLLGDPPPQLTLLRPPQSGALVSISEVIQVHRKYWRSLRLMKMEDKEECSSSRLVIKKLPPTASPVSAKEMTTPKGKVPEESVRKTIAALPGKESTLGQAKSKMAKAVLAQGQSSEQAAKGTTLDLATSKETVGGATTDLWASAAAPENFPNQTTSVEALGETEPTPPASHTNKQTTGASPLQGVTAQQSLQLGVLSTLELSREAEEAHDSEEGLLGEAAGGQDMNSLMLTQGFGDFNTQDVFYAVTPLSWCPHLMAVCPIPAAGLDVSQPCKTCGTVQENWVCLTCYQVYCSRYVNAHMVCHHEASEHPLVLSCVDLSTWCYVCQAYVHHEDLQDVKNAAHQNKFGEDMPHSH
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----MTSTGQDSSTR
----CCCCCCCHHHH
46.4228576409
15PhosphorylationSSTRQRKSRHNPQSP
HHHHHHHHCCCCCCC
40.7519367708
21PhosphorylationKSRHNPQSPLQESSA
HHCCCCCCCHHHCCH
28.9125521595
26PhosphorylationPQSPLQESSATLKRG
CCCCHHHCCHHHHCC
16.5926643407
27PhosphorylationQSPLQESSATLKRGG
CCCHHHCCHHHHCCC
25.2326643407
29PhosphorylationPLQESSATLKRGGKK
CHHHCCHHHHCCCEE
34.4621454597
32MethylationESSATLKRGGKKCAV
HCCHHHHCCCEECCC
63.3124129315
42PhosphorylationKKCAVPHSSPNLAEV
EECCCCCCCCCHHHH
41.2326824392
43PhosphorylationKCAVPHSSPNLAEVK
ECCCCCCCCCHHHHH
18.1227087446
59PhosphorylationKGKMKKLSQPAEEDL
HCCCCCCCCCHHHCC
42.8926824392
107PhosphorylationWDDSFPESPERLHAI
CCCCCCCCHHHHHHH
32.09-
857PhosphorylationVIKKLPPTASPVSAK
EEEECCCCCCCCCCC
37.5226239621
859PhosphorylationKKLPPTASPVSAKEM
EECCCCCCCCCCCCC
28.4521082442
862PhosphorylationPPTASPVSAKEMTTP
CCCCCCCCCCCCCCC
36.6926745281
909PhosphorylationAVLAQGQSSEQAAKG
HHHHCCCCHHHHHCC
42.5427087446
910PhosphorylationVLAQGQSSEQAAKGT
HHHCCCCHHHHHCCC
26.3221183079
923PhosphorylationGTTLDLATSKETVGG
CCCEEECCCCCCCCC
47.8627841257
924PhosphorylationTTLDLATSKETVGGA
CCEEECCCCCCCCCH
23.9227841257
958PhosphorylationSVEALGETEPTPPAS
CEEECCCCCCCCCCC
45.53-
961PhosphorylationALGETEPTPPASHTN
ECCCCCCCCCCCCCC
35.3522067460
967PhosphorylationPTPPASHTNKQTTGA
CCCCCCCCCCCCCCC
41.43-
971PhosphorylationASHTNKQTTGASPLQ
CCCCCCCCCCCCCCC
28.89-
975PhosphorylationNKQTTGASPLQGVTA
CCCCCCCCCCCCCCH
27.73-
1034PhosphorylationQGFGDFNTQDVFYAV
CCCCCCCHHHCEEEE
26.58-
1148PhosphorylationFGEDMPHSH------
CCCCCCCCC------
25.6425521595

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

Oops, there are no upstream regulatory protein records of HDAC6_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HDAC6_MOUSE !!

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 HDAC6_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
11689694
PLAP_MOUSEPlaaphysical
11689694
TBA1A_MOUSETuba1aphysical
12486003
HS90B_MOUSEHsp90ab1physical
15916966
HDAC6_HUMANHDAC6physical
20360068
GARS_HUMANGARSphysical
20360068
PLAP_HUMANPLAAphysical
20360068
UBP47_HUMANUSP47physical
20360068
UBC_MOUSEUbcphysical
16810319
TERA_MOUSEVcpphysical
16810319
FBX32_MOUSEFbxo32physical
25516595
KAT5_MOUSEKat5physical
24302573
EP400_MOUSEEp400physical
24302573
ODBA_HUMANBCKDHAphysical
26496610
ODBB_HUMANBCKDHBphysical
26496610
ODB2_HUMANDBTphysical
26496610
ODP2_HUMANDLATphysical
26496610
DLDH_HUMANDLDphysical
26496610
ODO2_HUMANDLSTphysical
26496610
IREB2_HUMANIREB2physical
26496610
MKLN1_HUMANMKLN1physical
26496610
ODO1_HUMANOGDHphysical
26496610
ODPA_HUMANPDHA1physical
26496610
ODPB_HUMANPDHBphysical
26496610
PDK2_HUMANPDK2physical
26496610
SRSF3_HUMANSRSF3physical
26496610
TDG_HUMANTDGphysical
26496610
TERA_HUMANVCPphysical
26496610
ODPX_HUMANPDHXphysical
26496610
PLAP_HUMANPLAAphysical
26496610
VINEX_HUMANSORBS3physical
26496610
HPS5_HUMANHPS5physical
26496610
KAT6B_HUMANKAT6Bphysical
26496610
UBP47_HUMANUSP47physical
26496610
TTC7A_HUMANTTC7Aphysical
26496610
IFIH1_HUMANIFIH1physical
26496610
MILK2_HUMANMICALL2physical
26496610
RT36_HUMANMRPS36physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDAC6_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.

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