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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
4 | Phosphorylation | ----MTSTGQDSSTR ----CCCCCCCHHHH | 46.42 | 28576409 | |
15 | Phosphorylation | SSTRQRKSRHNPQSP HHHHHHHHCCCCCCC | 40.75 | 19367708 | |
21 | Phosphorylation | KSRHNPQSPLQESSA HHCCCCCCCHHHCCH | 28.91 | 25521595 | |
26 | Phosphorylation | PQSPLQESSATLKRG CCCCHHHCCHHHHCC | 16.59 | 26643407 | |
27 | Phosphorylation | QSPLQESSATLKRGG CCCHHHCCHHHHCCC | 25.23 | 26643407 | |
29 | Phosphorylation | PLQESSATLKRGGKK CHHHCCHHHHCCCEE | 34.46 | 21454597 | |
32 | Methylation | ESSATLKRGGKKCAV HCCHHHHCCCEECCC | 63.31 | 24129315 | |
42 | Phosphorylation | KKCAVPHSSPNLAEV EECCCCCCCCCHHHH | 41.23 | 26824392 | |
43 | Phosphorylation | KCAVPHSSPNLAEVK ECCCCCCCCCHHHHH | 18.12 | 27087446 | |
59 | Phosphorylation | KGKMKKLSQPAEEDL HCCCCCCCCCHHHCC | 42.89 | 26824392 | |
107 | Phosphorylation | WDDSFPESPERLHAI CCCCCCCCHHHHHHH | 32.09 | - | |
857 | Phosphorylation | VIKKLPPTASPVSAK EEEECCCCCCCCCCC | 37.52 | 26239621 | |
859 | Phosphorylation | KKLPPTASPVSAKEM EECCCCCCCCCCCCC | 28.45 | 21082442 | |
862 | Phosphorylation | PPTASPVSAKEMTTP CCCCCCCCCCCCCCC | 36.69 | 26745281 | |
909 | Phosphorylation | AVLAQGQSSEQAAKG HHHHCCCCHHHHHCC | 42.54 | 27087446 | |
910 | Phosphorylation | VLAQGQSSEQAAKGT HHHCCCCHHHHHCCC | 26.32 | 21183079 | |
923 | Phosphorylation | GTTLDLATSKETVGG CCCEEECCCCCCCCC | 47.86 | 27841257 | |
924 | Phosphorylation | TTLDLATSKETVGGA CCEEECCCCCCCCCH | 23.92 | 27841257 | |
958 | Phosphorylation | SVEALGETEPTPPAS CEEECCCCCCCCCCC | 45.53 | - | |
961 | Phosphorylation | ALGETEPTPPASHTN ECCCCCCCCCCCCCC | 35.35 | 22067460 | |
967 | Phosphorylation | PTPPASHTNKQTTGA CCCCCCCCCCCCCCC | 41.43 | - | |
971 | Phosphorylation | ASHTNKQTTGASPLQ CCCCCCCCCCCCCCC | 28.89 | - | |
975 | Phosphorylation | NKQTTGASPLQGVTA CCCCCCCCCCCCCCH | 27.73 | - | |
1034 | Phosphorylation | QGFGDFNTQDVFYAV CCCCCCCHHHCEEEE | 26.58 | - | |
1148 | Phosphorylation | FGEDMPHSH------ CCCCCCCCC------ | 25.64 | 25521595 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HDAC6_MOUSE !! |
* 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 !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |