| UniProt ID | HDAC3_HUMAN | |
|---|---|---|
| UniProt AC | O15379 | |
| Protein Name | Histone deacetylase 3 | |
| Gene Name | HDAC3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 428 | |
| Subcellular Localization | Nucleus . Cytoplasm . Cytoplasm, cytosol . Colocalizes with XBP1 and AKT1 in the cytoplasm (PubMed:25190803). Predominantly expressed in the nucleus in the presence of CCAR2. | |
| Protein Description | Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. 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. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation. [PubMed: 21444723] | |
| Protein Sequence | MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAISEELPYSEYFEYFAPDFTLHPDVSTRIENQNSRQYLDQIRQTIFENLKMLNHAPSVQIHDVPADLLTYDRTDEADAEERGPEENYSRPEAPNEFYDGDHDNDKESDVEI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Ubiquitination | -----MAKTVAYFYD -----CCCEEEEEEC | 42.08 | - | |
| 25 | Ubiquitination | YGAGHPMKPHRLALT CCCCCCCCHHHHHHH | 41.97 | - | |
| 43 | Ubiquitination | VLHYGLYKKMIVFKP HHHHCCCCEEEEECC | 40.69 | 22817900 | |
| 44 | Ubiquitination | LHYGLYKKMIVFKPY HHHCCCCEEEEECCC | 21.94 | 18655026 | |
| 49 | Ubiquitination | YKKMIVFKPYQASQH CCEEEEECCCCCCCC | 31.74 | 22817900 | |
| 66 | Phosphorylation | CRFHSEDYIDFLQRV HCCCCHHHHHHHHHH | 9.80 | - | |
| 74 | Phosphorylation | IDFLQRVSPTNMQGF HHHHHHHCCCCCCCC | 28.35 | 28348404 | |
| 76 | Phosphorylation | FLQRVSPTNMQGFTK HHHHHCCCCCCCCCC | 35.50 | 27732954 | |
| 121 | Ubiquitination | GATQLNNKICDIAIN HHHHCCCHHHHEEEE | 43.57 | - | |
| 189 | Phosphorylation | YLTDRVMTVSFHKYG HCCCEEEEEEEEEEC | 15.33 | 20068231 | |
| 191 | Phosphorylation | TDRVMTVSFHKYGNY CCEEEEEEEEEECCC | 16.68 | 22817900 | |
| 207 | Phosphorylation | FPGTGDMYEVGAESG CCCCCCCEEECCCCC | 16.53 | 28857561 | |
| 231 | Phosphorylation | RDGIDDQSYKHLFQP CCCCCCCHHHHHHHH | 43.05 | 28857561 | |
| 325 | Phosphorylation | AISEELPYSEYFEYF HHCCCCCHHHHHHHH | 27.10 | - | |
| 328 | Phosphorylation | EELPYSEYFEYFAPD CCCCHHHHHHHHCCC | 8.86 | - | |
| 331 | Phosphorylation | PYSEYFEYFAPDFTL CHHHHHHHHCCCCEE | 8.64 | - | |
| 404 | Phosphorylation | ERGPEENYSRPEAPN HHCCCCCCCCCCCCC | 14.88 | 20873877 | |
| 405 | Phosphorylation | RGPEENYSRPEAPNE HCCCCCCCCCCCCCC | 53.60 | 20873877 | |
| 414 | Phosphorylation | PEAPNEFYDGDHDND CCCCCCCCCCCCCCC | 16.91 | 23663014 | |
| 424 | Phosphorylation | DHDNDKESDVEI--- CCCCCCCCCCCC--- | 53.34 | 15805470 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 325 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| 328 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| 331 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| 424 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
| 424 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | SIAH2 | O43255 | PMID:20691163 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HDAC3_HUMAN !! | ||||||
* 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 HDAC3_HUMAN !! | ||||||
| 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 | |
| DB02546 | Vorinostat |
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| Phosphorylation | |
| Reference | PubMed |
| "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-424, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells."; Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.; Proteomics 8:2885-2896(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-44, AND MASSSPECTROMETRY. | |
