| UniProt ID | HDA3_YEAST | |
|---|---|---|
| UniProt AC | Q06623 | |
| Protein Name | HDA1 complex subunit 3 | |
| Gene Name | HDA3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 655 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is 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.. | |
| Protein Sequence | MDLLRILDTKPIPTIVDATTLGISGNTSGDYWLPTTMSLYQKELTDQIVSLHYSDILRYFETSHYKEDVILESMKTMCLNGSLVATHPYLLIDHYMPKSLITRDVPAHLAENSGKFSVLRDLINLVQEYETETAIVCRPGRTMDLLEALLLGNKVHIKRYDGHSIKSKQKANDFSCTVHLFSSEGINFTKYPIKSKARFDMLICLDTTVDTSQKDIQYLLQYKRERKGLERYAPIVRLVAINSIDHCRLFFGKKFDKNSREYLENVTAAMVILRDRLGTLPPDLRPIYSQKLHYLVEWLENPTVPWPLPDIYPLKQYTSMDVERSLLTEVHFKKSDDQLEDAFSNCSKKRGRHGANKAASSTVAGIEDNITPSFYSTKRLKNDYYTNPLKQDMTQLTGITTADNSSNVNYHLSSGIITHKLIQSMGEVYMDICVQKQELDDYSCLDDLQNDHLKFFSNEDEKIIKEYETVLRTNNENLNRSHELEVENNLKFSQIETLEKDIETLKGSLMAQGETLSKLKDAFVKTDNVQDEIEKEERVSVSRDTEKKYMEQEIKRAVDAIRENEEETHKLNEKQNGLESELKLKFEKSEISTKELNEKIGFLKKELKLENDLNEELVGQLSKTMDNLENLTIPRVRTQNGNTKKKSRAKKPGNV | |
| 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 |
|---|---|---|---|---|---|
| 45 | Phosphorylation | SLYQKELTDQIVSLH HHHHHHHHHHHHHHC | 27.27 | 28889911 | |
| 50 | Phosphorylation | ELTDQIVSLHYSDIL HHHHHHHHHCHHHHH | 15.85 | 28889911 | |
| 59 | Phosphorylation | HYSDILRYFETSHYK CHHHHHHHHHCCCCC | 11.43 | 28889911 | |
| 62 | Phosphorylation | DILRYFETSHYKEDV HHHHHHHCCCCCHHH | 15.76 | 28889911 | |
| 182 | Phosphorylation | SCTVHLFSSEGINFT EEEEEEEECCCCCCC | 33.56 | 27017623 | |
| 183 | Phosphorylation | CTVHLFSSEGINFTK EEEEEEECCCCCCCC | 32.29 | 27017623 | |
| 262 | Phosphorylation | FDKNSREYLENVTAA CCCCHHHHHHHHHHH | 20.43 | 21126336 | |
| 344 | Phosphorylation | DQLEDAFSNCSKKRG HHHHHHHHHHHHHHC | 38.35 | 20377248 | |
| 347 | Phosphorylation | EDAFSNCSKKRGRHG HHHHHHHHHHHCCCC | 45.52 | 28889911 | |
| 360 | Phosphorylation | HGANKAASSTVAGIE CCCCHHHHHHCCCCC | 31.25 | 19823750 | |
| 361 | Phosphorylation | GANKAASSTVAGIED CCCHHHHHHCCCCCC | 23.36 | 19823750 | |
| 362 | Phosphorylation | ANKAASSTVAGIEDN CCHHHHHHCCCCCCC | 16.33 | 19823750 | |
| 371 | Phosphorylation | AGIEDNITPSFYSTK CCCCCCCCCCHHCCC | 21.09 | 19823750 | |
| 373 | Phosphorylation | IEDNITPSFYSTKRL CCCCCCCCHHCCCCC | 28.32 | 19823750 | |
| 375 | Phosphorylation | DNITPSFYSTKRLKN CCCCCCHHCCCCCCC | 21.55 | 19823750 | |
| 376 | Phosphorylation | NITPSFYSTKRLKND CCCCCHHCCCCCCCC | 25.99 | 19823750 | |
| 377 | Phosphorylation | ITPSFYSTKRLKNDY CCCCHHCCCCCCCCC | 14.59 | 19823750 | |
| 378 | Acetylation | TPSFYSTKRLKNDYY CCCHHCCCCCCCCCC | 50.20 | 24489116 | |
| 442 | Phosphorylation | QKQELDDYSCLDDLQ ECCCCCCCCCHHHHC | 10.84 | 21440633 | |
| 535 | Acetylation | NVQDEIEKEERVSVS CCHHHHHHHHCCCCC | 71.22 | 24489116 |
| 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 HDA3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HDA3_YEAST !! | ||||||
* 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 HDA3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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