UniProt ID | HDAC1_HUMAN | |
---|---|---|
UniProt AC | Q13547 | |
Protein Name | Histone deacetylase 1 | |
Gene Name | HDAC1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 482 | |
Subcellular Localization | Nucleus . | |
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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.. | |
Protein Sequence | MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA | |
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 | ----MAQTQGTRRKV ----CCCCCCCCEEE | 21.30 | 27470641 | |
10 | Ubiquitination | QTQGTRRKVCYYYDG CCCCCCEEEEEEECC | 33.11 | 21890473 | |
31 | Acetylation | YGQGHPMKPHRIRMT ECCCCCCCCCEECCH | 41.97 | 25953088 | |
31 | Ubiquitination | YGQGHPMKPHRIRMT ECCCCCCCCCEECCH | 41.97 | - | |
36 | Methylation | PMKPHRIRMTHNLLL CCCCCEECCHHHHHH | 24.73 | - | |
38 | Phosphorylation | KPHRIRMTHNLLLNY CCCEECCHHHHHHHH | 9.58 | 24719451 | |
45 | Phosphorylation | THNLLLNYGLYRKME HHHHHHHHHHHHCCE | 14.42 | 28258704 | |
48 | Phosphorylation | LLLNYGLYRKMEIYR HHHHHHHHHCCEEEC | 12.11 | 24719451 | |
50 | Ubiquitination | LNYGLYRKMEIYRPH HHHHHHHCCEEECCC | 27.59 | - | |
54 | Phosphorylation | LYRKMEIYRPHKANA HHHCCEEECCCCCCH | 12.56 | 28258704 | |
58 | Ubiquitination | MEIYRPHKANAEEMT CEEECCCCCCHHHHH | 46.12 | - | |
66 | Acetylation | ANAEEMTKYHSDDYI CCHHHHHHHCCHHHH | 39.39 | 23236377 | |
66 | Ubiquitination | ANAEEMTKYHSDDYI CCHHHHHHHCCHHHH | 39.39 | 21906983 | |
72 | Phosphorylation | TKYHSDDYIKFLRSI HHHCCHHHHHHHHHH | 15.82 | - | |
74 | Acetylation | YHSDDYIKFLRSIRP HCCHHHHHHHHHHCC | 31.92 | 19608861 | |
74 | Ubiquitination | YHSDDYIKFLRSIRP HCCHHHHHHHHHHCC | 31.92 | 21890473 | |
84 | Sulfoxidation | RSIRPDNMSEYSKQM HHHCCCCHHHHHHHH | 4.14 | 21406390 | |
85 | Phosphorylation | SIRPDNMSEYSKQMQ HHCCCCHHHHHHHHH | 39.37 | 28450419 | |
87 | Phosphorylation | RPDNMSEYSKQMQRF CCCCHHHHHHHHHHC | 17.54 | - | |
87 | Nitration | RPDNMSEYSKQMQRF CCCCHHHHHHHHHHC | 17.54 | - | |
88 | Phosphorylation | PDNMSEYSKQMQRFN CCCHHHHHHHHHHCC | 16.62 | 20860994 | |
89 | Sumoylation | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | - | |
89 | Sumoylation | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | 19608861 | |
89 | Acetylation | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | 23749302 | |
89 | Ubiquitination | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | 21890473 | |
89 | Methylation | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | 19608861 | |
89 | Malonylation | DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC | 49.22 | 26320211 | |
114 | O-linked_Glycosylation | FEFCQLSTGGSVASA HHHHHCCCCCCHHHH | 54.90 | 23301498 | |
126 | Ubiquitination | ASAVKLNKQQTDIAV HHHHHCCCCCCCEEE | 54.97 | 21890473 | |
143 | Ubiquitination | AGGLHHAKKSEASGF CCCCCCCCCCCCCCC | 53.10 | - | |
144 | Ubiquitination | GGLHHAKKSEASGFC CCCCCCCCCCCCCCH | 55.07 | - | |
195 | Phosphorylation | YTTDRVMTVSFHKYG EECCCEEEEEEECCC | 15.33 | 20068231 | |
197 | Phosphorylation | TDRVMTVSFHKYGEY CCCEEEEEEECCCCC | 16.68 | 20068231 | |
200 | Acetylation | VMTVSFHKYGEYFPG EEEEEEECCCCCCCC | 53.60 | 25953088 | |
200 | Ubiquitination | VMTVSFHKYGEYFPG EEEEEEECCCCCCCC | 53.60 | 21890473 | |
201 | Phosphorylation | MTVSFHKYGEYFPGT EEEEEECCCCCCCCC | 13.45 | 28152594 | |
204 | Phosphorylation | SFHKYGEYFPGTGDL EEECCCCCCCCCCCC | 15.65 | 28152594 | |
218 | Ubiquitination | LRDIGAGKGKYYAVN CEECCCCCCCEEEEE | 52.26 | - | |
218 | Acetylation | LRDIGAGKGKYYAVN CEECCCCCCCEEEEE | 52.26 | 8439433 | |
220 | Acetylation | DIGAGKGKYYAVNYP ECCCCCCCEEEEECC | 38.28 | 19608861 | |
220 | Ubiquitination | DIGAGKGKYYAVNYP ECCCCCCCEEEEECC | 38.28 | 19608861 | |
220 | Malonylation | DIGAGKGKYYAVNYP ECCCCCCCEEEEECC | 38.28 | 26320211 | |
221 | Phosphorylation | IGAGKGKYYAVNYPL CCCCCCCEEEEECCC | 12.82 | 20068231 | |
222 | Phosphorylation | GAGKGKYYAVNYPLR CCCCCCEEEEECCCC | 13.94 | 20068231 | |
226 | Phosphorylation | GKYYAVNYPLRDGID CCEEEEECCCCCCCC | 9.31 | 20068231 | |
236 | Phosphorylation | RDGIDDESYEAIFKP CCCCCCHHHHHHHHH | 34.96 | 20068231 | |
237 | Phosphorylation | DGIDDESYEAIFKPV CCCCCHHHHHHHHHH | 13.82 | 20068231 | |
242 | Ubiquitination | ESYEAIFKPVMSKVM HHHHHHHHHHHHHHH | 30.50 | 21906983 | |
261 | Glutathionylation | PSAVVLQCGSDSLSG CCEEEEECCCCCCCC | 5.01 | 22555962 | |
261 | S-nitrosylation | PSAVVLQCGSDSLSG CCEEEEECCCCCCCC | 5.01 | - | |
261 | S-nitrosocysteine | PSAVVLQCGSDSLSG CCEEEEECCCCCCCC | 5.01 | - | |
263 | O-linked_Glycosylation | AVVLQCGSDSLSGDR EEEEECCCCCCCCCC | 31.49 | 23301498 | |
273 | S-nitrosylation | LSGDRLGCFNLTIKG CCCCCEECEEEEECC | 2.12 | - | |
273 | S-nitrosocysteine | LSGDRLGCFNLTIKG CCCCCEECEEEEECC | 2.12 | - | |
279 | Ubiquitination | GCFNLTIKGHAKCVE ECEEEEECCCHHHHH | 39.13 | - | |
283 | Ubiquitination | LTIKGHAKCVEFVKS EEECCCHHHHHHHHH | 32.89 | - | |
290 | Phosphorylation | KCVEFVKSFNLPMLM HHHHHHHHCCCCEEE | 17.67 | - | |
303 | Phosphorylation | LMLGGGGYTIRNVAR EEECCCCCHHHCHHH | 11.41 | 17081983 | |
304 | Phosphorylation | MLGGGGYTIRNVARC EECCCCCHHHCHHHC | 19.41 | 20068231 | |
333 | Phosphorylation | NELPYNDYFEYFGPD CCCCCCCCHHHHCCC | 8.48 | - | |
336 | Phosphorylation | PYNDYFEYFGPDFKL CCCCCHHHHCCCCEE | 12.16 | - | |
342 | Sumoylation | EYFGPDFKLHISPSN HHHCCCCEEEECCCC | 46.68 | - | |
346 | Phosphorylation | PDFKLHISPSNMTNQ CCCEEEECCCCCCCC | 16.13 | 28450419 | |
348 | Phosphorylation | FKLHISPSNMTNQNT CEEEECCCCCCCCCH | 32.23 | 21406692 | |
350 | Sulfoxidation | LHISPSNMTNQNTNE EEECCCCCCCCCHHH | 4.34 | 28183972 | |
351 | Phosphorylation | HISPSNMTNQNTNEY EECCCCCCCCCHHHH | 37.59 | 21406692 | |
355 | Phosphorylation | SNMTNQNTNEYLEKI CCCCCCCHHHHHHHH | 21.47 | 21406692 | |
358 | Phosphorylation | TNQNTNEYLEKIKQR CCCCHHHHHHHHHHH | 23.41 | 21406692 | |
361 | Ubiquitination | NTNEYLEKIKQRLFE CHHHHHHHHHHHHHH | 53.24 | 21890473 | |
361 | Acetylation | NTNEYLEKIKQRLFE CHHHHHHHHHHHHHH | 53.24 | 19608861 | |
363 | Ubiquitination | NEYLEKIKQRLFENL HHHHHHHHHHHHHHH | 40.20 | - | |
365 | Methylation | YLEKIKQRLFENLRM HHHHHHHHHHHHHCC | 36.02 | - | |
393 | Phosphorylation | EDAIPEESGDEDEDD CCCCCCCCCCCCCCC | 50.29 | 29255136 | |
406 | Phosphorylation | DDPDKRISICSSDKR CCCCCCEEEECCCCE | 22.90 | 30266825 | |
409 | Phosphorylation | DKRISICSSDKRIAC CCCEEEECCCCEEEE | 39.64 | 23927012 | |
410 | Phosphorylation | KRISICSSDKRIACE CCEEEECCCCEEEEE | 42.62 | 30266825 | |
412 | Ubiquitination | ISICSSDKRIACEEE EEEECCCCEEEEECC | 47.88 | - | |
412 | Acetylation | ISICSSDKRIACEEE EEEECCCCEEEEECC | 47.88 | 23749302 | |
421 | Phosphorylation | IACEEEFSDSEEEGE EEEECCCCCCHHCCC | 43.43 | 29255136 | |
423 | Phosphorylation | CEEEFSDSEEEGEGG EECCCCCCHHCCCCC | 45.79 | 29255136 | |
432 | Methylation | EEGEGGRKNSSNFKK HCCCCCCCCCHHHHH | 65.54 | 18438403 | |
432 | Acetylation | EEGEGGRKNSSNFKK HCCCCCCCCCHHHHH | 65.54 | 8439421 | |
434 | Phosphorylation | GEGGRKNSSNFKKAK CCCCCCCCHHHHHHH | 29.69 | 23927012 | |
435 | Phosphorylation | EGGRKNSSNFKKAKR CCCCCCCHHHHHHHC | 56.53 | 23927012 | |
438 | Ubiquitination | RKNSSNFKKAKRVKT CCCCHHHHHHHCCCC | 56.95 | - | |
438 | Acetylation | RKNSSNFKKAKRVKT CCCCHHHHHHHCCCC | 56.95 | 25953088 | |
438 | Sumoylation | RKNSSNFKKAKRVKT CCCCHHHHHHHCCCC | 56.95 | 28112733 | |
439 | Acetylation | KNSSNFKKAKRVKTE CCCHHHHHHHCCCCH | 55.81 | 8439409 | |
441 | Acetylation | SSNFKKAKRVKTEDE CHHHHHHHCCCCHHH | 67.61 | 8439427 | |
444 | Sumoylation | FKKAKRVKTEDEKEK HHHHHCCCCHHHHCC | 50.67 | 11960997 | |
444 | Sumoylation | FKKAKRVKTEDEKEK HHHHHCCCCHHHHCC | 50.67 | - | |
445 | Phosphorylation | KKAKRVKTEDEKEKD HHHHCCCCHHHHCCC | 45.90 | 30576142 | |
457 | Sumoylation | EKDPEEKKEVTEEEK CCCHHHHHCCCHHHH | 61.77 | 25218447 | |
457 | Sumoylation | EKDPEEKKEVTEEEK CCCHHHHHCCCHHHH | 61.77 | - | |
460 | Phosphorylation | PEEKKEVTEEEKTKE HHHHHCCCHHHHHHH | 38.48 | 28122231 | |
476 | Sumoylation | KPEAKGVKEEVKLA- CCCCCCCCHHHCCC- | 57.75 | 11960997 | |
476 | Sumoylation | KPEAKGVKEEVKLA- CCCCCCCCHHHCCC- | 57.75 | - | |
480 | Sumoylation | KGVKEEVKLA----- CCCCHHHCCC----- | 41.81 | 28112733 | |
480 | Ubiquitination | KGVKEEVKLA----- CCCCHHHCCC----- | 41.81 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
421 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
421 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
421 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
421 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
423 | S | Phosphorylation | Kinase | CSNK2A1 | P68400 | GPS |
423 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
423 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
423 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
- | K | Ubiquitination | E3 ubiquitin ligase | KCTD11 | Q693B1 | PMID:20081843 |
- | K | Ubiquitination | E3 ubiquitin ligase | CHFR | Q96EP1 | PMID:19182791 |
- | K | Ubiquitination | E3 ubiquitin ligase | RCHY1 | Q96PM5 | PMID:18344599 |
* 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 HDAC1_HUMAN !! |
Kegg Disease | |
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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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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, AND MASSSPECTROMETRY. | |
Methylation | |
Reference | PubMed |
"Protein lysine methyltransferase G9a acts on non-histone targets."; Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R.,Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.; Nat. Chem. Biol. 4:344-346(2008). Cited for: METHYLATION AT LYS-432. | |
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-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY. | |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND MASSSPECTROMETRY. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY. | |
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, ANDMASS SPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND MASSSPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND MASSSPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, ANDMASS SPECTROMETRY. | |
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY. | |
"Histone deacetylase 1 phosphorylation promotes enzymatic activity andcomplex formation."; Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L.; J. Biol. Chem. 276:47733-47741(2001). Cited for: PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 ANDSER-423, AND MASS SPECTROMETRY. | |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, AND MASSSPECTROMETRY. | |
Sumoylation | |
Reference | PubMed |
"SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates itsbiological activities."; David G., Neptune M.A., DePinho R.A.; J. Biol. Chem. 277:23658-23663(2002). Cited for: SUMOYLATION AT LYS-444 AND LYS-476. |