HDAC1_RAT
ID HDAC1_RAT Reviewed; 482 AA.
AC Q4QQW4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Histone deacetylase 1;
DE Short=HD1;
DE EC=3.5.1.98 {ECO:0000250|UniProtKB:Q13547};
DE AltName: Full=Protein deacetylase HDAC1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE AltName: Full=Protein decrotonylase HDAC1;
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
GN Name=Hdac1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC and plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. Histone deacetylases act via the
CC formation of large multiprotein complexes. Also functions as
CC deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3 and
CC TSHZ3. Deacetylates SP proteins, SP1 and SP3, and regulates their
CC function. Component of the BRG1-RB1-HDAC1 complex, which negatively
CC regulates the CREST-mediated transcription in resting neurons. Upon
CC calcium stimulation, HDAC1 is released from the complex and CREBBP is
CC recruited, which facilitates transcriptional activation. Deacetylates
CC TSHZ3 and regulates its transcriptional repressor activity.
CC Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional
CC activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of
CC KAT5-mediated relieving of NR1D2 transcription repression activity (By
CC similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that
CC suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC genes implicated in multilineage blood cell development. Involved in
CC CIART-mediated transcriptional repression of the circadian
CC transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for
CC the transcriptional repression of circadian target genes, such as PER1,
CC mediated by the large PER complex or CRY1 through histone deacetylation
CC (By similarity). In addition to protein deacetylase activity, also has
CC protein-lysine deacylase activity: acts as a protein decrotonylase by
CC mediating decrotonylation ((2E)-butenoyl) of histones (By similarity).
CC {ECO:0000250|UniProtKB:O09106, ECO:0000250|UniProtKB:Q13547}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000250|UniProtKB:Q13547};
CC -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with
CC MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome
CC remodeling and histone deacetylation (NuRD) complex, or with SIN3,
CC SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC
CC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35,
CC KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain
CC ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor
CC complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1
CC and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the
CC interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of
CC a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28,
CC HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL,
CC MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the
CC histone deacetylation is composed of at least HDAC1, PER2, SFPQ and
CC SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in
CC a complex with DNMT3A and HDAC7. Interacts with the non-histone region
CC of MACROH2A1. Interacts with TRIM28; the interaction recruits HDAC1 to
CC E2F1 and inhibits its acetylation. Interacts with SP1; the interaction
CC deacetylates SP1 and regulates its transcriptional activity. Interacts
CC with SP3; the interaction deacetylates SP3 and regulates its
CC transcriptional activity. In vitro, C(18) ceramides increase this
CC interaction and the subsequent SP3 deacetylation and SP3-mediated
CC repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus);
CC the interaction is direct. Interacts with APEX1; the interaction is not
CC dependent on the acetylated status of APEX1. Interacts with
CC C10orf90/FATS (via its N-terminal); the interaction prevents binding of
CC HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization
CC of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed
CC to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with
CC NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this
CC interaction affects HDAC1 activity on MYOG promoter and thus inhibits
CC MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6,
CC BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX,
CC DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4,
CC NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6,
CC PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2,
CC SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541.
CC Interacts with KDM5A; this interaction impairs histone deacetylation
CC (By similarity). Interacts with DNTTIP1. Identified in a histone
CC deacetylase complex that contains DNTTIP1, HDAC1 and MIDEAS; this
CC complex assembles into a tetramer that contains four copies of each
CC protein chain. Interacts with CCAR2. Interacts with PPHLN1. Found in a
CC complex with YY1, SIN3A and GON4L. Interacts with CHD4. Found in a
CC complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC and TET1. Interacts with SIN3A. Interacts with DHX36; this interaction
CC occurs in a RNA-dependent manner (By similarity). Interacts with ZBTB7A
CC (By similarity). Interacts with SMAD4; positively regulated by ZBTB7A
CC (By similarity). Interacts with PACS2 (By similarity). Forms a complex
CC comprising APPL1, RUVBL2, APPL2, CTNNB1 and HDAC2 (By similarity).
CC Interacts with ZNF638 (By similarity). Interacts with SPHK2 (By
CC similarity). Interacts with ERCC6 (By similarity). Interacts with NSD2
CC (By similarity). Interacts with SMYD4 (via MYND-type zinc finger) (By
CC similarity). Interacts with PWWP2A in a MTA1-dependent manner (By
CC similarity). Interacts with PWWP2B (By similarity). Interacts with
CC ZNF516 and BRCC3; these interactions are enhanced in the presence of
CC PWWP2B (By similarity). Interacts with SANBR (via the BTB domain) (By
CC similarity). {ECO:0000250|UniProtKB:O09106,
CC ECO:0000250|UniProtKB:Q13547}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13547}.
CC -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
CC activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.
CC -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity
CC and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.
CC {ECO:0000250|UniProtKB:Q13547}.
CC -!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by
CC the proteasome. {ECO:0000250|UniProtKB:Q13547}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC subfamily. {ECO:0000305}.
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DR EMBL; BC097943; AAH97943.1; -; mRNA.
DR EMBL; BC107476; AAI07477.1; -; mRNA.
DR RefSeq; NP_001020580.1; NM_001025409.1.
DR AlphaFoldDB; Q4QQW4; -.
DR SMR; Q4QQW4; -.
DR BioGRID; 255695; 6.
DR IntAct; Q4QQW4; 3.
DR MINT; Q4QQW4; -.
DR STRING; 10116.ENSRNOP00000012854; -.
DR BindingDB; Q4QQW4; -.
DR ChEMBL; CHEMBL2915; -.
DR DrugCentral; Q4QQW4; -.
DR iPTMnet; Q4QQW4; -.
DR PhosphoSitePlus; Q4QQW4; -.
DR jPOST; Q4QQW4; -.
DR PaxDb; Q4QQW4; -.
DR PRIDE; Q4QQW4; -.
DR Ensembl; ENSRNOT00000012854; ENSRNOP00000012854; ENSRNOG00000009568.
DR GeneID; 297893; -.
DR KEGG; rno:297893; -.
DR UCSC; RGD:619975; rat.
DR CTD; 3065; -.
DR RGD; 1309799; Hdac1.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000154301; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q4QQW4; -.
DR OMA; HFGMTHP; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q4QQW4; -.
DR TreeFam; TF106171; -.
DR Reactome; R-RNO-1538133; G0 and Early G1.
DR Reactome; R-RNO-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-RNO-3214815; HDACs deacetylate histones.
DR Reactome; R-RNO-350054; Notch-HLH transcription pathway.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-RNO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-RNO-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-RNO-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR Reactome; R-RNO-9022692; Regulation of MECP2 expression and activity.
DR Reactome; R-RNO-9701898; STAT3 nuclear events downstream of ALK signaling.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q4QQW4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009568; Expressed in thymus and 20 other tissues.
DR Genevisible; Q4QQW4; RN.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0016581; C:NuRD complex; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016580; C:Sin3 complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0019213; F:deacetylase activity; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0070888; F:E-box binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0004407; F:histone deacetylase activity; IMP:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; ISO:RGD.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; ISO:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IGI:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0009913; P:epidermal cell differentiation; ISO:RGD.
DR GO; GO:0061029; P:eyelid development in camera-type eye; ISO:RGD.
DR GO; GO:0061198; P:fungiform papilla formation; ISO:RGD.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR GO; GO:0016575; P:histone deacetylation; ISO:RGD.
DR GO; GO:0070932; P:histone H3 deacetylation; IMP:RGD.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:0032732; P:positive regulation of interleukin-1 production; IMP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IMP:RGD.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IMP:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:RGD.
DR GO; GO:0006476; P:protein deacetylation; ISO:RGD.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; IMP:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Acetylation; Biological rhythms; Chromatin regulator; Hydrolase;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; S-nitrosylation; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..482
FT /note="Histone deacetylase 1"
FT /id="PRO_0000304731"
FT REGION 9..321
FT /note="Histone deacetylase"
FT REGION 390..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 261
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P70288"
FT MOD_RES 273
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P70288"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 432
FT /note="N6-methylated lysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92769"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13547"
SQ SEQUENCE 482 AA; 55093 MW; 7F6563C17F5E4844 CRC64;
MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF
SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
MA
