Q32PJ8 (HDAC1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 76. History...
Names and origin
|Protein names||Recommended name:|
Histone deacetylase 1
|Organism||Bos taurus (Bovine) [Reference proteome]|
|Taxonomic identifier||9913 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos|
|Sequence length||482 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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. 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. 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 By similarity.
Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with BAZ2A/TIP5, BCOR, BRMS1L, DAXX, DNMT1, EP300, HCFC1, NFE4, PCAF, PHB2, MIER1, KDM4A, MINT, NRIP1, PRDM6, RERE, SETDB1, SMYD2, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with BANP, CBFA2T3 and KDM5B. Interacts with E4F1 and KLF1. Interacts with CHFR, PRDM16, SP1, SP3, and SMAD3. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with NR4A2/NURR1 and BRMS1. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SAMSN1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21 Interacts with CDKN1A/p21; the interaction is prevented by binding of C10orf90/FATS facilitating acetylation and stabilization of CDKN1A/p21. Binds to CDK5 complexed to CDK5R1 (p25). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B By similarity. Interacts with ZMYND15. Interacts with DDX5. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with BCL6 and DDIT3/CHOP By similarity.
Nucleus By similarity.
Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1 By similarity.
Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5 By similarity.
Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome By similarity.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 482||482||Histone deacetylase 1||PRO_0000304729|
|Region||9 – 321||313||Histone deacetylase|
|Active site||141||1||By similarity|
Amino acid modifications
|Modified residue||74||1||N6-acetyllysine By similarity|
|Modified residue||220||1||N6-acetyllysine By similarity|
|Modified residue||393||1||Phosphoserine By similarity|
|Modified residue||421||1||Phosphoserine By similarity|
|Modified residue||423||1||Phosphoserine By similarity|
|Modified residue||432||1||N6-methylated lysine; by EHMT2 By similarity|
|Cross-link||444||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|Cross-link||476||Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity|
|||"Characterization of 954 bovine full-CDS cDNA sequences."|
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
|||NIH - Mammalian Gene Collection (MGC) project|
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
|BT030718 mRNA. Translation: ABS45034.1.|
BC108088 mRNA. Translation: AAI08089.1.
|RefSeq||NP_001032521.1. NM_001037444.2. |
3D structure databases
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSBTAT00000016877; ENSBTAP00000016877; ENSBTAG00000012698. |
Enzyme and pathway databases
Gene expression databases
Family and domain databases
|Gene3D||3.40.800.20. 1 hit. |
|InterPro||IPR000286. His_deacetylse. |
|PANTHER||PTHR10625. PTHR10625. 1 hit. |
|Pfam||PF00850. Hist_deacetyl. 1 hit. |
|PIRSF||PIRSF037913. His_deacetylse_1. 1 hit. |
|PRINTS||PR01270. HDASUPER. |
|Accession||Primary (citable) accession number: Q32PJ8|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families