Predicate | Object |
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rdf:type | |
biopax3:comment |
FUNCTION: 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. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor 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. CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone. SUBUNIT: Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region) (By similarity). Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, 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, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A. and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. SUBCELLULAR LOCATION: Nucleus. TISSUE SPECIFICITY: Widely expressed; lower levels in brain and lung. PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys- 262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching (By similarity). SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily. SEQUENCE CAUTION: Sequence=AAH31055.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=BAG59420.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAI14206.1; Type=Miscellaneous discrepancy; Note=Erroneous gene model prediction; GENE SYNONYMS:HDAC2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 488 AA; 55364 MW; 775419CCCDAE07FA CRC64;
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biopax3:xref |
urn:biopax:RelationshipXref:HGNC_HGNC:4853,
urn:biopax:RelationshipXref:NCBI GENE_3066,
urn:biopax:RelationshipXref:REFSEQ_NP_001518,
urn:biopax:UnificationXref:UNIPROT_B4DL58,
urn:biopax:UnificationXref:UNIPROT_E1P561,
urn:biopax:UnificationXref:UNIPROT_Q5SRI8,
urn:biopax:UnificationXref:UNIPROT_Q5SZ86,
urn:biopax:UnificationXref:UNIPROT_Q8NEH4,
urn:biopax:UnificationXref:UNIPROT_Q92769
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biopax3:displayName |
HDAC2_HUMAN
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biopax3:name |
3.5.1.98,
HD2,
HDAC2
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biopax3:entityFeature |
urn:biopax:ModificationFeature:HDAC2_HUMAN_1,
urn:biopax:ModificationFeature:HDAC2_HUMAN_2,
urn:biopax:ModificationFeature:HDAC2_HUMAN_3,
urn:biopax:ModificationFeature:HDAC2_HUMAN_4,
urn:biopax:ModificationFeature:HDAC2_HUMAN_5,
urn:biopax:ModificationFeature:HDAC2_HUMAN_6,
urn:biopax:ModificationFeature:HDAC2_HUMAN_7,
urn:biopax:ModificationFeature:HDAC2_HUMAN_8
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biopax3:organism | |
biopax3:sequence |
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDTKGTKSEQLSNP
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biopax3:standardName |
Histone deacetylase 2
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