P56517 (HDAC1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 1
Short name=HD1
EC=3.5.1.98

Gene names

Name:	HDAC1
Synonyms:	HDAC1A

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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 By similarity.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Forms a complex with RBAP48 By similarity.
Subcellular location	Nucleus Potential.
Sequence similarities	Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation by host of viral transcription Inferred from electronic annotation. Source: Compara negative regulation of androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of receptor biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara
Cellular_component	NuRD complex Inferred from electronic annotation. Source: Compara Sin3 complex Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 12711221. Source: UniProtKB cytosol Inferred from electronic annotation. Source: Compara histone deacetylase complex Traceable author statement PubMed 12711221. Source: UniProtKB
Molecular_function	NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC RNA polymerase II transcription corepressor activity Inferred from electronic annotation. Source: Compara core promoter binding Inferred from electronic annotation. Source: Compara histone deacetylase activity Traceable author statement PubMed 12711221. Source: UniProtKB transcription factor binding Traceable author statement PubMed 12711221. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 480	480	Histone deacetylase 1		PRO_0000114689
Regions
	Region	9 – 321	313	Histone deacetylase
	Compositional bias	299 – 302	4	Poly-Gly
	Compositional bias	396 – 399	4	Poly-Glu
	Compositional bias	446 – 453	8	Poly-Glu
Sites
	Active site	141	1	By similarity
Experimental info
	Sequence conflict	3 – 4	2	LT → VM in AAB99850. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P56517 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 82C78CE285C779D9	FASTA	480	54,939
	10 20 30 40 50 60 MALTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN 70 80 90 100 110 120 AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSAGGSVAS 130 140 150 160 170 180 AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG 190 200 210 220 230 240 DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 250 260 270 280 290 300 FKPVISKVME TFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 310 320 330 340 350 360 GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 370 380 390 400 410 420 KIKQRLFENL RMLPHAPGVQ MQPIPEDAVQ EDSGDEEEED PEKRISIRNS DKRISCDEEF 430 440 450 460 470 480 SDSEDEGEGG RKNVANFKKA KRVKTEEEKE EEEKKDEKEE EKAKEEKAEP KGVKEETKST

References

[1]	Takami Y. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Sun J.M., Chen H.Y., Davie J.R. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF039751 mRNA. Translation: AAB96923.1. AF043328 mRNA. Translation: AAB99850.1. AF044169 mRNA. Translation: AAC00504.1.
IPI	IPI00581674.
RefSeq	NP_989487.1. NM_204156.1.
UniGene	Gga.10603.
3D structure databases
ProteinModelPortal	P56517.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000005212.
Proteomic databases
PaxDb	P56517.
PRIDE	P56517.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000005221; ENSGALP00000005212; ENSGALG00000003297.
GeneID	373961.
KEGG	gga:373961.
Organism-specific databases
CTD	3065.
Phylogenomic databases
eggNOG	COG0123.
GeneTree	ENSGT00530000062889.
HOGENOM	HOG000225180.
HOVERGEN	HBG057112.
InParanoid	P56517.
KO	K06067.
OMA	RISCDEE.
OrthoDB	EOG4868CH.
Enzyme and pathway databases
BRENDA	3.5.1.98. 1306.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...
Other
BindingDB	P56517.
ChEMBL	CHEMBL4582.
NextBio	20813492.

Entry information

Entry name

HDAC1_CHICK

Accession

Primary (citable) accession number: P56517

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program