P83038 (HDAC4_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 4
Short name=HD4
EC=3.5.1.98

Gene names

Name:

HDAC4

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	1080 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.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Traceable author statement PubMed 12711221. Source: UniProtKB histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC inflammatory response Traceable author statement PubMed 12711221. Source: UniProtKB negative regulation of striated muscle tissue development Traceable author statement PubMed 12711221. Source: UniProtKB negative regulation of transcription, DNA-dependent Traceable author statement PubMed 12711221. Source: UniProtKB nervous system development Traceable author statement PubMed 12711221. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	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 histone deacetylase activity Traceable author statement PubMed 12711221. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 1080	1080	Histone deacetylase 4		PRO_0000114700
Regions
	Region	651 – 1080	430	Histone deacetylase
Sites
	Active site	799	1	By similarity
	Metal binding	663	1	Zinc By similarity
	Metal binding	665	1	Zinc By similarity
	Metal binding	671	1	Zinc By similarity
	Metal binding	747	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P83038 [UniParc]. Last modified August 14, 2001. Version 1. Checksum: B6416E2C43F1428C	FASTA	1,080	119,468
	10 20 30 40 50 60 MSSQSHPDGL SGRDQPVELL NPPRVNHMPS SVDVSTALPL QVAPTSVPMD LRLDHQFPMP 70 80 90 100 110 120 VTEPTLREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQEMLAM 130 140 150 160 170 180 KHQQELLEHQ RKLEQHRQEQ ELEKQHREQK LQQLKNKEKG KESAVASTEV KMKLQEFVLN 190 200 210 220 230 240 KKKALAHRNL NHCISSDPRF WYGKTQHSSL DQSSPPQSGV SGTYNHPVLG MYDSKDDFPL 250 260 270 280 290 300 RKTASEPNLK LRSRLKQKVA ERRSSPLLRR KDGPVVTALK KRPLDVTDSA CNSAPGSGPS 310 320 330 340 350 360 SPNNSSNNIS AENGITGSVT SIQAETSLAH RLVNREGSVT QLPLYTSPSL PNITLGLPAT 370 380 390 400 410 420 GPSSGGSAQQ DAERLAIPAL QQRISLFPGT HLTPYLSTTT LERDGGTAHN PLLQHMVLLE 430 440 450 460 470 480 QPTAQTPLVT GLPLHAQSLV GGERVSPSIH KLRQHRPLGR TQSAPLPQNA QALQQLVIQQ 490 500 510 520 530 540 QHQQFLEKHK QQFQQQQLHI NKIISKPNEP ARQHESHPEE TEEELREHQA LLEEPYSDRV 550 560 570 580 590 600 SSQKEVPGLA NMVQVKQEPI ESDEEEAEPQ QELESGQRQA EQELLFRQQA LLLEQQRIHQ 610 620 630 640 650 660 LRNYQASLEA AGMPVSFGGH RPLSRAQSSP ASATFPMSVQ EPPTKPRFTT GLVYDTLMLK 670 680 690 700 710 720 HQCTCGNTNS HPEHAGRIQS IWSRLQETGL RGKCECIRGR KATLEELQTV HSEAHTLLYG 730 740 750 760 770 780 TNPLNRQKLD SKKLLGSLTS MFVRLPCGGV GVDSDTIWNE VHSSGAARLA VGCVIELVFK 790 800 810 820 830 840 VATGELKNGF AVVRPPGHHA EESTPMGFCY FNSVAIAAKL LQQRLNVSKI LIVDWDVHHG 850 860 870 880 890 900 NGTQQAFYND PNVLYISLHR YDDGNFFPGS GAPDEVGTGA GVGFNVNMAF TGGLDPPMGD 910 920 930 940 950 960 TEYLTAFRTV VMPIANEFAP DVVLVSSGFD AVEGHPTPLG GYNLSAKCFG YLTKQLMGLA 970 980 990 1000 1010 1020 GGRVVLALEG GHDLTAICDA SEACVSALLG NELDPLPEKV LQQRANANAV HSMEKVIEIH 1030 1040 1050 1060 1070 1080 SKYWHSLQRY ASTVGYSLVE AQKCENEEAE TVTAMASLSV GVKPAEKRPD DEPMEEEPPL

References

[1]	Takechi S., Azuma R., Nakayama T. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB052839 mRNA. Translation: BAB60957.1.
IPI	IPI00597373.
RefSeq	NP_989644.1. NM_204313.1.
UniGene	Gga.3689.
3D structure databases
ProteinModelPortal	P83038.
SMR	P83038. Positions 62-128, 646-1047.
ModBase	Search...
Protein-protein interaction databases
STRING	9031.ENSGALP00000006811.
Proteomic databases
PaxDb	P83038.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	374207.
KEGG	gga:374207.
Organism-specific databases
CTD	9759.
Phylogenomic databases
eggNOG	COG0123.
HOGENOM	HOG000232065.
HOVERGEN	HBG057100.
InParanoid	P83038.
KO	K11406.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. IPR024643. Hist_deacetylase_Gln_rich_N. IPR017320. Histone_deAcase_II_euk. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF12203. HDAC4_Gln. 1 hit. PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037911. HDAC_II_euk. 1 hit.
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...
Other
BindingDB	P83038.
ChEMBL	CHEMBL5599.
NextBio	20813711.

Entry information

Entry name

HDAC4_CHICK

Accession

Primary (citable) accession number: P83038

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	August 14, 2001
Last modified:	April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program