Reviewed, UniProtKB/Swiss-Prot Q80ZH1 (HDAC5_CRIGR)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 5
      Short name=HD5
    EC=3.5.1.98

Gene names

Name:

HDAC5

Organism

Cricetulus griseus (Chinese hamster)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	1111 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with KDM5B By similarity. Interacts with BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2, AHRR, and a 14-3-3 chaperone protein.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-250 and Ser-489 by CaMK By similarity.
Domain	The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.
Post-translational modification	Phosphorylated by CaMK at Ser-250 and Ser-489. The phosphorylation is required for the export to the cytoplasm By similarity. Ubiquitinated. Polyubiquitination however does not lead to its degradation By similarity.
Sequence similarities	Belongs to the histone deacetylase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell histone deacetylase complex Inferred from electronic annotation. Source: InterPro
Molecular function	histone deacetylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1111	1111	Histone deacetylase 5		PRO_0000357050
Regions
	Region	671 – 1017	347	Histone deacetylase
	Motif	1070 – 1109	40	Nuclear export signal By similarity
	Compositional bias	47 – 52	6	Poly-Gly
	Compositional bias	85 – 92	8	Poly-Gln
	Compositional bias	578 – 588	11	Poly-Glu
Sites
	Active site	822	1	By similarity
Amino acid modifications
	Modified residue	250	1	Phosphoserine; by CaMK By similarity
	Modified residue	489	1	Phosphoserine; by CaMK By similarity
	Modified residue	524	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q80ZH1-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 52559AE959E190E6	FASTA	1,111	120,988
	10 20 30 40 50 60 MNSPNESDGM PGREPSLEIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR 70 80 90 100 110 120 GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 130 140 150 160 170 180 QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE 190 200 210 220 230 240 FLLSKSKEPT PGSLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR 250 260 270 280 290 300 DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS 310 320 330 340 350 360 VCNSAPGSGP SSPNSSHSAI AENGFTGSVP NIPTEMLPQH RALPLDSSPN QFSLYTSPSL 370 380 390 400 410 420 PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG 430 440 450 460 470 480 VTLEGDTSPH GHASLLQHVL LLEQARQQST LIAVPLHGQS PLVTGERVAT SMRTVGKLPR 490 500 510 520 530 540 HRPLSRTQSS PLPQSPQALQ QLVMQQQHQQ FLEKQKQQQM QLGKILTKTG ELPRQPTTHP 550 560 570 580 590 600 EETEEELTEQ QEALLGEGAL TMPREGSTES ESTQEDLEEE EDEEEEDEDC IQVKDEEGES 610 620 630 640 650 660 GPDEGPDLEE SSAGYKKLFT DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS 670 680 690 700 710 720 PPDQPTKHLF TTGVVYDTFM LKHQCMCGNT HVHPEHAGRI QSIWSRLQET GLLSKCERIR 730 740 750 760 770 780 GRKATLDEIQ TVHSEYHTLL YGTSPLNRQK LDSKKLLGPI SQKMYAMLPC GGIGVDSDTV 790 800 810 820 830 840 WNEMHSSSAV RMAVGCLVEL AFKVAAGELK NGFAIIRPPG HHAEESTAMG FCFFNSVAIT 850 860 870 880 890 900 AKLLQQKLNV GKVLIVDWDI HHGNGTQQAF YDDPSVLYIS LHRYDNGNFF PGSGAPEEVG 910 920 930 940 950 960 GGPGMGYNVN VAWTGGVDPP IGDVEYLTAF RTVVMPIAHE FSPDVVLVSA GFDAVEGHLS 970 980 990 1000 1010 1020 PLGGYSVTAR CFGHLTRQLM TLAGGRVVLA LEGGHDLTAI CDASEACVSA LLSVELQPLD 1030 1040 1050 1060 1070 1080 EAVLQQKPSI NAVATLEKVI EIQSKHWSCV QRFATGLGCS LQEAQAGETE EAETVSAMAL 1090 1100 1110 LSVGAEQAQA VATQEHSPRP AEEPMEQEPT L

References

[1]	"Suppressors of alpha(1,3)fucosylation identified by expression cloning in the LEC11B gain-of-function CHO mutant." Chen W., Tang J., Stanley P. Glycobiology 15:259-269(2005) [PubMed: 15525819] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY145846 mRNA. Translation: AAN46420.1.
3D structure databases
SMR	Q80ZH1. Positions 670-1052.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q80ZH1.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR017320. Histone_deAcase_II_euk. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037911. HDAC_II_euk. 1 hit.
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...

Entry information

Entry name

HDAC5_CRIGR

Accession

Primary (citable) accession number: Q80ZH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	June 1, 2003
Last modified:	October 13, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)