Q9UQL6 (HDAC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
Antigen NY-CO-9

Gene names

Name:	HDAC5
Synonyms:	KIAA0600

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1122 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with AHRR By similarity. Interacts with BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with KDM5B. Interacts with MYOCD By similarity. Interacts with GRK5. Ref.9 Ref.11 Ref.14 Ref.18
Subcellular location	Nucleus. Cytoplasm. 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-259 and Ser-498 by AMPK, CaMK1 and SIK1. Ref.10 Ref.15
Tissue specificity	Ubiquitous.
Domain	The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm By similarity.
Post-translational modification	Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and Ser-498. The phosphorylation is required for the export to the cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylated by GRK5, leading to nuclear export of HDAC5 and allowing MEF2-mediated transcription By similarity. Ubiquitinated. Polyubiquitination however does not lead to its degradation. Ref.13
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.
Sequence caution	The sequence AAC18040.1 differs from that shown. Reason: Frameshift at position 1085. The sequence BAA25526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	B cell differentiation Traceable author statement. Source: UniProtKB cellular response to insulin stimulus Non-traceable author statement Ref.15. Source: BHF-UCL chromatin remodeling Traceable author statement. Source: ProtInc chromatin silencing Traceable author statement. Source: ProtInc inflammatory response Traceable author statement. Source: UniProtKB negative regulation of cell migration involved in sprouting angiogenesis Inferred from mutant phenotype. Source: BHF-UCL negative regulation of myotube differentiation Inferred from mutant phenotype Ref.10. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL regulation of protein binding Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA histone deacetylase complex Traceable author statement. Source: UniProtKB
Molecular function	NAD-dependent histone deacetylase activity (H3-K14 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 (H3-K16 specific) Inferred from electronic annotation. Source: EC protein kinase C binding Inferred from physical interaction Ref.20. Source: UniProtKB repressing transcription factor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRMS1	Q9HCU9	2	EBI-715576,EBI-714781

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UQL6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UQL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     684-768: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9UQL6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     7-7: S → SA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1122	1122	Histone deacetylase 5		PRO_0000114701
Regions
	Region	684 – 1028	345	Histone deacetylase
	Motif	1081 – 1122	42	Nuclear export signal
	Compositional bias	47 – 52	6	Poly-Gly
	Compositional bias	85 – 92	8	Poly-Gln
	Compositional bias	596 – 599	4	Poly-Glu
	Compositional bias	1099 – 1104	6	Poly-Ala
Sites
	Active site	833	1	By similarity
Amino acid modifications
	Modified residue	259	1	Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1
	Modified residue	292	1	Phosphothreonine; by PKC Ref.20
	Modified residue	498	1	Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1
	Modified residue	533	1	N6-acetyllysine Ref.19
	Modified residue	661	1	Phosphoserine Ref.17
Natural variations
	Alternative sequence	7	1	S → SA in isoform 3.		VSP_039180
	Alternative sequence	684 – 768	85	Missing in isoform 2.		VSP_002081
	Natural variant	137	1	R → Q. Corresponds to variant rs438096 [ dbSNP | Ensembl ].		VAR_055903
	Natural variant	565	1	G → A. Corresponds to variant rs33916560 [ dbSNP | Ensembl ].		VAR_055904
Experimental info
	Mutagenesis	259	1	S → A: Reduces AMPK- and caMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498. Does not affect phosphorylation by PKN1 and PKN2. Ref.10 Ref.15 Ref.20
	Mutagenesis	279	1	S → A: No effect. Ref.10
	Mutagenesis	291	1	S → A: Does not affect phosphorylation by PKC. Ref.20
	Mutagenesis	292	1	T → A: Abolishes phosphorylation by PKC. Ref.20
	Mutagenesis	498	1	S → A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. Ref.10 Ref.15
	Mutagenesis	661	1	S → A: No effect. Ref.10
	Mutagenesis	713	1	S → A: No effect. Ref.10
	Mutagenesis	1086	1	V → A: Reduces CaMK-dependent nuclear export. Ref.12
	Mutagenesis	1092	1	L → A: Reduces CaMK-dependent nuclear export. Ref.12
	Sequence conflict	37	1	V → L in BX458255. Ref.6
	Sequence conflict	139	1	Q → R in BX458255. Ref.6
	Sequence conflict	147	1	R → G in BX458255. Ref.6
	Sequence conflict	593	1	D → E in AAD29047. Ref.1
	Sequence conflict	593	1	D → E in AAH51824. Ref.5
	Sequence conflict	593	1	D → E in AAC18040. Ref.7
	Sequence conflict	671	1	S → N in AAC18040. Ref.7
	Sequence conflict	684	1	G → S in AAC18040. Ref.7
	Sequence conflict	1026	1	E → K in AAC18040. Ref.7
	Sequence conflict	1074	1	E → G in AAC18040. Ref.7
	Sequence conflict	1093	1	S → L in AAC18040. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: CF4BE774E3588FEC	FASTA	1,122	121,978
	10 20 30 40 50 60 MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR 70 80 90 100 110 120 GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 130 140 150 160 170 180 QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS 190 200 210 220 230 240 TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL 250 260 270 280 290 300 PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI 310 320 330 340 350 360 TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ 370 380 390 400 410 420 FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST 430 440 450 460 470 480 SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS 490 500 510 520 530 540 MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE 550 560 570 580 590 600 LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED 610 620 630 640 650 660 CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ 670 680 690 700 710 720 SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSIWSRLQE 730 740 750 760 770 780 TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP 790 800 810 820 830 840 CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM 850 860 870 880 890 900 GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF 910 920 930 940 950 960 FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS 970 980 990 1000 1010 1020 AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS 1030 1040 1050 1060 1070 1080 ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET 1090 1100 1110 1120 EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL
	Isoform 2 [UniParc]. Checksum: D4F09B907D2C1457	FASTA	1,037	112,191
	10 20 30 40 50 60 MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR 70 80 90 100 110 120 GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ 130 140 150 160 170 180 QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS 190 200 210 220 230 240 TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL 250 260 270 280 290 300 PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI 310 320 330 340 350 360 TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ 370 380 390 400 410 420 FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST 430 440 450 460 470 480 SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS 490 500 510 520 530 540 MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE 550 560 570 580 590 600 LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED 610 620 630 640 650 660 CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ 670 680 690 700 710 720 SSPAAPGGMK SPPDQPVKHL FTTGPISQKM YAVLPCGGIG VDSDTVWNEM HSSSAVRMAV 730 740 750 760 770 780 GCLLELAFKV AAGELKNGFA IIRPPGHHAE ESTAMGFCFF NSVAITAKLL QQKLNVGKVL 790 800 810 820 830 840 IVDWDIHHGN GTQQAFYNDP SVLYISLHRY DNGNFFPGSG APEEVGGGPG VGYNVNVAWT 850 860 870 880 890 900 GGVDPPIGDV EYLTAFRTVV MPIAHEFSPD VVLVSAGFDA VEGHLSPLGG YSVTARCFGH 910 920 930 940 950 960 LTRQLMTLAG GRVVLALEGG HDLTAICDAS EACVSALLSV ELQPLDEAVL QQKPNINAVA 970 980 990 1000 1010 1020 TLEKVIEIQS KHWSCVQKFA AGLGRSLREA QAGETEEAET VSAMALLSVG AEQAQAAAAR 1030 EHSPRPAEEP MEQEPAL
	Isoform 3 [UniParc]. Checksum: 909ED5CCFEE3FB4F	FASTA	1,123	122,049
	10 20 30 40 50 60 MNSPNESADG MSGREPSLEI LPRTSLHSIP VTVEVKPVLP RAMPSSMGGG GGGSPSPVEL 70 80 90 100 110 120 RGALVGSVDP TLREQQLQQE LLALKQQQQL QKQLLFAEFQ KQHDHLTRQH EVQLQKHLKQ 130 140 150 160 170 180 QQEMLAAKQQ QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA 190 200 210 220 230 240 STEVKLRLQE FLLSKSKEPT PGGLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK 250 260 270 280 290 300 LPLPGPYDSR DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE 310 320 330 340 350 360 ITGAGPGASS VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMLPQH RALPLDSSPN 370 380 390 400 410 420 QFSLYTSPSL PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS 430 440 450 460 470 480 TSSIPGCLLG VALEGDGSPH GHASLLQHVL LLEQARQQST LIAVPLHGQS PLVTGERVAT 490 500 510 520 530 540 SMRTVGKLPR HRPLSRTQSS PLPQSPQALQ QLVMQQQHQQ FLEKQKQQQL QLGKILTKTG 550 560 570 580 590 600 ELPRQPTTHP EETEEELTEQ QEVLLGEGAL TMPREGSTES ESTQEDLEEE DEEDDGEEEE 610 620 630 640 650 660 DCIQVKDEEG ESGAEEGPDL EEPGAGYKKL FSDAQPLQPL QVYQAPLSLA TVPHQALGRT 670 680 690 700 710 720 QSSPAAPGGM KSPPDQPVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG RIQSIWSRLQ 730 740 750 760 770 780 ETGLLSKCER IRGRKATLDE IQTVHSEYHT LLYGTSPLNR QKLDSKKLLG PISQKMYAVL 790 800 810 820 830 840 PCGGIGVDSD TVWNEMHSSS AVRMAVGCLL ELAFKVAAGE LKNGFAIIRP PGHHAEESTA 850 860 870 880 890 900 MGFCFFNSVA ITAKLLQQKL NVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN 910 920 930 940 950 960 FFPGSGAPEE VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA HEFSPDVVLV 970 980 990 1000 1010 1020 SAGFDAVEGH LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT AICDASEACV 1030 1040 1050 1060 1070 1080 SALLSVELQP LDEAVLQQKP NINAVATLEK VIEIQSKHWS CVQKFAAGLG RSLREAQAGE 1090 1100 1110 1120 TEEAETVSAM ALLSVGAEQA QAAAAREHSP RPAEEPMEQE PAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three proteins define a class of human histone deacetylases related to yeast Hda1p." Grozinger C.M., Hassig C.A., Schreiber S.L. Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999) [PubMed: 10220385] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed: 9628581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye and Testis.
[6]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3). Tissue: Neuroblastoma.
[7]	"Characterization of human colon cancer antigens recognized by autologous antibodies." Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J. Int. J. Cancer 76:652-658(1998) [PubMed: 9610721] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-1122 (ISOFORM 1). Tissue: Colon carcinoma.
[8]	"Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5)." Mahlknecht U., Schnittger S., Ottmann O.G., Schoch C., Mosebach M., Hiddemann W., Hoelzer D. Biochim. Biophys. Acta 1493:342-348(2000) [PubMed: 11018260] [Abstract] Cited for: GENE ORGANIZATION.
[9]	"BCoR, a novel corepressor involved in BCL-6 repression." Huynh K.D., Fischle W., Verdin E., Bardwell V.J. Genes Dev. 14:1810-1823(2000) [PubMed: 10898795] [Abstract] Cited for: INTERACTION WITH BCOR.
[10]	"Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation." McKinsey T.A., Zhang C.-L., Lu J., Olson E.N. Nature 408:106-111(2000) [PubMed: 11081517] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-259; SER-279; SER-498; SER-661 AND SER-713.
[11]	"Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5." McKinsey T.A., Zhang C.-L., Olson E.N. Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000) [PubMed: 11114197] [Abstract] Cited for: INTERACTION WITH 14-3-3, PHOSPHORYLATION AT SER-259 AND SER-498.
[12]	"Identification of a signal-responsive nuclear export sequence in class II histone deacetylases." McKinsey T.A., Zhang C.-L., Olson E.N. Mol. Cell. Biol. 21:6312-6321(2001) [PubMed: 11509672] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF VAL-1086 AND LEU-1092.
[13]	"Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes." Hook S.S., Orian A., Cowley S.M., Eisenman R.N. Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002) [PubMed: 12354939] [Abstract] Cited for: UBIQUITINATION.
[14]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed: 17373667] [Abstract] Cited for: INTERACTION WITH KDM5B.
[15]	"AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5." McGee S.L., van Denderen B.J., Howlett K.F., Mollica J., Schertzer J.D., Kemp B.E., Hargreaves M. Diabetes 57:860-867(2008) [PubMed: 18184930] [Abstract] Cited for: PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-259 AND SER-498.
[16]	"Protein kinase D-dependent phosphorylation and nuclear export of histone deacetylase 5 mediates vascular endothelial growth factor-induced gene expression and angiogenesis." Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K., McKinsey T.A., Olson E.N., Jin Z.G. J. Biol. Chem. 283:14590-14599(2008) [PubMed: 18332134] [Abstract] Cited for: PHOSPHORYLATION AT SER-259 AND SER-498.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Human BAHD1 promotes heterochromatic gene silencing." Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M., Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J., Cossart P. Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009) [PubMed: 19666599] [Abstract] Cited for: INTERACTION WITH BAHD1.
[19]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, MASS SPECTROMETRY.
[20]	"Protein kinase C-related kinase targets nuclear localization signals in a subset of class IIa histone deacetylases." Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B., McKinsey T.A. FEBS Lett. 584:1103-1110(2010) [PubMed: 20188095] [Abstract] Cited for: PHOSPHORYLATION AT THR-292, MUTAGENESIS OF SER-259; SER-291 AND THR-292.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF132608 mRNA. Translation: AAD29047.1. AB011172 mRNA. Translation: BAA25526.2. Different initiation. AC023855 Genomic DNA. No translation available. BC013140 mRNA. Translation: AAH13140.1. Different termination. BC051824 mRNA. Translation: AAH51824.1. BX458255 mRNA. No translation available. AF039691 mRNA. Translation: AAC18040.1. Frameshift. BK000028 Genomic DNA. Translation: DAA00017.1.
IPI	IPI00217801. IPI00328289. IPI00556288.
RefSeq	NP_001015053.1. NM_001015053.1. NP_005465.2. NM_005474.4.
UniGene	Hs.438782.
3D structure databases
ProteinModelPortal	Q9UQL6.
SMR	Q9UQL6. Positions 67-133, 681-1081.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38260N.
IntAct	Q9UQL6. 7 interactions.
MINT	MINT-1407477.
STRING	Q9UQL6.
PTM databases
PhosphoSite	Q9UQL6.
Polymorphism databases
DMDM	296434519.
Proteomic databases
PRIDE	Q9UQL6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000393622; ENSP00000377244; ENSG00000108840.
GeneID	10014.
KEGG	hsa:10014.
UCSC	uc002ifd.1. human. uc010czp.1. human.
Organism-specific databases
CTD	10014.
GeneCards	GC17M042164.
H-InvDB	HIX0013862.
HGNC	HGNC:14068. HDAC5.
HPA	CAB019400. HPA030991.
MIM	605315. gene.
neXtProt	NX_Q9UQL6.
PharmGKB	PA29230.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04652.
GeneTree	ENSGT00530000062809.
HOVERGEN	HBG057100.
InParanoid	Q9UQL6.
OMA	NESADGM.
PhylomeDB	Q9UQL6.
Enzyme and pathway databases
Pathway_Interaction_DB	hdac_classi_pathway. Signaling events mediated by HDAC Class I. hdac_classii_pathway. Signaling events mediated by HDAC Class II.
Gene expression databases
ArrayExpress	Q9UQL6.
Bgee	Q9UQL6.
CleanEx	HS_HDAC5.
Genevestigator	Q9UQL6.
GermOnline	ENSG00000108840. Homo sapiens.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. IPR024643. Hist_deacetylase_Gln_rich_N. IPR017320. Histone_deAcase_II_euk. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
KO	K11406.
PANTHER	PTHR10625. His_deacetylse. 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
NextBio	37831.
SOURCE	Search...

Entry information

Entry name

HDAC5_HUMAN

Accession

Primary (citable) accession number: Q9UQL6
Secondary accession number(s): C9JFV9 , O60340, O60528, Q96DY4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.