MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Histone deacetylase 5; Short=HD5; EC=3.5.1.98; AltName: Full=Antigen NY-CO-9; |
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| MyHits synonyms | HDAC5_HUMAN , Q9UQL6 , C9JFV9 , O60340 , O60528 , Q96DY4 , CF4BE774E3588FEC |
 Legends: 1, ACT_SITE {ECO:0000250}; 2, Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1. {ECO:0000269|PubMed:11114197, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:18332134}; 3, Phosphothreonine; by PKC. {ECO:0000269|PubMed:20188095}; 4, N6-acetyllysine. {ECO:0000244|PubMed:19608861}; 5, Phosphoserine. {ECO:0000244|PubMed:23186163}; 6, VAR_SEQ S -> SA (in isoform 3). {ECO:0000303|Ref.6}; 7, VARIANT R -> Q (in dbSNP:rs438096); 8, VARIANT G -> A (in dbSNP:rs33916560); 9, MUTAGEN 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. {ECO:0000269|PubMed:11081517, ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:20188095}; 10, MUTAGEN S->A: No effect. {ECO:0000269|PubMed:11081517}; 11, MUTAGEN S->A: Does not affect phosphorylation by PKC. {ECO:0000269|PubMed:20188095}; 12, MUTAGEN T->A: Abolishes phosphorylation by PKC. {ECO:0000269|PubMed:20188095}; 13, MUTAGEN S->A: Reduces AMPK- and CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259. {ECO:0000269|PubMed:11081517, ECO:0000269|PubMed:18184930}; 14, MUTAGEN V->A: Reduces CaMK-dependent nuclear export. {ECO:0000269|PubMed:11509672}; 15, MUTAGEN L->A: Reduces CaMK-dependent nuclear export. {ECO:0000269|PubMed:11509672}; 16, CONFLICT V -> L (in Ref. 6; BX458255). {ECO:0000305}; 17, CONFLICT Q -> R (in Ref. 6; BX458255). {ECO:0000305}; 18, CONFLICT R -> G (in Ref. 6; BX458255). {ECO:0000305}; 19, CONFLICT D -> E (in Ref. 1; AAD29047, 5; AAH51824 and 7; AAC18040). {ECO:0000305}; 20, CONFLICT S -> N (in Ref. 7; AAC18040). {ECO:0000305}; 21, CONFLICT G -> S (in Ref. 7; AAC18040). {ECO:0000305}; 22, CONFLICT E -> K (in Ref. 7; AAC18040). {ECO:0000305}; 23, CONFLICT E -> G (in Ref. 7; AAC18040). {ECO:0000305}; 24, CONFLICT S -> L (in Ref. 7; AAC18040). {ECO:0000305}; 25, MOTIF Nuclear export signal; 26, COMPBIAS Poly-Gly; 27, COMPBIAS Poly-Gln; 28, COMPBIAS Poly-Glu; 29, COMPBIAS Poly-Ala; 30, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:9628581}; 31, ipfam:HDAC4_Gln [T].
| |
ID HDAC5_HUMAN Reviewed; 1122 AA.
AC Q9UQL6; C9JFV9; O60340; O60528; Q96DY4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 30-NOV-2016, entry version 177.
DE RecName: Full=Histone deacetylase 5;
DE Short=HD5;
DE EC=3.5.1.98;
DE AltName: Full=Antigen NY-CO-9;
GN Name=HDAC5; Synonyms=KIAA0600;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10220385; DOI=10.1073/pnas.96.9.4868;
RA Grozinger C.M., Hassig C.A., Schreiber S.L.;
RT "Three proteins define a class of human histone deacetylases related
RT to yeast Hda1p.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4868-4873(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 189-1122 (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=9610721;
RX DOI=10.1002/(SICI)1097-0215(19980529)76:5<652::AID-IJC7>3.0.CO;2-P;
RA Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E.,
RA Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.;
RT "Characterization of human colon cancer antigens recognized by
RT autologous antibodies.";
RL Int. J. Cancer 76:652-658(1998).
RN [8]
RP GENE ORGANIZATION.
RX PubMed=11018260; DOI=10.1016/S0167-4781(00)00191-3;
RA Mahlknecht U., Schnittger S., Ottmann O.G., Schoch C., Mosebach M.,
RA Hiddemann W., Hoelzer D.;
RT "Chromosomal organization and localization of the human histone
RT deacetylase 5 gene (HDAC5).";
RL Biochim. Biophys. Acta 1493:342-348(2000).
RN [9]
RP INTERACTION WITH BCOR.
RX PubMed=10898795;
RA Huynh K.D., Fischle W., Verdin E., Bardwell V.J.;
RT "BCoR, a novel corepressor involved in BCL-6 repression.";
RL Genes Dev. 14:1810-1823(2000).
RN [10]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF SER-259;
RP SER-279; SER-498; SER-661 AND SER-713.
RX PubMed=11081517; DOI=10.1038/35040593;
RA McKinsey T.A., Zhang C.-L., Lu J., Olson E.N.;
RT "Signal-dependent nuclear export of a histone deacetylase regulates
RT muscle differentiation.";
RL Nature 408:106-111(2000).
RN [11]
RP INTERACTION WITH 14-3-3, AND PHOSPHORYLATION AT SER-259 AND SER-498.
RX PubMed=11114197; DOI=10.1073/pnas.260501497;
RA McKinsey T.A., Zhang C.-L., Olson E.N.;
RT "Activation of the myocyte enhancer factor-2 transcription factor by
RT calcium/calmodulin-dependent protein kinase-stimulated binding of 14-
RT 3-3 to histone deacetylase 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14400-14405(2000).
RN [12]
RP NUCLEAR EXPORT SIGNAL, AND MUTAGENESIS OF VAL-1086 AND LEU-1092.
RX PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
RA McKinsey T.A., Zhang C.-L., Olson E.N.;
RT "Identification of a signal-responsive nuclear export sequence in
RT class II histone deacetylases.";
RL Mol. Cell. Biol. 21:6312-6321(2001).
RN [13]
RP UBIQUITINATION.
RX PubMed=12354939; DOI=10.1073/pnas.172511699;
RA Hook S.S., Orian A., Cowley S.M., Eisenman R.N.;
RT "Histone deacetylase 6 binds polyubiquitin through its zinc finger
RT (PAZ domain) and copurifies with deubiquitinating enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13425-13430(2002).
RN [14]
RP INTERACTION WITH BCL6.
RX PubMed=12504096; DOI=10.1016/S0006-291X(02)02873-5;
RA Mascle X., Albagli O., Lemercier C.;
RT "Point mutations in BCL6 DNA-binding domain reveal distinct roles for
RT the six zinc fingers.";
RL Biochem. Biophys. Res. Commun. 300:391-396(2003).
RN [15]
RP INTERACTION WITH KDM5B.
RX PubMed=17373667; DOI=10.1002/ijc.22673;
RA Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
RA Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E.,
RA Freemont P., Taylor-Papadimitriou J.;
RT "Breast cancer associated transcriptional repressor PLU-1/JARID1B
RT interacts directly with histone deacetylases.";
RL Int. J. Cancer 121:265-275(2007).
RN [16]
RP INTERACTION WITH DDIT3.
RX PubMed=17872950; DOI=10.1074/jbc.M703735200;
RA Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.;
RT "Critical and functional regulation of CHOP (C/EBP homologous protein)
RT through the N-terminal portion.";
RL J. Biol. Chem. 282:35687-35694(2007).
RN [17]
RP PHOSPHORYLATION AT SER-259 AND SER-498, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-259 AND SER-498.
RX PubMed=18184930; DOI=10.2337/db07-0843;
RA McGee S.L., van Denderen B.J., Howlett K.F., Mollica J.,
RA Schertzer J.D., Kemp B.E., Hargreaves M.;
RT "AMP-activated protein kinase regulates GLUT4 transcription by
RT phosphorylating histone deacetylase 5.";
RL Diabetes 57:860-867(2008).
RN [18]
RP PHOSPHORYLATION AT SER-259 AND SER-498.
RX PubMed=18332134; DOI=10.1074/jbc.M800264200;
RA Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K.,
RA McKinsey T.A., Olson E.N., Jin Z.G.;
RT "Protein kinase D-dependent phosphorylation and nuclear export of
RT histone deacetylase 5 mediates vascular endothelial growth factor-
RT induced gene expression and angiogenesis.";
RL J. Biol. Chem. 283:14590-14599(2008).
RN [19]
RP INTERACTION WITH BAHD1.
RX PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C.,
RA Feunteun J., Cossart P.;
RT "Human BAHD1 promotes heterochromatic gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-533, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION AT THR-292, AND MUTAGENESIS OF SER-259; SER-291 AND
RP THR-292.
RX PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
RA Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
RA McKinsey T.A.;
RT "Protein kinase C-related kinase targets nuclear localization signals
RT in a subset of class IIa histone deacetylases.";
RL FEBS Lett. 584:1103-1110(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP INTERACTION WITH ANKRA2.
RX PubMed=22649097; DOI=10.1126/scisignal.2002979;
RA Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
RA Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
RA Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
RT "Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
RT repeat tumbler lock.";
RL Sci. Signal. 5:RA39-RA39(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611; SER-661 AND
RP SER-1108, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP FUNCTION, AND INTERACTION WITH EP300.
RX PubMed=24413532; DOI=10.1158/0008-5472.CAN-13-2020;
RA Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y.,
RA Kim Y.N., Seong J.K., Lee M.O.;
RT "Differential regulation of estrogen receptor alpha expression in
RT breast cancer cells by metastasis-associated protein 1.";
RL Cancer Res. 74:1484-1494(2014).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP INTERACTION WITH CUL7.
RX PubMed=25752541; DOI=10.1016/j.str.2015.02.001;
RA Nie J., Xu C., Jin J., Aka J.A., Tempel W., Nguyen V., You L.,
RA Weist R., Min J., Pawson T., Yang X.J.;
RT "Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome
RT protein CCDC8.";
RL Structure 23:700-712(2015).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC Histone deacetylation gives a tag for epigenetic repression and
CC plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. Histone deacetylases act via
CC the formation of large multiprotein complexes. Involved in muscle
CC maturation by repressing transcription of myocyte enhancer MEF2C.
CC During muscle differentiation, it shuttles into the cytoplasm,
CC allowing the expression of myocyte enhancer factors. Involved in
CC the MTA1-mediated epigenetic regulation of ESR1 expression in
CC breast cancer. {ECO:0000269|PubMed:24413532}.
CC -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC a histone to yield a deacetylated histone.
CC -!- SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1,
CC MEF2C, NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein.
CC Interacts with BCL6, DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts
CC with EP300 in the presence of TFAP2C. Interacts with ANKRA2.
CC Interacts with CUL7 (as part of the 3M complex); negatively
CC regulated by ANKRA2. {ECO:0000269|PubMed:10898795,
CC ECO:0000269|PubMed:11114197, ECO:0000269|PubMed:12504096,
CC ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:17872950,
CC ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:22649097,
CC ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:25752541}.
CC -!- INTERACTION:
CC Q9HCU9:BRMS1; NbExp=2; IntAct=EBI-715576, EBI-714781;
CC P08393:ICP0 (xeno); NbExp=3; IntAct=EBI-715576, EBI-6148881;
CC Q13761:RUNX3; NbExp=5; IntAct=EBI-715576, EBI-925990;
CC P31947:SFN; NbExp=3; IntAct=EBI-715576, EBI-476295;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-715576, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC the nucleus and the cytoplasm. In muscle cells, it shuttles into
CC the cytoplasm during myocyte differentiation. The export to
CC cytoplasm depends on the interaction with a 14-3-3 chaperone
CC protein and is due to its phosphorylation at Ser-259 and Ser-498
CC by AMPK, CaMK1 and SIK1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UQL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UQL6-2; Sequence=VSP_002081;
CC Note=No experimental confirmation available.;
CC Name=3;
CC IsoId=Q9UQL6-3; Sequence=VSP_039180;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC the nucleus and the cytoplasm. {ECO:0000250}.
CC -!- PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-259 and
CC Ser-498. The phosphorylation is required for the export to the
CC cytoplasm and inhibition. Phosphorylated by the PKC kinases PKN1
CC and PKN2, impairing nuclear import. Phosphorylated by GRK5,
CC leading to nuclear export of HDAC5 and allowing MEF2-mediated
CC transcription (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Polyubiquitination however does not lead to
CC its degradation. {ECO:0000269|PubMed:12354939}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18040.1; Type=Frameshift; Positions=1085; Evidence={ECO:0000305};
CC Sequence=BAA25526.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR EMBL; AF132608; AAD29047.1; -; mRNA.
DR EMBL; AB011172; BAA25526.2; ALT_INIT; mRNA.
DR EMBL; AC023855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013140; AAH13140.1; ALT_TERM; mRNA.
DR EMBL; BC051824; AAH51824.1; -; mRNA.
DR EMBL; BX458255; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF039691; AAC18040.1; ALT_FRAME; mRNA.
DR EMBL; BK000028; DAA00017.1; -; Genomic_DNA.
DR CCDS; CCDS32663.1; -. [Q9UQL6-3]
DR CCDS; CCDS45696.1; -. [Q9UQL6-1]
DR RefSeq; NP_001015053.1; NM_001015053.1. [Q9UQL6-3]
DR RefSeq; NP_005465.2; NM_005474.4. [Q9UQL6-1]
DR RefSeq; XP_005256963.1; XM_005256906.4. [Q9UQL6-1]
DR UniGene; Hs.438782; -.
DR ProteinModelPortal; Q9UQL6; -.
DR SMR; Q9UQL6; -.
DR BioGrid; 115331; 346.
DR DIP; DIP-38260N; -.
DR IntAct; Q9UQL6; 30.
DR MINT; MINT-1407477; -.
DR STRING; 9606.ENSP00000225983; -.
DR BindingDB; Q9UQL6; -.
DR ChEMBL; CHEMBL2563; -.
DR DrugBank; DB06603; Panobinostat.
DR GuidetoPHARMACOLOGY; 2660; -.
DR iPTMnet; Q9UQL6; -.
DR PhosphoSitePlus; Q9UQL6; -.
DR BioMuta; HDAC5; -.
DR DMDM; 296434519; -.
DR PaxDb; Q9UQL6; -.
DR PeptideAtlas; Q9UQL6; -.
DR PRIDE; Q9UQL6; -.
DR Ensembl; ENST00000225983; ENSP00000225983; ENSG00000108840. [Q9UQL6-3]
DR Ensembl; ENST00000336057; ENSP00000337290; ENSG00000108840. [Q9UQL6-2]
DR Ensembl; ENST00000586802; ENSP00000468004; ENSG00000108840. [Q9UQL6-1]
DR GeneID; 10014; -.
DR KEGG; hsa:10014; -.
DR UCSC; uc002ifd.2; human. [Q9UQL6-1]
DR CTD; 10014; -.
DR DisGeNET; 10014; -.
DR GeneCards; HDAC5; -.
DR H-InvDB; HIX0013862; -.
DR HGNC; HGNC:14068; HDAC5.
DR HPA; CAB019400; -.
DR HPA; HPA030991; -.
DR MIM; 605315; gene.
DR neXtProt; NX_Q9UQL6; -.
DR OpenTargets; ENSG00000108840; -.
DR PharmGKB; PA29230; -.
DR eggNOG; KOG1343; Eukaryota.
DR eggNOG; COG0123; LUCA.
DR GeneTree; ENSGT00530000062809; -.
DR HOGENOM; HOG000232065; -.
DR HOVERGEN; HBG057100; -.
DR InParanoid; Q9UQL6; -.
DR KO; K11406; -.
DR OMA; AANMRTV; -.
DR OrthoDB; EOG091G0EQO; -.
DR PhylomeDB; Q9UQL6; -.
DR TreeFam; TF106174; -.
DR BioCyc; ZFISH:HS03168-MONOMER; -.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR SIGNOR; Q9UQL6; -.
DR ChiTaRS; HDAC5; human.
DR GeneWiki; Histone_deacetylase_5; -.
DR GenomeRNAi; 10014; -.
DR PRO; PR:Q9UQL6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000108840; -.
DR CleanEx; HS_HDAC5; -.
DR ExpressionAtlas; Q9UQL6; baseline and differential.
DR Genevisible; Q9UQL6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR GO; GO:0033558; F:protein deacetylase activity; IMP:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0001025; F:RNA polymerase III transcription factor binding; IPI:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; NAS:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR GO; GO:0006342; P:chromatin silencing; TAS:ProtInc.
DR GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR GO; GO:0006476; P:protein deacetylation; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0010830; P:regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR030703; Histone_deacetylase_5.
DR PANTHER; PTHR10625; PTHR10625; 2.
DR PANTHER; PTHR10625:SF57; PTHR10625:SF57; 2.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator;
KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1 1122 Histone deacetylase 5.
FT /FTId=PRO_0000114701.
FT REGION 684 1028 Histone deacetylase.
FT MOTIF 1081 1122 Nuclear export signal.
FT COMPBIAS 47 52 Poly-Gly.
FT COMPBIAS 85 92 Poly-Gln.
FT COMPBIAS 596 599 Poly-Glu.
FT COMPBIAS 1099 1104 Poly-Ala.
FT ACT_SITE 833 833 {ECO:0000250}.
FT METAL 696 696 Zinc. {ECO:0000250}.
FT METAL 698 698 Zinc. {ECO:0000250}.
FT METAL 704 704 Zinc. {ECO:0000250}.
FT METAL 781 781 Zinc. {ECO:0000250}.
FT MOD_RES 259 259 Phosphoserine; by AMPK, CaMK1, SIK1 and
FT PKD/PRKD1. {ECO:0000269|PubMed:11114197,
FT ECO:0000269|PubMed:18184930,
FT ECO:0000269|PubMed:18332134}.
FT MOD_RES 292 292 Phosphothreonine; by PKC.
FT {ECO:0000269|PubMed:20188095}.
FT MOD_RES 498 498 Phosphoserine; by AMPK, CaMK1, SIK1 and
FT PKD/PRKD1. {ECO:0000269|PubMed:11114197,
FT ECO:0000269|PubMed:18184930,
FT ECO:0000269|PubMed:18332134}.
FT MOD_RES 533 533 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 611 611 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 661 661 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 1108 1108 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 7 7 S -> SA (in isoform 3).
FT {ECO:0000303|Ref.6}.
FT /FTId=VSP_039180.
FT VAR_SEQ 684 768 Missing (in isoform 2).
FT {ECO:0000303|PubMed:9628581}.
FT /FTId=VSP_002081.
FT VARIANT 137 137 R -> Q (in dbSNP:rs438096).
FT /FTId=VAR_055903.
FT VARIANT 565 565 G -> A (in dbSNP:rs33916560).
FT /FTId=VAR_055904.
FT MUTAGEN 259 259 S->A: Reduces AMPK- and caMK-dependent
FT phosphorylation and the subsequent
FT nuclear export. Abolishes nuclear export;
FT when associated with A-498. Does not
FT affect phosphorylation by PKN1 and PKN2.
FT {ECO:0000269|PubMed:11081517,
FT ECO:0000269|PubMed:18184930,
FT ECO:0000269|PubMed:20188095}.
FT MUTAGEN 279 279 S->A: No effect.
FT {ECO:0000269|PubMed:11081517}.
FT MUTAGEN 291 291 S->A: Does not affect phosphorylation by
FT PKC. {ECO:0000269|PubMed:20188095}.
FT MUTAGEN 292 292 T->A: Abolishes phosphorylation by PKC.
FT {ECO:0000269|PubMed:20188095}.
FT MUTAGEN 498 498 S->A: Reduces AMPK- and CaMK-dependent
FT phosphorylation and the subsequent
FT nuclear export. Abolishes nuclear export;
FT when associated with A-259.
FT {ECO:0000269|PubMed:11081517,
FT ECO:0000269|PubMed:18184930}.
FT MUTAGEN 661 661 S->A: No effect.
FT {ECO:0000269|PubMed:11081517}.
FT MUTAGEN 713 713 S->A: No effect.
FT {ECO:0000269|PubMed:11081517}.
FT MUTAGEN 1086 1086 V->A: Reduces CaMK-dependent nuclear
FT export. {ECO:0000269|PubMed:11509672}.
FT MUTAGEN 1092 1092 L->A: Reduces CaMK-dependent nuclear
FT export. {ECO:0000269|PubMed:11509672}.
FT CONFLICT 37 37 V -> L (in Ref. 6; BX458255).
FT {ECO:0000305}.
FT CONFLICT 139 139 Q -> R (in Ref. 6; BX458255).
FT {ECO:0000305}.
FT CONFLICT 147 147 R -> G (in Ref. 6; BX458255).
FT {ECO:0000305}.
FT CONFLICT 593 593 D -> E (in Ref. 1; AAD29047, 5; AAH51824
FT and 7; AAC18040). {ECO:0000305}.
FT CONFLICT 671 671 S -> N (in Ref. 7; AAC18040).
FT {ECO:0000305}.
FT CONFLICT 684 684 G -> S (in Ref. 7; AAC18040).
FT {ECO:0000305}.
FT CONFLICT 1026 1026 E -> K (in Ref. 7; AAC18040).
FT {ECO:0000305}.
FT CONFLICT 1074 1074 E -> G (in Ref. 7; AAC18040).
FT {ECO:0000305}.
FT CONFLICT 1093 1093 S -> L (in Ref. 7; AAC18040).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 67 164 ipfam:HDAC4_Gln [T]
FT MYHIT 704 1022 ipfam:Hist_deacetyl [T]
SQ SEQUENCE 1122 AA; 121978 MW; CF4BE774E3588FEC CRC64;
MNSPNESDGM SGREPSLEIL PRTSLHSIPV TVEVKPVLPR AMPSSMGGGG GGSPSPVELR
GALVGSVDPT LREQQLQQEL LALKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
QEMLAAKQQQ EMLAAKRQQE LEQQRQREQQ RQEELEKQRL EQQLLILRNK EKSKESAIAS
TEVKLRLQEF LLSKSKEPTP GGLNHSLPQH PKCWGAHHAS LDQSSPPQSG PPGTPPSYKL
PLPGPYDSRD DFPLRKTASE PNLKVRSRLK QKVAERRSSP LLRRKDGTVI STFKKRAVEI
TGAGPGASSV CNSAPGSGPS SPNSSHSTIA ENGFTGSVPN IPTEMLPQHR ALPLDSSPNQ
FSLYTSPSLP NISLGLQATV TVTNSHLTAS PKLSTQQEAE RQALQSLRQG GTLTGKFMST
SSIPGCLLGV ALEGDGSPHG HASLLQHVLL LEQARQQSTL IAVPLHGQSP LVTGERVATS
MRTVGKLPRH RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQLQ LGKILTKTGE
LPRQPTTHPE ETEEELTEQQ EVLLGEGALT MPREGSTESE STQEDLEEED EEDDGEEEED
CIQVKDEEGE SGAEEGPDLE EPGAGYKKLF SDAQPLQPLQ VYQAPLSLAT VPHQALGRTQ
SSPAAPGGMK SPPDQPVKHL FTTGVVYDTF MLKHQCMCGN THVHPEHAGR IQSIWSRLQE
TGLLSKCERI RGRKATLDEI QTVHSEYHTL LYGTSPLNRQ KLDSKKLLGP ISQKMYAVLP
CGGIGVDSDT VWNEMHSSSA VRMAVGCLLE LAFKVAAGEL KNGFAIIRPP GHHAEESTAM
GFCFFNSVAI TAKLLQQKLN VGKVLIVDWD IHHGNGTQQA FYNDPSVLYI SLHRYDNGNF
FPGSGAPEEV GGGPGVGYNV NVAWTGGVDP PIGDVEYLTA FRTVVMPIAH EFSPDVVLVS
AGFDAVEGHL SPLGGYSVTA RCFGHLTRQL MTLAGGRVVL ALEGGHDLTA ICDASEACVS
ALLSVELQPL DEAVLQQKPN INAVATLEKV IEIQSKHWSC VQKFAAGLGR SLREAQAGET
EEAETVSAMA LLSVGAEQAQ AAAAREHSPR PAEEPMEQEP AL
//
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