HDAC7_MOUSE
ID HDAC7_MOUSE Reviewed; 938 AA.
AC Q8C2B3; Q8C2C9; Q8C8X4; Q8CB80; Q8CDA3; Q9JL72;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Histone deacetylase 7;
DE Short=HD7;
DE EC=3.5.1.98;
DE AltName: Full=Histone deacetylase 7A;
DE Short=HD7a;
GN Name=Hdac7; Synonyms=Hdac7a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH NCOR2 AND SIN3A.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10640276;
RA Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT "Isolation of a novel histone deacetylase reveals that class I and class II
RT deacetylases promote SMRT-mediated repression.";
RL Genes Dev. 14:55-66(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC4; HDAC5; NCOR1; NCOR2; SIN3A;
RP SIN3B; RBBP4; RBBP7; MTA1L1; SAP30 AND MBD3, AND MUTAGENESIS OF HIS-657;
RP ASP-692; ASP-694 AND HIS-717.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MEF2C, AND
RP MUTAGENESIS OF HIS-657.
RX PubMed=11279209; DOI=10.1074/jbc.m101508200;
RA Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
RA Muscat G.E.O.;
RT "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
RL J. Biol. Chem. 276:17007-17013(2001).
RN [6]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH YWHAE; MEF2A; MEF2B
RP AND MEF2C, AND MUTAGENESIS OF SER-178; SER-344 AND SER-479.
RX PubMed=11585834; DOI=10.1074/jbc.m107631200;
RA Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.;
RT "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7.";
RL J. Biol. Chem. 276:47496-47507(2001).
RN [7]
RP NUCLEAR EXPORT SIGNAL.
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 class II
RT histone deacetylases.";
RL Mol. Cell. Biol. 21:6312-6321(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
RX PubMed=18509061; DOI=10.1073/pnas.0802857105;
RA Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.;
RT "Control of endothelial cell proliferation and migration by VEGF signaling
RT to histone deacetylase 7.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP INTERACTION WITH FOXP3.
RX PubMed=19696312; DOI=10.1126/science.1176077;
RA Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
RA Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
RA Ostrowski M.C., Pardoll D.M.;
RT "Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T cells.";
RL Science 325:1142-1146(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP INTERACTION WITH ZMYND15.
RX PubMed=20675388; DOI=10.1074/jbc.m110.116418;
RA Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA Saunders L., Verdin E., Charo I.F.;
RT "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor
RT essential for spermiogenesis and male fertility.";
RL J. Biol. Chem. 285:31418-31426(2010).
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. Histone deacetylases act via the formation of
CC large multiprotein complexes. Involved in muscle maturation by
CC repressing transcription of myocyte enhancer factors such as MEF2A,
CC MEF2B and MEF2C. During muscle differentiation, it shuttles into the
CC cytoplasm, allowing the expression of myocyte enhancer factors.
CC Positively regulates the transcriptional repressor activity of FOXP3
CC (By similarity). Serves as a corepressor of RARA, causing its
CC deacetylation and inhibition of RARE DNA element binding (By
CC similarity). In association with RARA, plays a role in the repression
CC of microRNA-10a and thereby in the inflammatory response (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUI4,
CC ECO:0000269|PubMed:10640276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC -!- SUBUNIT: Interacts with KDM5B (By similarity). Interacts with KAT5 and
CC EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2,
CC SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the
CC 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with ZMYND15.
CC Interacts with PML (By similarity). Interacts with FOXP3. Interacts
CC with RARA (By similarity). {ECO:0000250|UniProtKB:Q8WUI4,
CC ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530,
CC ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834,
CC ECO:0000269|PubMed:19696312, ECO:0000269|PubMed:20675388}.
CC -!- INTERACTION:
CC Q8C2B3; P62259: Ywhae; NbExp=5; IntAct=EBI-643830, EBI-356480;
CC Q8C2B3-1; Q15139: PRKD1; Xeno; NbExp=3; IntAct=EBI-15705168, EBI-1181072;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it
CC associates with distinct subnuclear dot-like structures. Shuttles
CC between the nucleus and the cytoplasm. In muscle cells, it shuttles
CC into the cytoplasm during myocyte differentiation. The export to
CC cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and
CC is due to its phosphorylation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8C2B3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C2B3-2; Sequence=VSP_007432, VSP_007434, VSP_007435;
CC Name=3;
CC IsoId=Q8C2B3-3; Sequence=VSP_007432, VSP_007434;
CC Name=4;
CC IsoId=Q8C2B3-4; Sequence=VSP_007433, VSP_007434, VSP_007435;
CC Name=5;
CC IsoId=Q8C2B3-5; Sequence=VSP_007432;
CC Name=6;
CC IsoId=Q8C2B3-6; Sequence=VSP_007433;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and lung. Expressed at
CC intermediate level in muscle. {ECO:0000269|PubMed:10640276,
CC ECO:0000269|PubMed:11279209}.
CC -!- DOMAIN: The nuclear export sequence mediates the shuttling between the
CC nucleus and the cytoplasm. {ECO:0000250}.
CC -!- PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases
CC PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-178 by
CC MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and
CC export from the nucleus. Phosphorylation at Ser-178 is a prerequisite
CC for phosphorylation at Ser-204 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA), a
CC known histone deacetylase inhibitor.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF207749; AAF31419.1; -; mRNA.
DR EMBL; AK030863; BAC27161.1; -; mRNA.
DR EMBL; AK036586; BAC29493.1; -; mRNA.
DR EMBL; AK044287; BAC31856.1; -; mRNA.
DR EMBL; AK088828; BAC40598.1; -; mRNA.
DR EMBL; AK088945; BAC40666.1; -; mRNA.
DR EMBL; BC057332; AAH57332.1; -; mRNA.
DR CCDS; CCDS37188.1; -. [Q8C2B3-1]
DR CCDS; CCDS57004.1; -. [Q8C2B3-5]
DR CCDS; CCDS57005.1; -. [Q8C2B3-2]
DR CCDS; CCDS57006.1; -. [Q8C2B3-3]
DR CCDS; CCDS57007.1; -. [Q8C2B3-4]
DR RefSeq; NP_001191204.1; NM_001204275.1. [Q8C2B3-3]
DR RefSeq; NP_001191205.1; NM_001204276.1. [Q8C2B3-2]
DR RefSeq; NP_001191206.1; NM_001204277.1. [Q8C2B3-4]
DR RefSeq; NP_001191207.1; NM_001204278.1. [Q8C2B3-5]
DR RefSeq; NP_062518.2; NM_019572.3. [Q8C2B3-1]
DR RefSeq; XP_006521268.1; XM_006521205.2. [Q8C2B3-3]
DR RefSeq; XP_006521270.1; XM_006521207.3. [Q8C2B3-3]
DR RefSeq; XP_006521271.1; XM_006521208.3. [Q8C2B3-3]
DR RefSeq; XP_006521272.1; XM_006521209.2. [Q8C2B3-3]
DR RefSeq; XP_006521273.1; XM_006521210.2. [Q8C2B3-3]
DR AlphaFoldDB; Q8C2B3; -.
DR SMR; Q8C2B3; -.
DR BioGRID; 207862; 8.
DR CORUM; Q8C2B3; -.
DR DIP; DIP-42594N; -.
DR ELM; Q8C2B3; -.
DR IntAct; Q8C2B3; 6.
DR MINT; Q8C2B3; -.
DR STRING; 10090.ENSMUSP00000085744; -.
DR BindingDB; Q8C2B3; -.
DR ChEMBL; CHEMBL3832944; -.
DR iPTMnet; Q8C2B3; -.
DR PhosphoSitePlus; Q8C2B3; -.
DR EPD; Q8C2B3; -.
DR jPOST; Q8C2B3; -.
DR MaxQB; Q8C2B3; -.
DR PaxDb; Q8C2B3; -.
DR PRIDE; Q8C2B3; -.
DR ProteomicsDB; 269772; -. [Q8C2B3-1]
DR ProteomicsDB; 269773; -. [Q8C2B3-2]
DR ProteomicsDB; 269774; -. [Q8C2B3-3]
DR ProteomicsDB; 269775; -. [Q8C2B3-4]
DR ProteomicsDB; 269776; -. [Q8C2B3-5]
DR ProteomicsDB; 269777; -. [Q8C2B3-6]
DR Antibodypedia; 1412; 665 antibodies from 42 providers.
DR DNASU; 56233; -.
DR Ensembl; ENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
DR Ensembl; ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
DR Ensembl; ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
DR Ensembl; ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
DR Ensembl; ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
DR GeneID; 56233; -.
DR KEGG; mmu:56233; -.
DR UCSC; uc007xle.2; mouse. [Q8C2B3-1]
DR UCSC; uc007xlf.2; mouse. [Q8C2B3-2]
DR UCSC; uc007xlg.2; mouse. [Q8C2B3-4]
DR UCSC; uc007xlh.2; mouse. [Q8C2B3-3]
DR CTD; 51564; -.
DR MGI; MGI:1891835; Hdac7.
DR VEuPathDB; HostDB:ENSMUSG00000022475; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159065; -.
DR HOGENOM; CLU_006530_0_1_1; -.
DR InParanoid; Q8C2B3; -.
DR OMA; WPLSWTR; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q8C2B3; -.
DR TreeFam; TF106173; -.
DR BRENDA; 3.5.1.98; 3474.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR BioGRID-ORCS; 56233; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Hdac7; mouse.
DR PRO; PR:Q8C2B3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C2B3; protein.
DR Bgee; ENSMUSG00000022475; Expressed in thymus and 208 other tissues.
DR ExpressionAtlas; Q8C2B3; baseline and differential.
DR Genevisible; Q8C2B3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; ISO:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR033660; HDAC4/7.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364; PTHR45364; 2.
DR PANTHER; PTHR45364:SF3; PTHR45364:SF3; 2.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm; Hydrolase;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..938
FT /note="Histone deacetylase 7"
FT /id="PRO_0000114706"
FT REGION 1..121
FT /note="Interaction with MEF2C"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..254
FT /note="Transcription repression 1"
FT REGION 72..172
FT /note="Interaction with MEF2A"
FT /evidence="ECO:0000269|PubMed:11585834"
FT REGION 155..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..533
FT /note="Transcription repression 2"
FT REGION 331..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..852
FT /note="Histone deacetylase"
FT REGION 864..938
FT /note="Interaction with SIN3A"
FT MOTIF 904..938
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 217..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT SITE 830
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 178
FT /note="Phosphoserine; by MARK2, MARK3 and PKD/PRKD1"
FT /evidence="ECO:0000305|PubMed:18509061"
FT MOD_RES 204
FT /note="Phosphoserine; by PKD/PRKD2"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 344
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:18509061"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 479
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:18509061"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007432"
FT VAR_SEQ 138..161
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007433"
FT VAR_SEQ 249
FT /note="E -> EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAPAR (in
FT isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007434"
FT VAR_SEQ 376..382
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007435"
FT MUTAGEN 178
FT /note="S->A: Strong reduction of CaMK1-dependent nuclear
FT export. Reduces interaction with YWHAE."
FT /evidence="ECO:0000269|PubMed:11585834"
FT MUTAGEN 344
FT /note="S->A: Strong reduction of CaMK1-dependent nuclear
FT export. Reduces interaction with YWHAE."
FT /evidence="ECO:0000269|PubMed:11585834"
FT MUTAGEN 479
FT /note="S->A: Strong reduction of CaMK1-dependent nuclear
FT export. Reduces interaction with YWHAE."
FT /evidence="ECO:0000269|PubMed:11585834"
FT MUTAGEN 657
FT /note="H->A: Abolishes deacetylase activity, but not the
FT interaction with HDAC2 and HDAC3."
FT /evidence="ECO:0000269|PubMed:10984530,
FT ECO:0000269|PubMed:11279209"
FT MUTAGEN 692
FT /note="D->A: Disrupts the dot-like nuclear pattern."
FT /evidence="ECO:0000269|PubMed:10984530"
FT MUTAGEN 694
FT /note="D->A: Disrupts the dot-like nuclear pattern.
FT Abolishes deacetylase activity, but not the interaction
FT with HDAC2 and HDAC3."
FT /evidence="ECO:0000269|PubMed:10984530"
FT MUTAGEN 717
FT /note="H->A: Abolishes deacetylase activity, but not the
FT interaction with HDAC2 and HDAC3."
FT /evidence="ECO:0000269|PubMed:10984530"
FT CONFLICT 169
FT /note="E -> G (in Ref. 2; BAC27161)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="K -> M (in Ref. 2; BAC29493)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="P -> T (in Ref. 2; BAC27161)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> M (in Ref. 1; AAF31419 and 2; BAC40598/
FT BAC40666)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="K -> R (in Ref. 2; BAC29493)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="S -> P (in Ref. 2; BAC40598)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="G -> A (in Ref. 1; AAF31419)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 938 AA; 101287 MW; 8D4B455CE6F95483 CRC64;
MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL HRHLFLAGLH
QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR SAVASSVVKQ KLAEVILKKQ
QAALERTVHP SSPSIPYRTL EPLDTEGAAR SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP
NLKLRYKPKK SLERRKNPLL RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH
GPNPALGSEA DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP
SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS ATASPLLAPL
QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE DLETDGGGVG PMANDGLEHR
ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS
PAAPVSLLSP EPTCQTQVLN SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS
RLQERGLRSQ CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF
VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV VRPPGHHADH
STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG TQQTFYQDPS VLYISLHRHD
DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG GLDPPMGDPE YLAAFRIVVM PIAREFAPDL
VLVSAGFDAA EGHPAPLGGY HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE
ACVAALLGNK VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP
GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL
