HDA11_HUMAN
ID HDA11_HUMAN Reviewed; 347 AA.
AC Q96DB2; B4DDK1; Q9H6I7; Q9H6X3; Q9NTC9;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Histone deacetylase 11;
DE Short=HD11;
DE EC=3.5.1.98 {ECO:0000269|PubMed:11948178};
GN Name=HDAC11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-347 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH HDAC6.
RX PubMed=11948178; DOI=10.1074/jbc.m111871200;
RA Gao L., Cueto M.A., Asselbergs F., Atadja P.;
RT "Cloning and functional characterization of HDAC11, a novel member of the
RT human histone deacetylase family.";
RL J. Biol. Chem. 277:25748-25755(2002).
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. {ECO:0000269|PubMed:11948178}.
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 Evidence={ECO:0000269|PubMed:11948178};
CC -!- SUBUNIT: Interacts with HDAC6. {ECO:0000269|PubMed:11948178}.
CC -!- INTERACTION:
CC Q96DB2; Q8IXM6: NRM; NbExp=3; IntAct=EBI-301713, EBI-10262547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11948178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DB2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DB2-2; Sequence=VSP_043082, VSP_043083;
CC -!- TISSUE SPECIFICITY: Weakly expressed in most tissues. Strongly
CC expressed in brain, heart, skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:11948178}.
CC -!- MISCELLANEOUS: Its activity is inhibited by trapoxin, a known histone
CC deacetylase inhibitor.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15127.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB70712.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK025426; BAB15127.1; ALT_SEQ; mRNA.
DR EMBL; AK025890; BAB15272.1; -; mRNA.
DR EMBL; AK293223; BAG56762.1; -; mRNA.
DR EMBL; AC027124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009676; AAH09676.1; -; mRNA.
DR EMBL; AL137362; CAB70712.1; ALT_FRAME; mRNA.
DR CCDS; CCDS2615.1; -. [Q96DB2-1]
DR CCDS; CCDS46760.1; -. [Q96DB2-2]
DR RefSeq; NP_001129513.1; NM_001136041.2. [Q96DB2-2]
DR RefSeq; NP_079103.2; NM_024827.3. [Q96DB2-1]
DR RefSeq; XP_011532437.1; XM_011534135.1.
DR AlphaFoldDB; Q96DB2; -.
DR SMR; Q96DB2; -.
DR BioGRID; 122970; 151.
DR IntAct; Q96DB2; 142.
DR MINT; Q96DB2; -.
DR STRING; 9606.ENSP00000295757; -.
DR BindingDB; Q96DB2; -.
DR ChEMBL; CHEMBL3310; -.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB06603; Panobinostat.
DR DrugCentral; Q96DB2; -.
DR GuidetoPHARMACOLOGY; 2615; -.
DR iPTMnet; Q96DB2; -.
DR PhosphoSitePlus; Q96DB2; -.
DR BioMuta; HDAC11; -.
DR DMDM; 26394832; -.
DR EPD; Q96DB2; -.
DR MassIVE; Q96DB2; -.
DR PaxDb; Q96DB2; -.
DR PeptideAtlas; Q96DB2; -.
DR PRIDE; Q96DB2; -.
DR ProteomicsDB; 76267; -. [Q96DB2-1]
DR ProteomicsDB; 76268; -. [Q96DB2-2]
DR Antibodypedia; 10901; 446 antibodies from 38 providers.
DR DNASU; 79885; -.
DR Ensembl; ENST00000295757.8; ENSP00000295757.3; ENSG00000163517.15. [Q96DB2-1]
DR Ensembl; ENST00000522202.5; ENSP00000429794.1; ENSG00000163517.15. [Q96DB2-2]
DR GeneID; 79885; -.
DR KEGG; hsa:79885; -.
DR MANE-Select; ENST00000295757.8; ENSP00000295757.3; NM_024827.4; NP_079103.2.
DR UCSC; uc003bxy.4; human. [Q96DB2-1]
DR CTD; 79885; -.
DR DisGeNET; 79885; -.
DR GeneCards; HDAC11; -.
DR HGNC; HGNC:19086; HDAC11.
DR HPA; ENSG00000163517; Tissue enhanced (brain).
DR MIM; 607226; gene.
DR neXtProt; NX_Q96DB2; -.
DR OpenTargets; ENSG00000163517; -.
DR PharmGKB; PA38793; -.
DR VEuPathDB; HostDB:ENSG00000163517; -.
DR eggNOG; KOG1344; Eukaryota.
DR GeneTree; ENSGT00940000156308; -.
DR InParanoid; Q96DB2; -.
DR OMA; RVFTFSM; -.
DR PhylomeDB; Q96DB2; -.
DR TreeFam; TF106176; -.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q96DB2; -.
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 Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR SignaLink; Q96DB2; -.
DR SIGNOR; Q96DB2; -.
DR BioGRID-ORCS; 79885; 14 hits in 1092 CRISPR screens.
DR ChiTaRS; HDAC11; human.
DR GeneWiki; HDAC11; -.
DR GenomeRNAi; 79885; -.
DR Pharos; Q96DB2; Tclin.
DR PRO; PR:Q96DB2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96DB2; protein.
DR Bgee; ENSG00000163517; Expressed in left testis and 172 other tissues.
DR ExpressionAtlas; Q96DB2; baseline and differential.
DR Genevisible; Q96DB2; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR CDD; cd09993; HDAC_classIV; 1.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR044150; HDAC_classIV.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Hydrolase; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..347
FT /note="Histone deacetylase 11"
FT /id="PRO_0000114715"
FT REGION 14..326
FT /note="Histone deacetylase"
FT ACT_SITE 143
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043082"
FT VAR_SEQ 85..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043083"
FT CONFLICT 15
FT /note="R -> P (in Ref. 1; BAB15272)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="P -> A (in Ref. 4; CAB70712)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="D -> Y (in Ref. 4; CAB70712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 39183 MW; 0D976CAF6EAC7A15 CRC64;
MLHTTQLYQH VPETRWPIVY SPRYNITFMG LEKLHPFDAG KWGKVINFLK EEKLLSDSML
VEAREASEED LLVVHTRRYL NELKWSFAVA TITEIPPVIF LPNFLVQRKV LRPLRTQTGG
TIMAGKLAVE RGWAINVGGG FHHCSSDRGG GFCAYADITL AIKFLFERVE GISRATIIDL
DAHQGNGHER DFMDDKRVYI MDVYNRHIYP GDRFAKQAIR RKVELEWGTE DDEYLDKVER
NIKKSLQEHL PDVVVYNAGT DILEGDRLGG LSISPAGIVK RDELVFRMVR GRRVPILMVT
SGGYQKRTAR IIADSILNLF GLGLIGPESP SVSAQNSDTP LLPPAVP
