GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: HDA11_HUMAN A0A024R2I1_HUMAN
LinkDB: HDA11_HUMAN A0A024R2I1_HUMAN
Original site: HDA11_HUMAN A0A024R2I1_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   27-SEP-2017, entry version 147.
DE   RecName: Full=Histone deacetylase 11;
DE            Short=HD11;
DE            EC=3.5.1.98;
GN   Name=HDAC11;
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 [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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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
RT   project: 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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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   CHARACTERIZATION, FUNCTION, AND 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
RT   the human histone deacetylase family.";
RL   J. Biol. Chem. 277:25748-25755(2002).
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.
CC       {ECO:0000269|PubMed:11948178}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with HDAC6. {ECO:0000269|PubMed:11948178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Predominantly nuclear.
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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Weakly expressed in most tissues. Strongly
CC       expressed in brain, heart, skeletal muscle, kidney and testis.
CC   -!- MISCELLANEOUS: Its activity is inhibited by trapoxin, a known
CC       histone deacetylase inhibitor.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15127.1; Type=Erroneous termination; Positions=107; Note=Translated as Gln.; Evidence={ECO:0000305};
CC       Sequence=CAB70712.1; Type=Frameshift; Positions=177, 198, 200; Evidence={ECO:0000305};
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   UniGene; Hs.744132; -.
DR   ProteinModelPortal; Q96DB2; -.
DR   BioGrid; 122970; 147.
DR   IntAct; Q96DB2; 130.
DR   MINT; MINT-1411829; -.
DR   STRING; 9606.ENSP00000295757; -.
DR   BindingDB; Q96DB2; -.
DR   ChEMBL; CHEMBL3310; -.
DR   DrugBank; DB05015; Belinostat.
DR   DrugBank; DB06603; Panobinostat.
DR   GuidetoPHARMACOLOGY; 2615; -.
DR   iPTMnet; Q96DB2; -.
DR   PhosphoSitePlus; Q96DB2; -.
DR   BioMuta; HDAC11; -.
DR   DMDM; 26394832; -.
DR   PaxDb; Q96DB2; -.
DR   PeptideAtlas; Q96DB2; -.
DR   PRIDE; Q96DB2; -.
DR   DNASU; 79885; -.
DR   Ensembl; ENST00000295757; ENSP00000295757; ENSG00000163517. [Q96DB2-1]
DR   Ensembl; ENST00000522202; ENSP00000429794; ENSG00000163517. [Q96DB2-2]
DR   GeneID; 79885; -.
DR   KEGG; hsa:79885; -.
DR   UCSC; uc003bxy.4; human. [Q96DB2-1]
DR   CTD; 79885; -.
DR   DisGeNET; 79885; -.
DR   EuPathDB; HostDB:ENSG00000163517.14; -.
DR   GeneCards; HDAC11; -.
DR   HGNC; HGNC:19086; HDAC11.
DR   MIM; 607226; gene.
DR   neXtProt; NX_Q96DB2; -.
DR   OpenTargets; ENSG00000163517; -.
DR   PharmGKB; PA38793; -.
DR   eggNOG; KOG1344; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   GeneTree; ENSGT00390000003411; -.
DR   HOGENOM; HOG000280018; -.
DR   HOVERGEN; HBG051893; -.
DR   InParanoid; Q96DB2; -.
DR   KO; K11418; -.
DR   OMA; RVFTFSM; -.
DR   OrthoDB; EOG091G0EQP; -.
DR   PhylomeDB; Q96DB2; -.
DR   TreeFam; TF106176; -.
DR   BRENDA; 3.5.1.98; 2681.
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   ChiTaRS; HDAC11; human.
DR   GeneWiki; HDAC11; -.
DR   GenomeRNAi; 79885; -.
DR   PRO; PR:Q96DB2; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000163517; -.
DR   CleanEx; HS_HDAC11; -.
DR   ExpressionAtlas; Q96DB2; baseline and differential.
DR   Genevisible; Q96DB2; HS.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
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:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0008134; F:transcription factor binding; TAS: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   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Hydrolase; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    347       Histone deacetylase 11.
FT                                /FTId=PRO_0000114715.
FT   REGION       14    326       Histone deacetylase.
FT   ACT_SITE    143    143       {ECO:0000250}.
FT   VAR_SEQ       1     28       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043082.
FT   VAR_SEQ      85    107       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_043083.
FT   CONFLICT     15     15       R -> P (in Ref. 1; BAB15272).
FT                                {ECO:0000305}.
FT   CONFLICT    113    113       P -> A (in Ref. 4; CAB70712).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       D -> Y (in Ref. 4; CAB70712).
FT                                {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
//
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Ontology (12)   
   GO (12)   
Disease (1)   
   OMIM (1)   
Drug (3)   
   DrugBank (2)   
   CHEMBL-UP (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (10)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (5)   
Protein sequence (3)   
   RefSeq(pep) (3)   
DNA sequence (6)   
   EMBL (6)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (5)   
   PubMed (5)   
Enzyme (1)   
   BRENDA (1)   
All databases (45)   

Download RDF
ID   A0A024R2I1_HUMAN        Unreviewed;       347 AA.
AC   A0A024R2I1;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-SEP-2017, entry version 29.
DE   SubName: Full=Histone deacetylase 11, isoform CRA_i {ECO:0000313|EMBL:EAW64168.1};
GN   Name=HDAC11 {ECO:0000313|EMBL:EAW64168.1};
GN   ORFNames=hCG_28391 {ECO:0000313|EMBL:EAW64168.1};
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 {ECO:0000313|EMBL:EAW64168.1};
RN   [1] {ECO:0000313|EMBL:EAW64168.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D.,
RA   Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q.,
RA   Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G.,
RA   Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S.,
RA   Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J.,
RA   Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R.,
RA   Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A.,
RA   Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K.,
RA   Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V.,
RA   Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z.,
RA   Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A.,
RA   Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V.,
RA   Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B.,
RA   Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J.,
RA   Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C.,
RA   Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L.,
RA   Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S.,
RA   Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A.,
RA   Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D.,
RA   Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L.,
RA   Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N.,
RA   Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S.,
RA   Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F.,
RA   Kline L., Koduru S., Love A., Mann F., May D., McCawley S.,
RA   McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K.,
RA   Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N.,
RA   Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M.,
RA   Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F.,
RA   Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A.,
RA   Mi H., Lazareva B., Hatton T., Narechania A., Diemer K.,
RA   Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R.,
RA   Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J.,
RA   Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H.,
RA   Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D.,
RA   Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A.,
RA   Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S.,
RA   Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L.,
RA   Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W.,
RA   McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M.,
RA   Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:EAW64168.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH471055; EAW64165.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW64168.1; -; Genomic_DNA.
DR   RefSeq; NP_079103.2; NM_024827.3.
DR   UniGene; Hs.744132; -.
DR   GeneID; 79885; -.
DR   KEGG; hsa:79885; -.
DR   CTD; 79885; -.
DR   EuPathDB; HostDB:ENSG00000163517.14; -.
DR   eggNOG; KOG1344; Eukaryota.
DR   eggNOG; COG0123; LUCA.
DR   KO; K11418; -.
DR   OMA; RVFTFSM; -.
DR   OrthoDB; EOG091G0EQP; -.
DR   GenomeRNAi; 79885; -.
DR   Bgee; ENSG00000163517; -.
DR   ExpressionAtlas; A0A024R2I1; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR   Gene3D; 3.40.800.20; -; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|SAAS:SAAS00671995}.
FT   DOMAIN       35    316       Hist_deacetyl. {ECO:0000259|Pfam:
FT                                PF00850}.
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
//
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Ontology (3)   
   GO (3)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (13)   

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