HDAC7_HUMAN
ID HDAC7_HUMAN Reviewed; 952 AA.
AC Q8WUI4; B3KY08; B4DWI0; B4E0Q5; Q6P1W9; Q6W9G7; Q7Z4K2; Q7Z5I1; Q96K01;
AC Q9BR73; Q9H7L0; Q9NW41; Q9NWA9; Q9NYK9; Q9UFU7;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 204.
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 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 [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RA Li S., Fischle W., Verdin E., Walsh M.J.;
RT "A novel class II HDAC is associated with the transcriptional homeodomain
RT repressor CCAAT displacement protein.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 5).
RA Petrie K., Zelent A.;
RT "Genomic organization of the human histone deacetylase 7 gene.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Zhi Y., Su E.W.;
RT "Homo sapiens histone deacetylase 7A (HDAC7A), transcript variant 3.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6; 8 AND 9),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-952 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 651-952.
RC TISSUE=Embryo, Mammary gland, Placenta, Spleen, Teratocarcinoma, and
RC Thymus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 242-952 (ISOFORM 1).
RC TISSUE=B-cell, Colon, and PNS;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-952 (ISOFORM 1).
RC TISSUE=Uterus;
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 [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH EDNRA.
RX PubMed=11262386; DOI=10.1074/jbc.c000909200;
RA Lee H.-J., Chun M., Kandror K.V.;
RT "Tip60 and HDAC7 interact with the endothelin receptor a and may be
RT involved in downstream signaling.";
RL J. Biol. Chem. 276:16597-16600(2001).
RN [11]
RP INTERACTION WITH HDAC3.
RX PubMed=11466315; DOI=10.1074/jbc.m104935200;
RA Fischle W., Dequiedt F., Fillion M., Hendzel M.J., Voelter W., Verdin E.;
RT "Human HDAC7 histone deacetylase activity is associated with HDAC3 in
RT vivo.";
RL J. Biol. Chem. 276:35826-35835(2001).
RN [12]
RP FUNCTION.
RX PubMed=12239305; DOI=10.1128/jvi.76.20.10290-10298.2002;
RA Bryant H., Farrell P.J.;
RT "Signal transduction and transcription factor modification during
RT reactivation of Epstein-Barr virus from latency.";
RL J. Virol. 76:10290-10298(2002).
RN [13]
RP INTERACTION WITH KAT5.
RX PubMed=12551922; DOI=10.1074/jbc.m210816200;
RA Xiao H., Chung J., Kao H.-Y., Yang Y.-C.;
RT "Tip60 is a co-repressor for STAT3.";
RL J. Biol. Chem. 278:11197-11204(2003).
RN [14]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-155 AND SER-181, AND
RP MUTAGENESIS OF LEU-150; SER-155; SER-181; SER-358 AND SER-486.
RX PubMed=16980613; DOI=10.1128/mcb.00231-06;
RA Dequiedt F., Martin M., Von Blume J., Vertommen D., Lecomte E., Mari N.,
RA Heinen M.F., Bachmann M., Twizere J.C., Huang M.C., Rider M.H.,
RA Piwnica-Worms H., Seufferlein T., Kettmann R.;
RT "New role for hPar-1 kinases EMK and C-TAK1 in regulating localization and
RT activity of class IIa histone deacetylases.";
RL Mol. Cell. Biol. 26:7086-7102(2006).
RN [15]
RP PHOSPHORYLATION AT SER-181.
RX PubMed=17962809; DOI=10.1038/sj.emboj.7601891;
RA von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A., Auer A.,
RA Van Lint J., Adler G., Seufferlein T.;
RT "Phosphorylation at Ser244 by CK1 determines nuclear localization and
RT substrate targeting of PKD2.";
RL EMBO J. 26:4619-4633(2007).
RN [16]
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., Freemont P.,
RA Taylor-Papadimitriou J.;
RT "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts
RT directly with histone deacetylases.";
RL Int. J. Cancer 121:265-275(2007).
RN [17]
RP FUNCTION, AND INTERACTION WITH FOXP3.
RX PubMed=17360565; DOI=10.1073/pnas.0700298104;
RA Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
RA Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
RT "FOXP3 interactions with histone acetyltransferase and class II histone
RT deacetylases are required for repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-283; THR-286 AND
RP SER-486, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION.
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 in a
RT subset of class IIa histone deacetylases.";
RL FEBS Lett. 584:1103-1110(2010).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-283 AND THR-286, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-486, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP INTERACTION WITH PML.
RX PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
RA Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I.,
RA Yamada T.;
RT "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
RT function in colorectal cancer cells.";
RL Gastroenterology 142:572-581(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-181; SER-405;
RP SER-486; SER-487; SER-507 AND SER-595, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-486, AND
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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP FUNCTION, AND INTERACTION WITH RARA.
RX PubMed=28167758; DOI=10.1073/pnas.1621425114;
RA Lee D.Y., Lin T.E., Lee C.I., Zhou J., Huang Y.H., Lee P.L., Shih Y.T.,
RA Chien S., Chiu J.J.;
RT "MicroRNA-10a is crucial for endothelial response to different flow
RT patterns via interaction of retinoid acid receptors and histone
RT deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:2072-2077(2017).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 482-903, ZINC-BINDING SITES, AND
RP MUTAGENESIS OF HIS-843.
RX PubMed=18285338; DOI=10.1074/jbc.m707362200;
RA Schuetz A., Min J., Allali-Hassani A., Schapira M., Shuen M., Loppnau P.,
RA Mazitschek R., Kwiatkowski N.P., Lewis T.A., Maglathin R.L., McLean T.H.,
RA Bochkarev A., Plotnikov A.N., Vedadi M., Arrowsmith C.H.;
RT "Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding
RT motif and cryptic deacetylase activity.";
RL J. Biol. Chem. 283:11355-11363(2008).
RN [29]
RP VARIANT [LARGE SCALE ANALYSIS] MET-43.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (By
CC similarity). May be involved in Epstein-Barr virus (EBV) latency,
CC possibly by repressing the viral BZLF1 gene. Positively regulates the
CC transcriptional repressor activity of FOXP3 (PubMed:17360565). Serves
CC as a corepressor of RARA, causing its deacetylation and inhibition of
CC RARE DNA element binding (PubMed:28167758). In association with RARA,
CC plays a role in the repression of microRNA-10a and thereby in the
CC inflammatory response (PubMed:28167758). {ECO:0000250|UniProtKB:Q8C2B3,
CC ECO:0000269|PubMed:12239305, ECO:0000269|PubMed:17360565,
CC ECO:0000269|PubMed:28167758}.
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 HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1,
CC NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts
CC with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C (By similarity).
CC Interacts with KAT5 and EDNRA. Interacts with KDM5B. Interacts with
CC ZMYND15 (By similarity). Interacts with PML (isoform PML-4). Interacts
CC with FOXP3. Interacts with RARA (PubMed:28167758).
CC {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000269|PubMed:11262386,
CC ECO:0000269|PubMed:11466315, ECO:0000269|PubMed:12551922,
CC ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17373667,
CC ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:28167758}.
CC -!- INTERACTION:
CC Q8WUI4; P00533: EGFR; NbExp=3; IntAct=EBI-1048378, EBI-297353;
CC Q8WUI4; Q9BZS1-1: FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-9695448;
CC Q8WUI4; Q9BZS1-2: FOXP3; NbExp=2; IntAct=EBI-1048378, EBI-16338471;
CC Q8WUI4; Q9BZL6: PRKD2; NbExp=6; IntAct=EBI-1048378, EBI-1384325;
CC Q8WUI4; P31947: SFN; NbExp=3; IntAct=EBI-1048378, EBI-476295;
CC Q8WUI4; P63104: YWHAZ; NbExp=4; IntAct=EBI-1048378, EBI-347088;
CC Q8WUI4; P08393: ICP0; Xeno; NbExp=3; IntAct=EBI-1048378, EBI-6148881;
CC Q8WUI4; Q8CFN5: Mef2c; Xeno; NbExp=2; IntAct=EBI-1048378, EBI-643797;
CC Q8WUI4-5; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-10276431, EBI-739580;
CC Q8WUI4-5; Q04864: REL; NbExp=3; IntAct=EBI-10276431, EBI-307352;
CC Q8WUI4-5; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-10276431, EBI-10226430;
CC Q8WUI4-6; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-12094670, EBI-17721098;
CC Q8WUI4-6; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-12094670, EBI-713602;
CC Q8WUI4-6; Q03989: ARID5A; NbExp=3; IntAct=EBI-12094670, EBI-948603;
CC Q8WUI4-6; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-12094670, EBI-10693038;
CC Q8WUI4-6; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-12094670, EBI-18036948;
CC Q8WUI4-6; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-12094670, EBI-739580;
CC Q8WUI4-6; P60953: CDC42; NbExp=3; IntAct=EBI-12094670, EBI-81752;
CC Q8WUI4-6; Q7L2Z9: CENPQ; NbExp=3; IntAct=EBI-12094670, EBI-2350265;
CC Q8WUI4-6; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12094670, EBI-742054;
CC Q8WUI4-6; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-12094670, EBI-12260294;
CC Q8WUI4-6; Q9UBI6: GNG12; NbExp=3; IntAct=EBI-12094670, EBI-358636;
CC Q8WUI4-6; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12094670, EBI-5916454;
CC Q8WUI4-6; A5PKX9: INADL; NbExp=3; IntAct=EBI-12094670, EBI-12035052;
CC Q8WUI4-6; Q9BXK1: KLF16; NbExp=3; IntAct=EBI-12094670, EBI-5457991;
CC Q8WUI4-6; Q6ZNG9: KRBA2; NbExp=3; IntAct=EBI-12094670, EBI-13309813;
CC Q8WUI4-6; O43679: LDB2; NbExp=3; IntAct=EBI-12094670, EBI-2865580;
CC Q8WUI4-6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12094670, EBI-16439278;
CC Q8WUI4-6; Q9BRT3: MIEN1; NbExp=5; IntAct=EBI-12094670, EBI-6137472;
CC Q8WUI4-6; O00746: NME4; NbExp=3; IntAct=EBI-12094670, EBI-744871;
CC Q8WUI4-6; Q9BQI9: NRIP2; NbExp=6; IntAct=EBI-12094670, EBI-3913975;
CC Q8WUI4-6; B7ZLY0: PHC2; NbExp=3; IntAct=EBI-12094670, EBI-14568740;
CC Q8WUI4-6; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-12094670, EBI-710402;
CC Q8WUI4-6; P63000: RAC1; NbExp=4; IntAct=EBI-12094670, EBI-413628;
CC Q8WUI4-6; P15153: RAC2; NbExp=3; IntAct=EBI-12094670, EBI-489652;
CC Q8WUI4-6; P60763: RAC3; NbExp=3; IntAct=EBI-12094670, EBI-767084;
CC Q8WUI4-6; Q04864-2: REL; NbExp=3; IntAct=EBI-12094670, EBI-10829018;
CC Q8WUI4-6; Q0D2K3: RIPPLY1; NbExp=6; IntAct=EBI-12094670, EBI-10226430;
CC Q8WUI4-6; P62070: RRAS2; NbExp=3; IntAct=EBI-12094670, EBI-491037;
CC Q8WUI4-6; O15427: SLC16A3; NbExp=3; IntAct=EBI-12094670, EBI-7600166;
CC Q8WUI4-6; O94964-4: SOGA1; NbExp=3; IntAct=EBI-12094670, EBI-14083835;
CC Q8WUI4-6; O95411: TIAF1; NbExp=3; IntAct=EBI-12094670, EBI-302378;
CC Q8WUI4-6; O95164: UBL3; NbExp=3; IntAct=EBI-12094670, EBI-12876508;
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. Treatment with EDN1 results in
CC shuttling from the nucleus to the perinuclear region. 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=10;
CC Name=1;
CC IsoId=Q8WUI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUI4-2; Sequence=VSP_007429, VSP_007431;
CC Name=3;
CC IsoId=Q8WUI4-3; Sequence=VSP_008772;
CC Name=4;
CC IsoId=Q8WUI4-4; Sequence=VSP_007430;
CC Name=5;
CC IsoId=Q8WUI4-5; Sequence=VSP_038104;
CC Name=6;
CC IsoId=Q8WUI4-6; Sequence=VSP_038105;
CC Name=7;
CC IsoId=Q8WUI4-7; Sequence=VSP_038104, VSP_008772;
CC Name=8;
CC IsoId=Q8WUI4-8; Sequence=VSP_038106, VSP_038107;
CC Name=9;
CC IsoId=Q8WUI4-9; Sequence=VSP_038102;
CC Name=10;
CC IsoId=Q8WUI4-10; Sequence=VSP_038103;
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-155 by
CC MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and
CC export from the nucleus. Phosphorylation at Ser-155 is a prerequisite
CC for phosphorylation at Ser-181. {ECO:0000269|PubMed:16980613,
CC ECO:0000269|PubMed:17962809, ECO:0000269|PubMed:20188095}.
CC -!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA), a
CC known histone deacetylase inhibitor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF63491.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91474.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55363.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC56929.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF239243; AAF63491.1; ALT_FRAME; mRNA.
DR EMBL; AY302468; AAQ18232.1; -; mRNA.
DR EMBL; AY321367; AAP84704.1; -; mRNA.
DR EMBL; BT009771; AAP88773.1; -; mRNA.
DR EMBL; AK001032; BAA91474.1; ALT_INIT; mRNA.
DR EMBL; AK001190; BAA91545.1; ALT_INIT; mRNA.
DR EMBL; AK024469; BAB15759.1; ALT_INIT; mRNA.
DR EMBL; AK027781; BAB55363.1; ALT_INIT; mRNA.
DR EMBL; AK122588; BAC56929.1; ALT_SEQ; mRNA.
DR EMBL; AK128383; BAG54670.1; -; mRNA.
DR EMBL; AK299292; BAG61307.1; -; mRNA.
DR EMBL; AK301545; BAG63042.1; -; mRNA.
DR EMBL; AK303481; BAG64517.1; -; mRNA.
DR EMBL; AC004466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW57957.1; -; Genomic_DNA.
DR EMBL; BC006453; AAH06453.2; -; mRNA.
DR EMBL; BC020505; AAH20505.2; -; mRNA.
DR EMBL; BC064840; AAH64840.1; -; mRNA.
DR EMBL; AL117455; CAB55935.1; -; mRNA.
DR CCDS; CCDS41776.1; -. [Q8WUI4-7]
DR CCDS; CCDS81685.1; -. [Q8WUI4-6]
DR CCDS; CCDS8756.2; -. [Q8WUI4-5]
DR PIR; T17245; T17245.
DR RefSeq; NP_001091886.1; NM_001098416.3. [Q8WUI4-7]
DR RefSeq; NP_001295019.1; NM_001308090.1. [Q8WUI4-6]
DR RefSeq; NP_056216.2; NM_015401.4. [Q8WUI4-5]
DR RefSeq; XP_011536783.1; XM_011538481.1. [Q8WUI4-1]
DR RefSeq; XP_011536784.1; XM_011538482.1. [Q8WUI4-1]
DR PDB; 3C0Y; X-ray; 2.10 A; A/B/C=482-903.
DR PDB; 3C0Z; X-ray; 2.10 A; A/B/C=482-903.
DR PDB; 3C10; X-ray; 2.00 A; A/B/C=482-903.
DR PDB; 3ZNR; X-ray; 2.40 A; A/B/C=482-903.
DR PDB; 3ZNS; X-ray; 2.45 A; A/B/C=482-903.
DR PDBsum; 3C0Y; -.
DR PDBsum; 3C0Z; -.
DR PDBsum; 3C10; -.
DR PDBsum; 3ZNR; -.
DR PDBsum; 3ZNS; -.
DR AlphaFoldDB; Q8WUI4; -.
DR SMR; Q8WUI4; -.
DR BioGRID; 119613; 133.
DR CORUM; Q8WUI4; -.
DR DIP; DIP-29860N; -.
DR IntAct; Q8WUI4; 67.
DR MINT; Q8WUI4; -.
DR STRING; 9606.ENSP00000080059; -.
DR BindingDB; Q8WUI4; -.
DR ChEMBL; CHEMBL2716; -.
DR DrugBank; DB05015; Belinostat.
DR DrugBank; DB06603; Panobinostat.
DR DrugBank; DB04297; Trichostatin A.
DR DrugCentral; Q8WUI4; -.
DR GuidetoPHARMACOLOGY; 2661; -.
DR GlyGen; Q8WUI4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WUI4; -.
DR PhosphoSitePlus; Q8WUI4; -.
DR BioMuta; HDAC7; -.
DR DMDM; 30913097; -.
DR EPD; Q8WUI4; -.
DR jPOST; Q8WUI4; -.
DR MassIVE; Q8WUI4; -.
DR MaxQB; Q8WUI4; -.
DR PaxDb; Q8WUI4; -.
DR PeptideAtlas; Q8WUI4; -.
DR PRIDE; Q8WUI4; -.
DR ProteomicsDB; 74678; -. [Q8WUI4-1]
DR ProteomicsDB; 74679; -. [Q8WUI4-10]
DR ProteomicsDB; 74680; -. [Q8WUI4-2]
DR ProteomicsDB; 74681; -. [Q8WUI4-3]
DR ProteomicsDB; 74682; -. [Q8WUI4-4]
DR ProteomicsDB; 74683; -. [Q8WUI4-5]
DR ProteomicsDB; 74684; -. [Q8WUI4-6]
DR ProteomicsDB; 74685; -. [Q8WUI4-7]
DR ProteomicsDB; 74686; -. [Q8WUI4-8]
DR ProteomicsDB; 74687; -. [Q8WUI4-9]
DR ABCD; Q8WUI4; 1 sequenced antibody.
DR Antibodypedia; 1412; 665 antibodies from 42 providers.
DR DNASU; 51564; -.
DR Ensembl; ENST00000080059.12; ENSP00000080059.7; ENSG00000061273.18. [Q8WUI4-5]
DR Ensembl; ENST00000354334.7; ENSP00000351326.3; ENSG00000061273.18. [Q8WUI4-7]
DR Ensembl; ENST00000427332.6; ENSP00000404394.2; ENSG00000061273.18. [Q8WUI4-1]
DR Ensembl; ENST00000552960.5; ENSP00000448532.1; ENSG00000061273.18. [Q8WUI4-6]
DR GeneID; 51564; -.
DR KEGG; hsa:51564; -.
DR MANE-Select; ENST00000080059.12; ENSP00000080059.7; NM_015401.5; NP_056216.2. [Q8WUI4-5]
DR UCSC; uc001rqj.5; human. [Q8WUI4-1]
DR CTD; 51564; -.
DR DisGeNET; 51564; -.
DR GeneCards; HDAC7; -.
DR HGNC; HGNC:14067; HDAC7.
DR HPA; ENSG00000061273; Low tissue specificity.
DR MIM; 606542; gene.
DR neXtProt; NX_Q8WUI4; -.
DR OpenTargets; ENSG00000061273; -.
DR PharmGKB; PA162390579; -.
DR VEuPathDB; HostDB:ENSG00000061273; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159065; -.
DR HOGENOM; CLU_006530_0_1_1; -.
DR InParanoid; Q8WUI4; -.
DR OMA; WPLSWTR; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; Q8WUI4; -.
DR TreeFam; TF106174; -.
DR BRENDA; 3.5.1.98; 2681.
DR PathwayCommons; Q8WUI4; -.
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-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q8WUI4; -.
DR SIGNOR; Q8WUI4; -.
DR BioGRID-ORCS; 51564; 27 hits in 1094 CRISPR screens.
DR ChiTaRS; HDAC7; human.
DR EvolutionaryTrace; Q8WUI4; -.
DR GeneWiki; HDAC7; -.
DR GenomeRNAi; 51564; -.
DR Pharos; Q8WUI4; Tclin.
DR PRO; PR:Q8WUI4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WUI4; protein.
DR Bgee; ENSG00000061273; Expressed in sural nerve and 191 other tissues.
DR ExpressionAtlas; Q8WUI4; baseline and differential.
DR Genevisible; Q8WUI4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
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; IPI:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IDA:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; TAS:Reactome.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0007043; P:cell-cell junction assembly; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR GO; GO:0006476; P:protein deacetylation; IMP:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR Gene3D; 3.40.800.20; -; 1.
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 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 3D-structure; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Hydrolase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..952
FT /note="Histone deacetylase 7"
FT /id="PRO_0000114705"
FT REGION 1..268
FT /note="Transcription repression 1"
FT /evidence="ECO:0000250"
FT REGION 1..98
FT /note="Interaction with MEF2C"
FT /evidence="ECO:0000250"
FT REGION 49..149
FT /note="Interaction with MEF2A"
FT /evidence="ECO:0000250"
FT REGION 130..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..546
FT /note="Transcription repression 2"
FT /evidence="ECO:0000250"
FT REGION 261..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..865
FT /note="Histone deacetylase"
FT REGION 877..952
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000250"
FT MOTIF 918..952
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 670
FT /evidence="ECO:0000250"
FT BINDING 533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 535
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 843
FT /note="Contributes to catalysis"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine; by MARK2, MARK3 and PKD/PRKD1"
FT /evidence="ECO:0000305|PubMed:16980613"
FT MOD_RES 181
FT /note="Phosphoserine; by PKD/PRKD2"
FT /evidence="ECO:0000269|PubMed:16980613,
FT ECO:0000269|PubMed:17962809, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 358
FT /note="Phosphoserine; by PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:Q8C2B3"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..527
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038102"
FT VAR_SEQ 1..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007429"
FT VAR_SEQ 1..338
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038103"
FT VAR_SEQ 1
FT /note="M -> MHSPGADGTQVSPGAHYCSPTGAGCPRPCADTPGPQPQPM (in
FT isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_038104"
FT VAR_SEQ 1
FT /note="M -> MHSPGAGCPRPCADTPGPQPQPM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038105"
FT VAR_SEQ 1
FT /note="M -> MSDLRKRELGALFTSRGTGGVEWDGTQVSPGAHYCSPTGAGCPRPCA
FT DTPGPQPQPM (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038106"
FT VAR_SEQ 227..263
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_008772"
FT VAR_SEQ 227..256
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_007430"
FT VAR_SEQ 473..520
FT /note="LAQGGHRPLSRAQSSPAAPASLSAPEPASQARVLSSSETPARTLPFTT ->
FT MQACVGVRGVYPPGSMWVPAVAVLACSLQPRPWGVRTPWVPALTLAPA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007431"
FT VAR_SEQ 892..952
FT /note="SKYWGCMQRLASCPDSWVPRVPGADKEEVEAVTALASLSVGILAEDRPSEQL
FT VEEEEPMNL -> MGALTLSQIPGHGSSQQQAGGAFSRPGHPCRAAVVMVNTGAACSAW
FT PPVQTPGCLECQGLTKKKWRQ (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038107"
FT VARIANT 43
FT /note="V -> M (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1165948169)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036043"
FT MUTAGEN 150
FT /note="L->A: Abolishes phosphorylation at S-155."
FT /evidence="ECO:0000269|PubMed:16980613"
FT MUTAGEN 155
FT /note="S->A: Abolishes nuclear export; when associated with
FT A-181; A-358 and A-486. Abolishes phosphorylation by MARK2
FT and MARK3, interaction with 14-3-3 and localization to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:16980613"
FT MUTAGEN 181
FT /note="S->A: Abolishes nuclear export; when associated with
FT A-155; A-358 and A-486."
FT /evidence="ECO:0000269|PubMed:16980613"
FT MUTAGEN 358
FT /note="S->A: Abolishes nuclear export; when associated with
FT A-192; A-1118 and A-486."
FT /evidence="ECO:0000269|PubMed:16980613"
FT MUTAGEN 486
FT /note="S->A: Abolishes nuclear export; when associated with
FT A-192; A-1118 and A-358."
FT /evidence="ECO:0000269|PubMed:16980613"
FT MUTAGEN 843
FT /note="H->A: Enhanced deacetylase activity."
FT /evidence="ECO:0000269|PubMed:18285338"
FT MUTAGEN 843
FT /note="H->F: Enhanced deacetylase activity."
FT /evidence="ECO:0000269|PubMed:18285338"
FT MUTAGEN 843
FT /note="H->Y: 6000 fold increase in deacetylase activity."
FT /evidence="ECO:0000269|PubMed:18285338"
FT CONFLICT 50
FT /note="M -> T (in Ref. 5; BAG64517)"
FT /evidence="ECO:0000305"
FT CONFLICT 225..264
FT /note="Missing (in Ref. 1; AAF63491)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="P -> L (in Ref. 5; BAA91545)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="R -> L (in Ref. 5; BAA91545)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="V -> E (in Ref. 1; AAF63491)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="S -> R (in Ref. 5; BAB15759)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="R -> W (in Ref. 5; BAA91474)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="K -> KASK (in Ref. 1; AAF63491)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="G -> S (in Ref. 5; BAA91545)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="A -> T (in Ref. 5; BAB55363)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="Q -> H (in Ref. 5; BAA91474)"
FT /evidence="ECO:0000305"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 546..557
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 564..567
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:3C10"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 583..590
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 601..609
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:3C10"
FT TURN 631..633
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 634..653
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 656..662
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 684..695
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 712..718
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 724..731
FT /evidence="ECO:0007829|PDB:3C10"
FT TURN 733..736
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 756..761
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 771..780
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 782..789
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 792..798
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 817..827
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:3C10"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 845..860
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 866..868
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 871..873
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 878..891
FT /evidence="ECO:0007829|PDB:3C10"
FT TURN 892..894
FT /evidence="ECO:0007829|PDB:3C10"
FT HELIX 896..898
FT /evidence="ECO:0007829|PDB:3C10"
SQ SEQUENCE 952 AA; 102927 MW; 786785B084667731 CRC64;
MDLRVGQRPP VEPPPEPTLL ALQRPQRLHH HLFLAGLQQQ RSVEPMRLSM DTPMPELQVG
PQEQELRQLL HKDKSKRSAV ASSVVKQKLA EVILKKQQAA LERTVHPNSP GIPYRTLEPL
ETEGATRSML SSFLPPVPSL PSDPPEHFPL RKTVSEPNLK LRYKPKKSLE RRKNPLLRKE
SAPPSLRRRP AETLGDSSPS SSSTPASGCS SPNDSEHGPN PILGSEALLG QRLRLQETSV
APFALPTVSL LPAITLGLPA PARADSDRRT HPTLGPRGPI LGSPHTPLFL PHGLEPEAGG
TLPSRLQPIL LLDPSGSHAP LLTVPGLGPL PFHFAQSLMT TERLSGSGLH WPLSRTRSEP
LPPSATAPPP PGPMQPRLEQ LKTHVQVIKR SAKPSEKPRL RQIPSAEDLE TDGGGPGQVV
DDGLEHRELG HGQPEARGPA PLQQHPQVLL WEQQRLAGRL PRGSTGDTVL LPLAQGGHRP
LSRAQSSPAA PASLSAPEPA SQARVLSSSE TPARTLPFTT GLIYDSVMLK HQCSCGDNSR
HPEHAGRIQS IWSRLQERGL RSQCECLRGR KASLEELQSV HSERHVLLYG TNPLSRLKLD
NGKLAGLLAQ RMFVMLPCGG VGVDTDTIWN ELHSSNAARW AAGSVTDLAF KVASRELKNG
FAVVRPPGHH ADHSTAMGFC FFNSVAIACR QLQQQSKASK ILIVDWDVHH GNGTQQTFYQ
DPSVLYISLH RHDDGNFFPG SGAVDEVGAG SGEGFNVNVA WAGGLDPPMG DPEYLAAFRI
VVMPIAREFS PDLVLVSAGF DAAEGHPAPL GGYHVSAKCF GYMTQQLMNL AGGAVVLALE
GGHDLTAICD ASEACVAALL GNRVDPLSEE GWKQKPNLNA IRSLEAVIRV HSKYWGCMQR
LASCPDSWVP RVPGADKEEV EAVTALASLS VGILAEDRPS EQLVEEEEPM NL
