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 27-MAR-2024, entry version 213. 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; O95411: MYO18A; NbExp=3; IntAct=EBI-12094670, EBI-302378; 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_011536784.1; XM_011538482.1. 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; 142. 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; DB12565; Abexinostat. DR DrugBank; DB05015; Belinostat. DR DrugBank; DB01262; Decitabine. DR DrugBank; DB11841; Entinostat. DR DrugBank; DB12645; Givinostat. DR DrugBank; DB06603; Panobinostat. DR DrugBank; DB06819; Phenylbutyric acid. DR DrugBank; DB03766; Propanoic acid. DR DrugBank; DB12847; Pyroxamide. DR DrugBank; DB06176; Romidepsin. DR DrugBank; DB04297; Trichostatin A. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB02546; Vorinostat. 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; 9606-ENSP00000080059; -. DR PeptideAtlas; 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 Pumba; Q8WUI4; -. DR ABCD; Q8WUI4; 1 sequenced antibody. DR Antibodypedia; 1412; 736 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 AGR; HGNC:14067; -. 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; 124800at2759; -. 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; 31 hits in 1173 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 193 other cell types or tissues. DR ExpressionAtlas; Q8WUI4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. 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; ISS:UniProtKB. 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:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL. DR GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; 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; IEA:Ensembl. 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:0016925; P:protein sumoylation; TAS:Reactome. DR GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProt. DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl. DR CDD; cd10008; HDAC7; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR046949; HDAC4/5/7/9. 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 PANTHER; PTHR10625:SF44; HISTONE DEACETYLASE 7; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037911; HDAC_II_euk; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. DR Genevisible; Q8WUI4; HS. 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 //