T3DB: Histone deacetylase 6

Name	Histone deacetylase 6
Synonyms	3.5.1.98 HD6 KIAA0901
Gene Name	HDAC6
Organism	Human
Amino acid sequence	>lcl\|BSEQ0037198\|Histone deacetylase 6 MTSTGQDSTTTRQRRSRQNPQSPPQDSSVTSKRNIKKGAVPRSIPNLAEVKKKGKMKKLG QAMEEDLIVGLQGMDLNLEAEALAGTGLVLDEQLNEFHCLWDDSFPEGPERLHAIKEQLI QEGLLDRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLADTYDSVYLHPNS YSCACLASGSVLRLVDAVLGAEIRNGMAIIRPPGHHAQHSLMDGYCMFNHVAVAARYAQQ KHRIRRVLIVDWDVHHGQGTQFTFDQDPSVLYFSIHRYEQGRFWPHLKASNWSTTGFGQG QGYTINVPWNQVGMRDADYIAAFLHVLLPVALEFQPQLVLVAAGFDALQGDPKGEMAATP AGFAQLTHLLMGLAGGKLILSLEGGYNLRALAEGVSASLHTLLGDPCPMLESPGAPCRSA QASVSCALEALEPFWEVLVRSTETVERDNMEEDNVEESEEEGPWEPPVLPILTWPVLQSR TGLVYDQNMMNHCNLWDSHHPEVPQRILRIMCRLEELGLAGRCLTLTPRPATEAELLTCH SAEYVGHLRATEKMKTRELHRESSNFDSIYICPSTFACAQLATGAACRLVEAVLSGEVLN GAAVVRPPGHHAEQDAACGFCFFNSVAVAARHAQTISGHALRILIVDWDVHHGNGTQHMF EDDPSVLYVSLHRYDHGTFFPMGDEGASSQIGRAAGTGFTVNVAWNGPRMGDADYLAAWH RLVLPIAYEFNPELVLVSAGFDAARGDPLGGCQVSPEGYAHLTHLLMGLASGRIILILEG GYNLTSISESMAACTRSLLGDPPPLLTLPRPPLSGALASITETIQVHRRYWRSLRVMKVE DREGPSSSKLVTKKAPQPAKPRLAERMTTREKKVLEAGMGKVTSASFGEESTPGQTNSET AVVALTQDQPSEAATGGATLAQTISEAAIGGAMLGQTTSEEAVGGATPDQTTSEETVGGA ILDQTTSEDAVGGATLGQTTSEEAVGGATLAQTTSEAAMEGATLDQTTSEEAPGGTELIQ TPLASSTDHQTPPTSPVQGTTPQISPSTLIGSLRTLELGSESQGASESQAPGEENLLGEA AGGQDMADSMLMQGSRGLTDQAIFYAVTPLPWCPHLVAVCPIPAAGLDVTQPCGDCGTIQ ENWVCLSCYQVYCGRYINGHMLQHHGNSGHPLVLSYIDLSAWCYYCQAYVHHQALLDVKN IAHQNKFGEDMPHPH
Number of residues	1215
Molecular Weight	131418.19
Theoretical pI	4.98
GO Classification	Functions histone deacetylase activity polyubiquitin binding tau protein binding misfolded protein binding Hsp90 protein binding enzyme binding alpha-tubulin binding core promoter binding histone deacetylase binding dynein complex binding NAD-dependent histone deacetylase activity (H3-K14 specific) zinc ion binding ubiquitin protein ligase binding beta-catenin binding microtubule binding tubulin deacetylase activity Processes peptidyl-lysine deacetylation positive regulation of signal transduction cellular response to hydrogen peroxide histone deacetylation aggresome assembly negative regulation of transcription, DNA-templated mitophagy in response to mitochondrial depolarization response to misfolded protein negative regulation of oxidoreductase activity negative regulation of hydrogen peroxide metabolic process response to organic substance protein polyubiquitination negative regulation of protein complex disassembly negative regulation of proteolysis regulation of gene expression, epigenetic cellular response to misfolded protein positive regulation of receptor biosynthetic process cellular response to topologically incorrect protein protein deacetylation cellular response to heat response to toxic substance Hsp90 deacetylation response to growth factor regulation of protein stability lysosome localization tubulin deacetylation positive regulation of epithelial cell migration organelle organization polyubiquitinated misfolded protein transport regulation of microtubule-based movement mitochondrion localization regulation of androgen receptor signaling pathway regulation of receptor activity positive regulation of chaperone-mediated protein complex assembly misfolded or incompletely synthesized protein catabolic process intracellular protein transport transcription, DNA-templated positive regulation of hydrogen peroxide-mediated programmed cell death ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway negative regulation of microtubule depolymerization protein complex disassembly regulation of fat cell differentiation macroautophagy regulation of establishment of protein localization Components axon microtubule associated complex cytosol histone deacetylase complex perinuclear region of cytoplasm aggresome dendrite cytoplasmic microtubule perikaryon cell leading edge caveola cytoplasm microtubule nucleus inclusion body
General Function	Zinc ion binding
Specific Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.
Pfam Domain Function	Hist_deacetyl (PF00850 ) zf-UBP (PF02148 )
Transmembrane Regions	Not Available
GenBank Protein ID	4754911
UniProtKB ID	Q9UBN7
UniProtKB Entry Name	HDAC6_HUMAN
Cellular Location	Nucleus
Gene sequence	>lcl\|BSEQ0021857\|Histone deacetylase 6 (HDAC6) ATGACCTCAACCGGCCAGGATTCCACCACAACCAGGCAGCGAAGAAGTAGGCAGAACCCC CAGTCGCCCCCTCAGGACTCCAGTGTCACTTCGAAGCGAAATATTAAAAAGGGAGCCGTT CCCCGCTCTATCCCCAATCTAGCGGAGGTAAAGAAGAAAGGCAAAATGAAGAAGCTCGGC CAAGCAATGGAAGAAGACCTAATCGTGGGACTGCAAGGGATGGATCTGAACCTTGAGGCT GAAGCACTGGCTGGCACTGGCTTGGTGTTGGATGAGCAGTTAAATGAATTCCATTGCCTC TGGGATGACAGCTTCCCGGAAGGCCCTGAGCGGCTCCATGCCATCAAGGAGCAACTGATC CAGGAGGGCCTCCTAGATCGCTGCGTGTCCTTTCAGGCCCGGTTTGCTGAAAAGGAAGAG CTGATGTTGGTTCACAGCCTAGAATATATTGATCTGATGGAAACAACCCAGTACATGAAT GAGGGAGAACTCCGTGTCCTAGCAGACACCTACGACTCAGTTTATCTGCATCCGAACTCA TACTCCTGTGCCTGCCTGGCCTCAGGCTCTGTCCTCAGGCTGGTGGATGCGGTCCTGGGG GCTGAGATCCGGAATGGCATGGCCATCATTAGGCCTCCTGGACATCACGCCCAGCACAGT CTTATGGATGGCTATTGCATGTTCAACCACGTGGCTGTGGCAGCCCGCTATGCTCAACAG AAACACCGCATCCGGAGGGTCCTTATCGTAGATTGGGATGTGCACCACGGTCAAGGAACA CAGTTCACCTTCGACCAGGACCCCAGTGTCCTCTATTTCTCCATCCACCGCTACGAGCAG GGTAGGTTCTGGCCCCACCTGAAGGCCTCTAACTGGTCCACCACAGGTTTCGGCCAAGGC CAAGGATATACCATCAATGTGCCTTGGAACCAGGTGGGGATGCGGGATGCTGACTACATT GCTGCTTTCCTGCACGTCCTGCTGCCAGTCGCCCTCGAGTTCCAGCCTCAGCTGGTCCTG GTGGCTGCTGGATTTGATGCCCTGCAAGGGGACCCCAAGGGTGAGATGGCCGCCACTCCG GCAGGGTTCGCCCAGCTAACCCACCTGCTCATGGGTCTGGCAGGAGGCAAGCTGATCCTG TCTCTGGAGGGTGGCTACAACCTCCGCGCCCTGGCTGAAGGCGTCAGTGCTTCGCTCCAC ACCCTTCTGGGAGACCCTTGCCCCATGCTGGAGTCACCTGGTGCCCCCTGCCGGAGTGCC CAGGCTTCAGTTTCCTGTGCTCTGGAAGCCCTTGAGCCCTTCTGGGAGGTTCTTGTGAGA TCAACTGAGACCGTGGAGAGGGACAACATGGAGGAGGACAATGTAGAGGAGAGCGAGGAG GAAGGACCCTGGGAGCCCCCTGTGCTCCCAATCCTGACATGGCCAGTGCTACAGTCTCGC ACAGGGCTGGTCTATGACCAAAATATGATGAATCACTGCAACTTGTGGGACAGCCACCAC CCTGAGGTACCCCAGCGCATCTTGCGGATCATGTGCCGTCTGGAGGAGCTGGGCCTTGCC GGGCGCTGCCTCACCCTGACACCGCGCCCTGCCACAGAGGCTGAGCTGCTCACCTGTCAC AGTGCTGAGTACGTGGGTCATCTCCGGGCCACAGAGAAAATGAAAACCCGGGAGCTGCAC CGTGAGAGTTCCAACTTTGACTCCATCTATATCTGCCCCAGTACCTTCGCCTGTGCACAG CTTGCCACTGGCGCTGCCTGCCGCCTGGTGGAGGCTGTGCTCTCAGGAGAGGTTCTGAAT GGTGCTGCTGTGGTGCGTCCCCCAGGACACCACGCAGAGCAGGATGCAGCTTGCGGTTTT TGCTTTTTCAACTCTGTGGCTGTGGCTGCTCGCCATGCCCAGACTATCAGTGGGCATGCC CTACGGATCCTGATTGTGGATTGGGATGTCCACCACGGTAATGGAACTCAGCACATGTTT GAGGATGACCCCAGTGTGCTATATGTGTCCCTGCACCGCTATGATCATGGCACCTTCTTC CCCATGGGGGATGAGGGTGCCAGCAGCCAGATCGGCCGGGCTGCGGGCACAGGCTTCACC GTCAACGTGGCATGGAACGGGCCCCGCATGGGTGATGCTGACTACCTAGCTGCCTGGCAT CGCCTGGTGCTTCCCATTGCCTACGAGTTTAACCCAGAACTGGTGCTGGTCTCAGCTGGC TTTGATGCTGCACGGGGGGATCCGCTGGGGGGCTGCCAGGTGTCACCTGAGGGTTATGCC CACCTCACCCACCTGCTGATGGGCCTTGCCAGTGGCCGCATTATCCTTATCCTAGAGGGT GGCTATAACCTGACATCCATCTCAGAGTCCATGGCTGCCTGCACTCGCTCCCTCCTTGGA GACCCACCACCCCTGCTGACCCTGCCACGGCCCCCACTATCAGGGGCCCTGGCCTCAATC ACTGAGACCATCCAAGTCCATCGCAGATACTGGCGCAGCTTACGGGTCATGAAGGTAGAA GACAGAGAAGGACCCTCCAGTTCTAAGTTGGTCACCAAGAAGGCACCCCAACCAGCCAAA CCTAGGTTAGCTGAGCGGATGACCACACGAGAAAAGAAGGTTCTGGAAGCAGGCATGGGG AAAGTCACCTCGGCATCATTTGGGGAAGAGTCCACTCCAGGCCAGACTAACTCAGAGACA GCTGTGGTGGCCCTCACTCAGGACCAGCCCTCAGAGGCAGCCACAGGGGGAGCCACTCTG GCCCAGACCATTTCTGAGGCAGCCATTGGGGGAGCCATGCTGGGCCAGACCACCTCAGAG GAGGCTGTCGGGGGAGCCACTCCGGACCAGACCACCTCAGAGGAGACTGTGGGAGGAGCC ATTCTGGACCAGACCACCTCAGAGGATGCTGTTGGGGGAGCCACGCTGGGCCAGACTACC TCAGAGGAGGCTGTAGGAGGAGCTACACTGGCCCAGACCACCTCGGAGGCAGCCATGGAG GGAGCCACACTGGACCAGACTACGTCAGAGGAGGCTCCAGGGGGCACCGAGCTGATCCAA ACTCCTCTAGCCTCGAGCACAGACCACCAGACCCCCCCAACCTCACCTGTGCAGGGAACT ACACCCCAGATATCTCCCAGTACACTGATTGGGAGTCTCAGGACCTTGGAGCTAGGCAGC GAATCTCAGGGGGCCTCAGAATCTCAGGCCCCAGGAGAGGAGAACCTACTAGGAGAGGCA GCTGGAGGTCAGGACATGGCTGATTCGATGCTGATGCAGGGATCTAGGGGCCTCACTGAT CAGGCCATATTTTATGCTGTGACACCACTGCCCTGGTGTCCCCATTTGGTGGCAGTATGC CCCATACCTGCAGCAGGCCTAGACGTGACCCAACCTTGTGGGGACTGTGGAACAATCCAA GAGAATTGGGTGTGTCTCTCTTGCTATCAGGTCTACTGTGGTCGTTACATCAATGGCCAC ATGCTCCAACACCATGGAAATTCTGGACACCCGCTGGTCCTCAGCTACATCGACCTGTCA GCCTGGTGTTACTACTGTCAGGCCTATGTCCACCACCAGGCTCTCCTAGATGTGAAGAAC ATCGCCCACCAGAACAAGTTTGGGGAGGATATGCCCCACCCACACTAA
GenBank Gene ID	AF132609
GeneCard ID	Not Available
GenAtlas ID	HDAC6
HGNC ID	HGNC:14064
Chromosome Location	X
Locus	Xp11.23
References	Grozinger CM, Hassig CA, Schreiber SL: Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4868-73. 10220385 Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Dec 31;5(6):355-64. 10048485 Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. 15772651 Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334 Amann JM, Nip J, Strom DK, Lutterbach B, Harada H, Lenny N, Downing JR, Meyers S, Hiebert SW: ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. Mol Cell Biol. 2001 Oct;21(19):6470-83. 11533236 Gao L, Cueto MA, Asselbergs F, Atadja P: Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family. J Biol Chem. 2002 Jul 12;277(28):25748-55. Epub 2002 Apr 10. 11948178 Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 2002 Jun 3;21(11):2682-91. 12032081 Hook SS, Orian A, Cowley SM, Eisenman RN: Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13425-30. Epub 2002 Sep 27. 12354939 Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida M, Wang XF, Yao TP: HDAC6 is a microtubule-associated deacetylase. Nature. 2002 May 23;417(6887):455-8. 12024216 North BJ, Marshall BL, Borra MT, Denu JM, Verdin E: The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003 Feb;11(2):437-44. 12620231 Pugacheva EN, Jablonski SA, Hartman TR, Henske EP, Golemis EA: HEF1-dependent Aurora A activation induces disassembly of the primary cilium. Cell. 2007 Jun 29;129(7):1351-63. 17604723 Ohoka N, Hattori T, Kitagawa M, Onozaki K, Hayashi H: Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion. J Biol Chem. 2007 Dec 7;282(49):35687-94. Epub 2007 Sep 14. 17872950 Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD, Chin LS: Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol. 2007 Sep 10;178(6):1025-38. 17846173 Nahhas F, Dryden SC, Abrams J, Tainsky MA: Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin. Mol Cell Biochem. 2007 Sep;303(1-2):221-30. Epub 2007 May 22. 17516032 Loktev AV, Zhang Q, Beck JS, Searby CC, Scheetz TE, Bazan JF, Slusarski DC, Sheffield VC, Jackson PK, Nachury MV: A BBSome subunit links ciliogenesis, microtubule stability, and acetylation. Dev Cell. 2008 Dec;15(6):854-65. doi: 10.1016/j.devcel.2008.11.001. 19081074 Kalveram B, Schmidtke G, Groettrup M: The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition. J Cell Sci. 2008 Dec 15;121(Pt 24):4079-88. doi: 10.1242/jcs.035006. Epub 2008 Nov 25. 19033385 Zhuang Y, Nguyen HT, Lasky JA, Cao S, Li C, Hu J, Guo X, Burow ME, Shan B: Requirement of a novel splicing variant of human histone deacetylase 6 for TGF-beta1-mediated gene activation. Biochem Biophys Res Commun. 2010 Feb 19;392(4):608-13. doi: 10.1016/j.bbrc.2010.01.091. Epub 2010 Jan 25. 20102703 Wickstrom SA, Masoumi KC, Khochbin S, Fassler R, Massoumi R: CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin. EMBO J. 2010 Jan 6;29(1):131-44. doi: 10.1038/emboj.2009.317. Epub 2009 Nov 5. 19893491 Simon D, Laloo B, Barillot M, Barnetche T, Blanchard C, Rooryck C, Marche M, Burgelin I, Coupry I, Chassaing N, Gilbert-Dussardier B, Lacombe D, Grosset C, Arveiler B: A mutation in the 3'-UTR of the HDAC6 gene abolishing the post-transcriptional regulation mediated by hsa-miR-433 is linked to a new form of dominant X-linked chondrodysplasia. Hum Mol Genet. 2010 May 15;19(10):2015-27. doi: 10.1093/hmg/ddq083. Epub 2010 Feb 24. 20181727 Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460 Kang HJ, Lee MH, Kang HL, Kim SH, Ahn JR, Na H, Na TY, Kim YN, Seong JK, Lee MO: Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1. Cancer Res. 2014 Mar 1;74(5):1484-94. doi: 10.1158/0008-5472.CAN-13-2020. Epub 2014 Jan 10. 24413532 Balasubramanian A, Kawahara G, Gupta VA, Rozkalne A, Beauvais A, Kunkel LM, Gussoni E: Fam65b is important for formation of the HDAC6-dysferlin protein complex during myogenic cell differentiation. FASEB J. 2014 Jul;28(7):2955-69. doi: 10.1096/fj.13-246470. Epub 2014 Mar 31. 24687993 Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569