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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
TISSUE=Fetus;
DOI=10.1074/jbc.274.4.2440; PubMed=9891014 [NCBI, ExPASy, EBI, Israel, Japan]
Verdel A.,
Khochbin S.;
"Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers.";
J. Biol. Chem. 274:2440-2445(1999).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NCOR2.
STRAIN=C57BL/6;
PubMed=10640276 [NCBI, ExPASy, EBI, Israel, Japan]
Kao H.-Y.,
Downes M.,
Ordentlich P.,
Evans R.M.;
"Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression.";
Genes Dev. 14:55-66(2000).
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[3]
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INTERACTION WITH HDAC7, NUCLEAR EXPORT, AND MUTAGENESIS OF HIS-824 AND HIS-884.
DOI=10.1073/pnas.97.19.10330; PubMed=10984530 [NCBI, ExPASy, EBI, Israel, Japan]
Downes M.,
Ordentlich P.,
Kao H.-Y.,
Alvarez J.G.A.,
Evans R.M.;
"Identification of a nuclear domain with deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
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[4]
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INTERACTION WITH CTBP1 AND HDAC9.
DOI=10.1074/jbc.M007364200; PubMed=11022042 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang C.L.,
McKinsey T.A.,
Lu J.R.,
Olson E.N.;
"Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor.";
J. Biol. Chem. 276:35-39(2001).
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[5]
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INTERACTION WITH PHB2.
DOI=10.1074/jbc.M312300200; PubMed=15140878 [NCBI, ExPASy, EBI, Israel, Japan]
Kurtev V.,
Margueron R.,
Kroboth K.,
Ogris E.,
Cavailles V.,
Seiser C.;
"Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases.";
J. Biol. Chem. 279:24834-24843(2004).
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[6]
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INTERACTION WITH NRIP1.
DOI=10.1093/nar/gkh524; PubMed=15060175 [NCBI, ExPASy, EBI, Israel, Japan]
Castet A.,
Boulahtouf A.,
Versini G.,
Bonnet S.,
Augereau P.,
Vignon F.,
Khochbin S.,
Jalaguier S.,
Cavailles V.;
"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition.";
Nucleic Acids Res. 32:1957-1966(2004).
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[7]
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INTERACTION WITH AHRR.
DOI=10.1016/j.bbrc.2007.09.131; PubMed=17949687 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima M.,
Mimura J.,
Yamamoto M.,
Fujii-Kuriyama Y.;
"Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5.";
Biochem. Biophys. Res. Commun. 364:276-282(2007).
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- 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. Involved in muscle maturation by repressing transcription of myocyte enhancer MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity).
- CATALYTIC ACTIVITY: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.
- SUBUNIT: Interacts with JARID1B (By similarity). Interacts with BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2, AHRR, and a 14-3-3 chaperone protein.
- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By similarity). Note=Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-250 and Ser-488 by CaMK (By similarity).
- DOMAIN: The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.
- PTM: Phosphorylated by CaMK at Ser-250 and Ser-488. The phosphorylation is required for the export to the cytoplasm (By similarity).
- PTM: Ubiquitinated. Polyubiquitination however does not lead to its degradation (By similarity).
- SIMILARITY: Belongs to the histone deacetylase family. Type 2 subfamily.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 1113 AA [This is the length of the unprocessed precursor] |
Molecular weight: 120942 Da [This is the MW of the unprocessed precursor] |
CRC64: 63071AF45B87815A [This is a checksum on the sequence] |
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10 20 30 40 50 60
MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR
70 80 90 100 110 120
GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
130 140 150 160 170 180
QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE
190 200 210 220 230 240
FLLSKSKEPT PGGLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR
250 260 270 280 290 300
DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
310 320 330 340 350 360
VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN QFSLYTSPSL
370 380 390 400 410 420
PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG
430 440 450 460 470 480
VALEGDTSPH GHASLLQHVC SWTGRQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH
490 500 510 520 530 540
RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE
550 560 570 580 590 600
ETEEELTEQQ EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES
610 620 630 640 650 660
GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS
670 680 690 700 710 720
PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG RIQSIWSRLQ ETGLLGKCER
730 740 750 760 770 780
IRGRKATLDE IQTVHSEYHT LLYGTSPLNR QKLDSKKLLG PISQKMYAML PCGGIGVDSD
790 800 810 820 830 840
TVWNEMHSSS AVRMAVGCLV ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA
850 860 870 880 890 900
ITAKLLQQKL SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE
910 920 930 940 950 960
VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV SAGFDAVEGH
970 980 990 1000 1010 1020
LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT AICDASEACV SALLSVELQP
1030 1040 1050 1060 1070 1080
LDEAVLQQKP SVNAVATLEK VIEIQSKHWS CVQRFAAGLG CSLREAQTGE KEEAETVSAM
1090 1100 1110
ALLSVGAEQA QAVATQEHSP RPAEEPMEQE PAL
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Q9Z2V6 in FASTA format |
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ExPASy Home page
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