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Histone deacetylase 7 (HD7) (EC 3.5.1.98) (Histone deacetylase 7A) (HD7a)

 HDAC7_MOUSE             Reviewed;         938 AA.
Q8C2B3; Q8C2C9; Q8C8X4; Q8CB80; Q8CDA3; Q9JL72;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
22-NOV-2017, entry version 154.
RecName: Full=Histone deacetylase 7;
Short=HD7;
EC=3.5.1.98;
AltName: Full=Histone deacetylase 7A;
Short=HD7a;
Name=Hdac7; Synonyms=Hdac7a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH NCOR2 AND SIN3A.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=10640276;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Retina, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC4; HDAC5; NCOR1; NCOR2;
SIN3A; SIN3B; RBBP4; RBBP7; MTA1L1; SAP30 AND MBD3, AND MUTAGENESIS OF
HIS-657; ASP-692; ASP-694 AND HIS-717.
PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
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).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MEF2C, AND
MUTAGENESIS OF HIS-657.
PubMed=11279209; DOI=10.1074/jbc.M101508200;
Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
Muscat G.E.O.;
"A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
J. Biol. Chem. 276:17007-17013(2001).
[6]
SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH YWHAE; MEF2A;
MEF2B AND MEF2C, AND MUTAGENESIS OF SER-178; SER-344 AND SER-479.
PubMed=11585834; DOI=10.1074/jbc.M107631200;
Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.;
"Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7.";
J. Biol. Chem. 276:47496-47507(2001).
[7]
NUCLEAR EXPORT SIGNAL.
PubMed=11509672; DOI=10.1128/MCB.21.18.6312-6321.2001;
McKinsey T.A., Zhang C.-L., Olson E.N.;
"Identification of a signal-responsive nuclear export sequence in
class II histone deacetylases.";
Mol. Cell. Biol. 21:6312-6321(2001).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION AT SER-178; SER-344 AND SER-479.
PubMed=18509061; DOI=10.1073/pnas.0802857105;
Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.;
"Control of endothelial cell proliferation and migration by VEGF
signaling to histone deacetylase 7.";
Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[11]
INTERACTION WITH FOXP3.
PubMed=19696312; DOI=10.1126/science.1176077;
Pan F., Yu H., Dang E.V., Barbi J., Pan X., Grosso J.F., Jinasena D.,
Sharma S.M., McCadden E.M., Getnet D., Drake C.G., Liu J.O.,
Ostrowski M.C., Pardoll D.M.;
"Eos mediates Foxp3-dependent gene silencing in CD4+ regulatory T
cells.";
Science 325:1142-1146(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
INTERACTION WITH ZMYND15.
PubMed=20675388; DOI=10.1074/jbc.M110.116418;
Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
Saunders L., Verdin E., Charo I.F.;
"Zmynd15 encodes a histone deacetylase-dependent transcriptional
repressor essential for spermiogenesis and male fertility.";
J. Biol. Chem. 285:31418-31426(2010).
-!- 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 factors
such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it
shuttles into the cytoplasm, allowing the expression of myocyte
enhancer factors. Positively regulates the transcriptional
repressor activity of FOXP3 (By similarity).
{ECO:0000250|UniProtKB:Q8WUI4, ECO:0000269|PubMed:10640276}.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- SUBUNIT: Interacts with KDM5B (By similarity). Interacts with KAT5
and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5,
NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3.
Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C.
Interacts with ZMYND15. Interacts with PML (By similarity).
Interacts with FOXP3. {ECO:0000250|UniProtKB:Q8WUI4,
ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11279209, ECO:0000269|PubMed:11585834,
ECO:0000269|PubMed:19696312, ECO:0000269|PubMed:20675388}.
-!- INTERACTION:
Q15139:PRKD1 (xeno); NbExp=3; IntAct=EBI-15705168, EBI-1181072;
P62259:Ywhae; NbExp=6; IntAct=EBI-643830, EBI-356480;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=In the nucleus, it
associates with distinct subnuclear dot-like structures. 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 the 14-3-3
protein YWHAE and is due to its phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q8C2B3-1; Sequence=Displayed;
Name=2;
IsoId=Q8C2B3-2; Sequence=VSP_007432, VSP_007434, VSP_007435;
Name=3;
IsoId=Q8C2B3-3; Sequence=VSP_007432, VSP_007434;
Name=4;
IsoId=Q8C2B3-4; Sequence=VSP_007433, VSP_007434, VSP_007435;
Name=5;
IsoId=Q8C2B3-5; Sequence=VSP_007432;
Name=6;
IsoId=Q8C2B3-6; Sequence=VSP_007433;
-!- TISSUE SPECIFICITY: Highly expressed in heart and lung. Expressed
at intermediate level in muscle. {ECO:0000269|PubMed:10640276,
ECO:0000269|PubMed:11279209}.
-!- DOMAIN: The nuclear export sequence mediates the shuttling between
the nucleus and the cytoplasm. {ECO:0000250}.
-!- PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC
kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation
at Ser-178 by MARK2, MARK3 and PRKD1 promotes interaction with 14-
3-3 proteins and export from the nucleus. Phosphorylation at Ser-
178 is a prerequisite for phosphorylation at Ser-204 (By
similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA),
a known histone deacetylase inhibitor.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
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EMBL; AF207749; AAF31419.1; -; mRNA.
EMBL; AK030863; BAC27161.1; -; mRNA.
EMBL; AK036586; BAC29493.1; -; mRNA.
EMBL; AK044287; BAC31856.1; -; mRNA.
EMBL; AK088828; BAC40598.1; -; mRNA.
EMBL; AK088945; BAC40666.1; -; mRNA.
EMBL; BC057332; AAH57332.1; -; mRNA.
CCDS; CCDS37188.1; -. [Q8C2B3-1]
CCDS; CCDS57004.1; -. [Q8C2B3-5]
CCDS; CCDS57005.1; -. [Q8C2B3-2]
CCDS; CCDS57006.1; -. [Q8C2B3-3]
CCDS; CCDS57007.1; -. [Q8C2B3-4]
RefSeq; NP_001191204.1; NM_001204275.1. [Q8C2B3-3]
RefSeq; NP_001191205.1; NM_001204276.1. [Q8C2B3-2]
RefSeq; NP_001191206.1; NM_001204277.1. [Q8C2B3-4]
RefSeq; NP_001191207.1; NM_001204278.1. [Q8C2B3-5]
RefSeq; NP_062518.2; NM_019572.3. [Q8C2B3-1]
RefSeq; XP_006521268.1; XM_006521205.2.
RefSeq; XP_006521270.1; XM_006521207.3. [Q8C2B3-3]
RefSeq; XP_006521271.1; XM_006521208.3. [Q8C2B3-3]
RefSeq; XP_006521272.1; XM_006521209.2. [Q8C2B3-3]
RefSeq; XP_006521273.1; XM_006521210.2. [Q8C2B3-3]
UniGene; Mm.384027; -.
ProteinModelPortal; Q8C2B3; -.
SMR; Q8C2B3; -.
BioGrid; 207862; 5.
CORUM; Q8C2B3; -.
DIP; DIP-42594N; -.
ELM; Q8C2B3; -.
IntAct; Q8C2B3; 6.
MINT; MINT-1551781; -.
STRING; 10090.ENSMUSP00000112110; -.
ChEMBL; CHEMBL3832944; -.
iPTMnet; Q8C2B3; -.
PhosphoSitePlus; Q8C2B3; -.
PaxDb; Q8C2B3; -.
PRIDE; Q8C2B3; -.
Ensembl; ENSMUST00000079838; ENSMUSP00000078766; ENSMUSG00000022475. [Q8C2B3-4]
Ensembl; ENSMUST00000088402; ENSMUSP00000085744; ENSMUSG00000022475. [Q8C2B3-1]
Ensembl; ENSMUST00000116408; ENSMUSP00000112109; ENSMUSG00000022475. [Q8C2B3-5]
Ensembl; ENSMUST00000116409; ENSMUSP00000112110; ENSMUSG00000022475. [Q8C2B3-3]
Ensembl; ENSMUST00000118294; ENSMUSP00000113380; ENSMUSG00000022475. [Q8C2B3-2]
GeneID; 56233; -.
KEGG; mmu:56233; -.
UCSC; uc007xle.2; mouse. [Q8C2B3-1]
UCSC; uc007xlf.2; mouse. [Q8C2B3-2]
UCSC; uc007xlg.2; mouse. [Q8C2B3-4]
UCSC; uc007xlh.2; mouse. [Q8C2B3-3]
CTD; 51564; -.
MGI; MGI:1891835; Hdac7.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOGENOM; HOG000232065; -.
HOVERGEN; HBG057100; -.
InParanoid; Q8C2B3; -.
KO; K11408; -.
OMA; AFRIVVM; -.
OrthoDB; EOG091G0EQO; -.
PhylomeDB; Q8C2B3; -.
TreeFam; TF106173; -.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
ChiTaRS; Hdac7; mouse.
PMAP-CutDB; Q8C2B3; -.
PRO; PR:Q8C2B3; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022475; -.
CleanEx; MM_HDAC7; -.
ExpressionAtlas; Q8C2B3; baseline and differential.
Genevisible; Q8C2B3; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
GO; GO:0007043; P:cell-cell junction assembly; IMP:MGI.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR037138; His_deacetylse_dom_sf.
InterPro; IPR017320; Histone_deAcase_II_euk.
InterPro; IPR023696; Ureohydrolase_dom_sf.
PANTHER; PTHR10625; PTHR10625; 4.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037911; HDAC_II_euk; 1.
PRINTS; PR01270; HDASUPER.
SUPFAM; SSF52768; SSF52768; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Complete proteome;
Cytoplasm; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc.
CHAIN 1 938 Histone deacetylase 7.
/FTId=PRO_0000114706.
REGION 1 121 Interaction with MEF2C.
REGION 2 254 Transcription repression 1.
REGION 72 172 Interaction with MEF2A.
{ECO:0000269|PubMed:11585834}.
REGION 241 533 Transcription repression 2.
REGION 505 852 Histone deacetylase.
REGION 864 938 Interaction with SIN3A.
MOTIF 904 938 Nuclear export signal. {ECO:0000250}.
COMPBIAS 220 226 Poly-Ser.
ACT_SITE 657 657 {ECO:0000250}.
METAL 520 520 Zinc. {ECO:0000250}.
METAL 522 522 Zinc. {ECO:0000250}.
METAL 528 528 Zinc. {ECO:0000250}.
METAL 605 605 Zinc. {ECO:0000250}.
SITE 830 830 Contributes to catalysis. {ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WUI4}.
MOD_RES 178 178 Phosphoserine; by MARK2, MARK3 and
PKD/PRKD1. {ECO:0000305|PubMed:18509061}.
MOD_RES 204 204 Phosphoserine; by PKD/PRKD2.
{ECO:0000250|UniProtKB:Q8WUI4}.
MOD_RES 344 344 Phosphoserine; by PKD/PRKD1.
{ECO:0000269|PubMed:18509061}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WUI4}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WUI4}.
MOD_RES 479 479 Phosphoserine; by PKD/PRKD1.
{ECO:0000269|PubMed:18509061}.
MOD_RES 480 480 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WUI4}.
MOD_RES 582 582 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 22 Missing (in isoform 2, isoform 3 and
isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007432.
VAR_SEQ 138 161 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007433.
VAR_SEQ 249 249 E -> EALLGQRLRLQETSLAPFALPTVSLLPAITLGLPAP
AR (in isoform 2, isoform 3 and isoform
4). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_007434.
VAR_SEQ 376 382 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_007435.
MUTAGEN 178 178 S->A: Strong reduction of CaMK1-dependent
nuclear export. Reduces interaction with
YWHAE. {ECO:0000269|PubMed:11585834}.
MUTAGEN 344 344 S->A: Strong reduction of CaMK1-dependent
nuclear export. Reduces interaction with
YWHAE. {ECO:0000269|PubMed:11585834}.
MUTAGEN 479 479 S->A: Strong reduction of CaMK1-dependent
nuclear export. Reduces interaction with
YWHAE. {ECO:0000269|PubMed:11585834}.
MUTAGEN 657 657 H->A: Abolishes deacetylase activity, but
not the interaction with HDAC2 and HDAC3.
{ECO:0000269|PubMed:10984530,
ECO:0000269|PubMed:11279209}.
MUTAGEN 692 692 D->A: Disrupts the dot-like nuclear
pattern. {ECO:0000269|PubMed:10984530}.
MUTAGEN 694 694 D->A: Disrupts the dot-like nuclear
pattern. Abolishes deacetylase activity,
but not the interaction with HDAC2 and
HDAC3. {ECO:0000269|PubMed:10984530}.
MUTAGEN 717 717 H->A: Abolishes deacetylase activity, but
not the interaction with HDAC2 and HDAC3.
{ECO:0000269|PubMed:10984530}.
CONFLICT 169 169 E -> G (in Ref. 2; BAC27161).
{ECO:0000305}.
CONFLICT 183 183 K -> M (in Ref. 2; BAC29493).
{ECO:0000305}.
CONFLICT 228 228 P -> T (in Ref. 2; BAC27161).
{ECO:0000305}.
CONFLICT 487 487 L -> M (in Ref. 1; AAF31419 and 2;
BAC40598/BAC40666). {ECO:0000305}.
CONFLICT 645 645 K -> R (in Ref. 2; BAC29493).
{ECO:0000305}.
CONFLICT 661 661 S -> P (in Ref. 2; BAC40598).
{ECO:0000305}.
CONFLICT 737 737 G -> A (in Ref. 1; AAF31419).
{ECO:0000305}.
SEQUENCE 938 AA; 101287 MW; 8D4B455CE6F95483 CRC64;
MHSPGAGCPA LQPDTPGSQP QPMDLRVGQR PTVEPPPEPA LLTLQHPQRL HRHLFLAGLH
QQQRSAEPMR LSMDPPMPEL QGGQQEQELR QLLNKDKSKR SAVASSVVKQ KLAEVILKKQ
QAALERTVHP SSPSIPYRTL EPLDTEGAAR SVLSSFLPPV PSLPTEPPEH FPLRKTVSEP
NLKLRYKPKK SLERRKNPLL RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH
GPNPALGSEA DGDRRTHSTL GPRGPVLGNP HAPLFLHHGL EPEAGGTLPS RLQPILLLDP
SVSHAPLWTV PGLGPLPFHF AQPLLTTERL SGSGLHRPLN RTRSEPLPPS ATASPLLAPL
QPRQDRLKPH VQLIKPAISP PQRPAKPSEK PRLRQIPSAE DLETDGGGVG PMANDGLEHR
ESGRGPPEGR GSISLQQHQQ VPPWEQQHLA GRLSQGSPGD SVLIPLAQVG HRPLSRTQSS
PAAPVSLLSP EPTCQTQVLN SSETPATGLV YDSVMLKHQC SCGDNSKHPE HAGRIQSIWS
RLQERGLRSQ CECLRGRKAS LEELQSVHSE RHVLLYGTNP LSRLKLDNGK LTGLLAQRTF
VMLPCGGVGV DTDTIWNELH SSNAARWAAG SVTDLAFKVA SRELKNGFAV VRPPGHHADH
STAMGFCFFN SVAIACRQLQ QHGKASKILI VDWDVHHGNG TQQTFYQDPS VLYISLHRHD
DGNFFPGSGA VDEVGTGSGE GFNVNVAWAG GLDPPMGDPE YLAAFRIVVM PIAREFAPDL
VLVSAGFDAA EGHPAPLGGY HVSAKCFGYM TQQLMNLAGG AVVLALEGGH DLTAICDASE
ACVAALLGNK VDPLSEESWK QKPNLSAIRS LEAVVRVHRK YWGCMQRLAS CPDSWLPRVP
GADAEVEAVT ALASLSVGIL AEDRPSERLV EEEEPMNL


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