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Histone-lysine N-methyltransferase ATXR6 (EC 2.1.1.43) (Protein SET DOMAIN GROUP 34) (Trithorax-related protein 6) (TRX-related protein 6)

 ATXR6_ARATH             Reviewed;         349 AA.
Q9FNE9;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 118.
RecName: Full=Histone-lysine N-methyltransferase ATXR6;
EC=2.1.1.43;
AltName: Full=Protein SET DOMAIN GROUP 34;
AltName: Full=Trithorax-related protein 6;
Short=TRX-related protein 6;
Name=ATXR6; Synonyms=SDG34, SET34; OrderedLocusNames=At5g24330;
ORFNames=MOP9.18;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9405937; DOI=10.1093/dnares/4.4.291;
Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. II.
Sequence features of the regions of 1,044,062 bp covered by thirteen
physically assigned P1 clones.";
DNA Res. 4:291-300(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10048488; DOI=10.1093/dnares/5.6.379;
Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VIII.
Sequence features of the regions of 1,081,958 bp covered by seventeen
physically assigned P1 and TAC clones.";
DNA Res. 5:379-391(1998).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NOMENCLATURE.
PubMed=11691919; DOI=10.1093/nar/29.21.4319;
Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
"The Arabidopsis thaliana genome contains at least 29 active genes
encoding SET domain proteins that can be assigned to four
evolutionarily conserved classes.";
Nucleic Acids Res. 29:4319-4333(2001).
[6]
FUNCTION, INTERACTION WITH PCNA1 AND PCNA2, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=16771839; DOI=10.1111/j.1365-313X.2006.02799.x;
Raynaud C., Sozzani R., Glab N., Domenichini S., Perennes C.,
Cella R., Kondorosi E., Bergounioux C.;
"Two cell-cycle regulated SET-domain proteins interact with
proliferating cell nuclear antigen (PCNA) in Arabidopsis.";
Plant J. 47:395-407(2006).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19503079; DOI=10.1038/nsmb.1611;
Jacob Y., Feng S., LeBlanc C.A., Bernatavichute Y.V., Stroud H.,
Cokus S., Johnson L.M., Pellegrini M., Jacobsen S.E., Michaels S.D.;
"ATXR5 and ATXR6 are H3K27 monomethyltransferases required for
chromatin structure and gene silencing.";
Nat. Struct. Mol. Biol. 16:763-768(2009).
[8]
INTERACTION WITH IPS1.
PubMed=19812700; DOI=10.1371/journal.pone.0007364;
Meng P.H., Raynaud C., Tcherkez G., Blanchet S., Massoud K.,
Domenichini S., Henry Y., Soubigou-Taconnat L., Lelarge-Trouverie C.,
Saindrenan P., Renou J.P., Bergounioux C.;
"Crosstalks between myo-inositol metabolism, programmed cell death and
basal immunity in Arabidopsis.";
PLoS ONE 4:E7364-E7364(2009).
[9]
FUNCTION, INTERACTION WITH HTR1, AND MUTAGENESIS OF LEU-49; GLN-92;
ILE-95; PHE-98; PHE-99 AND TYR-243.
PubMed=20631708; DOI=10.1038/nature09290;
Jacob Y., Stroud H., Leblanc C., Feng S., Zhuo L., Caro E., Hassel C.,
Gutierrez C., Michaels S.D., Jacobsen S.E.;
"Regulation of heterochromatic DNA replication by histone H3 lysine 27
methyltransferases.";
Nature 466:987-991(2010).
[10]
FUNCTION.
PubMed=22549957; DOI=10.1101/gad.182865.111;
Pontvianne F., Blevins T., Chandrasekhara C., Feng W., Stroud H.,
Jacobsen S.E., Michaels S.D., Pikaard C.S.;
"Histone methyltransferases regulating rRNA gene dose and dosage
control in Arabidopsis.";
Genes Dev. 26:945-957(2012).
[11]
INTERACTION WITH IPS1.
PubMed=23341037; DOI=10.1093/nar/gks1458;
Latrasse D., Jegu T., Meng P.H., Mazubert C., Hudik E., Delarue M.,
Charon C., Crespi M., Hirt H., Raynaud C., Bergounioux C.,
Benhamed M.;
"Dual function of MIPS1 as a metabolic enzyme and transcriptional
regulator.";
Nucleic Acids Res. 41:2907-2917(2013).
[12]
SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF GLU-186; MET-190; ARG-309
AND TYR-339.
PubMed=24626927; DOI=10.1126/science.1248357;
Jacob Y., Bergamin E., Donoghue M.T., Mongeon V., LeBlanc C.,
Voigt P., Underwood C.J., Brunzelle J.S., Michaels S.D., Reinberg D.,
Couture J.F., Martienssen R.A.;
"Selective methylation of histone H3 variant H3.1 regulates
heterochromatin replication.";
Science 343:1249-1253(2014).
-!- FUNCTION: Histone methyltransferase that specifically
monomethylates 'Lys-37' of histone H3 (H3K27me1). Has higher
activity on nucleosomes containing H3.1 than H3.3. Involved in the
formation of constitutive heterochromatin and the silencing of
heterochromatic elements. May act as a positive regulator of the
G1-S transition. Influences which sets of rRNA gene variants are
expressed or silenced. Up-regulated by E2FB.
{ECO:0000269|PubMed:16771839, ECO:0000269|PubMed:19503079,
ECO:0000269|PubMed:20631708, ECO:0000269|PubMed:22549957}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Interacts with PCNA1 and PCNA2. Interacts (via PHD
domain) with HTR1 (via N-terminus). Interacts with IPS1.
{ECO:0000269|PubMed:16771839, ECO:0000269|PubMed:19812700,
ECO:0000269|PubMed:20631708, ECO:0000269|PubMed:23341037}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16771839}.
-!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
siliques. Up-regulated in tissues where cell division is active.
{ECO:0000269|PubMed:16771839}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Atxr5 and atxr6 double
mutant is smaller than wild-type plants, shows partial
decondensation of the chromocenter, decreased H3K27
monomethylation and increased DNA re-replication.
{ECO:0000269|PubMed:19503079}.
-!- MISCELLANEOUS: The binding to histone H3.2 is unaffected by mono-,
di, or trimethylation at H3K9, but is strongly reduced by
increasing levels of H3K4 methylation.
{ECO:0000305|PubMed:20631708}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-----------------------------------------------------------------------
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EMBL; AB006701; BAB10399.1; -; Genomic_DNA.
EMBL; AB016884; BAB10399.1; JOINED; Genomic_DNA.
EMBL; CP002688; AED93294.1; -; Genomic_DNA.
EMBL; BT012223; AAS76710.1; -; mRNA.
EMBL; BT012421; AAS92337.1; -; mRNA.
RefSeq; NP_197821.1; NM_122341.3.
UniGene; At.30965; -.
ProteinModelPortal; Q9FNE9; -.
SMR; Q9FNE9; -.
BioGrid; 17778; 4.
DIP; DIP-48530N; -.
IntAct; Q9FNE9; 2.
STRING; 3702.AT5G24330.1; -.
PaxDb; Q9FNE9; -.
PRIDE; Q9FNE9; -.
EnsemblPlants; AT5G24330.1; AT5G24330.1; AT5G24330.
GeneID; 832503; -.
Gramene; AT5G24330.1; AT5G24330.1; AT5G24330.
KEGG; ath:AT5G24330; -.
Araport; AT5G24330; -.
TAIR; locus:2169779; AT5G24330.
eggNOG; ENOG410ITIY; Eukaryota.
eggNOG; ENOG410Y5CZ; LUCA.
HOGENOM; HOG000238747; -.
InParanoid; Q9FNE9; -.
OMA; AKKPKQF; -.
OrthoDB; EOG09360KQ7; -.
PhylomeDB; Q9FNE9; -.
PRO; PR:Q9FNE9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FNE9; baseline and differential.
Genevisible; Q9FNE9; AT.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009901; P:anther dehiscence; IMP:TAIR.
GO; GO:0070734; P:histone H3-K27 methylation; IDA:TAIR.
GO; GO:0051726; P:regulation of cell cycle; IEP:TAIR.
GO; GO:0006275; P:regulation of DNA replication; IGI:TAIR.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001214; SET_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00628; PHD; 1.
Pfam; PF00856; SET; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; Metal-binding;
Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
CHAIN 1 349 Histone-lysine N-methyltransferase ATXR6.
/FTId=PRO_0000233363.
DOMAIN 214 337 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
ZN_FING 32 82 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 224 226 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 287 291 S-adenosyl-L-methionine binding.
{ECO:0000250}.
REGION 339 340 substrate binding. {ECO:0000250}.
MOTIF 92 99 PIP motif.
BINDING 190 190 Substrate. {ECO:0000250}.
BINDING 309 309 Substrate. {ECO:0000250}.
BINDING 343 343 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
BINDING 349 349 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
MUTAGEN 49 49 L->W: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 92 92 Q->A: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 95 95 I->A: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 98 98 F->A: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 99 99 F->A: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 186 186 E->D: 24% methylation activity on histone
H3.1 and loss of methylation activity on
histone H3.3.
{ECO:0000269|PubMed:24626927}.
MUTAGEN 186 186 E->S,A: Loss of methylation activity.
{ECO:0000269|PubMed:24626927}.
MUTAGEN 190 190 M->A: 87% methylation activity on histone
H3.1 and 2% methylation activity on
histone H3.3.
{ECO:0000269|PubMed:24626927}.
MUTAGEN 243 243 Y->N: Loss of methylation activity.
{ECO:0000269|PubMed:20631708}.
MUTAGEN 309 309 R->A: 2% methylation activity on histone
H3.1 and 2% methylation activity on
histone H3.3.
{ECO:0000269|PubMed:24626927}.
MUTAGEN 309 309 R->Q: Loss of methylation activity.
{ECO:0000269|PubMed:24626927}.
MUTAGEN 339 339 Y->A: 98% methylation activity on histone
H3.1 and 22% methylation activity on
histone H3.3.
{ECO:0000269|PubMed:24626927}.
SEQUENCE 349 AA; 39640 MW; ED8D4FA7C92283BA CRC64;
MVAVRRRRTQ ASNPRSEPPQ HMSDHDSDSD WDTVCEECSS GKQPAKLLLC DKCDKGFHLF
CLRPILVSVP KGSWFCPSCS KHQIPKSFPL IQTKIIDFFR IKRSPDSSQI SSSSDSIGKK
RKKTSLVMSK KKRRLLPYNP SNDPQRRLEQ MASLATALRA SNTKFSNELT YVSGKAPRSA
NQAAFEKGGM QVLSKEGVET LALCKKMMDL GECPPLMVVF DPYEGFTVEA DRFIKDWTII
TEYVGDVDYL SNREDDYDGD SMMTLLHASD PSQCLVICPD RRSNIARFIS GINNHSPEGR
KKQNLKCVRF NINGEARVLL VANRDISKGE RLYYDYNGYE HEYPTEHFV


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