GenomeNet

Database: UniProt
Entry: Q8VZJ1
LinkDB: Q8VZJ1
Original site: Q8VZJ1 
ID   ATXR5_ARATH             Reviewed;         379 AA.
AC   Q8VZJ1; F4KFB9; Q1AJM5; Q9FXW6; Q9LXE2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   13-FEB-2019, entry version 125.
DE   RecName: Full=Histone-lysine N-methyltransferase ATXR5;
DE            EC=2.1.1.43;
DE   AltName: Full=Protein SET DOMAIN GROUP 15;
DE   AltName: Full=Trithorax-related protein 5;
DE            Short=TRX-related protein 5;
DE   Flags: Precursor;
GN   Name=ATXR5; Synonyms=SDG15, SET15; OrderedLocusNames=At5g09790;
GN   ORFNames=17I14.20, MTH16.26;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING,
RP   INTERACTION WITH PCNA1 AND PCNA2, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16771839; DOI=10.1111/j.1365-313X.2006.02799.x;
RA   Raynaud C., Sozzani R., Glab N., Domenichini S., Perennes C.,
RA   Cella R., Kondorosi E., Bergounioux C.;
RT   "Two cell-cycle regulated SET-domain proteins interact with
RT   proliferating cell nuclear antigen (PCNA) in Arabidopsis.";
RL   Plant J. 47:395-407(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX.
RT   Sequence features of the regions of 1,011,550 bp covered by seventeen
RT   P1 and TAC clones.";
RL   DNA Res. 6:183-195(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA   Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA   Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT   "The Arabidopsis thaliana genome contains at least 29 active genes
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19503079; DOI=10.1038/nsmb.1611;
RA   Jacob Y., Feng S., LeBlanc C.A., Bernatavichute Y.V., Stroud H.,
RA   Cokus S., Johnson L.M., Pellegrini M., Jacobsen S.E., Michaels S.D.;
RT   "ATXR5 and ATXR6 are H3K27 monomethyltransferases required for
RT   chromatin structure and gene silencing.";
RL   Nat. Struct. Mol. Biol. 16:763-768(2009).
RN   [8]
RP   INTERACTION WITH IPS1.
RX   PubMed=19812700; DOI=10.1371/journal.pone.0007364;
RA   Meng P.H., Raynaud C., Tcherkez G., Blanchet S., Massoud K.,
RA   Domenichini S., Henry Y., Soubigou-Taconnat L., Lelarge-Trouverie C.,
RA   Saindrenan P., Renou J.P., Bergounioux C.;
RT   "Crosstalks between myo-inositol metabolism, programmed cell death and
RT   basal immunity in Arabidopsis.";
RL   PLoS ONE 4:E7364-E7364(2009).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH HTR1.
RX   PubMed=20631708; DOI=10.1038/nature09290;
RA   Jacob Y., Stroud H., Leblanc C., Feng S., Zhuo L., Caro E., Hassel C.,
RA   Gutierrez C., Michaels S.D., Jacobsen S.E.;
RT   "Regulation of heterochromatic DNA replication by histone H3 lysine 27
RT   methyltransferases.";
RL   Nature 466:987-991(2010).
RN   [10]
RP   FUNCTION.
RX   PubMed=22549957; DOI=10.1101/gad.182865.111;
RA   Pontvianne F., Blevins T., Chandrasekhara C., Feng W., Stroud H.,
RA   Jacobsen S.E., Michaels S.D., Pikaard C.S.;
RT   "Histone methyltransferases regulating rRNA gene dose and dosage
RT   control in Arabidopsis.";
RL   Genes Dev. 26:945-957(2012).
RN   [11]
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=24626927; DOI=10.1126/science.1248357;
RA   Jacob Y., Bergamin E., Donoghue M.T., Mongeon V., LeBlanc C.,
RA   Voigt P., Underwood C.J., Brunzelle J.S., Michaels S.D., Reinberg D.,
RA   Couture J.F., Martienssen R.A.;
RT   "Selective methylation of histone H3 variant H3.1 regulates
RT   heterochromatin replication.";
RL   Science 343:1249-1253(2014).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher
CC       activity on nucleosomes containing H3.1 than H3.3. Involved in the
CC       formation of constitutive heterochromatin and the silencing of
CC       heterochromatic elements. Influences which sets of rRNA gene
CC       variants are expressed or silenced. {ECO:0000269|PubMed:19503079,
CC       ECO:0000269|PubMed:20631708, ECO:0000269|PubMed:22549957}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Isoform 1 but not isoform 2 interacts with PCNA1 and
CC       PCNA2. Interacts (via PHD domain) with HTR1 (via N-terminus).
CC       Isoform 2 interacts with IPS1. {ECO:0000269|PubMed:16771839,
CC       ECO:0000269|PubMed:19812700, ECO:0000269|PubMed:20631708}.
CC   -!- INTERACTION:
CC       Q9FEN9:SHL; NbExp=3; IntAct=EBI-15200822, EBI-4458733;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16771839}.
CC       Plastid, chloroplast {ECO:0000269|PubMed:16771839}. Note=Never
CC       found in plastids and the nucleus within the same cell.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VZJ1-2; Sequence=Displayed;
CC         Note=Major isoform.;
CC       Name=2;
CC         IsoId=Q8VZJ1-1; Sequence=VSP_054858;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers,
CC       siliques and developing pollen. Up-regulated in tissues where cell
CC       division is active. {ECO:0000269|PubMed:16771839}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Atxr5 and atxr6 double
CC       mutant is smaller than wild-type plants, shows partial
CC       decondensation of the chromocenter, decreased H3K27
CC       monomethylation and increased DNA re-replication.
CC       {ECO:0000269|PubMed:19503079}.
CC   -!- MISCELLANEOUS: The binding to histone H3.2 is unaffected by mono-,
CC       di, or trimethylation at H3K9, but is strongly reduced by
CC       increasing levels of H3K4 methylation.
CC       {ECO:0000305|PubMed:20631708}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09537.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; DQ074689; AAZ31374.1; -; mRNA.
DR   EMBL; AB020752; BAB09537.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL353994; CAB89351.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91447.1; -; Genomic_DNA.
DR   EMBL; AY064131; AAL36039.1; -; mRNA.
DR   EMBL; AY120701; AAM52244.1; -; mRNA.
DR   PIR; T49919; T49919.
DR   RefSeq; NP_001078559.1; NM_001085090.2. [Q8VZJ1-2]
DR   RefSeq; NP_001318519.1; NM_001343068.1.
DR   UniGene; At.27076; -.
DR   ProteinModelPortal; Q8VZJ1; -.
DR   SMR; Q8VZJ1; -.
DR   BioGrid; 16117; 11.
DR   DIP; DIP-48529N; -.
DR   IntAct; Q8VZJ1; 11.
DR   STRING; 3702.AT5G09790.2; -.
DR   PaxDb; Q8VZJ1; -.
DR   PRIDE; Q8VZJ1; -.
DR   EnsemblPlants; AT5G09790.2; AT5G09790.2; AT5G09790. [Q8VZJ1-2]
DR   GeneID; 830839; -.
DR   Gramene; AT5G09790.2; AT5G09790.2; AT5G09790. [Q8VZJ1-2]
DR   KEGG; ath:AT5G09790; -.
DR   Araport; AT5G09790; -.
DR   TAIR; locus:2144841; AT5G09790.
DR   eggNOG; KOG1083; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000238747; -.
DR   InParanoid; Q8VZJ1; -.
DR   OMA; DELTYMP; -.
DR   OrthoDB; 1014608at2759; -.
DR   PRO; PR:Q8VZJ1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8VZJ1; baseline and differential.
DR   Genevisible; Q8VZJ1; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009294; P:DNA mediated transformation; IMP:TAIR.
DR   GO; GO:0070734; P:histone H3-K27 methylation; IDA:TAIR.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0051726; P:regulation of cell cycle; IEP:TAIR.
DR   GO; GO:0006275; P:regulation of DNA replication; IGI:TAIR.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Chromatin regulator;
KW   Complete proteome; Metal-binding; Methyltransferase; Nucleus; Plastid;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Transit peptide; Zinc; Zinc-finger.
FT   TRANSIT       1     44       Chloroplast. {ECO:0000255}.
FT   CHAIN        45    379       Histone-lysine N-methyltransferase ATXR5.
FT                                /FTId=PRO_0000429173.
FT   DOMAIN      245    367       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      64    114       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   REGION      255    257       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      317    321       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      369    370       substrate binding. {ECO:0000250}.
FT   MOTIF       122    129       PIP motif.
FT   COMPBIAS     52     59       Poly-Glu.
FT   BINDING     221    221       Substrate. {ECO:0000250}.
FT   BINDING     339    339       Substrate. {ECO:0000250}.
FT   BINDING     366    366       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     373    373       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   VAR_SEQ     120    146       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14593172}.
FT                                /FTId=VSP_054858.
FT   CONFLICT    347    347       R -> P (in Ref. 1; AAZ31374).
FT                                {ECO:0000305}.
SQ   SEQUENCE   379 AA;  43034 MW;  F5A792C7E491BB48 CRC64;
     MATWNASSPA ASPCSSRRRT KAPARRPSSE SPPPRKMKSM AEIMAKSVPV VEQEEEEDED
     SYSNVTCEKC GSGEGDDELL LCDKCDRGFH MKCLRPIVVR VPIGTWLCVD CSDQRPVRRL
     SQKKILHFFR IEKHTHQTDK LELSQEETRK RRRSCSLTVK KRRRKLLPLV PSEDPDQRLA
     QMGTLASALT ALGIKYSDGL NYVPGMAPRS ANQSKLEKGG MQVLCKEDLE TLEQCQSMYR
     RGECPPLVVV FDPLEGYTVE ADGPIKDLTF IAEYTGDVDY LKNREKDDCD SIMTLLLSED
     PSKTLVICPD KFGNISRFIN GINNHNPVAK KKQNCKCVRY SINGECRVLL VATRDISKGE
     RLYYDYNGYE HEYPTHHFL
//
DBGET integrated database retrieval system