ASHH1_ARATH
ID ASHH1_ARATH Reviewed; 492 AA.
AC Q84WW6; C0SV35; Q945S9; Q9SRE2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histone-lysine N-methyltransferase ASHH1 {ECO:0000305};
DE EC=2.1.1.354 {ECO:0000305};
DE AltName: Full=ASH1 homolog 1;
DE AltName: Full=Protein SET DOMAIN GROUP 26;
GN Name=ASHH1; Synonyms=SDG26, SET26; OrderedLocusNames=At1g76710;
GN ORFNames=F28O16.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-311, AND 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 encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25409787; DOI=10.1111/tpj.12729;
RA Berr A., Shafiq S., Pinon V., Dong A., Shen W.;
RT "The trxG family histone methyltransferase SET DOMAIN GROUP 26 promotes
RT flowering via a distinctive genetic pathway.";
RL Plant J. 81:316-328(2015).
CC -!- FUNCTION: Histone methyltransferase involved in regulation of flowering
CC time. Required for the expression of the SOC1/AGL20 gene. Required for
CC histone H3 trimethylation on 'Lys-4' (H3K4me3) at the SOC1 locus.
CC Prevents trimethylation on 'Lys-27' (H3K27me3) at the same locus.
CC {ECO:0000269|PubMed:25409787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Note=Associates with centromeric constitutive
CC heterochromatin. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Late flowering. {ECO:0000269|PubMed:25409787}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF04434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010718; AAF04434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35879.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35880.1; -; Genomic_DNA.
DR EMBL; BT001913; AAN71912.1; -; mRNA.
DR EMBL; AB493538; BAH30376.1; -; mRNA.
DR EMBL; AF408059; AAL01110.1; -; mRNA.
DR PIR; E96795; E96795.
DR RefSeq; NP_177797.2; NM_106321.4.
DR RefSeq; NP_974158.1; NM_202429.2.
DR AlphaFoldDB; Q84WW6; -.
DR SMR; Q84WW6; -.
DR BioGRID; 29224; 7.
DR IntAct; Q84WW6; 4.
DR STRING; 3702.AT1G76710.2; -.
DR iPTMnet; Q84WW6; -.
DR PaxDb; Q84WW6; -.
DR PRIDE; Q84WW6; -.
DR ProteomicsDB; 246680; -.
DR EnsemblPlants; AT1G76710.1; AT1G76710.1; AT1G76710.
DR EnsemblPlants; AT1G76710.2; AT1G76710.2; AT1G76710.
DR GeneID; 844005; -.
DR Gramene; AT1G76710.1; AT1G76710.1; AT1G76710.
DR Gramene; AT1G76710.2; AT1G76710.2; AT1G76710.
DR KEGG; ath:AT1G76710; -.
DR Araport; AT1G76710; -.
DR TAIR; locus:2030131; AT1G76710.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_026268_0_0_1; -.
DR InParanoid; Q84WW6; -.
DR PhylomeDB; Q84WW6; -.
DR PRO; PR:Q84WW6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84WW6; baseline and differential.
DR Genevisible; Q84WW6; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0010224; P:response to UV-B; IEP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromatin regulator; Chromosome; Flowering; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..492
FT /note="Histone-lysine N-methyltransferase ASHH1"
FT /id="PRO_0000233370"
FT DOMAIN 36..87
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 84..206
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 213..229
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 259..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55285 MW; 87795D3EAAB01C5D CRC64;
MQFSCDPDQE GDELPQYEHI YQNDFSYRKH KKQKEEDISI CECKFDFGDP DSACGERCLN
VITNTECTPG YCPCGVYCKN QKFQKCEYAK TKLIKCEGRG WGLVALEEIK AGQFIMEYCG
EVISWKEAKK RAQTYETHGV KDAYIISLNA SEAIDATKKG SLARFINHSC RPNCETRKWN
VLGEVRVGIF AKESISPRTE LAYDYNFEWY GGAKVRCLCG AVACSGFLGA KSRGFQEDTY
VWEDGDDRYS VDKIPVYDSA EDELTSEPSK NGESNTNEEK EKDISTENHL ESTALNIQQQ
SDSTPTPMEE DVVTETVKTE TSEDMKLLSQ NSQEDSSPKT AIVSRVHGNI SKIKSESLPK
KRGRPFSGGK TKNVAQKHVD IANVVQLLAT KEAQDEVLKY EEVKKEAAVR LSSLYDEIRP
AIEEHERDSQ DSVATSVAEK WIQASCNKLK AEFDLYSSVI KNIASTPIKP QDTKTKVAEA
GNEDHIKLLE AK
