ID ASHR2_ARATH Reviewed; 398 AA.
AC Q9ZUM9; Q84WB9; Q94CD2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 24-JAN-2024, entry version 134.
DE RecName: Full=Histone-lysine N-methyltransferase ASHR2;
DE EC=2.1.1.-;
DE AltName: Full=ASH1-related protein 2;
DE AltName: Full=Protein SET DOMAIN GROUP 39;
GN Name=ASHR2; Synonyms=SDG39, SET39; OrderedLocusNames=At2g19640;
GN ORFNames=F3P11.24;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORMS 1 AND 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., 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 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).
CC -!- FUNCTION: Histone methyltransferase. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC 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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZUM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZUM9-2; Sequence=VSP_018134, VSP_018135;
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}.
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DR EMBL; AC005917; AAD10162.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06906.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06907.1; -; Genomic_DNA.
DR EMBL; AY034953; AAK59459.1; -; mRNA.
DR EMBL; AY070027; AAL47498.1; -; mRNA.
DR EMBL; BT004010; AAO42047.1; -; mRNA.
DR PIR; C84579; C84579.
DR RefSeq; NP_565457.1; NM_127522.2. [Q9ZUM9-2]
DR RefSeq; NP_849991.1; NM_179660.2. [Q9ZUM9-1]
DR AlphaFoldDB; Q9ZUM9; -.
DR SMR; Q9ZUM9; -.
DR BioGRID; 1838; 1.
DR STRING; 3702.Q9ZUM9; -.
DR PaxDb; 3702-AT2G19640-2; -.
DR ProteomicsDB; 246788; -. [Q9ZUM9-1]
DR EnsemblPlants; AT2G19640.1; AT2G19640.1; AT2G19640. [Q9ZUM9-2]
DR EnsemblPlants; AT2G19640.2; AT2G19640.2; AT2G19640. [Q9ZUM9-1]
DR GeneID; 816483; -.
DR Gramene; AT2G19640.1; AT2G19640.1; AT2G19640. [Q9ZUM9-2]
DR Gramene; AT2G19640.2; AT2G19640.2; AT2G19640. [Q9ZUM9-1]
DR KEGG; ath:AT2G19640; -.
DR Araport; AT2G19640; -.
DR TAIR; AT2G19640; ASHR2.
DR eggNOG; KOG2084; Eukaryota.
DR HOGENOM; CLU_064842_0_0_1; -.
DR InParanoid; Q9ZUM9; -.
DR OMA; VIRMIHD; -.
DR OrthoDB; 166337at2759; -.
DR PhylomeDB; Q9ZUM9; -.
DR PRO; PR:Q9ZUM9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUM9; baseline and differential.
DR Genevisible; Q9ZUM9; AT.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd20071; SET_SMYD; 1.
DR Gene3D; 1.10.220.160; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR044238; ASHR2-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR47420; HISTONE-LYSINE N-METHYLTRANSFERASE ASHR2; 1.
DR PANTHER; PTHR47420:SF3; HISTONE-LYSINE N-METHYLTRANSFERASE ASHR2; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Chromosome; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..398
FT /note="Histone-lysine N-methyltransferase ASHR2"
FT /id="PRO_0000233375"
FT DOMAIN 11..270
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT VAR_SEQ 330..341
FT /note="GENEEEVCGNGV -> DICVRRRIVLAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_018134"
FT VAR_SEQ 342..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_018135"
SQ SEQUENCE 398 AA; 43761 MW; 32CFC10C8B546F64 CRC64;
MINDGGAKPE TLLRVAEIGG RGRSLVAAQS LRAGQVILRE SPLLLYSAFP FLSSSVSPYC
DHCFRLLASS AHQKCQSCSL VSFCSPNCFA SHTPWLCESL RRLHQSSSSA FSDQPSDRQV
QARFLLSAYN LAAASPSDFQ ILLSLQGSGS SNGDPSCSAG DSAAAGFLHS LLSSVCPSLP
VSISPDLTAA LLSKDKVNAF GLMEPCSVSN EKRSVRAYGI YPKTSFFNHD CLPNACRFDY
VDSASDGNTD IIIRMIHDVP EGREVCLSYF PVNMNYSSRQ KRLLEDYGFK CDCDRCKVEF
SWSEGEEDEN EIMEEMEDQD EQEEMEDSVG ENEEEVCGNG VDDESNFPHA YFFVRYMCEK
ENCFGTLAPL PPKTHDASRV LECNVCGSVK EDEVGVNQ
//
