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Database: UniProt/SWISS-PROT
Entry: ASHH3_ARATH
LinkDB: ASHH3_ARATH
Original site: ASHH3_ARATH 
ID   ASHH3_ARATH             Reviewed;         363 AA.
AC   Q945S8; O80584; Q94AQ1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   23-MAY-2018, entry version 97.
DE   RecName: Full=Histone-lysine N-methyltransferase ASHH3;
DE            EC=2.1.1.43;
DE   AltName: Full=ASH1 homolog 3;
DE   AltName: Full=Protein SET DOMAIN GROUP 7;
GN   Name=ASHH3; Synonyms=SDG7, SET7; OrderedLocusNames=At2g44150;
GN   ORFNames=F6E13.28;
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 [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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference 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.,
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-135, 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
RT   encoding SET domain proteins that can be assigned to four
RT   evolutionarily conserved classes.";
RL   Nucleic Acids Res. 29:4319-4333(2001).
CC   -!- FUNCTION: Histone methyltransferase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00911}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00911}.
DR   EMBL; AC004005; AAC23419.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10383.1; -; Genomic_DNA.
DR   EMBL; AY045886; AAK76560.1; -; mRNA.
DR   EMBL; AY091447; AAM14386.1; -; mRNA.
DR   EMBL; AF408060; AAL01111.1; -; mRNA.
DR   PIR; T00695; T00695.
DR   RefSeq; NP_566010.1; NM_129978.4.
DR   UniGene; At.25522; -.
DR   ProteinModelPortal; Q945S8; -.
DR   SMR; Q945S8; -.
DR   IntAct; Q945S8; 10.
DR   STRING; 3702.AT2G44150.1; -.
DR   PaxDb; Q945S8; -.
DR   EnsemblPlants; AT2G44150.1; AT2G44150.1; AT2G44150.
DR   GeneID; 819021; -.
DR   Gramene; AT2G44150.1; AT2G44150.1; AT2G44150.
DR   KEGG; ath:AT2G44150; -.
DR   Araport; AT2G44150; -.
DR   TAIR; locus:2051769; AT2G44150.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000034098; -.
DR   InParanoid; Q945S8; -.
DR   KO; K11423; -.
DR   OMA; SSTCKCE; -.
DR   OrthoDB; EOG09360H9D; -.
DR   PhylomeDB; Q945S8; -.
DR   PRO; PR:Q945S8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q945S8; baseline and differential.
DR   Genevisible; Q945S8; AT.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:TAIR.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR025787; Hist-Lys_N-MeTrfase_SET2_plant.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51578; SAM_MT43_SET2_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Centromere; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    363       Histone-lysine N-methyltransferase ASHH3.
FT                                /FTId=PRO_0000233372.
FT   DOMAIN       63    114       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      116    233       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      239    255       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   CONFLICT     55     55       K -> E (in Ref. 4; AAL01111).
FT                                {ECO:0000305}.
SQ   SEQUENCE   363 AA;  41286 MW;  BA4CB48ACF54DFBF CRC64;
     MPASKKISDR NHLGQVFDKL LNQIGESEEF ELPEWLNKGK PTPYIFIRRN IYLTKKVKRR
     VEDDGIFCSC SSSSPGSSST VCGSNCHCGM LFSSCSSSCK CGSECNNKPF QQRHVKKMKL
     IQTEKCGSGI VAEEEIEAGE FIIEYVGEVI DDKTCEERLW KMKHRGETNF YLCEITRDMV
     IDATHKGNKS RYINHSCNPN TQMQKWIIDG ETRIGIFATR GIKKGEHLTY DYQFVQFGAD
     QDCHCGAVGC RRKLGVKPSK PKIASDEAFN LVAHELAQTL PKVHQNGLVN RHIDAGKSWN
     NLSQRDTCSR NCIGVVIRLS RPTSDRCFGL VRHFDEYSRK HSVMFEDGVT EFVDMSREDW
     EIV
//
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