ID ASHH2_ARATH Reviewed; 1759 AA. AC Q2LAE1; O80663; Q56WW4; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 1. DT 16-JUN-2009, entry version 33. DE RecName: Full=Histone-lysine N-methyltransferase ASHH2; DE EC=2.1.1.43; DE AltName: Full=H3-K4-HMTase; DE AltName: Full=Histone H3-K36 methyltransferase 8; DE AltName: Full=H3-K36-HMTase; DE AltName: Full=ASH1 homolog 2; DE AltName: Full=Protein EARLY FLOWERING IN SHORT DAYS; DE AltName: Full=Protein SET DOMAIN GROUP 8; GN Name=ASHH2; Synonyms=EFS, SDG8, SET8; OrderedLocusNames=At1g77300; GN ORFNames=T14N5.15; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=16299497; DOI=10.1038/ncb1329; RA Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H.; RT "Prevention of early flowering by expression of FLOWERING LOCUS C RT requires methylation of histone H3 K36."; RL Nat. Cell Biol. 7:1256-1260(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1299-1759 (ISOFORM 2). RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., RA Hayashizaki Y., Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NOMENCLATURE. RX MEDLINE=21550130; 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 [5] RP FUNCTION. RX MEDLINE=99449572; PubMed=10518493; RA Soppe W.J.J., Bentsink L., Koornneef M.; RT "The early-flowering mutant efs is involved in the autonomous RT promotion pathway of Arabidopsis thaliana."; RL Development 126:4763-4770(1999). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16258034; DOI=10.1105/tpc.105.034645; RA Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R.; RT "Establishment of the vernalization-responsive, winter-annual habit in RT Arabidopsis requires a putative histone H3 methyl transferase."; RL Plant Cell 17:3301-3310(2005). CC -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' and 'Lys- CC 36' of histone H3. H3 'Lys-4' and 'Lys-36' methylations represent CC specific tags for epigenetic transcriptional activation. Regulates CC positively FLC transcription to prevent early flowering CC transition. Required for flowering transition in response to CC vernalization. Seems also to modulate several traits including CC floral organ size, root size and dormancy. Promotes apical CC dominance. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine = CC S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). Centromere (Probable). CC Note=Associates with centromeric constitutive heterochromatin CC (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q2LAE1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q2LAE1-2; Sequence=VSP_018133; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in young CC tissues, including shoot and root apex. CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase CC family. SET2 subfamily. CC -!- SIMILARITY: Contains 1 AWS domain. CC -!- SIMILARITY: Contains 1 CW-type zinc finger. CC -!- SIMILARITY: Contains 1 post-SET domain. CC -!- SIMILARITY: Contains 1 SET domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAC34358.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ340869; ABC69038.1; -; mRNA. DR EMBL; AC004260; AAC34358.1; ALT_SEQ; Genomic_DNA. DR EMBL; AK221916; BAD94318.1; ALT_INIT; mRNA. DR IPI; IPI00542920; -. DR IPI; IPI00759360; -. DR PIR; T00458; T00458. DR HSSP; Q8X225; 1PEG. DR PRIDE; Q2LAE1; -. DR GenomeReviews; CT485782_GR; AT1G77300. DR TAIR; At1g77300; -. DR BRENDA; 2.1.1.43; 302. DR GermOnline; AT1G77300; Arabidopsis thaliana. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 s...; IDA:TAIR. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0016116; P:carotenoid metabolic process; IMP:TAIR. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR. DR GO; GO:0031062; P:positive regulation of histone methylation; IDA:TAIR. DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR. DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR. DR InterPro; IPR006560; AWS. DR InterPro; IPR003616; Post-SET_Zn_bd. DR InterPro; IPR001214; SET. DR InterPro; IPR011124; Znf_CW. DR Pfam; PF00856; SET; 1. DR Pfam; PF07496; zf-CW; 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; PS50280; SET; 1. DR PROSITE; PS51050; ZF_CW; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Centromere; Chromatin regulator; KW Complete proteome; Metal-binding; Methyltransferase; Nucleus; KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger. FT CHAIN 1 1759 Histone-lysine N-methyltransferase ASHH2. FT /FTId=PRO_0000233371. FT DOMAIN 974 1024 AWS. FT DOMAIN 1025 1147 SET. FT DOMAIN 1151 1167 Post-SET. FT ZN_FING 859 912 CW-type. FT VAR_SEQ 1447 1447 G -> GLQMLHNIMKQYRGDFKRIPIIRKLLKVLEYLATRK FT ILALEHIIRRP (in isoform 2). FT /FTId=VSP_018133. FT CONFLICT 1426 1426 I -> T (in Ref. 3; BAD94318). SQ SEQUENCE 1759 AA; 193228 MW; 5616BE25ECEF2155 CRC64; MDCKENGVGD ASGCNIDANS LASNLAMNTN EDFYEKLSSR GQNLDSVSSL EIPQTASSVN HTIEGQRKCF TEIEQMGYGN SNSQEDAGNT DDDLYVCYNA DDTQEQGVVS GELEQSQELI CDTDLLVNCN KLDDGKESQD TNVSLVSIFS GSMQEKEAPQ AKEDEGYGGT TLPIGGSGID TESTFVNDAP EQFESLETTK HIKPDEVESD GISYRFDDGG KEGRNGPSSD LDTGSSDDIS LSQSFSFPDS LLDSSVFGCS ATESYLEDAI DIEGNGTIVV SPSLAITEML NNDDGGLCSH DLNKITVTET INPDLKLVRE DRLDTDLSVM NEKMLKNHVG DSSSESAVAA LSMNNGMAAD LRAENFSQSS PIDEKTLDME ANSPITDSSL IWNFPLNFGS GGIEVCNPEN AVEPLRIVDD NGRIGGEVAS ASGSDFCEAG MSSSRRKARD GKQCKVVQTK TSARHLRKSS RKKQSERDIE SIFKCSKQKR SSLLKTSRSS EWGLPSKTTE IFLQSNNIPY DGPPHHEPQR SQGNLNNGEH NRSSHNGNVE GSNRNIQASS GSCLRLKVKF GKSGGQNPLN ITVSKVSGNS LPGNGIVKAG TCLELPGSAH FGEDKMQTVE TKEDLVEKSN PVEKVSYLQS SDSMRDKKYN QDAGGLCRKV GGDVLDDDPH LSSIRMVEEC ERATGTQSLD AETSPDSEVI NSVPDSIVNI EHKEGLHHGF FSTPEDVVKK NRVLEKEDEL RASKSPSENG SHLIPNAKKA KHPKSKSNGT KKGKSKFSES AKDGRKNESH EGVEQRKSLN TSMGRDDSDY PEVGRIESHK TTGALLDADI GKTSATYGTI SSDVTHGEMV VDVTIEDSYS TESAWVRCDD CFKWRRIPAS VVGSIDESSR WICMNNSDKR FADCSKSQEM SNEEINEELG IGQDEADAYD CDAAKRGKEK EQKSKRLTGK QKACFKAIKT NQFLHRNRKS QTIDEIMVCH CKPSPDGRLG CGEECLNRML NIECLQGTCP AGDLCSNQQF QKRKYVKFER FQSGKKGYGL RLLEDVREGQ FLIEYVGEVL DMQSYETRQK EYAFKGQKHF YFMTLNGNEV IDAGAKGNLG RFINHSCEPN CRTEKWMVNG EICVGIFSMQ DLKKGQELTF DYNYVRVFGA AAKKCYCGSS HCRGYIGGDP LNGDVIIQSD SDEEYPELVI LDDDESGEGI LGATSRTFTD DADEQMPQSF EKVNGYKDLA PDNTQTQSSV SVKLPEREIP PPLLQPTEVL KELSSGISIT AVQQEVPAEK KTKSTSPTSS SLSRMSPGGT NSDKTTKHGS GEDKKILPRP RPRMKTSRSS ESSKRDKGGI YPGVNKAQVI PVNKLQQQPI KSKGSEKVSP SIETFEGKLN ELLDAVGGIS KRRDSAKGYL KLLLLTAASR GTDEEGIYSN RDLSMILDAL LKTKSKSVLV DIINKNGPFA GMESFKDSVL SFTEHDDYTV HNIARSFRDR WIPKHFRKPW RINREERSES MRSPINRRFR ASQEPRYDHQ SPRPAEPAAS VTSSKAATPE TASVSEGYSE PNSGLPETNG RKRKSRWDQP SKTKEQRIMT ILSQQTDETN GNQDVQDDLP PGFSSPCTDV PDAITAQPQQ KFLSRLPVSY GIPLSIVHQF GSPGKEDPTT WSVAPGMPFY PFPPLPPVSH GEFFAKRNVR ACSSSMGNLT YSNEILPATP VTDSTAPTRK RELFSSDIGT TYFRQQKQSV PPWLRNNGGE KTANSPIPGN LTLEKKLNS //