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Database: UniProt
Entry: Q949T8
LinkDB: Q949T8
Original site: Q949T8 
ID   ASHR3_ARATH             Reviewed;         497 AA.
AC   Q949T8; O65563;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JAN-2019, entry version 124.
DE   RecName: Full=Histone-lysine N-methyltransferase ASHR3;
DE            EC=2.1.1.43;
DE   AltName: Full=ASH1-related protein 3;
DE   AltName: Full=Protein SET DOMAIN GROUP 4;
DE   AltName: Full=Protein stamen loss;
GN   Name=ASHR3; Synonyms=SDG4, SET4, SML; OrderedLocusNames=At4g30860;
GN   ORFNames=F6I18.230;
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 [GENOMIC DNA].
RA   Cartagena J.A., Matsunaga S., Kurihara D., Fujimoto S., Azumi Y.,
RA   Uchiyama S., Fukui K.;
RT   "The chromosome-associated protein SML regulates lateral stamen
RT   development in Arabidopsis.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
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   [5]
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   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH AMS.
RX   PubMed=17978851; DOI=10.1007/s11103-007-9251-y;
RA   Thorstensen T., Grini P.E., Mercy I.S., Alm V., Erdal S., Aasland R.,
RA   Aalen R.B.;
RT   "The Arabidopsis SET-domain protein ASHR3 is involved in stamen
RT   development and interacts with the bHLH transcription factor ABORTED
RT   MICROSPORES (AMS).";
RL   Plant Mol. Biol. 66:47-59(2008).
CC   -!- FUNCTION: Histone methyltransferase (By similarity). Involved in
CC       stamen development. {ECO:0000250}.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00911};
CC   -!- SUBUNIT: Interacts with AMS/bHLH21 by its SET domain and PHD
CC       finger. {ECO:0000269|PubMed:17978851}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17978851}.
CC       Chromosome {ECO:0000305|PubMed:17978851}. Note=Associated to the
CC       euchromatin.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, flowers and buds, the
CC       anther and in stamen filaments. {ECO:0000269|PubMed:17978851}.
CC   -!- DEVELOPMENTAL STAGE: First observed at low levels in the
CC       vasculature and around hydathodes of developing leaves. In
CC       flowers, restricted to anthers tapetum at a post-meiosis stage, to
CC       filaments, and to microspores during their development. Disappears
CC       as pollen matures. In developing roots, expressed throughout the
CC       lower part, in the cap, in the epidermis and in non-epidermal
CC       tissue in the division and elongation zone. Also detected in cells
CC       lining lateral root formation.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79804.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AB195469; BAD72877.1; -; Genomic_DNA.
DR   EMBL; AL022198; CAA18207.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161577; CAB79804.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85821.1; -; Genomic_DNA.
DR   EMBL; AY050894; AAK92831.1; -; mRNA.
DR   EMBL; AY096675; AAM20309.1; -; mRNA.
DR   PIR; C85361; C85361.
DR   RefSeq; NP_567859.1; NM_119233.2.
DR   UniGene; At.26551; -.
DR   ProteinModelPortal; Q949T8; -.
DR   SMR; Q949T8; -.
DR   BioGrid; 14497; 4.
DR   IntAct; Q949T8; 3.
DR   STRING; 3702.AT4G30860.1; -.
DR   PaxDb; Q949T8; -.
DR   PRIDE; Q949T8; -.
DR   EnsemblPlants; AT4G30860.1; AT4G30860.1; AT4G30860.
DR   GeneID; 829210; -.
DR   Gramene; AT4G30860.1; AT4G30860.1; AT4G30860.
DR   KEGG; ath:AT4G30860; -.
DR   Araport; AT4G30860; -.
DR   TAIR; locus:2126714; AT4G30860.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000005950; -.
DR   InParanoid; Q949T8; -.
DR   OMA; HRPLAHK; -.
DR   OrthoDB; 507784at2759; -.
DR   PhylomeDB; Q949T8; -.
DR   PRO; PR:Q949T8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q949T8; baseline and differential.
DR   Genevisible; Q949T8; AT.
DR   GO; GO:0000785; C:chromatin; IDA:TAIR.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
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   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 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.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Chromosome; Complete proteome;
KW   Developmental protein; Metal-binding; Methyltransferase; Nucleus;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    497       Histone-lysine N-methyltransferase ASHR3.
FT                                /FTId=PRO_0000233376.
FT   DOMAIN      283    326       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      326    443       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      449    465       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     118    186       PHD-type.
FT   COMPBIAS    287    317       Cys-rich.
SQ   SEQUENCE   497 AA;  56122 MW;  10D9C7EC779C2108 CRC64;
     MLDLGNMSMS ASVALTCCPS FLPAASGPEL AKSINSPENL AGECNGKHLP MIPPEEEVKD
     IKIANGVTAF TRKQNPSDRV KKGFVLDDHV KDWVKRRVAS GVSESTCFLP FLVGAKKMVD
     CLVCHKPVYP GEDLSCSVRG CQGAYHSLCA KESLGFSKSS KFKCPQHECF VCKQRTQWRC
     VKCPMAAHDK HSPWSKEILH LKDQPGRAVC WRHPTDWRLD TKHAVAQSEI EEVFCQLPLP
     YVEEEFKIDL AWKDSVVKED PPSYVHIRRN IYLVKKKRDN ANDGVGCTNC GPNCDRSCVC
     RVQCISCSKG CSCPESCGNR PFRKEKKIKI VKTEHCGWGV EAAESINKED FIVEYIGEVI
     SDAQCEQRLW DMKHKGMKDF YMCEIQKDFT IDATFKGNAS RFLNHSCNPN CVLEKWQVEG
     ETRVGVFAAR QIEAGEPLTY DYRFVQFGPE VKCNCGSENC QGYLGTKRKE PNCLVVSWGA
     KRRRLFHRPI ARKPQQD
//
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