GenomeNet

Database: UniProt
Entry: Q9SUE7
LinkDB: Q9SUE7
Original site: Q9SUE7 
ID   ATX4_ARATH              Reviewed;        1027 AA.
AC   Q9SUE7; Q941H0;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   16-JAN-2019, entry version 130.
DE   RecName: Full=Histone-lysine N-methyltransferase ATX4;
DE            EC=2.1.1.43;
DE   AltName: Full=Protein SET DOMAIN GROUP 16;
DE   AltName: Full=Trithorax-homolog protein 4;
DE            Short=TRX-homolog protein 4;
DE            Short=Trithorax 4;
GN   Name=ATX4; Synonyms=SDG16, SET16, TX4; OrderedLocusNames=At4g27910;
GN   ORFNames=T13J8.20;
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=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   [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 [MRNA] OF 743-1027, 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:
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79593.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035524; CAB36760.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161572; CAB79593.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85408.1; -; Genomic_DNA.
DR   EMBL; AY049754; AAL12215.1; -; mRNA.
DR   PIR; T02892; T02892.
DR   RefSeq; NP_194520.3; NM_118929.5.
DR   UniGene; At.43382; -.
DR   ProteinModelPortal; Q9SUE7; -.
DR   SMR; Q9SUE7; -.
DR   STRING; 3702.AT4G27910.1; -.
DR   iPTMnet; Q9SUE7; -.
DR   PaxDb; Q9SUE7; -.
DR   PRIDE; Q9SUE7; -.
DR   EnsemblPlants; AT4G27910.1; AT4G27910.1; AT4G27910.
DR   GeneID; 828904; -.
DR   Gramene; AT4G27910.1; AT4G27910.1; AT4G27910.
DR   KEGG; ath:AT4G27910; -.
DR   Araport; AT4G27910; -.
DR   TAIR; locus:2132912; AT4G27910.
DR   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG5141; LUCA.
DR   HOGENOM; HOG000030707; -.
DR   InParanoid; Q9SUE7; -.
DR   OMA; NSYFCPY; -.
DR   OrthoDB; 112057at2759; -.
DR   PhylomeDB; Q9SUE7; -.
DR   Reactome; R-ATH-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q9SUE7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SUE7; baseline and differential.
DR   Genevisible; Q9SUE7; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IGI:TAIR.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR034732; EPHD.
DR   InterPro; IPR025780; Hist-Lys_N-MeTrfase_ATX.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 3.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 2.
DR   PROSITE; PS51805; EPHD; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS51566; SAM_MT43_TRX_MLL; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1027       Histone-lysine N-methyltransferase ATX4.
FT                                /FTId=PRO_0000233357.
FT   DOMAIN      207    276       PWWP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN      885   1002       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1011   1027       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   ZN_FING     646    680       C2HC pre-PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   ZN_FING     704    761       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01146}.
FT   REGION      962    963       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   COMPBIAS    135    140       Poly-Glu.
FT   METAL       965    965       Zinc. {ECO:0000250}.
FT   METAL      1015   1015       Zinc. {ECO:0000250}.
FT   METAL      1017   1017       Zinc. {ECO:0000250}.
FT   METAL      1022   1022       Zinc. {ECO:0000250}.
FT   BINDING     895    895       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     939    939       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    787    787       K -> E (in Ref. 3; AAL12215).
FT                                {ECO:0000305}.
FT   CONFLICT    851    853       AAI -> TAV (in Ref. 3; AAL12215).
FT                                {ECO:0000305}.
FT   CONFLICT    901    901       A -> G (in Ref. 3; AAL12215).
FT                                {ECO:0000305}.
FT   CONFLICT    947    947       V -> L (in Ref. 3; AAL12215).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1027 AA;  116739 MW;  925666F8ADEFC0B4 CRC64;
     MIIKRKFKTQ IPSLERCKLG NESRKKKRKL NLGGGGYYYP LNLLGEIAAG IVPGNGRNGF
     SASWCTEVTK PVEVEESLSK RRSDSGTVRD SPPAEVSRPP LVRTSRGRIQ VLPSRFNDSV
     LDNWRKDSKS DCDLEEEEIE CRNEKVVSFR VPKATNLKSK ELDRKSKYSA LCKEERFHEQ
     HNDEARARVD EKLPNKKGTF GPENFYSGDL VWAKSGRNEP FWPAIVIDPM TQAPELVLRS
     CIPDAACVVF FGHSGNENER DYAWVRRGMI FPFVDYVARF QEQPELQGCK PGNFQMALEE
     AFLADQGFTE KLMHDIHLAA GNSTFDDSFY RWIQETAVSN QELNNNAPRQ GLLKKHRNPL
     ACAGCETVIS FEMAKKMKDL IPGDQLLCKP CSRLTKSKHI CGICKKIRNH LDNKSWVRCD
     GCKVRIHAEC DQISDRHLKD LRETDYYCPT CRAKFNFDLS DSEKQNSKSK VAKGDGQMVL
     PDKVIVVCAG VEGVYFPRLH LVVCKCGSCG PKKKALSEWE RHTGSKSKNW KTSVKVKSSK
     LALEDWMMNL AELHANATAA KVPKRPSIKQ RKQRLLAFLS ETYEPVNAKW TTERCAVCRW
     VEDWDYNKII ICNRCQIAVH QECYGARHVR DFTSWVCKAC ERPDIKRECC LCPVKGGALK
     PTDVETLWVH VTCAWFQPEV CFASEEKMEP AVGILSIPST NFVKICVICK QIHGSCTQCC
     KCSTYYHAMC ASRAGYRMEL HCLEKNGQQI TKMVSYCAYH RAPNPDNVLI IQTPSGAFSA
     KSLVQNKKKG GSRLISLIRE DDEAPAENTI TCDPFSAARC RVFKRKINSK KRIEEEAIPH
     HTRGPRHHAS AAIQTLNTFR HVPEEPKSFS SFRERLHHLQ RTEMDRVCFG RSGIHGWGLF
     ARRNIQEGEM VLEYRGEQVR GSIADLREAR YRRVGKDCYL FKISEEVVVD ATDKGNIARL
     INHSCTPNCY ARIMSVGDEE SRIVLIAKAN VAVGEELTYD YLFDPDEAEE LKVPCLCKAP
     NCRKFMN
//
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