Q9M364 (ATX3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase ATX3
EC=2.1.1.43

Alternative name(s):
Protein SET DOMAIN GROUP 14
Trithorax-homolog protein 3
Short name=TRX-homolog protein 3

Gene names

Name:	ATX3
Synonyms:	SDG14, SET14
Ordered Locus Names:	At3g61740
ORF Names:	F15G16.130

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1018 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Histone methyltransferase By similarity.
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 2 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 PWWP domain. Contains 1 SET domain.
Sequence caution	The sequence CAB71104.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9M364-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1018	1018	Histone-lysine N-methyltransferase ATX3		PRO_0000233356
Regions
	Domain	189 – 258	70	PWWP
	Domain	874 – 997	124	SET
	Domain	1002 – 1018	17	Post-SET
	Zinc finger	362 – 418	57	PHD-type 1
	Zinc finger	546 – 597	52	PHD-type 2
	Region	952 – 953	2	S-adenosyl-L-methionine binding By similarity
Sites
	Metal binding	955	1	Zinc By similarity
	Metal binding	1006	1	Zinc By similarity
	Metal binding	1008	1	Zinc By similarity
	Metal binding	1013	1	Zinc By similarity
	Binding site	885	1	S-adenosyl-L-methionine By similarity
	Binding site	929	1	S-adenosyl-L-methionine By similarity
Experimental info
	Sequence conflict	87	1	P → S in BAE99361. Ref.3
	Sequence conflict	1000	1	E → G in BAE99361. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: DC6D1992C4AA66D2	FASTA	1,018	115,689
	10 20 30 40 50 60 MILKRTLTTF ENQNLKRCKI DSEIEYGRKK GEIIVYKKRQ RATVDQPCSK EPELLTSSSS 70 80 90 100 110 120 SLTSKEESQQ VCSDQSKSSR GRVRAVPSRF KDSIVGTWKS SRRKGESTES SHDDDDVSLG 130 140 150 160 170 180 KKVKGFSGSS KLHRSKDSKV FPRKDNGDSS EVDCDYWDVQ ISYDDANFGM PKKSDASRKG 190 200 210 220 230 240 VYKPEEFTVG DLVWAKCGKR FPAWPAVVID PISQAPDGVL KHCVPGAICV MFFGYSKDGT 250 260 270 280 290 300 QRDYAWVRQG MVYPFTEFMD KFQDQTNLFN YKASEFNKAL EEAVLAENGN FGDAEIISPD 310 320 330 340 350 360 SSATESDQDY GPASRFQGSY HEDIRTCDGC GSVMPLKSLK RTKDSQPEEL LCKHCSKLRK 370 380 390 400 410 420 SNQYCGICKR IWHPSDDGDW VCCDGCDVWV HAECDNITNE RFKELEHNNY YCPDCKVQHE 430 440 450 460 470 480 LTPTILEEQN SVFKSTEKTT ETGLPDAITV VCNGMEGTYI RKFHAIECKC GSCGSRKQSP 490 500 510 520 530 540 SEWERHTGCR AKKWKYSVRV KDTMLPLEKW IAEFSTYTLE TQMLDKQKML SLLEEKYEPV 550 560 570 580 590 600 RAKWTTERCA VCRWVEDWEE NKMIICNRCQ VAVHQECYGV SKSQDLTSWV CRACETPDIE 610 620 630 640 650 660 RDCCLCPVKG GALKPSDVEG LWVHVTCAWF RPEVGFLNHE NMEPAVGLFK IPANSFLKVC 670 680 690 700 710 720 TICKQTHGSC VHCCKCATHF HAMCASRAGY NMELHCLEKN GVQRTRKSVY CSFHRKPDPD 730 740 750 760 770 780 SVVVVHTPSG VFGSRNLLQN QYGRAKGSRL VLTKKMKLPG FQTQTQAEQS RVFDSLSAAR 790 800 810 820 830 840 CRIYSRSNTK IDLEAISHRL KGPSHHSLSA IENLNSFKAS FSFRAPFMSV FCFLGATFSE 850 860 870 880 890 900 YLRKILISIY LVTHQEADFT SFRERLKHLQ RTENFRVCFG KSGIHGWGLF ARKSIQEGEM 910 920 930 940 950 960 IIEYRGVKVR RSVADLREAN YRSQGKDCYL FKISEEIVID ATDSGNIARL INHSCMPNCY 970 980 990 1000 1010 ARIVSMGDGE DNRIVLIAKT NVAAGEELTY DYLFEVDESE EIKVPCLCKA PNCRKFMN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"ORF cloning and analysis of Arabidopsis transcription factor genes." Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y., Takagi M. Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The Arabidopsis thaliana genome contains at least 29 active genes encoding SET domain proteins that can be assigned to four evolutionarily conserved classes." Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K., Assalkhou R., Schulz I., Reuter G., Aalen R.B. Nucleic Acids Res. 29:4319-4333(2001) [PubMed: 11691919] [Abstract] Cited for: NOMENCLATURE.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL132959 Genomic DNA. Translation: CAB71104.1. Sequence problems. CP002686 Genomic DNA. Translation: AEE80250.1. AK227351 mRNA. Translation: BAE99361.1. AB493660 mRNA. Translation: BAH30498.1.
IPI	IPI00517321.
PIR	T47966.
RefSeq	NP_191733.3. NM_116039.4.
UniGene	At.47229.
3D structure databases
ProteinModelPortal	Q9M364.
SMR	Q9M364. Positions 187-283, 364-416, 546-595, 827-1018.
ModBase	Search...
Proteomic databases
PRIDE	Q9M364.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT3G61740.1; AT3G61740.1; AT3G61740.
GeneID	825347.
GenomeReviews	Gene locus AT3G61740 in contig BA000014_GR.
KEGG	ath:AT3G61740.
Organism-specific databases
TAIR	At3g61740.
Phylogenomic databases
GeneTree	EPGT00070000029016.
HOGENOM	HBG318189.
InParanoid	Q9M364.
PhylomeDB	Q9M364.
ProtClustDB	CLSN2920181.
Gene expression databases
Genevestigator	Q9M364.
GermOnline	AT3G61740. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR003616. Post-SET_dom. IPR000313. PWWP. IPR010919. SAND_dom-like. IPR001214. SET_dom. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Gene3D	G3DSA:3.10.390.10. SAND. 1 hit. G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.
Pfam	PF00628. PHD. 2 hits. PF00855. PWWP. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00249. PHD. 3 hits. SM00508. PostSET. 1 hit. SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITE	PS50868. POST_SET. 1 hit. PS50812. PWWP. 1 hit. PS50280. SET. 1 hit. PS01359. ZF_PHD_1. 2 hits. PS50016. ZF_PHD_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATX3_ARATH

Accession

Primary (citable) accession number: Q9M364
Secondary accession number(s): C0SVF7, Q0WU37

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	September 22, 2009
Last modified:	January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program