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Q9SUE7 (ATX4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase ATX4
EC=2.1.1.43
Alternative name(s):
Protein SET DOMAIN GROUP 16
Trithorax-homolog protein 4
Short name=TRX-homolog protein 4
Short name=Trithorax 4
Gene names
Name:ATX4
Synonyms:SDG16, SET16, TX4
Ordered Locus Names:At4g27910
ORF Names:T13J8.20
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length1027 AA.
Sequence statusComplete.
Protein existenceEvidence 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 CAB36760.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79593.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10271027Histone-lysine N-methyltransferase ATX4
PRO_0000233357

Regions

Domain207 – 27670PWWP
Domain884 – 1006123SET
Domain1011 – 102717Post-SET
Zinc finger398 – 45457PHD-type 1
Zinc finger592 – 64352PHD-type 2
Region962 – 9632S-adenosyl-L-methionine binding By similarity
Compositional bias135 – 1406Poly-Glu

Sites

Metal binding9651Zinc By similarity
Metal binding10151Zinc By similarity
Metal binding10171Zinc By similarity
Metal binding10221Zinc By similarity
Binding site8951S-adenosyl-L-methionine By similarity
Binding site9391S-adenosyl-L-methionine By similarity

Experimental info

Sequence conflict7871K → E in AAL12215. Ref.3
Sequence conflict851 – 8533AAI → TAV in AAL12215. Ref.3
Sequence conflict9011A → G in AAL12215. Ref.3
Sequence conflict9471V → L in AAL12215. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9SUE7 [UniParc].

Last modified March 24, 2009. Version 3.
Checksum: 925666F8ADEFC0B4

FASTA1,027116,739
        10         20         30         40         50         60 
MIIKRKFKTQ IPSLERCKLG NESRKKKRKL NLGGGGYYYP LNLLGEIAAG IVPGNGRNGF 

        70         80         90        100        110        120 
SASWCTEVTK PVEVEESLSK RRSDSGTVRD SPPAEVSRPP LVRTSRGRIQ VLPSRFNDSV 

       130        140        150        160        170        180 
LDNWRKDSKS DCDLEEEEIE CRNEKVVSFR VPKATNLKSK ELDRKSKYSA LCKEERFHEQ 

       190        200        210        220        230        240 
HNDEARARVD EKLPNKKGTF GPENFYSGDL VWAKSGRNEP FWPAIVIDPM TQAPELVLRS 

       250        260        270        280        290        300 
CIPDAACVVF FGHSGNENER DYAWVRRGMI FPFVDYVARF QEQPELQGCK PGNFQMALEE 

       310        320        330        340        350        360 
AFLADQGFTE KLMHDIHLAA GNSTFDDSFY RWIQETAVSN QELNNNAPRQ GLLKKHRNPL 

       370        380        390        400        410        420 
ACAGCETVIS FEMAKKMKDL IPGDQLLCKP CSRLTKSKHI CGICKKIRNH LDNKSWVRCD 

       430        440        450        460        470        480 
GCKVRIHAEC DQISDRHLKD LRETDYYCPT CRAKFNFDLS DSEKQNSKSK VAKGDGQMVL 

       490        500        510        520        530        540 
PDKVIVVCAG VEGVYFPRLH LVVCKCGSCG PKKKALSEWE RHTGSKSKNW KTSVKVKSSK 

       550        560        570        580        590        600 
LALEDWMMNL AELHANATAA KVPKRPSIKQ RKQRLLAFLS ETYEPVNAKW TTERCAVCRW 

       610        620        630        640        650        660 
VEDWDYNKII ICNRCQIAVH QECYGARHVR DFTSWVCKAC ERPDIKRECC LCPVKGGALK 

       670        680        690        700        710        720 
PTDVETLWVH VTCAWFQPEV CFASEEKMEP AVGILSIPST NFVKICVICK QIHGSCTQCC 

       730        740        750        760        770        780 
KCSTYYHAMC ASRAGYRMEL HCLEKNGQQI TKMVSYCAYH RAPNPDNVLI IQTPSGAFSA 

       790        800        810        820        830        840 
KSLVQNKKKG GSRLISLIRE DDEAPAENTI TCDPFSAARC RVFKRKINSK KRIEEEAIPH 

       850        860        870        880        890        900 
HTRGPRHHAS AAIQTLNTFR HVPEEPKSFS SFRERLHHLQ RTEMDRVCFG RSGIHGWGLF 

       910        920        930        940        950        960 
ARRNIQEGEM VLEYRGEQVR GSIADLREAR YRRVGKDCYL FKISEEVVVD ATDKGNIARL 

       970        980        990       1000       1010       1020 
INHSCTPNCY ARIMSVGDEE SRIVLIAKAN VAVGEELTYD YLFDPDEAEE LKVPCLCKAP 


NCRKFMN

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed: 10617198] [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]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 743-1027, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL035524 Genomic DNA. Translation: CAB36760.1. Sequence problems.
AL161572 Genomic DNA. Translation: CAB79593.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85408.1.
AY049754 mRNA. Translation: AAL12215.1.
IPIIPI00523194.
PIRT02892.
RefSeqNP_194520.3. NM_118929.4.
UniGeneAt.43382.

3D structure databases

ProteinModelPortalQ9SUE7.
SMRQ9SUE7. Positions 204-304, 398-453, 593-642, 846-1027.
ModBaseSearch...

Proteomic databases

PRIDEQ9SUE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G27910.1; AT4G27910.1; AT4G27910.
GeneID828904.
GenomeReviewsGene locus AT4G27910 in contig CT486007_GR.
KEGGath:AT4G27910.

Organism-specific databases

TAIRAt4g27910.

Phylogenomic databases

eggNOGKOG1080.
GeneTreeEPGT00070000029016.
HOGENOMHBG318189.
OMADIKRECC.
PhylomeDBQ9SUE7.
ProtClustDBCLSN2680527.

Gene expression databases

ArrayExpressQ9SUE7.
GenevestigatorQ9SUE7.
GermOnlineAT4G27910. Arabidopsis thaliana.

Family and domain databases

InterProIPR003616. Post-SET_dom.
IPR000313. PWWP.
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]
Gene3DG3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits.
PfamPF00628. PHD. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 3 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF57903. FYVE_PHD_ZnF. 2 hits.
PROSITEPS50868. POST_SET. 1 hit.
PS50812. PWWP. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATX4_ARATH
AccessionPrimary (citable) accession number: Q9SUE7
Secondary accession number(s): Q941H0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 24, 2009
Last modified: January 25, 2012
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents