Q9SU94 (ANM11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein arginine N-methyltransferase 1.1
Short name=AtPRMT11
EC=2.1.1.-
EC=2.1.1.125

Alternative name(s):
Arginine methyltransferase pam1
Histone-arginine N-methyltransferase PRMT11

Gene names

Name:	PRMT11
Synonyms:	PAM1, PRMT1.1
Ordered Locus Names:	At4g29510
ORF Names:	T16L4.20

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	390 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in a glycine and arginine-rich domain. Type I arginine methyltransferase active on both histones and non-histone proteins. Required for leaves and flowers development. Mediates the methylation of MBD7. Ref.7
Catalytic activity	S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Subunit structure	Interacts with MBD7. Ref.7
Subcellular location	Nucleus. Cytoplasm. Note: Excluded from nucleolus. Ref.7
Disruption phenotype	Reduced levels of proteins with asymmetrically dimethylated arginines. Altered leaf morphology and development (curled leaves), multiple rosettes with an increased number of leaves, delayed flowering, disturbed inflorescence morphology, increased sterility. Ref.7
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Chromatin regulator Methyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: TAIR nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction Ref.7. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	Protein arginine N-methyltransferase 1.1		PRO_0000293986
Experimental info
	Sequence conflict	260	1	D → G in AAL36326. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9SU94 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9BE43387CD7AE0B2	FASTA	390	43,894
	10 20 30 40 50 60 MTKNSNHDEN EFISFEPNQN TKIRFEDADE DEVAEGSGVA GEETPQDESM FDAGESADTA 70 80 90 100 110 120 EVTDDTTSAD YYFDSYSHFG IHEEMLKDVV RTKTYQNVIY QNKFLIKDKI VLDVGAGTGI 130 140 150 160 170 180 LSLFCAKAGA AHVYAVECSQ MADMAKEIVK ANGFSDVITV LKGKIEEIEL PTPKVDVIIS 190 200 210 220 230 240 EWMGYFLLFE NMLDSVLYAR DKWLVEGGVV LPDKASLHLT AIEDSEYKED KIEFWNSVYG 250 260 270 280 290 300 FDMSCIKKKA MMEPLVDTVD QNQIVTDSRL LKTMDISKMS SGDASFTAPF KLVAQRNDYI 310 320 330 340 350 360 HALVAYFDVS FTMCHKLLGF STGPKSRATH WKQTVLYLED VLTICEGETI TGTMSVSPNK 370 380 390 KNPRDIDIKL SYSLNGQHCK ISRTQHYKMR

References

	« Hide 'large scale' referencesShow '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. , 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]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"Identification and isolation of the first protein arginine methyltransferase from Arabidopsis thaliana." Salchert K., Breuer F., Koncz C. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-376. Strain: cv. Columbia.
[6]	"Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential." Krause C.D., Yang Z.-H., Kim Y.-S., Lee J.-H., Cook J.R., Pestka S. Pharmacol. Ther. 113:50-87(2007) [PubMed: 17005254] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[7]	"PRMT11: a new Arabidopsis MBD7 protein partner with arginine methyltransferase activity." Scebba F., De Bastiani M., Bernacchia G., Andreucci A., Galli A., Pitto L. Plant J. 52:210-222(2007) [PubMed: 17711414] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MBD7, SUBCELLULAR LOCATION. Strain: cv. Columbia and cv. Landsberg erecta.
+	Additional computationally mapped references.

Web resources

The Chromatin Database (ChromDB)

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL079344 Genomic DNA. Translation: CAB45311.1. AL161575 Genomic DNA. Translation: CAB79709.1. CP002687 Genomic DNA. Translation: AEE85638.1. AY150407 mRNA. Translation: AAN12952.1. AY063970 mRNA. Translation: AAL36326.1. AY087817 mRNA. Translation: AAM65371.1. AJ007582 mRNA. Translation: CAA07570.1.
IPI	IPI00522360.
PIR	T09914. T52248.
RefSeq	NP_194680.1. NM_119096.2.
UniGene	At.27463. At.31913.
3D structure databases
HSSP	HSSP built from PDB template 1ORH based on UniProtKB Q63009.
ProteinModelPortal	Q9SU94.
SMR	Q9SU94. Positions 73-390.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SU94. 6 interactions.
STRING	Q9SU94.
Proteomic databases
PRIDE	Q9SU94.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G29510.1; AT4G29510.1; AT4G29510.
GeneID	829072.
GenomeReviews	Gene locus AT4G29510 in contig CT486007_GR.
KEGG	ath:AT4G29510.
NMPDR	fig|3702.1.peg.20921.
Organism-specific databases
TAIR	At4g29510.
Phylogenomic databases
eggNOG	KOG1499.
GeneTree	EPGT00070000028859.
HOGENOM	HBG715060.
InParanoid	Q9SU94.
OMA	KINWWDD.
PhylomeDB	Q9SU94.
ProtClustDB	CLSN2683188.
Gene expression databases
Genevestigator	Q9SU94.
Family and domain databases
InterPro	IPR010456. Ribosomal-L11_MeTrfase_PrmA. [Graphical view]
KO	K11434.
Pfam	PF06325. PrmA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANM11_ARATH

Accession

Primary (citable) accession number: Q9SU94
Secondary accession number(s): O81813, Q8VZP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program