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Reviewed, UniProtKB/Swiss-Prot Q9SU94 (ANM11_ARATH)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable protein arginine N-methyltransferase 1.1
    EC=2.1.1.-
Alternative name(s):
    Arginine methyltransferase pam1
Gene names
Name: PRMT1.1
Synonyms: PAM1
Ordered Locus Names: At4g29510
ORF Names: T16L4.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 (can methylate histones) By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
   Cellular componentNucleus
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from direct assay. Source: TAIR

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: IntAct

protein-arginine N-methyltransferase activity

Inferred from direct assay. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-1382731,EBI-1382731
FIB2Q94AH91EBI-1382731,EBI-1382666
HIST1H4AP628051EBI-1382731,EBI-302023From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Probable protein arginine N-methyltransferase 1.1
PRO_0000293986

Experimental info

Sequence conflict2601D → G in AAL36326. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9SU94-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9BE43387CD7AE0B2

FASTA39043,894
        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 

« 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]"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. expand/collapse author list , 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.
[3]"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].
[4]"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.
[5]"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.

Cross-references

Sequence databases

AL079344 Genomic DNA. Translation: CAB45311.1.
AL161575 Genomic DNA. Translation: CAB79709.1.
AY150407 mRNA. Translation: AAN12952.1.
AY063970 mRNA. Translation: AAL36326.1.
AY087817 mRNA. Translation: AAM65371.1.
AJ007582 mRNA. Translation: CAA07570.1.
IPIIPI00522360.
PIRT09914.
T52248.
RefSeqNP_194680.1.
UniGeneAt.27463

3D structure databases

HSSPHSSP built from PDB template 1ORH based on UniProtKB Q63009.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9SU94. 3 interactions.

Proteomic databases

PRIDEQ9SU94.

Genome annotation databases

GeneID829072.
GenomeReviewsGene locus AT4G29510 in contig CT486007_GR.
KEGGath:AT4G29510.
NMPDRfig|3702.1.peg.20921.

Organism-specific databases

TAIRAt4g29510.

Phylogenomic databases

OMAQ9SU94. LIFPDKC.

Family and domain databases

InterProIPR013217. Methyltransf_12.
[Graphical view]
PfamPF08242. Methyltransf_12. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANM11_ARATH
AccessionPrimary (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: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents