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Q8GWT4 (ANM15_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein arginine N-methyltransferase 1.5

Short name=AtPMRT15
Short name=AtPMRT5
EC=2.1.1.-
EC=2.1.1.125
Alternative name(s):
Shk1 kinase-binding protein 1 homolog
Gene names
Name:PMRT15
Synonyms:PMRT5, SKB1
Ordered Locus Names:At4g31120
ORF Names:F6E21.40
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length642 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylates arginine residues of myelin basic protein (MBP) in vitro. Methylates symmetrically histone H4 of the FLC chromatin to form H4R3me2s, which in turn suppresses FLC expression to induce flowering. Ref.5

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in flowers, roots and siliques, lower expression in stems and mature leaves (at protein level). Abundant in shoot apex, young leaves and leaf primordia, floral and inflorescence meristems, gynoecium, stamens, sepals and young siliques, but not in older leaves, petals and vascular tissues. Ref.5

Developmental stage

High levels from 5 to 20 days after germination (at protein level). Ref.5

Disruption phenotype

Plants are late-flowering. Ref.5

Sequence similarities

Belongs to the protein arginine N-methyltransferase family.

Sequence caution

The sequence CAB79830.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8GWT4-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q8GWT4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     492-510: KAHKDLAHFETAYVVKLHS → RLIKILRTLKLLMLSSCIV
     511-642: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8GWT4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     585-642: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 642642Protein arginine N-methyltransferase 1.5
PRO_0000293993

Natural variations

Alternative sequence492 – 51019KAHKD…VKLHS → RLIKILRTLKLLMLSSCIV in isoform 2.
VSP_027572
Alternative sequence511 – 642132Missing in isoform 2.
VSP_027573
Alternative sequence585 – 64258Missing in isoform 3.
VSP_027574

Experimental info

Sequence conflict101E → G in AAO64842. Ref.3
Sequence conflict101E → G in BAC43244. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: F9F85054688D1B01

FASTA64271,870
        10         20         30         40         50         60 
MPLGERGGWE RTESRYCGVE TDFSNDVTHL LNFNISTGGF DYVLAPLVDP SYRPSLVEGN 

        70         80         90        100        110        120 
GVDTQVLPVC GSDLVLSPSQ WSSHVVGKIS SWIDLDSEDE VLRMDSETTL KQEIAWATHL 

       130        140        150        160        170        180 
SLQACLLPTP KGKSCANYAR CVNQILQGLT TLQLWLRVPL VKSEGDSMDD TSEGLNDSWE 

       190        200        210        220        230        240 
LWNSFRLLCE HDSKLSVALD VLSTLPSETS LGRWMGESVR AAILSTDAFL TNARGYPCLS 

       250        260        270        280        290        300 
KRHQKLIAGF FDHAAQVVIC GKPVHNLQKP LDSSSEGTEK NPLRIYLDYV AYLFQKMESL 

       310        320        330        340        350        360 
SEQERIELGY RDFLQAPLQP LMDNLEAQTY ETFERDSVKY IQYQRAVEKA LVDRVPDEKA 

       370        380        390        400        410        420 
SELTTVLMVV GAGRGPLVRA SLQAAEETDR KLKVYAVEKN PNAVVTLHNL VKMEGWEDVV 

       430        440        450        460        470        480 
TIISCDMRFW NAPEQADILV SELLGSFGDN ELSPECLDGA QRFLKPDGIS IPSSYTSFIQ 

       490        500        510        520        530        540 
PITASKLYND VKAHKDLAHF ETAYVVKLHS VAKLAPSQSV FTFTHPNFST KVNNQRYKKL 

       550        560        570        580        590        600 
QFSLPSDAGS ALVHGFAGYF DSVLYKDVHL GIEPTTATPN MFSWFPIFFP LRKPVEVHPD 

       610        620        630        640 
TPLEVHFWRC CGSSKVWYEW SVSSPTPSPM HNTNGRSYWV GL 

« Hide

Isoform 2 [UniParc].

Checksum: EBB12B9DEC5E838B
Show »

FASTA51056,926
Isoform 3 [UniParc].

Checksum: CEC3D1D3A3B458B4
Show »

FASTA58465,098

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]"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] (ISOFORM 2).
Strain: cv. Columbia.
[4]"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.
[5]"SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis."
Wang X., Zhang Y., Ma Q., Zhang Z., Xue Y., Bao S., Chong K.
EMBO J. 26:1934-1941(2007) [PubMed: 17363895] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL161578 Genomic DNA. Translation: CAB79830.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85860.1.
CP002687 Genomic DNA. Translation: AEE85861.1.
BT005907 mRNA. Translation: AAO64842.1.
AK118648 mRNA. Translation: BAC43244.1.
IPIIPI00544086.
IPI00548864.
IPI00854313.
PIRT10666.
RefSeqNP_194841.2. NM_119262.5.
NP_974647.1. NM_202918.2.
UniGeneAt.31771.
At.44014.

3D structure databases

ProteinModelPortalQ8GWT4.
SMRQ8GWT4. Positions 335-639.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8GWT4.

Proteomic databases

PRIDEQ8GWT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G31120.1; AT4G31120.1; AT4G31120.
GeneID829240.
GenomeReviewsGene locus AT4G31120 in contig CT486007_GR.
KEGGath:AT4G31120.
NMPDRfig|3702.1.peg.21109.

Organism-specific databases

TAIRAt4g31120.

Phylogenomic databases

eggNOGKOG0822.
GeneTreeEPGT00050000018246.
HOGENOMHBG628479.
InParanoidQ8GWT4.
OMALCDYNKR.
ProtClustDBCLSN2680196.

Gene expression databases

GenevestigatorQ8GWT4.

Family and domain databases

InterProIPR007857. Skb1_MeTrfase.
[Graphical view]
KOK02516.
PANTHERPTHR10738. Skb1_mtfrase. 1 hit.
PfamPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFPIRSF015894. Skb1_MeTrfase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameANM15_ARATH
AccessionPrimary (citable) accession number: Q8GWT4
Secondary accession number(s): Q9M090
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: November 16, 2011
This is version 54 of the entry and version 2 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