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Protein

Small RNA 2'-O-methyltransferase

Gene

HEN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methyltransferase that adds a methyl group to the ribose of the last nucleotide of small RNAs (sRNAs). This protects the 3'-end of sRNAs from uridylation activity and subsequent degradation. Can methylate 3'-end of microRNAs (miRNAs), small interfering RNAs (siRNas) and trans-acting small interfering RNAs (ta-siRNAs). Involved in plant development through its role in small RNAs processing. Required for the specification of reproductive organ identities and the probable repression of A class genes. May control floral determinacy possibly by regulating the expression of the C class floral homeotic gene AGAMOUS (AG).4 Publications

Catalytic activityi

S-adenosyl-L-methionine + small RNA = S-adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-methylnucleotide.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei726 – 7261S-adenosyl-L-methionineCombined sources1 Publication
Binding sitei745 – 7451S-adenosyl-L-methionineCombined sources1 Publication
Binding sitei795 – 7951S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication
Metal bindingi796 – 7961MagnesiumCombined sources1 Publication
Metal bindingi799 – 7991MagnesiumCombined sources1 Publication
Metal bindingi800 – 8001Magnesium; via tele nitrogenCombined sources1 Publication
Metal bindingi860 – 8601Magnesium; via tele nitrogenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

  • leaf proximal/distal pattern formation Source: TAIR
  • leaf vascular tissue pattern formation Source: TAIR
  • mRNA cleavage involved in gene silencing by miRNA Source: TAIR
  • production of miRNAs involved in gene silencing by miRNA Source: TAIR
  • production of siRNA involved in RNA interference Source: TAIR
  • regulation of flower development Source: TAIR
  • specification of floral organ identity Source: TAIR
  • virus induced gene silencing Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

RNA-mediated gene silencing

Keywords - Ligandi

Metal-binding, RNA-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Small RNA 2'-O-methyltransferase (EC:2.1.1.n8)
Alternative name(s):
Protein CORYMBOSA 2
Protein HUA ENHANCER 1
S-adenosylmethionine-dependent RNA methyltransferase HEN1
Gene namesi
Name:HEN1
Synonyms:CRM2
Ordered Locus Names:At4g20910
ORF Names:T13K14.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G20910.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Reduced organ size, altered rosette leaf shape and increased number of coflorescences. Urydilation of miRNA 3'-ends.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681Missing in crm2-1; compact inflorescence with several flower buds at the tip. 1 Publication
Mutagenesisi109 – 1091Y → A: No effect on RNA binding and transferase activity. 1 Publication
Mutagenesisi333 – 3331W → A: Loss of RNA binding and transferase activity. 1 Publication
Mutagenesisi604 – 6041L → P: No effect on transferase activity. 1 Publication
Mutagenesisi701 – 7011R → A: Reduces transferase activity. 1 Publication
Mutagenesisi719 – 7191D → N in hen1-2; alters organ development and floral determinacy. 1 Publication
Mutagenesisi796 – 7961E → A: Loss of transferase activity. 1 Publication
Mutagenesisi799 – 7991E → A: Loss of transferase activity; when associated with A-800. 1 Publication
Mutagenesisi800 – 8001H → A: Loss of transferase activity; when associated with A-799. 1 Publication
Mutagenesisi800 – 8001H → Q: Strongly decreases transferase activity. 1 Publication
Mutagenesisi856 – 8561R → A: Reduces transferase activity. 1 Publication
Mutagenesisi860 – 8601H → A or Q: Loss of transferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 942942Small RNA 2'-O-methyltransferasePRO_0000404658Add
BLAST

Proteomic databases

PaxDbiQ9C5Q8.
PRIDEiQ9C5Q8.

PTM databases

iPTMnetiQ9C5Q8.

Expressioni

Tissue specificityi

Expressed in stems, leaves and inflorescences.2 Publications

Gene expression databases

GenevisibleiQ9C5Q8. AT.

Interactioni

Subunit structurei

Binds small RNA duplexes as monomer.1 Publication

Protein-protein interaction databases

BioGridi13130. 3 interactions.
STRINGi3702.AT4G20910.1.

Structurei

Secondary structure

1
942
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 176Combined sources
Helixi18 – 225Combined sources
Beta strandi23 – 308Combined sources
Beta strandi50 – 567Combined sources
Beta strandi61 – 633Combined sources
Helixi70 – 8213Combined sources
Turni83 – 864Combined sources
Turni88 – 903Combined sources
Helixi96 – 11015Combined sources
Helixi114 – 1174Combined sources
Helixi122 – 1309Combined sources
Helixi134 – 1363Combined sources
Helixi142 – 1476Combined sources
Helixi150 – 15910Combined sources
Helixi162 – 1654Combined sources
Helixi168 – 18013Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi191 – 1966Combined sources
Helixi200 – 2089Combined sources
Beta strandi217 – 2248Combined sources
Beta strandi233 – 2397Combined sources
Helixi245 – 2528Combined sources
Beta strandi258 – 2636Combined sources
Helixi269 – 2724Combined sources
Beta strandi276 – 2816Combined sources
Helixi284 – 2874Combined sources
Helixi310 – 3167Combined sources
Beta strandi324 – 3318Combined sources
Beta strandi336 – 3416Combined sources
Helixi345 – 3539Combined sources
Helixi357 – 3659Combined sources
Turni368 – 3703Combined sources
Turni380 – 3823Combined sources
Helixi388 – 39710Combined sources
Turni398 – 4003Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi464 – 4696Combined sources
Helixi478 – 49417Combined sources
Turni548 – 5514Combined sources
Beta strandi557 – 56913Combined sources
Beta strandi603 – 61513Combined sources
Turni616 – 6183Combined sources
Helixi622 – 6287Combined sources
Beta strandi636 – 6438Combined sources
Helixi648 – 6547Combined sources
Helixi658 – 6647Combined sources
Beta strandi669 – 68113Combined sources
Beta strandi693 – 6953Combined sources
Helixi697 – 71115Combined sources
Beta strandi715 – 7206Combined sources
Beta strandi723 – 7253Combined sources
Helixi726 – 7316Combined sources
Beta strandi740 – 7467Combined sources
Helixi748 – 76114Combined sources
Turni762 – 7654Combined sources
Beta strandi770 – 7778Combined sources
Beta strandi791 – 7966Combined sources
Helixi798 – 8003Combined sources
Helixi803 – 81513Combined sources
Beta strandi820 – 8267Combined sources
Helixi829 – 8313Combined sources
Helixi832 – 8354Combined sources
Helixi866 – 87914Combined sources
Beta strandi882 – 89110Combined sources
Beta strandi893 – 8953Combined sources
Beta strandi900 – 90910Combined sources
Beta strandi926 – 9316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HTXX-ray3.10A/D1-942[»]
ProteinModelPortaliQ9C5Q8.
SMRiQ9C5Q8. Positions 7-933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C5Q8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 8769DRBMAdd
BLAST
Domaini93 – 204112HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni778 – 7792S-adenosyl-L-homocysteine bindingCombined sources1 Publication

Sequence similaritiesi

Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
HOGENOMiHOG000084447.
OMAiSANCESS.
PhylomeDBiQ9C5Q8.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR026610. Hen1.
IPR006630. Lupus_La_RNA-bd.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21404. PTHR21404. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C5Q8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGGKHTPT PKAIIHQKFG AKASYTVEEV HDSSQSGCLG LAIPQKGPCL
60 70 80 90 100
YRCHLQLPEF SVVSNVFKKK KDSEQSAAEL ALDKLGIRPQ NDDLTVDEAR
110 120 130 140 150
DEIVGRIKYI FSDEFLSAEH PLGAHLRAAL RRDGERCGSV PVSVIATVDA
160 170 180 190 200
KINSRCKIIN PSVESDPFLA ISYVMKAAAK LADYIVASPH GLRRKNAYPS
210 220 230 240 250
EIVEALATHV SDSLHSREVA AVYIPCIDEE VVELDTLYIS SNRHYLDSIA
260 270 280 290 300
ERLGLKDGNQ VMISRMFGKA SCGSECRLYS EIPKKYLDNS SDASGTSNED
310 320 330 340 350
SSHIVKSRNA RASYICGQDI HGDAILASVG YRWKSDDLDY DDVTVNSFYR
360 370 380 390 400
ICCGMSPNGI YKISRQAVIA AQLPFAFTTK SNWRGPLPRE ILGLFCHQHR
410 420 430 440 450
LAEPILSSST APVKSLSDIF RSHKKLKVSG VDDANENLSR QKEDTPGLGH
460 470 480 490 500
GFRCEVKIFT KSQDLVLECS PRKFYEKEND AIQNASLKAL LWFSKFFADL
510 520 530 540 550
DVDGEQSCDT DDDQDTKSSS PNVFAAPPIL QKEHSSESKN TNVLSAEKRV
560 570 580 590 600
QSITNGSVVS ICYSLSLAVD PEYSSDGESP REDNESNEEM ESEYSANCES
610 620 630 640 650
SVELIESNEE IEFEVGTGSM NPHIESEVTQ MTVGEYASFR MTPPDAAEAL
660 670 680 690 700
ILAVGSDTVR IRSLLSERPC LNYNILLLGV KGPSEERMEA AFFKPPLSKQ
710 720 730 740 750
RVEYALKHIR ESSASTLVDF GCGSGSLLDS LLDYPTSLQT IIGVDISPKG
760 770 780 790 800
LARAAKMLHV KLNKEACNVK SATLYDGSIL EFDSRLHDVD IGTCLEVIEH
810 820 830 840 850
MEEDQACEFG EKVLSLFHPK LLIVSTPNYE FNTILQRSTP ETQEENNSEP
860 870 880 890 900
QLPKFRNHDH KFEWTREQFN QWASKLGKRH NYSVEFSGVG GSGEVEPGFA
910 920 930 940
SQIAIFRREA SSVENVAESS MQPYKVIWEW KKEDVEKKKT DL
Length:942
Mass (Da):104,454
Last modified:June 1, 2001 - v1
Checksum:i7D8B5222C0D28779
GO

Sequence cautioni

The sequence CAB45886.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79091.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391L → P in AAC97105 (Ref. 1) Curated
Sequence conflicti39 – 391L → P in AAL05056 (PubMed:11874905).Curated
Sequence conflicti552 – 5521S → Y in AAC97105 (Ref. 1) Curated
Sequence conflicti660 – 6601R → K in AAC97105 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060248 Genomic DNA. Translation: AAC97105.1.
AF411383 mRNA. Translation: AAL05056.1.
AF327068 mRNA. Translation: AAK16435.1.
AL080282 Genomic DNA. Translation: CAB45886.1. Sequence problems.
AL161553 Genomic DNA. Translation: CAB79091.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84374.1.
CP002687 Genomic DNA. Translation: AEE84375.1.
PIRiT10633.
RefSeqiNP_001190782.1. NM_001203853.1.
NP_567616.1. NM_118209.2.
UniGeneiAt.3574.

Genome annotation databases

EnsemblPlantsiAT4G20910.1; AT4G20910.1; AT4G20910.
AT4G20910.2; AT4G20910.2; AT4G20910.
GeneIDi827839.
GrameneiAT4G20910.1; AT4G20910.1; AT4G20910.
AT4G20910.2; AT4G20910.2; AT4G20910.
KEGGiath:AT4G20910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060248 Genomic DNA. Translation: AAC97105.1.
AF411383 mRNA. Translation: AAL05056.1.
AF327068 mRNA. Translation: AAK16435.1.
AL080282 Genomic DNA. Translation: CAB45886.1. Sequence problems.
AL161553 Genomic DNA. Translation: CAB79091.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84374.1.
CP002687 Genomic DNA. Translation: AEE84375.1.
PIRiT10633.
RefSeqiNP_001190782.1. NM_001203853.1.
NP_567616.1. NM_118209.2.
UniGeneiAt.3574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HTXX-ray3.10A/D1-942[»]
ProteinModelPortaliQ9C5Q8.
SMRiQ9C5Q8. Positions 7-933.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13130. 3 interactions.
STRINGi3702.AT4G20910.1.

PTM databases

iPTMnetiQ9C5Q8.

Proteomic databases

PaxDbiQ9C5Q8.
PRIDEiQ9C5Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G20910.1; AT4G20910.1; AT4G20910.
AT4G20910.2; AT4G20910.2; AT4G20910.
GeneIDi827839.
GrameneiAT4G20910.1; AT4G20910.1; AT4G20910.
AT4G20910.2; AT4G20910.2; AT4G20910.
KEGGiath:AT4G20910.

Organism-specific databases

TAIRiAT4G20910.

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
HOGENOMiHOG000084447.
OMAiSANCESS.
PhylomeDBiQ9C5Q8.

Miscellaneous databases

EvolutionaryTraceiQ9C5Q8.
PROiQ9C5Q8.

Gene expression databases

GenevisibleiQ9C5Q8. AT.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR026610. Hen1.
IPR006630. Lupus_La_RNA-bd.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21404. PTHR21404. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Anther development defects in Arabidopsis thaliana male-sterile mutants."
    Sanders P.M., Bui A.Q., Weterings K., McIntire K.N., Hsu Y.C., Lee P.Y., Truong M.T., Beals T.B., Goldberg R.B.
    Sex. Plant Reprod. 11:297-322(1999)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Wassilewskija.
  2. "HEN1 functions pleiotropically in Arabidopsis development and acts in C function in the flower."
    Chen X., Liu J., Cheng Y., Jia D.
    Development 129:1085-1094(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-719.
    Strain: cv. Landsberg erecta.
  3. "Formation of corymb-like inflorescences due to delay in bolting and flower development in the corymbosa2 mutant of Arabidopsis."
    Suzuki M., Takahashi T., Komeda Y.
    Plant Cell Physiol. 43:298-306(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-68.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. Cited for: SUBCELLULAR LOCATION.
  7. "Methylation protects miRNAs and siRNAs from a 3'-end uridylation activity in Arabidopsis."
    Li J., Yang Z., Yu B., Liu J., Chen X.
    Curr. Biol. 15:1501-1507(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Methylation as a crucial step in plant microRNA biogenesis."
    Yu B., Yang Z., Li J., Minakhina S., Yang M., Padgett R.W., Steward R., Chen X.
    Science 307:932-935(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Structural insights into mechanisms of the small RNA methyltransferase HEN1."
    Huang Y., Ji L., Huang Q., Vassylyev D.G., Chen X., Ma J.B.
    Nature 461:823-827(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; S-ADENOSYL L-HOMOCYSTEINE AND MAGNESIUM ION, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-109; TRP-333; LEU-604; ARG-701; GLU-796; GLU-799; HIS-800; ARG-856 AND HIS-860.

Entry informationi

Entry nameiHEN1_ARATH
AccessioniPrimary (citable) accession number: Q9C5Q8
Secondary accession number(s): O65309, Q945R3, Q9SUC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: June 1, 2001
Last modified: February 17, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.