Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei726S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei745S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei795S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi796MagnesiumCombined sources1 Publication1
Metal bindingi799MagnesiumCombined sources1 Publication1
Metal bindingi800Magnesium; via tele nitrogenCombined sources1 Publication1
Metal bindingi860Magnesium; via tele nitrogenCombined sources1 Publication1

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
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi68Missing in crm2-1; compact inflorescence with several flower buds at the tip. 1 Publication1
Mutagenesisi109Y → A: No effect on RNA binding and transferase activity. 1 Publication1
Mutagenesisi333W → A: Loss of RNA binding and transferase activity. 1 Publication1
Mutagenesisi604L → P: No effect on transferase activity. 1 Publication1
Mutagenesisi701R → A: Reduces transferase activity. 1 Publication1
Mutagenesisi719D → N in hen1-2; alters organ development and floral determinacy. 1 Publication1
Mutagenesisi796E → A: Loss of transferase activity. 1 Publication1
Mutagenesisi799E → A: Loss of transferase activity; when associated with A-800. 1 Publication1
Mutagenesisi800H → A: Loss of transferase activity; when associated with A-799. 1 Publication1
Mutagenesisi800H → Q: Strongly decreases transferase activity. 1 Publication1
Mutagenesisi856R → A: Reduces transferase activity. 1 Publication1
Mutagenesisi860H → A or Q: Loss of transferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004046581 – 942Small RNA 2'-O-methyltransferaseAdd BLAST942

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 interactors.
STRINGi3702.AT4G20910.1.

Structurei

Secondary structure

1942
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 17Combined sources6
Helixi18 – 22Combined sources5
Beta strandi23 – 30Combined sources8
Beta strandi50 – 56Combined sources7
Beta strandi61 – 63Combined sources3
Helixi70 – 82Combined sources13
Turni83 – 86Combined sources4
Turni88 – 90Combined sources3
Helixi96 – 110Combined sources15
Helixi114 – 117Combined sources4
Helixi122 – 130Combined sources9
Helixi134 – 136Combined sources3
Helixi142 – 147Combined sources6
Helixi150 – 159Combined sources10
Helixi162 – 165Combined sources4
Helixi168 – 180Combined sources13
Beta strandi183 – 188Combined sources6
Beta strandi191 – 196Combined sources6
Helixi200 – 208Combined sources9
Beta strandi217 – 224Combined sources8
Beta strandi233 – 239Combined sources7
Helixi245 – 252Combined sources8
Beta strandi258 – 263Combined sources6
Helixi269 – 272Combined sources4
Beta strandi276 – 281Combined sources6
Helixi284 – 287Combined sources4
Helixi310 – 316Combined sources7
Beta strandi324 – 331Combined sources8
Beta strandi336 – 341Combined sources6
Helixi345 – 353Combined sources9
Helixi357 – 365Combined sources9
Turni368 – 370Combined sources3
Turni380 – 382Combined sources3
Helixi388 – 397Combined sources10
Turni398 – 400Combined sources3
Beta strandi405 – 407Combined sources3
Beta strandi456 – 461Combined sources6
Beta strandi464 – 469Combined sources6
Helixi478 – 494Combined sources17
Turni548 – 551Combined sources4
Beta strandi557 – 569Combined sources13
Beta strandi603 – 615Combined sources13
Turni616 – 618Combined sources3
Helixi622 – 628Combined sources7
Beta strandi636 – 643Combined sources8
Helixi648 – 654Combined sources7
Helixi658 – 664Combined sources7
Beta strandi669 – 681Combined sources13
Beta strandi693 – 695Combined sources3
Helixi697 – 711Combined sources15
Beta strandi715 – 720Combined sources6
Beta strandi723 – 725Combined sources3
Helixi726 – 731Combined sources6
Beta strandi740 – 746Combined sources7
Helixi748 – 761Combined sources14
Turni762 – 765Combined sources4
Beta strandi770 – 777Combined sources8
Beta strandi791 – 796Combined sources6
Helixi798 – 800Combined sources3
Helixi803 – 815Combined sources13
Beta strandi820 – 826Combined sources7
Helixi829 – 831Combined sources3
Helixi832 – 835Combined sources4
Helixi866 – 879Combined sources14
Beta strandi882 – 891Combined sources10
Beta strandi893 – 895Combined sources3
Beta strandi900 – 909Combined sources10
Beta strandi926 – 931Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9C5Q8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 87DRBMAdd BLAST69
Domaini93 – 204HTH La-type RNA-bindingPROSITE-ProRule annotationAdd BLAST112

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni778 – 779S-adenosyl-L-homocysteine bindingCombined sources1 Publication2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
HOGENOMiHOG000084447.
KOiK20798.
OMAiSANCESS.
OrthoDBiEOG0936015O.
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 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB79091 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti39L → P in AAC97105 (Ref. 1) Curated1
Sequence conflicti39L → P in AAL05056 (PubMed:11874905).Curated1
Sequence conflicti552S → Y in AAC97105 (Ref. 1) Curated1
Sequence conflicti660R → K in AAC97105 (Ref. 1) Curated1

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_001203853.2.
NP_567616.1. NM_118209.3.
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_001203853.2.
NP_567616.1. NM_118209.3.
UniGeneiAt.3574.

3D structure databases

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

Protein-protein interaction databases

BioGridi13130. 3 interactors.
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.
KOiK20798.
OMAiSANCESS.
OrthoDBiEOG0936015O.
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...

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: November 30, 2016
This is version 99 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.