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

Henmt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the 3'-end of piRNAs from uridylation activity and subsequent degradation. Stabilization of piRNAs is essential for gametogenesis.2 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791S-adenosyl-L-methionineBy similarity
Binding sitei115 – 1151S-adenosyl-L-methionineBy similarity
Metal bindingi133 – 1331MagnesiumBy similarity
Metal bindingi136 – 1361MagnesiumBy similarity
Metal bindingi137 – 1371Magnesium; via tele nitrogenBy similarity
Metal bindingi182 – 1821Magnesium; via tele nitrogenBy similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • O-methyltransferase activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW
  • RNA methyltransferase activity Source: UniProtKB

GO - Biological processi

  • gene silencing by RNA Source: UniProtKB-KW
  • piRNA metabolic process Source: UniProtKB
  • RNA methylation Source: UniProtKB
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):
HEN1 methyltransferase homolog 1
Short name:
mHEN1
Gene namesi
Name:Henmt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1913965. Henmt1.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 585DLGCG → NAVAV: Abolishes methyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Small RNA 2'-O-methyltransferasePRO_0000304141Add
BLAST

Proteomic databases

PaxDbiQ8CAE2.
PRIDEiQ8CAE2.

PTM databases

PhosphoSiteiQ8CAE2.

Expressioni

Tissue specificityi

Specifically expressed in testis.2 Publications

Gene expression databases

BgeeiQ8CAE2.
CleanExiMM_4921515J06RIK.
ExpressionAtlasiQ8CAE2. baseline and differential.
GenevisibleiQ8CAE2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054829.

Structurei

3D structure databases

ProteinModelPortaliQ8CAE2.
SMRiQ8CAE2. Positions 27-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
GeneTreeiENSGT00390000004798.
HOVERGENiHBG097349.
InParanoidiQ8CAE2.
OMAiMEFQTWA.
OrthoDBiEOG7RNK1Q.
PhylomeDBiQ8CAE2.
TreeFamiTF315178.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR026610. Hen1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21404. PTHR21404. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CAE2-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEMAESIPCN SVVGGNFKEV SPEKVIRFKP PLYKQRYQFV RDLVDRHEPK
60 70 80 90 100
KVADLGCGDA KLLKLLKIYP CIQLLVGVDI NEEKLHSNGH RLSPYLGEFV
110 120 130 140 150
KPRDLDLTVT LYHGSVVERD SRLLGFDLIT CIELIEHLDS DDLARFPDVV
160 170 180 190 200
FGYLSPAMVV ISTPNAEFNP LFPTVTLRDA DHKFEWSRME FQTWALHVAN
210 220 230 240 250
CYNYRVEFTG VGTPPAGSEH VGYCTQIGVF TKNGGKLSKP SVSQQCDQHV
260 270 280 290 300
YKPVYTTSYP SLQQEKVLKF VLVGELLIQV DRLRLRYQRM LRDREKDRGP
310 320 330 340 350
KPGDMDSCPA PHLLLGAVFT EAEKARIESS PKPFCEGEKF YIPLQRLLTY
360 370 380 390
PKLHRLCADE DRVRSLIADS VCLSSDGSAV VVDLHNSWDY RPEEN
Length:395
Mass (Da):44,921
Last modified:March 1, 2003 - v1
Checksum:iBA648D0289C2EEBE
GO
Isoform 2 (identifier: Q8CAE2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     9-51: Missing.

Note: No experimental confirmation available.
Show »
Length:352
Mass (Da):39,806
Checksum:iC13E5027C2956E49
GO

Sequence cautioni

The sequence BAC39480.1 differs from that shown. Reason: Frameshift at position 270. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191F → L in BAC39480 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei9 – 5143Missing in isoform 2. 1 PublicationVSP_028012Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038994 mRNA. Translation: BAC30196.1.
AK085587 mRNA. Translation: BAC39480.1. Frameshift.
AL671894 Genomic DNA. Translation: CAM20609.1.
BC099408 mRNA. Translation: AAH99408.1.
BC128494 mRNA. Translation: AAI28495.1.
BC128495 mRNA. Translation: AAI28496.1.
CCDSiCCDS38602.1. [Q8CAE2-1]
RefSeqiNP_001072114.1. NM_001078646.1. [Q8CAE2-1]
NP_079999.2. NM_025723.2. [Q8CAE2-1]
XP_006501960.1. XM_006501897.2. [Q8CAE2-1]
XP_006501961.1. XM_006501898.2. [Q8CAE2-2]
UniGeneiMm.158124.

Genome annotation databases

EnsembliENSMUST00000059946; ENSMUSP00000054829; ENSMUSG00000045662. [Q8CAE2-1]
ENSMUST00000106586; ENSMUSP00000102196; ENSMUSG00000045662. [Q8CAE2-1]
ENSMUST00000196533; ENSMUSP00000143574; ENSMUSG00000045662. [Q8CAE2-2]
GeneIDi66715.
KEGGimmu:66715.
UCSCiuc008qzz.1. mouse. [Q8CAE2-1]
uc008rab.1. mouse. [Q8CAE2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038994 mRNA. Translation: BAC30196.1.
AK085587 mRNA. Translation: BAC39480.1. Frameshift.
AL671894 Genomic DNA. Translation: CAM20609.1.
BC099408 mRNA. Translation: AAH99408.1.
BC128494 mRNA. Translation: AAI28495.1.
BC128495 mRNA. Translation: AAI28496.1.
CCDSiCCDS38602.1. [Q8CAE2-1]
RefSeqiNP_001072114.1. NM_001078646.1. [Q8CAE2-1]
NP_079999.2. NM_025723.2. [Q8CAE2-1]
XP_006501960.1. XM_006501897.2. [Q8CAE2-1]
XP_006501961.1. XM_006501898.2. [Q8CAE2-2]
UniGeneiMm.158124.

3D structure databases

ProteinModelPortaliQ8CAE2.
SMRiQ8CAE2. Positions 27-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000054829.

PTM databases

PhosphoSiteiQ8CAE2.

Proteomic databases

PaxDbiQ8CAE2.
PRIDEiQ8CAE2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059946; ENSMUSP00000054829; ENSMUSG00000045662. [Q8CAE2-1]
ENSMUST00000106586; ENSMUSP00000102196; ENSMUSG00000045662. [Q8CAE2-1]
ENSMUST00000196533; ENSMUSP00000143574; ENSMUSG00000045662. [Q8CAE2-2]
GeneIDi66715.
KEGGimmu:66715.
UCSCiuc008qzz.1. mouse. [Q8CAE2-1]
uc008rab.1. mouse. [Q8CAE2-2]

Organism-specific databases

CTDi113802.
MGIiMGI:1913965. Henmt1.

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
GeneTreeiENSGT00390000004798.
HOVERGENiHBG097349.
InParanoidiQ8CAE2.
OMAiMEFQTWA.
OrthoDBiEOG7RNK1Q.
PhylomeDBiQ8CAE2.
TreeFamiTF315178.

Miscellaneous databases

NextBioi322453.
PROiQ8CAE2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CAE2.
CleanExiMM_4921515J06RIK.
ExpressionAtlasiQ8CAE2. baseline and differential.
GenevisibleiQ8CAE2. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR026610. Hen1.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR21404. PTHR21404. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Hypothalamus and Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-355 (ISOFORM 2).
    Tissue: Oocyte.
  4. "2'-O-methyl modification in mouse piRNAs and its methylase."
    Kirino Y., Mourelatos Z.
    Nucleic Acids Symp. Ser. 51:417-418(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  5. "The mouse homolog of HEN1 is a potential methylase for Piwi-interacting RNAs."
    Kirino Y., Mourelatos Z.
    RNA 13:1397-1401(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF 54-ASP--GLY-58.

Entry informationi

Entry nameiHENMT_MOUSE
AccessioniPrimary (citable) accession number: Q8CAE2
Secondary accession number(s): A2VCS5, Q8C3K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
  3. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.