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
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601S-adenosyl-L-methionineBy similarity
Binding sitei78 – 781S-adenosyl-L-methionineBy similarity
Binding sitei114 – 1141S-adenosyl-L-methionineBy similarity
Metal bindingi132 – 1321MagnesiumBy similarity
Metal bindingi135 – 1351MagnesiumBy similarity
Metal bindingi136 – 1361Magnesium; via tele nitrogenBy similarity
Metal bindingi181 – 1811Magnesium; via tele nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

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

Enzyme and pathway databases

ReactomeiR-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Small RNA 2'-O-methyltransferase (EC:2.1.1.n8)
Alternative name(s):
HEN1 methyltransferase homolog 1
Gene namesi
Name:HENMT1
Synonyms:C1orf59
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26400. 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

Organism-specific databases

PharmGKBiPA128394748.

Polymorphism and mutation databases

BioMutaiHENMT1.
DMDMi74745527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Small RNA 2'-O-methyltransferasePRO_0000304139Add
BLAST

Proteomic databases

EPDiQ5T8I9.
MaxQBiQ5T8I9.
PaxDbiQ5T8I9.
PRIDEiQ5T8I9.

PTM databases

iPTMnetiQ5T8I9.
PhosphoSiteiQ5T8I9.

Expressioni

Gene expression databases

BgeeiQ5T8I9.
CleanExiHS_C1orf59.
ExpressionAtlasiQ5T8I9. baseline and differential.
GenevisibleiQ5T8I9. HS.

Organism-specific databases

HPAiHPA028464.
HPA028497.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
taxP140793EBI-9675710,EBI-9675698From a different organism.
TRAF2Q129333EBI-9675710,EBI-355744

Protein-protein interaction databases

BioGridi125261. 9 interactions.
IntActiQ5T8I9. 2 interactions.
STRINGi9606.ENSP00000359049.

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4616Combined sources
Beta strandi49 – 546Combined sources
Helixi60 – 656Combined sources
Beta strandi72 – 798Combined sources
Helixi82 – 843Combined sources
Helixi89 – 913Combined sources
Helixi95 – 995Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi107 – 1126Combined sources
Helixi120 – 1223Combined sources
Beta strandi126 – 1327Combined sources
Helixi134 – 1363Combined sources
Helixi139 – 14911Combined sources
Turni150 – 1534Combined sources
Beta strandi156 – 1638Combined sources
Helixi165 – 1673Combined sources
Helixi187 – 20014Combined sources
Beta strandi203 – 2108Combined sources
Helixi218 – 2203Combined sources
Beta strandi223 – 2319Combined sources
Beta strandi250 – 2578Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XCXX-ray2.84A14-262[»]
ProteinModelPortaliQ5T8I9.
SMRiQ5T8I9. Positions 26-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
GeneTreeiENSGT00390000004798.
HOGENOMiHOG000049068.
HOVERGENiHBG097349.
OrthoDBiEOG7RNK1Q.
PhylomeDBiQ5T8I9.
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.

Sequencei

Sequence statusi: Complete.

Q5T8I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEENNLQCSS VVDGNFEEVP RETAIQFKPP LYRQRYQFVK NLVDQHEPKK
60 70 80 90 100
VADLGCGDTS LLRLLKVNPC IELLVGVDIN EDKLRWRGDS LAPFLGDFLK
110 120 130 140 150
PRDLNLTITL YHGSVVERDS RLLGFDLITC IELIEHLDSG DLARFPEVVF
160 170 180 190 200
GYLSPSMIVI STPNSEFNPL FPSVTLRDSD HKFEWTRMEF QTWALYVANR
210 220 230 240 250
YDYSVEFTGV GEPPAGAENV GYCTQIGIFR KNGGKATESC LSEQHDQHVY
260 270 280 290 300
KAVFTTSYPS LQQERFFKLV LVNEVSQQVE SLRVSHLPRR KEQAGERGDK
310 320 330 340 350
PKDIGGSKAP VPCFGPVFTE VEKAKIENSP TPFCVGDKFF VPLQRLLAYP
360 370 380 390
KLNRLCANEE MMRSVIADSI PLSSDGSAVV ADLRNYFDEQ FEF
Length:393
Mass (Da):44,525
Last modified:December 21, 2004 - v1
Checksum:i897A46664A44F6C5
GO

Sequence cautioni

The sequence CAI12930.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI12931.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541S → F in BAB70852 (PubMed:14702039).Curated
Sequence conflicti365 – 3651V → A in BAB70852 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291T → A.
Corresponds to variant rs9988420 [ dbSNP | Ensembl ].
VAR_035017
Natural varianti230 – 2301R → Q.
Corresponds to variant rs35974434 [ dbSNP | Ensembl ].
VAR_035018
Natural varianti361 – 3611M → I.1 Publication
Corresponds to variant rs17850887 [ dbSNP | Ensembl ].
VAR_035019

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055087 mRNA. Translation: BAB70852.1.
AL160171 Genomic DNA. Translation: CAI12929.1.
AL160171 Genomic DNA. Translation: CAI12930.1. Sequence problems.
AL160171 Genomic DNA. Translation: CAI12931.1. Sequence problems.
CH471122 Genomic DNA. Translation: EAW56326.1.
BC012198 mRNA. Translation: AAH12198.1.
BC088366 mRNA. Translation: AAH88366.1.
CCDSiCCDS787.1.
RefSeqiNP_001096062.1. NM_001102592.1.
NP_653185.2. NM_144584.2.
UniGeneiHs.7962.

Genome annotation databases

EnsembliENST00000370032; ENSP00000359049; ENSG00000162639.
ENST00000402983; ENSP00000385655; ENSG00000162639.
GeneIDi113802.
KEGGihsa:113802.
UCSCiuc001dvt.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055087 mRNA. Translation: BAB70852.1.
AL160171 Genomic DNA. Translation: CAI12929.1.
AL160171 Genomic DNA. Translation: CAI12930.1. Sequence problems.
AL160171 Genomic DNA. Translation: CAI12931.1. Sequence problems.
CH471122 Genomic DNA. Translation: EAW56326.1.
BC012198 mRNA. Translation: AAH12198.1.
BC088366 mRNA. Translation: AAH88366.1.
CCDSiCCDS787.1.
RefSeqiNP_001096062.1. NM_001102592.1.
NP_653185.2. NM_144584.2.
UniGeneiHs.7962.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4XCXX-ray2.84A14-262[»]
ProteinModelPortaliQ5T8I9.
SMRiQ5T8I9. Positions 26-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125261. 9 interactions.
IntActiQ5T8I9. 2 interactions.
STRINGi9606.ENSP00000359049.

PTM databases

iPTMnetiQ5T8I9.
PhosphoSiteiQ5T8I9.

Polymorphism and mutation databases

BioMutaiHENMT1.
DMDMi74745527.

Proteomic databases

EPDiQ5T8I9.
MaxQBiQ5T8I9.
PaxDbiQ5T8I9.
PRIDEiQ5T8I9.

Protocols and materials databases

DNASUi113802.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370032; ENSP00000359049; ENSG00000162639.
ENST00000402983; ENSP00000385655; ENSG00000162639.
GeneIDi113802.
KEGGihsa:113802.
UCSCiuc001dvt.5. human.

Organism-specific databases

CTDi113802.
GeneCardsiHENMT1.
HGNCiHGNC:26400. HENMT1.
HPAiHPA028464.
HPA028497.
MIMi612178. gene.
neXtProtiNX_Q5T8I9.
PharmGKBiPA128394748.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1045. Eukaryota.
ENOG410XSD6. LUCA.
GeneTreeiENSGT00390000004798.
HOGENOMiHOG000049068.
HOVERGENiHBG097349.
OrthoDBiEOG7RNK1Q.
PhylomeDBiQ5T8I9.
TreeFamiTF315178.

Enzyme and pathway databases

ReactomeiR-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.

Miscellaneous databases

ChiTaRSiHENMT1. human.
GenomeRNAii113802.
NextBioi78910.
PROiQ5T8I9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T8I9.
CleanExiHS_C1orf59.
ExpressionAtlasiQ5T8I9. baseline and differential.
GenevisibleiQ5T8I9. HS.

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

  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ILE-361.
    Tissue: Skin and Testis.

Entry informationi

Entry nameiHENMT_HUMAN
AccessioniPrimary (citable) accession number: Q5T8I9
Secondary accession number(s): A8MRR6
, B1AM16, B1AM17, Q96EJ7, Q96NN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: March 16, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.