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Small RNA 2'-O-methyltransferase (EC 2.1.1.n8) (HEN1 methyltransferase homolog 1)

 HENMT_HUMAN             Reviewed;         393 AA.
Q5T8I9; A8MRR6; B1AM16; B1AM17; Q96EJ7; Q96NN0;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
27-SEP-2017, entry version 97.
RecName: Full=Small RNA 2'-O-methyltransferase;
EC=2.1.1.n8 {ECO:0000250|UniProtKB:Q8CAE2};
AltName: Full=HEN1 methyltransferase homolog 1;
Name=HENMT1; Synonyms=C1orf59;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-361.
TISSUE=Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 14-262 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE.
Walker J.R., Zeng H., Dong A., Li Y., Wernimont A., Bountra C.,
Arrowsmith C.H., Edwards A.M., Brown P.J., Wu H.;
"Crystal structure of human C1ORF59 in complex with SAH.";
Submitted (DEC-2014) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:Q8CAE2}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + small RNA = S-
adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-
methylnucleotide. {ECO:0000250|UniProtKB:Q8CAE2}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9C5Q8};
-!- INTERACTION:
P14079:tax (xeno); NbExp=3; IntAct=EBI-9675710, EBI-9675698;
Q12933:TRAF2; NbExp=3; IntAct=EBI-9675710, EBI-355744;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}.
Note=Component of the meiotic nuage, also named P granule, a germ-
cell-specific organelle required to repress transposon activity
during meiosis. {ECO:0000250|UniProtKB:Q568P9}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI12930.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI12931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK055087; BAB70852.1; -; mRNA.
EMBL; AL160171; CAI12929.1; -; Genomic_DNA.
EMBL; AL160171; CAI12930.1; ALT_SEQ; Genomic_DNA.
EMBL; AL160171; CAI12931.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471122; EAW56326.1; -; Genomic_DNA.
EMBL; BC012198; AAH12198.1; -; mRNA.
EMBL; BC088366; AAH88366.1; -; mRNA.
CCDS; CCDS787.1; -.
RefSeq; NP_001096062.1; NM_001102592.1.
RefSeq; NP_653185.2; NM_144584.2.
UniGene; Hs.7962; -.
PDB; 4XCX; X-ray; 2.84 A; A=14-262.
PDBsum; 4XCX; -.
ProteinModelPortal; Q5T8I9; -.
SMR; Q5T8I9; -.
BioGrid; 125261; 10.
IntAct; Q5T8I9; 2.
STRING; 9606.ENSP00000359049; -.
iPTMnet; Q5T8I9; -.
PhosphoSitePlus; Q5T8I9; -.
BioMuta; HENMT1; -.
DMDM; 74745527; -.
EPD; Q5T8I9; -.
MaxQB; Q5T8I9; -.
PaxDb; Q5T8I9; -.
PeptideAtlas; Q5T8I9; -.
PRIDE; Q5T8I9; -.
DNASU; 113802; -.
Ensembl; ENST00000370032; ENSP00000359049; ENSG00000162639.
Ensembl; ENST00000402983; ENSP00000385655; ENSG00000162639.
GeneID; 113802; -.
KEGG; hsa:113802; -.
UCSC; uc001dvt.5; human.
CTD; 113802; -.
DisGeNET; 113802; -.
EuPathDB; HostDB:ENSG00000162639.15; -.
GeneCards; HENMT1; -.
HGNC; HGNC:26400; HENMT1.
HPA; HPA028464; -.
HPA; HPA028497; -.
MIM; 612178; gene.
neXtProt; NX_Q5T8I9; -.
OpenTargets; ENSG00000162639; -.
PharmGKB; PA128394748; -.
eggNOG; KOG1045; Eukaryota.
eggNOG; ENOG410XSD6; LUCA.
GeneTree; ENSGT00390000004798; -.
HOGENOM; HOG000049068; -.
HOVERGEN; HBG097349; -.
KO; K20798; -.
PhylomeDB; Q5T8I9; -.
TreeFam; TF315178; -.
Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
ChiTaRS; HENMT1; human.
GenomeRNAi; 113802; -.
PRO; PR:Q5T8I9; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162639; -.
CleanEx; HS_C1orf59; -.
ExpressionAtlas; Q5T8I9; baseline and differential.
Genevisible; Q5T8I9; HS.
GO; GO:0043186; C:P granule; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008171; F:O-methyltransferase activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
GO; GO:0001510; P:RNA methylation; ISS:UniProtKB.
InterPro; IPR026610; Hen1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21404; PTHR21404; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Metal-binding;
Methyltransferase; Polymorphism; Reference proteome; RNA-binding;
RNA-mediated gene silencing; S-adenosyl-L-methionine; Transferase.
CHAIN 1 393 Small RNA 2'-O-methyltransferase.
/FTId=PRO_0000304139.
METAL 132 132 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 135 135 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 136 136 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 181 181 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 36 36 S-adenosyl-L-methionine.
{ECO:0000244|PDB:4XCX,
ECO:0000269|Ref.5}.
BINDING 55 55 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:4XCX,
ECO:0000269|Ref.5}.
BINDING 78 78 S-adenosyl-L-methionine.
{ECO:0000244|PDB:4XCX,
ECO:0000269|Ref.5}.
BINDING 83 83 S-adenosyl-L-methionine.
{ECO:0000244|PDB:4XCX,
ECO:0000269|Ref.5}.
BINDING 115 115 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000244|PDB:4XCX}.
BINDING 131 131 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:4XCX}.
VARIANT 129 129 T -> A (in dbSNP:rs9988420).
/FTId=VAR_035017.
VARIANT 230 230 R -> Q (in dbSNP:rs35974434).
/FTId=VAR_035018.
VARIANT 361 361 M -> I (in dbSNP:rs17850887).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_035019.
CONFLICT 154 154 S -> F (in Ref. 1; BAB70852).
{ECO:0000305}.
CONFLICT 365 365 V -> A (in Ref. 1; BAB70852).
{ECO:0000305}.
HELIX 31 46 {ECO:0000244|PDB:4XCX}.
STRAND 49 54 {ECO:0000244|PDB:4XCX}.
HELIX 60 65 {ECO:0000244|PDB:4XCX}.
STRAND 72 79 {ECO:0000244|PDB:4XCX}.
HELIX 82 84 {ECO:0000244|PDB:4XCX}.
HELIX 89 91 {ECO:0000244|PDB:4XCX}.
HELIX 95 99 {ECO:0000244|PDB:4XCX}.
STRAND 102 104 {ECO:0000244|PDB:4XCX}.
STRAND 107 112 {ECO:0000244|PDB:4XCX}.
HELIX 120 122 {ECO:0000244|PDB:4XCX}.
STRAND 126 132 {ECO:0000244|PDB:4XCX}.
HELIX 134 136 {ECO:0000244|PDB:4XCX}.
HELIX 139 149 {ECO:0000244|PDB:4XCX}.
TURN 150 153 {ECO:0000244|PDB:4XCX}.
STRAND 156 163 {ECO:0000244|PDB:4XCX}.
HELIX 165 167 {ECO:0000244|PDB:4XCX}.
HELIX 187 200 {ECO:0000244|PDB:4XCX}.
STRAND 203 210 {ECO:0000244|PDB:4XCX}.
HELIX 218 220 {ECO:0000244|PDB:4XCX}.
STRAND 223 231 {ECO:0000244|PDB:4XCX}.
STRAND 250 257 {ECO:0000244|PDB:4XCX}.
SEQUENCE 393 AA; 44525 MW; 897A46664A44F6C5 CRC64;
MEENNLQCSS VVDGNFEEVP RETAIQFKPP LYRQRYQFVK NLVDQHEPKK VADLGCGDTS
LLRLLKVNPC IELLVGVDIN EDKLRWRGDS LAPFLGDFLK PRDLNLTITL YHGSVVERDS
RLLGFDLITC IELIEHLDSG DLARFPEVVF GYLSPSMIVI STPNSEFNPL FPSVTLRDSD
HKFEWTRMEF QTWALYVANR YDYSVEFTGV GEPPAGAENV GYCTQIGIFR KNGGKATESC
LSEQHDQHVY KAVFTTSYPS LQQERFFKLV LVNEVSQQVE SLRVSHLPRR KEQAGERGDK
PKDIGGSKAP VPCFGPVFTE VEKAKIENSP TPFCVGDKFF VPLQRLLAYP KLNRLCANEE
MMRSVIADSI PLSSDGSAVV ADLRNYFDEQ FEF


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