HENMT_HUMAN
ID HENMT_HUMAN Reviewed; 393 AA.
AC Q5T8I9; A8MRR6; B1AM16; B1AM17; Q96EJ7; Q96NN0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8 {ECO:0000250|UniProtKB:Q8CAE2};
DE AltName: Full=HEN1 methyltransferase homolog 1;
GN Name=HENMT1; Synonyms=C1orf59;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-361.
RC TISSUE=Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 14-262 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RA Walker J.R., Zeng H., Dong A., Li Y., Wernimont A., Bountra C.,
RA Arrowsmith C.H., Edwards A.M., Brown P.J., Wu H.;
RT "Crystal structure of human C1ORF59 in complex with SAH.";
RL Submitted (DEC-2014) to the PDB data bank.
CC -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a
CC Dicer-independent mechanism and are primarily derived from transposons
CC and other repeated sequence elements. This probably protects the 3'-end
CC of piRNAs from uridylation activity and subsequent degradation.
CC Stabilization of piRNAs is essential for gametogenesis.
CC {ECO:0000250|UniProtKB:Q8CAE2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.n8;
CC Evidence={ECO:0000250|UniProtKB:Q8CAE2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9C5Q8};
CC -!- INTERACTION:
CC Q5T8I9; Q96LY2-2: CCDC74B; NbExp=3; IntAct=EBI-9675710, EBI-17967022;
CC Q5T8I9; Q0VD86: INCA1; NbExp=3; IntAct=EBI-9675710, EBI-6509505;
CC Q5T8I9; Q12933: TRAF2; NbExp=3; IntAct=EBI-9675710, EBI-355744;
CC Q5T8I9; P14079: tax; Xeno; NbExp=3; IntAct=EBI-9675710, EBI-9675698;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q568P9}.
CC Note=Component of the meiotic nuage, also named P granule, a germ-cell-
CC specific organelle required to repress transposon activity during
CC meiosis. {ECO:0000250|UniProtKB:Q568P9}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
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DR EMBL; AK055087; BAB70852.1; -; mRNA.
DR EMBL; AL160171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56326.1; -; Genomic_DNA.
DR EMBL; BC012198; AAH12198.1; -; mRNA.
DR EMBL; BC088366; AAH88366.1; -; mRNA.
DR CCDS; CCDS787.1; -.
DR RefSeq; NP_001096062.1; NM_001102592.1.
DR RefSeq; NP_653185.2; NM_144584.2.
DR PDB; 4XCX; X-ray; 2.84 A; A=14-262.
DR PDB; 5WY0; X-ray; 2.00 A; A=31-258.
DR PDBsum; 4XCX; -.
DR PDBsum; 5WY0; -.
DR AlphaFoldDB; Q5T8I9; -.
DR SMR; Q5T8I9; -.
DR BioGRID; 125261; 11.
DR IntAct; Q5T8I9; 12.
DR MINT; Q5T8I9; -.
DR STRING; 9606.ENSP00000359049; -.
DR iPTMnet; Q5T8I9; -.
DR PhosphoSitePlus; Q5T8I9; -.
DR BioMuta; HENMT1; -.
DR DMDM; 74745527; -.
DR EPD; Q5T8I9; -.
DR jPOST; Q5T8I9; -.
DR MassIVE; Q5T8I9; -.
DR MaxQB; Q5T8I9; -.
DR PaxDb; Q5T8I9; -.
DR PeptideAtlas; Q5T8I9; -.
DR PRIDE; Q5T8I9; -.
DR ProteomicsDB; 64735; -.
DR Antibodypedia; 33732; 50 antibodies from 15 providers.
DR DNASU; 113802; -.
DR Ensembl; ENST00000370032.9; ENSP00000359049.5; ENSG00000162639.16.
DR Ensembl; ENST00000402983.5; ENSP00000385655.1; ENSG00000162639.16.
DR Ensembl; ENST00000651461.1; ENSP00000499017.1; ENSG00000162639.16.
DR GeneID; 113802; -.
DR KEGG; hsa:113802; -.
DR MANE-Select; ENST00000651461.1; ENSP00000499017.1; NM_001102592.2; NP_001096062.1.
DR UCSC; uc001dvt.5; human.
DR CTD; 113802; -.
DR DisGeNET; 113802; -.
DR GeneCards; HENMT1; -.
DR HGNC; HGNC:26400; HENMT1.
DR HPA; ENSG00000162639; Tissue enhanced (testis).
DR MIM; 612178; gene.
DR neXtProt; NX_Q5T8I9; -.
DR OpenTargets; ENSG00000162639; -.
DR PharmGKB; PA128394748; -.
DR VEuPathDB; HostDB:ENSG00000162639; -.
DR eggNOG; KOG1045; Eukaryota.
DR GeneTree; ENSGT00390000004798; -.
DR HOGENOM; CLU_044646_0_0_1; -.
DR OMA; QRHQFVV; -.
DR OrthoDB; 789470at2759; -.
DR PhylomeDB; Q5T8I9; -.
DR TreeFam; TF315178; -.
DR PathwayCommons; Q5T8I9; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q5T8I9; -.
DR BioGRID-ORCS; 113802; 21 hits in 1069 CRISPR screens.
DR ChiTaRS; HENMT1; human.
DR GenomeRNAi; 113802; -.
DR Pharos; Q5T8I9; Tdark.
DR PRO; PR:Q5T8I9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5T8I9; protein.
DR Bgee; ENSG00000162639; Expressed in oocyte and 157 other tissues.
DR ExpressionAtlas; Q5T8I9; baseline and differential.
DR Genevisible; Q5T8I9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IDA:FlyBase.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IDA:FlyBase.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; PTHR21404; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Magnesium; Metal-binding; Methyltransferase;
KW Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..393
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000304139"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4XCX"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4XCX"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4XCX"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4XCX"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:4XCX"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:4XCX"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT VARIANT 129
FT /note="T -> A (in dbSNP:rs9988420)"
FT /id="VAR_035017"
FT VARIANT 230
FT /note="R -> Q (in dbSNP:rs35974434)"
FT /id="VAR_035018"
FT VARIANT 361
FT /note="M -> I (in dbSNP:rs17850887)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035019"
FT CONFLICT 154
FT /note="S -> F (in Ref. 1; BAB70852)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="V -> A (in Ref. 1; BAB70852)"
FT /evidence="ECO:0000305"
FT HELIX 31..46
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4XCX"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:4XCX"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4XCX"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5WY0"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4XCX"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:5WY0"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:4XCX"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:5WY0"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:5WY0"
SQ 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
