MET22_HUMAN
ID MET22_HUMAN Reviewed; 404 AA.
AC Q9BUU2; B2RD29; D3DUF2; Q6XYB4; Q9HA03;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Methyltransferase-like protein 22;
DE EC=2.1.1.- {ECO:0000269|PubMed:23349634};
GN Name=METTL22; Synonyms=C16orf68; ORFNames=LP8272;
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] (ISOFORM 2).
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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT THR-366.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH HSP70 AND HSP90 FAMILY
RP MEMBERS, AND SUBCELLULAR LOCATION.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Protein N-lysine methyltransferase. Trimethylates KIN at Lys-
CC 135 (in vitro). {ECO:0000269|PubMed:23349634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000269|PubMed:23349634};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000305|PubMed:23349634};
CC -!- SUBUNIT: Interacts with members of the heat shock protein 90 and 70
CC families; these proteins probably are methylation substrates.
CC {ECO:0000269|PubMed:23349634}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23349634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BUU2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BUU2-2; Sequence=VSP_025107, VSP_025108;
CC Name=3;
CC IsoId=Q9BUU2-3; Sequence=VSP_025106;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL22
CC family. {ECO:0000305}.
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DR EMBL; AK022495; BAB14058.1; -; mRNA.
DR EMBL; AK315383; BAG37776.1; -; mRNA.
DR EMBL; AC007224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY203956; AAP34479.1; -; mRNA.
DR EMBL; CH471112; EAW85210.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85211.1; -; Genomic_DNA.
DR EMBL; BC001908; AAH01908.1; -; mRNA.
DR CCDS; CCDS10533.2; -. [Q9BUU2-1]
DR RefSeq; NP_077014.3; NM_024109.3. [Q9BUU2-1]
DR AlphaFoldDB; Q9BUU2; -.
DR SMR; Q9BUU2; -.
DR BioGRID; 122539; 26.
DR IntAct; Q9BUU2; 3.
DR STRING; 9606.ENSP00000371345; -.
DR iPTMnet; Q9BUU2; -.
DR PhosphoSitePlus; Q9BUU2; -.
DR BioMuta; METTL22; -.
DR DMDM; 147639349; -.
DR EPD; Q9BUU2; -.
DR jPOST; Q9BUU2; -.
DR MassIVE; Q9BUU2; -.
DR MaxQB; Q9BUU2; -.
DR PaxDb; Q9BUU2; -.
DR PeptideAtlas; Q9BUU2; -.
DR PRIDE; Q9BUU2; -.
DR ProteomicsDB; 79130; -. [Q9BUU2-1]
DR ProteomicsDB; 79131; -. [Q9BUU2-2]
DR ProteomicsDB; 79132; -. [Q9BUU2-3]
DR Antibodypedia; 51872; 32 antibodies from 11 providers.
DR DNASU; 79091; -.
DR Ensembl; ENST00000163678.11; ENSP00000163678.6; ENSG00000067365.15. [Q9BUU2-2]
DR Ensembl; ENST00000381920.8; ENSP00000371345.3; ENSG00000067365.15. [Q9BUU2-1]
DR GeneID; 79091; -.
DR KEGG; hsa:79091; -.
DR MANE-Select; ENST00000381920.8; ENSP00000371345.3; NM_024109.4; NP_077014.4.
DR UCSC; uc002czb.4; human. [Q9BUU2-1]
DR CTD; 79091; -.
DR GeneCards; METTL22; -.
DR HGNC; HGNC:28368; METTL22.
DR HPA; ENSG00000067365; Low tissue specificity.
DR MIM; 615261; gene.
DR neXtProt; NX_Q9BUU2; -.
DR OpenTargets; ENSG00000067365; -.
DR PharmGKB; PA144596479; -.
DR VEuPathDB; HostDB:ENSG00000067365; -.
DR eggNOG; KOG2497; Eukaryota.
DR GeneTree; ENSGT00510000048539; -.
DR HOGENOM; CLU_097585_0_0_1; -.
DR InParanoid; Q9BUU2; -.
DR OMA; ITCEAYS; -.
DR OrthoDB; 1612133at2759; -.
DR PhylomeDB; Q9BUU2; -.
DR TreeFam; TF324844; -.
DR PathwayCommons; Q9BUU2; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; Q9BUU2; -.
DR BioGRID-ORCS; 79091; 7 hits in 1073 CRISPR screens.
DR ChiTaRS; METTL22; human.
DR GenomeRNAi; 79091; -.
DR Pharos; Q9BUU2; Tdark.
DR PRO; PR:Q9BUU2; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BUU2; protein.
DR Bgee; ENSG00000067365; Expressed in sperm and 158 other tissues.
DR ExpressionAtlas; Q9BUU2; baseline and differential.
DR Genevisible; Q9BUU2; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; TAS:Reactome.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR038899; METTL22.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23108; PTHR23108; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..404
FT /note="Methyltransferase-like protein 22"
FT /id="PRO_0000286591"
FT REGION 60..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_025106"
FT VAR_SEQ 172..205
FT /note="EHTMATPLEDVGKQVWRGALLLADYILFRQDLFR -> GVAGRPAPGRLHPV
FT PTGPLPRMYSAGARGRHGAR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025107"
FT VAR_SEQ 206..404
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025108"
FT VARIANT 59
FT /note="W -> S (in dbSNP:rs2270286)"
FT /id="VAR_032134"
FT VARIANT 219
FT /note="A -> T (in dbSNP:rs2302607)"
FT /id="VAR_032135"
FT VARIANT 366
FT /note="A -> T (in dbSNP:rs1731000)"
FT /evidence="ECO:0000269|PubMed:15498874"
FT /id="VAR_059623"
FT VARIANT 375
FT /note="E -> K (in dbSNP:rs55747257)"
FT /id="VAR_061617"
SQ SEQUENCE 404 AA; 44486 MW; 049135469B80D6F9 CRC64;
MVQLAPAAAM DEVTFRSDTV LSDVHLYTPN HRHLMVRLNS VGQPVFLSQF KLLWSQDSWT
DSGAKGGSHR DVHTKEPPSA ETGSTGSPPG SGHGNEGFSL QAGTDTTGQE VAEAQLDEDG
DLDVVRRPRA ASDSNPAGPL RDKVHPMILA QEEDDVLGEE AQGSPHDIIR IEHTMATPLE
DVGKQVWRGA LLLADYILFR QDLFRGCTAL ELGAGTGLAS IIAATMARTV YCTDVGADLL
SMCQRNIALN SHLAATGGGI VRVKELDWLK DDLCTDPKVP FSWSQEEISD LYDHTTILFA
AEVFYDDDLT DAVFKTLSRL AHRLKNACTA ILSVEKRLNF TLRHLDVTCE AYDHFRSCLH
ALEQLADGKL RFVVEPVEAS FPQLLVYERL QQLELWKIIA EPVT
