MT21C_HUMAN
ID MT21C_HUMAN Reviewed; 264 AA.
AC Q5VZV1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein-lysine methyltransferase METTL21C;
DE EC=2.1.1.-;
DE AltName: Full=Methyltransferase-like protein 21C;
GN Name=METTL21C; Synonyms=C13orf39;
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, AND MUTAGENESIS OF ASP-141.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
RN [4]
RP INTERACTION WITH HSP70 FAMILY 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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 22-264 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RA Hong B.S., Tempel W., Dong A., Li Y., Arrowsmith C.H., Bountra C.,
RA Edwards A.M., Brown P.J.;
RT "Human methyltransferase-like protein 21C.";
RL Submitted (SEP-2013) to the PDB data bank.
CC -!- FUNCTION: Protein-lysine methyltransferase.
CC {ECO:0000269|PubMed:22948820}.
CC -!- SUBUNIT: Interacts with members of the heat shock protein 70 families;
CC these proteins may possibly be methylation substrates for the enzyme.
CC {ECO:0000269|PubMed:23349634}.
CC -!- INTERACTION:
CC Q5VZV1; Q15369: ELOC; NbExp=9; IntAct=EBI-10236049, EBI-301231;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23349634}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; AL158063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132748; AAI32749.1; -; mRNA.
DR EMBL; BC132750; AAI32751.1; -; mRNA.
DR CCDS; CCDS32003.1; -.
DR RefSeq; NP_001010977.1; NM_001010977.2.
DR RefSeq; XP_016875896.1; XM_017020407.1.
DR RefSeq; XP_016875897.1; XM_017020408.1.
DR PDB; 4MTL; X-ray; 1.65 A; A/B=22-264.
DR PDBsum; 4MTL; -.
DR AlphaFoldDB; Q5VZV1; -.
DR SMR; Q5VZV1; -.
DR BioGRID; 128220; 19.
DR IntAct; Q5VZV1; 2.
DR STRING; 9606.ENSP00000267273; -.
DR iPTMnet; Q5VZV1; -.
DR PhosphoSitePlus; Q5VZV1; -.
DR BioMuta; METTL21C; -.
DR DMDM; 74757117; -.
DR MassIVE; Q5VZV1; -.
DR MaxQB; Q5VZV1; -.
DR PaxDb; Q5VZV1; -.
DR PeptideAtlas; Q5VZV1; -.
DR PRIDE; Q5VZV1; -.
DR ProteomicsDB; 65729; -.
DR Antibodypedia; 25326; 123 antibodies from 15 providers.
DR DNASU; 196541; -.
DR Ensembl; ENST00000267273.7; ENSP00000267273.5; ENSG00000139780.8.
DR GeneID; 196541; -.
DR KEGG; hsa:196541; -.
DR MANE-Select; ENST00000267273.7; ENSP00000267273.5; NM_001010977.3; NP_001010977.1.
DR UCSC; uc001vpj.5; human.
DR CTD; 196541; -.
DR DisGeNET; 196541; -.
DR GeneCards; METTL21C; -.
DR HGNC; HGNC:33717; METTL21C.
DR HPA; ENSG00000139780; Tissue enriched (epididymis).
DR MIM; 615259; gene.
DR neXtProt; NX_Q5VZV1; -.
DR OpenTargets; ENSG00000139780; -.
DR PharmGKB; PA162378126; -.
DR VEuPathDB; HostDB:ENSG00000139780; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000156596; -.
DR HOGENOM; CLU_055721_0_0_1; -.
DR InParanoid; Q5VZV1; -.
DR OMA; AYLCQPG; -.
DR OrthoDB; 1494909at2759; -.
DR PhylomeDB; Q5VZV1; -.
DR TreeFam; TF354267; -.
DR PathwayCommons; Q5VZV1; -.
DR SignaLink; Q5VZV1; -.
DR SIGNOR; Q5VZV1; -.
DR BioGRID-ORCS; 196541; 7 hits in 1057 CRISPR screens.
DR ChiTaRS; METTL21C; human.
DR GenomeRNAi; 196541; -.
DR Pharos; Q5VZV1; Tbio.
DR PRO; PR:Q5VZV1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q5VZV1; protein.
DR Bgee; ENSG00000139780; Expressed in hindlimb stylopod muscle and 45 other tissues.
DR Genevisible; Q5VZV1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:UniProtKB.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..264
FT /note="Protein-lysine methyltransferase METTL21C"
FT /id="PRO_0000319590"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 120..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.5"
FT VARIANT 15
FT /note="G -> R (in dbSNP:rs2390760)"
FT /id="VAR_062229"
FT VARIANT 46
FT /note="N -> S (in dbSNP:rs16960383)"
FT /id="VAR_039013"
FT MUTAGEN 141
FT /note="D->A: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22948820"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4MTL"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:4MTL"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:4MTL"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:4MTL"
FT HELIX 228..240
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:4MTL"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:4MTL"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:4MTL"
SQ SEQUENCE 264 AA; 29565 MW; 239B4B24D62DC1D0 CRC64;
MDVCLSSAQQ PGRRGEGLSS PGGWLEAEKK GAPQKDSTGG VLEESNKIEP SLHSLQKFVP
TDYASYTQEH YRFAGKEIVI QESIESYGAV VWPGAMALCQ YLEEHAEELN FQDAKILEIG
AGPGLVSIVA SILGAQVTAT DLPDVLGNLQ YNLLKNTLQC TAHLPEVKEL VWGEDLDKNF
PKSAFYYDYV LASDVVYHHY FLDKLLTTMV YLSQPGTVLL WANKFRFSTD YEFLDKFKQV
FDTTLLAEYP ESSVKLFKGI LKWD
