HEMK1_HUMAN
ID HEMK1_HUMAN Reviewed; 338 AA.
AC Q9Y5R4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=MTRF1L release factor glutamine methyltransferase {ECO:0000303|PubMed:18541145};
DE EC=2.1.1.297 {ECO:0000305|PubMed:18541145};
DE AltName: Full=HemK methyltransferase family member 1;
DE AltName: Full=M.HsaHemKP;
GN Name=HEMK1; Synonyms=HEMK;
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 [MRNA].
RC TISSUE=Placenta;
RA Zeng Y.G., Forgacs E., Lerman M.I., Minna J.D.;
RT "Human Hemk protein homolog located in the 3p21.3 homozygous deletion
RT region is a candidate tumor suppressor gene.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 SUBCELLULAR LOCATION.
RX PubMed=18541145; DOI=10.1016/j.bbrc.2008.05.176;
RA Ishizawa T., Nozaki Y., Ueda T., Takeuchi N.;
RT "The human mitochondrial translation release factor HMRF1L is methylated in
RT the GGQ motif by the methyltransferase HMPrmC.";
RL Biochem. Biophys. Res. Commun. 373:99-103(2008).
CC -!- FUNCTION: N5-glutamine methyltransferase responsible for the
CC methylation of the glutamine residue in the universally conserved GGQ
CC motif of the mitochondrial translation release factor MTRF1L.
CC {ECO:0000269|PubMed:18541145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-
CC methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release
CC factor] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42896, Rhea:RHEA-
CC COMP:10271, Rhea:RHEA-COMP:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61891; EC=2.1.1.297;
CC Evidence={ECO:0000305|PubMed:18541145};
CC -!- INTERACTION:
CC Q9Y5R4; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-10329202, EBI-357530;
CC Q9Y5R4; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-10329202, EBI-12108222;
CC Q9Y5R4; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10329202, EBI-396137;
CC Q9Y5R4; P15882: CHN1; NbExp=8; IntAct=EBI-10329202, EBI-718947;
CC Q9Y5R4; P78358: CTAG1B; NbExp=3; IntAct=EBI-10329202, EBI-1188472;
CC Q9Y5R4; Q15038: DAZAP2; NbExp=3; IntAct=EBI-10329202, EBI-724310;
CC Q9Y5R4; A2RTY3: HEATR9; NbExp=3; IntAct=EBI-10329202, EBI-13049042;
CC Q9Y5R4; Q0VD86: INCA1; NbExp=5; IntAct=EBI-10329202, EBI-6509505;
CC Q9Y5R4; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-10329202, EBI-12811111;
CC Q9Y5R4; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-10329202, EBI-716006;
CC Q9Y5R4; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-10329202, EBI-724639;
CC Q9Y5R4; Q16633: POU2AF1; NbExp=3; IntAct=EBI-10329202, EBI-943588;
CC Q9Y5R4; P28070: PSMB4; NbExp=3; IntAct=EBI-10329202, EBI-603350;
CC Q9Y5R4; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-10329202, EBI-748621;
CC Q9Y5R4; O15266-2: SHOX; NbExp=3; IntAct=EBI-10329202, EBI-12825957;
CC Q9Y5R4; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-10329202, EBI-12288855;
CC Q9Y5R4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-10329202, EBI-11959123;
CC Q9Y5R4; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-10329202, EBI-12408727;
CC Q9Y5R4; Q96RT8: TUBGCP5; NbExp=3; IntAct=EBI-10329202, EBI-2555061;
CC Q9Y5R4; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10329202, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18541145}.
CC -!- SIMILARITY: Belongs to the protein N5-glutamine methyltransferase
CC family. {ECO:0000305}.
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DR EMBL; AF131220; AAD26417.1; -; mRNA.
DR EMBL; AF172244; AAD51328.1; -; mRNA.
DR EMBL; BC000781; AAH00781.1; -; mRNA.
DR CCDS; CCDS2830.1; -.
DR RefSeq; NP_001304780.1; NM_001317851.1.
DR RefSeq; NP_057257.1; NM_016173.4.
DR AlphaFoldDB; Q9Y5R4; -.
DR SMR; Q9Y5R4; -.
DR BioGRID; 119527; 32.
DR IntAct; Q9Y5R4; 24.
DR STRING; 9606.ENSP00000404843; -.
DR iPTMnet; Q9Y5R4; -.
DR PhosphoSitePlus; Q9Y5R4; -.
DR BioMuta; HEMK1; -.
DR DMDM; 18203634; -.
DR EPD; Q9Y5R4; -.
DR jPOST; Q9Y5R4; -.
DR MassIVE; Q9Y5R4; -.
DR PaxDb; Q9Y5R4; -.
DR PeptideAtlas; Q9Y5R4; -.
DR PRIDE; Q9Y5R4; -.
DR ProteomicsDB; 86481; -.
DR Antibodypedia; 30986; 172 antibodies from 22 providers.
DR DNASU; 51409; -.
DR Ensembl; ENST00000232854.9; ENSP00000232854.4; ENSG00000114735.10.
DR Ensembl; ENST00000434410.5; ENSP00000404843.1; ENSG00000114735.10.
DR Ensembl; ENST00000455834.5; ENSP00000404334.1; ENSG00000114735.10.
DR GeneID; 51409; -.
DR KEGG; hsa:51409; -.
DR MANE-Select; ENST00000232854.9; ENSP00000232854.4; NM_016173.5; NP_057257.1.
DR UCSC; uc003dau.4; human.
DR CTD; 51409; -.
DR DisGeNET; 51409; -.
DR GeneCards; HEMK1; -.
DR HGNC; HGNC:24923; HEMK1.
DR HPA; ENSG00000114735; Low tissue specificity.
DR MIM; 618609; gene.
DR neXtProt; NX_Q9Y5R4; -.
DR OpenTargets; ENSG00000114735; -.
DR PharmGKB; PA134884011; -.
DR VEuPathDB; HostDB:ENSG00000114735; -.
DR eggNOG; KOG2904; Eukaryota.
DR GeneTree; ENSGT00390000014125; -.
DR HOGENOM; CLU_018398_4_1_1; -.
DR InParanoid; Q9Y5R4; -.
DR OMA; FDARYWE; -.
DR OrthoDB; 1513943at2759; -.
DR PhylomeDB; Q9Y5R4; -.
DR TreeFam; TF324423; -.
DR BRENDA; 2.1.1.297; 2681.
DR PathwayCommons; Q9Y5R4; -.
DR SignaLink; Q9Y5R4; -.
DR BioGRID-ORCS; 51409; 9 hits in 1079 CRISPR screens.
DR GenomeRNAi; 51409; -.
DR Pharos; Q9Y5R4; Tbio.
DR PRO; PR:Q9Y5R4; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y5R4; protein.
DR Bgee; ENSG00000114735; Expressed in right uterine tube and 179 other tissues.
DR ExpressionAtlas; Q9Y5R4; baseline and differential.
DR Genevisible; Q9Y5R4; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR GO; GO:0102559; F:protein-(glutamine-N5) methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0006306; P:DNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004556; HemK-like.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR040758; PrmC_N.
DR InterPro; IPR019874; Release_fac_Glu-N5_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF17827; PrmC_N; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00536; hemK_fam; 1.
DR TIGRFAMs; TIGR03534; RF_mod_PrmC; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..338
FT /note="MTRF1L release factor glutamine methyltransferase"
FT /id="PRO_0000157178"
FT BINDING 167..171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 239..242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT VARIANT 192
FT /note="R -> Q (in dbSNP:rs2232250)"
FT /id="VAR_049503"
FT VARIANT 200
FT /note="H -> Q (in dbSNP:rs2232251)"
FT /id="VAR_049504"
SQ SEQUENCE 338 AA; 38231 MW; 5AB5DF554D9978B4 CRC64;
MELWGRMLWA LLSGPGRRGS TRGWAFSSWQ PQPPLAGLSS AIELVSHWTG VFEKRGIPEA
RESSEYIVAH VLGAKTFQSL RPALWTQPLT SQQLQCIREL SSRRLQRMPV QYILGEWDFQ
GLSLRMVPPV FIPRPETEEL VEWVLEEVAQ RSHAVGSPGS PLILEVGCGS GAISLSLLSQ
LPQSRVIAVD KREAAISLTH ENAQRLRLQD RIWIIHLDMT SERSWTHLPW GPMDLIVSNP
PYVFHQDMEQ LAPEIRSYED PAALDGGEEG MDIITHILAL APRLLKDSGS IFLEVDPRHP
ELVSSWLQSR PDLYLNLVAV RRDFCGRPRF LHIRRSGP
