HPM1_YEAST
ID HPM1_YEAST Reviewed; 377 AA.
AC P40481; D6VVH7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Histidine protein methyltransferase 1 {ECO:0000303|PubMed:20864530};
DE EC=2.1.1.85 {ECO:0000269|PubMed:24865971};
DE AltName: Full=Mitotic exit network interactor 1;
GN Name=HPM1 {ECO:0000303|PubMed:20864530}; Synonyms=MNI1;
GN OrderedLocusNames=YIL110W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15166135; DOI=10.1534/genetics.167.1.35;
RA Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.;
RT "Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a
RT synthetic interaction network and altered sensitivity to caspofungin.";
RL Genetics 167:35-49(2004).
RN [6]
RP EFFECT OF GENE DELETION.
RX PubMed=16234568; DOI=10.1093/jnci/dji316;
RA Dilda P.J., Don A.S., Tanabe K.M., Higgins V.J., Allen J.D., Dawes I.W.,
RA Hogg P.J.;
RT "Mechanism of selectivity of an angiogenesis inhibitor from screening a
RT genome-wide set of Saccharomyces cerevisiae deletion strains.";
RL J. Natl. Cancer Inst. 97:1539-1547(2005).
RN [7]
RP FUNCTION.
RX PubMed=20864530; DOI=10.1074/jbc.m110.170787;
RA Webb K.J., Zurita-Lopez C.I., Al-Hadid Q., Laganowsky A., Young B.D.,
RA Lipson R.S., Souda P., Faull K.F., Whitelegge J.P., Clarke S.G.;
RT "A novel 3-methylhistidine modification of yeast ribosomal protein Rpl3 is
RT dependent upon the YIL110W methyltransferase.";
RL J. Biol. Chem. 285:37598-37606(2010).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24865971; DOI=10.1128/mcb.01634-13;
RA Al-Hadid Q., Roy K., Munroe W., Dzialo M.C., Chanfreau G.F., Clarke S.G.;
RT "Histidine methylation of yeast ribosomal protein Rpl3p is required for
RT proper 60S subunit assembly.";
RL Mol. Cell. Biol. 34:2903-2916(2014).
RN [9]
RP FUNCTION.
RX PubMed=26826131; DOI=10.1261/rna.054569.115;
RA Al-Hadid Q., Roy K., Chanfreau G., Clarke S.G.;
RT "Methylation of yeast ribosomal protein Rpl3 promotes translational
RT elongation fidelity.";
RL RNA 22:489-498(2016).
CC -!- FUNCTION: Protein-histidine N-methyltransferase that mediates
CC methylation of RPL3 at 'His-243' (PubMed:20864530, PubMed:24865971).
CC Methylates ribosome-associated RPL3, but not free RPL3, thereby
CC regulating 60S subunit assembly (PubMed:24865971, PubMed:26826131). In
CC addition to RPL3, mediates His methylation of other proteins
CC (PubMed:26826131). {ECO:0000269|PubMed:20864530,
CC ECO:0000269|PubMed:24865971, ECO:0000269|PubMed:26826131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC Evidence={ECO:0000305|PubMed:20864530};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Loss of Protein-histidine methylation
CC (PubMed:24865971). Impaired early rRNA processing, resulting in a
CC deficiency of 60S subunits and translation initiation defects
CC (PubMed:24865971). A haploid deletion mutant leads to hypersensitivity
CC to echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-
CC glucan synthase inhibitor. Deletion confers sensitivity to the
CC synthetic tripeptide arsenical 4-(N-(S-glutathionylacetyl)amino)
CC phenylarsenoxide (GSAO) (PubMed:15166135).
CC {ECO:0000269|PubMed:15166135, ECO:0000269|PubMed:24865971}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL18
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38125; CAA86270.1; -; Genomic_DNA.
DR EMBL; AY558076; AAS56402.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08443.1; -; Genomic_DNA.
DR PIR; S48462; S48462.
DR RefSeq; NP_012156.1; NM_001179458.1.
DR AlphaFoldDB; P40481; -.
DR SMR; P40481; -.
DR BioGRID; 34881; 151.
DR DIP; DIP-4710N; -.
DR IntAct; P40481; 1.
DR STRING; 4932.YIL110W; -.
DR MaxQB; P40481; -.
DR PaxDb; P40481; -.
DR PRIDE; P40481; -.
DR EnsemblFungi; YIL110W_mRNA; YIL110W; YIL110W.
DR GeneID; 854696; -.
DR KEGG; sce:YIL110W; -.
DR SGD; S000001372; HPM1.
DR VEuPathDB; FungiDB:YIL110W; -.
DR eggNOG; KOG2920; Eukaryota.
DR GeneTree; ENSGT00390000000464; -.
DR HOGENOM; CLU_038704_1_1_1; -.
DR InParanoid; P40481; -.
DR OMA; WRTFLPL; -.
DR BioCyc; YEAST:G3O-31365-MON; -.
DR PRO; PR:P40481; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40481; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0018064; F:protein-L-histidine N-tele-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042038; P:peptidyl-histidine methylation, to form tele-methylhistidine; IDA:UniProtKB.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..377
FT /note="Histidine protein methyltransferase 1"
FT /id="PRO_0000202964"
SQ SEQUENCE 377 AA; 42515 MW; C90C67433B5BCA7A CRC64;
MSFSFGFTSN DFDDDELVAQ PETFVESSKE NENTTAYINP LDSDFLSQAG VVQPNVEDLG
TILESLKDVR LTFEEFQSPI YRKPLIKREL FDVKHQLMLE TDAQSNNNST ELDILLGDTS
EDLRKNIYEG GLKSWECSYD LVDLLSENVD RISNDIDAVV EIGCGTALPS EFLFRSALLR
NDRSKGLKFV LTDYNASVLR LVTIPNLVIT WAKTVLTKEQ WYALQKDECE DIPINNEELL
LTSKLLAAFY DDVQSRNISV TLISGSWGRK FSNLIHEVLS GSQKVLSLSS ETIYQPDNLP
VIAETILDIH NLPQTDVKTY VAAKDIYFGV GGSITEFEAY LDDKINSEHL PIHSERFKVN
SGLKRSIICI ETNKAIR
