HSL7_YEAST
ID HSL7_YEAST Reviewed; 827 AA.
AC P38274; A2NP39; D6VQD0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein arginine N-methyltransferase HSL7 {ECO:0000305|PubMed:10903903};
DE EC=2.1.1.320 {ECO:0000269|PubMed:10903903, ECO:0000269|PubMed:16426232, ECO:0000269|PubMed:18515076};
DE AltName: Full=Histone synthetic lethal protein 7 {ECO:0000303|PubMed:8647431};
DE AltName: Full=Type II protein arginine N-methyltransferase {ECO:0000303|PubMed:18515076};
DE Short=Type II PRMT {ECO:0000305|PubMed:18515076};
GN Name=HSL7 {ECO:0000303|PubMed:8647431};
GN OrderedLocusNames=YBR133C {ECO:0000312|SGD:S000000337}; ORFNames=YBR1008;
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 [GENOMIC DNA].
RX PubMed=8647431; DOI=10.1101/gad.10.11.1327;
RA Ma X.-J., Lu Q., Grunstein M.;
RT "A search for proteins that interact genetically with histone H3 and H4
RT amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 10:1327-1340(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH STE20.
RX PubMed=10411908; DOI=10.1073/pnas.96.15.8522;
RA Fujita A., Tonouchi A., Hiroko T., Inose F., Nagashima T., Satoh R.,
RA Tanaka S.;
RT "Hsl7p, a negative regulator of Ste20p protein kinase in the Saccharomyces
RT cerevisiae filamentous growth-signaling pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8522-8527(1999).
RN [6]
RP FUNCTION, INTERACTION WITH HSL1 AND SWE1, AND PHOSPHORYLATION.
RX PubMed=10490630; DOI=10.1128/mcb.19.10.6929;
RA McMillan J.N., Longtine M.S., Sia R.A.L., Theesfeld C.L., Bardes E.S.G.,
RA Pringle J.R., Lew D.J.;
RT "The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle
RT control of Swe1p degradation by Hsl1p and Hsl7p.";
RL Mol. Cell. Biol. 19:6929-6939(1999).
RN [7]
RP FUNCTION, INTERACTION WITH HSL1 AND SWE1, AND SUBCELLULAR LOCATION.
RX PubMed=10490648; DOI=10.1128/mcb.19.10.7123;
RA Shulewitz M.J., Inouye C.J., Thorner J.;
RT "Hsl7 localizes to a septin ring and serves as an adapter in a regulatory
RT pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:7123-7137(1999).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=10903903; DOI=10.1006/bbrc.2000.3049;
RA Lee J.-H., Cook J.R., Pollack B.P., Kinzy T.G., Norris D., Pestka S.;
RT "Hsl7p, the yeast homologue of human JBP1, is a protein
RT methyltransferase.";
RL Biochem. Biophys. Res. Commun. 274:105-111(2000).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=16426232; DOI=10.1042/bj20051771;
RA Miranda T.B., Sayegh J., Frankel A., Katz J.E., Miranda M., Clarke S.;
RT "Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation
RT of omega-N(G)-monomethylarginine in calf thymus histone H2A.";
RL Biochem. J. 395:563-570(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-387 AND GLY-389.
RX PubMed=18515076; DOI=10.1016/j.bbrc.2008.05.121;
RA Sayegh J., Clarke S.G.;
RT "Hsl7 is a substrate-specific type II protein arginine methyltransferase in
RT yeast.";
RL Biochem. Biophys. Res. Commun. 372:811-815(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND THR-614, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
CC methyltransferase that can catalyze both the mono- and symmetric (type
CC II) dimethylation of the guanidino nitrogens of arginine residues in
CC target proteins (PubMed:18515076). Involved in the control of the cell
CC cycle at the G2/M (mitosis) transition. Cooperates with HSL1 to
CC hyperphosphorylate SWE1, thereby targeting SWE1 for polyubiquitination
CC and subsequent degradation (PubMed:10490630, PubMed:10490648). Acts as
CC a negative regulator of the filamentous growth-signaling pathway
CC through inhibition of STE20 (PubMed:10411908).
CC {ECO:0000269|PubMed:10411908, ECO:0000269|PubMed:10490630,
CC ECO:0000269|PubMed:10490648, ECO:0000269|PubMed:18515076}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000269|PubMed:10903903, ECO:0000269|PubMed:16426232,
CC ECO:0000269|PubMed:18515076};
CC -!- SUBUNIT: Interacts with HSL1 and SWE1. Interacts with the amino-
CC terminal regulatory domain of STE20. {ECO:0000269|PubMed:10411908,
CC ECO:0000269|PubMed:10490630, ECO:0000269|PubMed:10490648}.
CC -!- INTERACTION:
CC P38274; P32944: SWE1; NbExp=4; IntAct=EBI-21618, EBI-18607;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:10490648}.
CC Note=Associates with the septin ring of the bud neck during cell
CC division. {ECO:0000269|PubMed:10490648}.
CC -!- PTM: Phosphorylated in a cell cycle-dependent manner.
CC {ECO:0000269|PubMed:10490630}.
CC -!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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DR EMBL; U65920; AAB07454.1; -; Genomic_DNA.
DR EMBL; X75891; CAA53492.1; -; Genomic_DNA.
DR EMBL; Z36002; CAA85090.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07250.1; -; Genomic_DNA.
DR PIR; S46002; S46002.
DR RefSeq; NP_009691.1; NM_001178481.1.
DR AlphaFoldDB; P38274; -.
DR SMR; P38274; -.
DR BioGRID; 32834; 125.
DR DIP; DIP-2762N; -.
DR IntAct; P38274; 9.
DR MINT; P38274; -.
DR STRING; 4932.YBR133C; -.
DR iPTMnet; P38274; -.
DR MaxQB; P38274; -.
DR PaxDb; P38274; -.
DR PRIDE; P38274; -.
DR EnsemblFungi; YBR133C_mRNA; YBR133C; YBR133C.
DR GeneID; 852431; -.
DR KEGG; sce:YBR133C; -.
DR SGD; S000000337; HSL7.
DR VEuPathDB; FungiDB:YBR133C; -.
DR eggNOG; KOG0822; Eukaryota.
DR GeneTree; ENSGT00390000001141; -.
DR HOGENOM; CLU_010247_2_0_1; -.
DR InParanoid; P38274; -.
DR OMA; IKYAWYE; -.
DR BioCyc; YEAST:G3O-29088-MON; -.
DR BRENDA; 2.1.1.320; 984.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR PRO; PR:P38274; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38274; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
DR GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:SGD.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IDA:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0034969; P:histone arginine methylation; IBA:GO_Central.
DR GO; GO:0035246; P:peptidyl-arginine N-methylation; IEA:InterPro.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR007857; Arg_MeTrfase_PRMT5.
DR InterPro; IPR035075; PRMT5.
DR InterPro; IPR035248; PRMT5_C.
DR InterPro; IPR035247; PRMT5_TIM.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10738; PTHR10738; 1.
DR Pfam; PF05185; PRMT5; 1.
DR Pfam; PF17286; PRMT5_C; 1.
DR Pfam; PF17285; PRMT5_TIM; 1.
DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Methyltransferase; Mitosis; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..827
FT /note="Protein arginine N-methyltransferase HSL7"
FT /id="PRO_0000212347"
FT DOMAIN 329..675
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 463
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT ACT_SITE 472
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 345
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 354..355
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 414
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT BINDING 441..442
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O14744"
FT SITE 348
FT /note="Critical for specifying symmetric addition of methyl
FT groups"
FT /evidence="ECO:0000250|UniProtKB:P46580"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 387
FT /note="G->A: Almost completely abolishes catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:18515076"
FT MUTAGEN 387
FT /note="G->V: Completely abolishes catalytic activity; when
FT associated with V-389."
FT /evidence="ECO:0000269|PubMed:18515076"
FT MUTAGEN 389
FT /note="G->V: Completely abolishes catalytic activity; when
FT associated with V-387."
FT /evidence="ECO:0000269|PubMed:18515076"
SQ SEQUENCE 827 AA; 95153 MW; 3066E300285962C9 CRC64;
MHSNVFVGVK PGFNHKQHSK KSRFLENVSS HSPELPSNYD YVLLPITTPR YKEIVGQVFK
DFQRQSIQNW KPLQIPEPQL QDICIPPFNV KKLDNDDTPS YIGLLSSWLE LESRDPNVRD
LGLKVLLNEC KYARFVGINK LILAPPRDLS NLQLYGQMIY RLLQNRIVFA APALTISISL
PLYEDSDPLA TWELWNTVRK QCEYHPSLTI SLALPRTRTP SYVLNRWLAE PVSCLLVSSS
IFASNQYDYP VLHKFNQNLI LKFQKVNGDS QILGNELCVI LHGMEKYANN VKGGESAYLE
YINYLLKKGD KVLNSNSNHQ FLLQEDSRIM PPLKPHSDNL LNSTYLTFEK DLVKYDLYES
AILEALQDLA PRASAKRPLV ILVAGAGRGP LVDRTFKIIS MLFMDSKVSI IAIEKNPQAY
LYLQKRNFDC WDNRVKLIKE DMTKWQINEP SEKRIQIDLC ISELLGSFGC NELSPECLWS
IEKYHSHNDT IFIPRSYSSY IAPISSPLFY QKLSQTNRSL EAPWIVHRVP YCILSSRVNE
VWRFEHPMAQ KDTVQDEDDF TVEFSQSSLN EFKIKHRGEI HGFIGFFSAN LYNNIFLSTL
PNDSTVRLKF SEETLMNTRR EENLIKKCDH TPNMTSWSPI IFPLKQPISF IDDSELSVLM
SRIHSDTEQK VWYEWSLESF IYLMLSNYTS AVTAASMTIP RSIVTDDTKT LAHNRHYSAT
TNQKLDNQID LDQDIENEEE QGFLSNLETG WQSVQDIHGL SETAKPDHLD SINKPMFDLK
STKALEPSNE LPRHEDLEED VPEVHVRVKT SVSTLHNVCG RAFSLPL
