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 27-MAR-2024, entry version 195. 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}; GN 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}. 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; 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; 128. DR DIP; DIP-2762N; -. DR IntAct; P38274; 9. DR MINT; P38274; -. DR STRING; 4932.YBR133C; -. DR iPTMnet; P38274; -. DR MaxQB; P38274; -. DR PaxDb; 4932-YBR133C; -. DR PeptideAtlas; P38274; -. DR EnsemblFungi; YBR133C_mRNA; YBR133C; YBR133C. DR GeneID; 852431; -. DR KEGG; sce:YBR133C; -. DR AGR; SGD:S000000337; -. 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; WEFSHPI; -. DR OrthoDB; 5489665at2759; -. DR BioCyc; YEAST:G3O-29088-MONOMER; -. DR BRENDA; 2.1.1.320; 984. DR BioGRID-ORCS; 852431; 5 hits in 10 CRISPR screens. 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:0008469; F:histone arginine N-methyltransferase activity; IBA:GO_Central. DR GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB. 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:0032259; P:methylation; IEA:UniProtKB-KW. 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 DNA-templated transcription; IBA:GO_Central. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1. DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 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; S-adenosyl-L-methionine-dependent methyltransferases; 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 //