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Protein arginine N-methyltransferase HSL7 (EC 2.1.1.320) (Histone synthetic lethal protein 7) (Type II protein arginine N-methyltransferase) (Type II PRMT)

 HSL7_YEAST              Reviewed;         827 AA.
P38274; A2NP39; D6VQD0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 159.
RecName: Full=Protein arginine N-methyltransferase HSL7 {ECO:0000305|PubMed:10903903};
EC=2.1.1.320 {ECO:0000269|PubMed:10903903, ECO:0000269|PubMed:16426232, ECO:0000269|PubMed:18515076};
AltName: Full=Histone synthetic lethal protein 7 {ECO:0000303|PubMed:8647431};
AltName: Full=Type II protein arginine N-methyltransferase {ECO:0000303|PubMed:18515076};
Short=Type II PRMT {ECO:0000305|PubMed:18515076};
Name=HSL7 {ECO:0000303|PubMed:8647431};
OrderedLocusNames=YBR133C {ECO:0000312|SGD:S000000337};
ORFNames=YBR1008;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8647431; DOI=10.1101/gad.10.11.1327;
Ma X.-J., Lu Q., Grunstein M.;
"A search for proteins that interact genetically with histone H3 and
H4 amino termini uncovers novel regulators of the Swe1 kinase in
Saccharomyces cerevisiae.";
Genes Dev. 10:1327-1340(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091856; DOI=10.1002/yea.320100002;
Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
Herbert C.J.;
"The sequence of 29.7 kb from the right arm of chromosome II reveals
13 complete open reading frames, of which ten correspond to new
genes.";
Yeast 10:S1-S11(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND INTERACTION WITH STE20.
PubMed=10411908; DOI=10.1073/pnas.96.15.8522;
Fujita A., Tonouchi A., Hiroko T., Inose F., Nagashima T., Satoh R.,
Tanaka S.;
"Hsl7p, a negative regulator of Ste20p protein kinase in the
Saccharomyces cerevisiae filamentous growth-signaling pathway.";
Proc. Natl. Acad. Sci. U.S.A. 96:8522-8527(1999).
[6]
FUNCTION, INTERACTION WITH HSL1 AND SWE1, AND PHOSPHORYLATION.
PubMed=10490630; DOI=10.1128/MCB.19.10.6929;
McMillan J.N., Longtine M.S., Sia R.A.L., Theesfeld C.L.,
Bardes E.S.G., Pringle J.R., Lew D.J.;
"The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle
control of Swe1p degradation by Hsl1p and Hsl7p.";
Mol. Cell. Biol. 19:6929-6939(1999).
[7]
FUNCTION, INTERACTION WITH HSL1 AND SWE1, AND SUBCELLULAR LOCATION.
PubMed=10490648; DOI=10.1128/MCB.19.10.7123;
Shulewitz M.J., Inouye C.J., Thorner J.;
"Hsl7 localizes to a septin ring and serves as an adapter in a
regulatory pathway that relieves tyrosine phosphorylation of Cdc28
protein kinase in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 19:7123-7137(1999).
[8]
CATALYTIC ACTIVITY.
PubMed=10903903; DOI=10.1006/bbrc.2000.3049;
Lee J.-H., Cook J.R., Pollack B.P., Kinzy T.G., Norris D., Pestka S.;
"Hsl7p, the yeast homologue of human JBP1, is a protein
methyltransferase.";
Biochem. Biophys. Res. Commun. 274:105-111(2000).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
CATALYTIC ACTIVITY.
PubMed=16426232; DOI=10.1042/BJ20051771;
Miranda T.B., Sayegh J., Frankel A., Katz J.E., Miranda M., Clarke S.;
"Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro
formation of omega-N(G)-monomethylarginine in calf thymus histone
H2A.";
Biochem. J. 395:563-570(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[12]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-387 AND GLY-389.
PubMed=18515076; DOI=10.1016/j.bbrc.2008.05.121;
Sayegh J., Clarke S.G.;
"Hsl7 is a substrate-specific type II protein arginine
methyltransferase in yeast.";
Biochem. Biophys. Res. Commun. 372:811-815(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND THR-614, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: S-adenosyl-L-methionine-dependent protein-arginine N-
methyltransferase that can catalyze both the mono- and symmetric
(type II) dimethylation of the guanidino nitrogens of arginine
residues in target proteins (PubMed:18515076). Involved in the
control of the cell cycle at the G2/M (mitosis) transition.
Cooperates with HSL1 to hyperphosphorylate SWE1, thereby targeting
SWE1 for polyubiquitination and subsequent degradation
(PubMed:10490630, PubMed:10490648). Acts as a negative regulator
of the filamentous growth-signaling pathway through inhibition of
STE20 (PubMed:10411908). {ECO:0000269|PubMed:10411908,
ECO:0000269|PubMed:10490630, ECO:0000269|PubMed:10490648,
ECO:0000269|PubMed:18515076}.
-!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + [protein]-L-
arginine = 2 S-adenosyl-L-homocysteine + [protein]-
N(omega),N(omega')-dimethyl-L-arginine.
{ECO:0000269|PubMed:10903903, ECO:0000269|PubMed:16426232,
ECO:0000269|PubMed:18515076}.
-!- SUBUNIT: Interacts with HSL1 and SWE1. Interacts with the amino-
terminal regulatory domain of STE20. {ECO:0000269|PubMed:10411908,
ECO:0000269|PubMed:10490630, ECO:0000269|PubMed:10490648}.
-!- INTERACTION:
P32944:SWE1; NbExp=4; IntAct=EBI-21618, EBI-18607;
-!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:10490648}.
Note=Associates with the septin ring of the bud neck during cell
division. {ECO:0000269|PubMed:10490648}.
-!- PTM: Phosphorylated in a cell cycle-dependent manner.
{ECO:0000269|PubMed:10490630}.
-!- MISCELLANEOUS: Present with 1180 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. Protein arginine N-
methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
-----------------------------------------------------------------------
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EMBL; U65920; AAB07454.1; -; Genomic_DNA.
EMBL; X75891; CAA53492.1; -; Genomic_DNA.
EMBL; Z36002; CAA85090.1; -; Genomic_DNA.
EMBL; BK006936; DAA07250.1; -; Genomic_DNA.
PIR; S46002; S46002.
RefSeq; NP_009691.1; NM_001178481.1.
ProteinModelPortal; P38274; -.
BioGrid; 32834; 116.
DIP; DIP-2762N; -.
IntAct; P38274; 9.
MINT; MINT-399055; -.
STRING; 4932.YBR133C; -.
iPTMnet; P38274; -.
MaxQB; P38274; -.
PRIDE; P38274; -.
EnsemblFungi; YBR133C; YBR133C; YBR133C.
GeneID; 852431; -.
KEGG; sce:YBR133C; -.
EuPathDB; FungiDB:YBR133C; -.
SGD; S000000337; HSL7.
GeneTree; ENSGT00390000001141; -.
HOGENOM; HOG000111188; -.
InParanoid; P38274; -.
KO; K02516; -.
OMA; INPLTHT; -.
OrthoDB; EOG092C0SQ8; -.
BioCyc; YEAST:G3O-29088-MONOMER; -.
Reactome; R-SCE-3214858; RMTs methylate histone arginines.
PRO; PR:P38274; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
GO; GO:0032174; C:cellular bud neck septin collar; IDA:SGD.
GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005824; C:outer plaque of spindle pole body; IDA:SGD.
GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:SGD.
GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000902; P:cell morphogenesis; IDA:UniProtKB.
GO; GO:0044257; P:cellular protein catabolic process; IMP:SGD.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:SGD.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
InterPro; IPR025799; Arg_MeTrfase.
InterPro; IPR007857; Arg_MeTrfase_PRMT5.
InterPro; IPR035075; PRMT5.
InterPro; IPR035248; PRMT5_C.
InterPro; IPR035247; PRMT5_TIM.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR10738; PTHR10738; 1.
Pfam; PF05185; PRMT5; 1.
Pfam; PF17286; PRMT5_C; 1.
Pfam; PF17285; PRMT5_TIM; 1.
PIRSF; PIRSF015894; Skb1_MeTrfase; 1.
SUPFAM; SSF53335; SSF53335; 2.
PROSITE; PS51678; SAM_MT_PRMT; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Methyltransferase;
Mitosis; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 827 Protein arginine N-methyltransferase
HSL7.
/FTId=PRO_0000212347.
DOMAIN 329 675 SAM-dependent MTase PRMT-type.
{ECO:0000255|PROSITE-ProRule:PRU01015}.
REGION 354 355 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O14744}.
REGION 441 442 S-adenosyl-L-methionine binding.
{ECO:0000250|UniProtKB:O14744}.
ACT_SITE 463 463 Proton donor/acceptor.
{ECO:0000250|UniProtKB:O14744}.
ACT_SITE 472 472 Proton donor/acceptor.
{ECO:0000250|UniProtKB:O14744}.
BINDING 345 345 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O14744}.
BINDING 414 414 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O14744}.
SITE 348 348 Critical for specifying symmetric
addition of methyl groups.
{ECO:0000250|UniProtKB:P46580}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 614 614 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 387 387 G->A: Almost completely abolishes
catalytic activity.
{ECO:0000269|PubMed:18515076}.
MUTAGEN 387 387 G->V: Completely abolishes catalytic
activity; when associated with V-389.
{ECO:0000269|PubMed:18515076}.
MUTAGEN 389 389 G->V: Completely abolishes catalytic
activity; when associated with V-387.
{ECO:0000269|PubMed:18515076}.
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


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