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Protein

Protein arginine N-methyltransferase HSL7

Gene

HSL7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).4 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei345 – 3451S-adenosyl-L-methionineBy similarity
Sitei348 – 3481Critical for specifying symmetric addition of methyl groupsBy similarity
Binding sitei414 – 4141S-adenosyl-L-methionineBy similarity
Active sitei463 – 4631Proton donor/acceptorBy similarity
Active sitei472 – 4721Proton donor/acceptorBy similarity

GO - Molecular functioni

  • histone methyltransferase activity Source: UniProtKB
  • protein-arginine omega-N monomethyltransferase activity Source: SGD
  • protein-arginine omega-N symmetric methyltransferase activity Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell morphogenesis Source: UniProtKB
  • cellular protein catabolic process Source: SGD
  • G2/M transition of mitotic cell cycle Source: SGD
  • histone methylation Source: GOC
  • mitotic nuclear division Source: UniProtKB-KW
  • peptidyl-arginine methylation, to symmetrical-dimethyl arginine Source: GOC
  • peptidyl-arginine omega-N-methylation Source: GOC
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • regulation of cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29088-MONOMER.
ReactomeiR-SCE-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase HSL71 Publication (EC:2.1.1.3203 Publications)
Alternative name(s):
Histone synthetic lethal protein 71 Publication
Type II protein arginine N-methyltransferase1 Publication
Short name:
Type II PRMT1 Publication
Gene namesi
Name:HSL71 Publication
Ordered Locus Names:YBR133CImported
ORF Names:YBR1008
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR133C.
SGDiS000000337. HSL7.

Subcellular locationi

  • Bud neck 1 Publication

  • Note: Associates with the septin ring of the bud neck during cell division.1 Publication

GO - Cellular componenti

  • cellular bud neck Source: UniProtKB
  • cellular bud neck septin collar Source: SGD
  • cellular bud neck septin ring Source: SGD
  • outer plaque of spindle pole body Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871G → A: Almost completely abolishes catalytic activity. 1 Publication
Mutagenesisi387 – 3871G → V: Completely abolishes catalytic activity; when associated with V-389. 1 Publication
Mutagenesisi389 – 3891G → V: Completely abolishes catalytic activity; when associated with V-387. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 827827Protein arginine N-methyltransferase HSL7PRO_0000212347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171PhosphoserineCombined sources
Modified residuei614 – 6141PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38274.
PeptideAtlasiP38274.

PTM databases

iPTMnetiP38274.

Interactioni

Subunit structurei

Interacts with HSL1 and SWE1. Interacts with the amino-terminal regulatory domain of STE20.3 Publications

Protein-protein interaction databases

BioGridi32834. 35 interactions.
DIPiDIP-2762N.
IntActiP38274. 7 interactions.
MINTiMINT-399055.

Structurei

3D structure databases

ProteinModelPortaliP38274.
SMRiP38274. Positions 39-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini329 – 675347SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3552S-adenosyl-L-methionine bindingBy similarity
Regioni441 – 4422S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000001141.
HOGENOMiHOG000111188.
InParanoidiP38274.
KOiK02516.
OMAiDWAEQKK.
OrthoDBiEOG7KSXMV.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 3 hits.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38274-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHSNVFVGVK PGFNHKQHSK KSRFLENVSS HSPELPSNYD YVLLPITTPR
60 70 80 90 100
YKEIVGQVFK DFQRQSIQNW KPLQIPEPQL QDICIPPFNV KKLDNDDTPS
110 120 130 140 150
YIGLLSSWLE LESRDPNVRD LGLKVLLNEC KYARFVGINK LILAPPRDLS
160 170 180 190 200
NLQLYGQMIY RLLQNRIVFA APALTISISL PLYEDSDPLA TWELWNTVRK
210 220 230 240 250
QCEYHPSLTI SLALPRTRTP SYVLNRWLAE PVSCLLVSSS IFASNQYDYP
260 270 280 290 300
VLHKFNQNLI LKFQKVNGDS QILGNELCVI LHGMEKYANN VKGGESAYLE
310 320 330 340 350
YINYLLKKGD KVLNSNSNHQ FLLQEDSRIM PPLKPHSDNL LNSTYLTFEK
360 370 380 390 400
DLVKYDLYES AILEALQDLA PRASAKRPLV ILVAGAGRGP LVDRTFKIIS
410 420 430 440 450
MLFMDSKVSI IAIEKNPQAY LYLQKRNFDC WDNRVKLIKE DMTKWQINEP
460 470 480 490 500
SEKRIQIDLC ISELLGSFGC NELSPECLWS IEKYHSHNDT IFIPRSYSSY
510 520 530 540 550
IAPISSPLFY QKLSQTNRSL EAPWIVHRVP YCILSSRVNE VWRFEHPMAQ
560 570 580 590 600
KDTVQDEDDF TVEFSQSSLN EFKIKHRGEI HGFIGFFSAN LYNNIFLSTL
610 620 630 640 650
PNDSTVRLKF SEETLMNTRR EENLIKKCDH TPNMTSWSPI IFPLKQPISF
660 670 680 690 700
IDDSELSVLM SRIHSDTEQK VWYEWSLESF IYLMLSNYTS AVTAASMTIP
710 720 730 740 750
RSIVTDDTKT LAHNRHYSAT TNQKLDNQID LDQDIENEEE QGFLSNLETG
760 770 780 790 800
WQSVQDIHGL SETAKPDHLD SINKPMFDLK STKALEPSNE LPRHEDLEED
810 820
VPEVHVRVKT SVSTLHNVCG RAFSLPL
Length:827
Mass (Da):95,153
Last modified:October 1, 1994 - v1
Checksum:i3066E300285962C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65920 Genomic DNA. Translation: AAB07454.1.
X75891 Genomic DNA. Translation: CAA53492.1.
Z36002 Genomic DNA. Translation: CAA85090.1.
BK006936 Genomic DNA. Translation: DAA07250.1.
PIRiS46002.
RefSeqiNP_009691.1. NM_001178481.1.

Genome annotation databases

EnsemblFungiiYBR133C; YBR133C; YBR133C.
GeneIDi852431.
KEGGisce:YBR133C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65920 Genomic DNA. Translation: AAB07454.1.
X75891 Genomic DNA. Translation: CAA53492.1.
Z36002 Genomic DNA. Translation: CAA85090.1.
BK006936 Genomic DNA. Translation: DAA07250.1.
PIRiS46002.
RefSeqiNP_009691.1. NM_001178481.1.

3D structure databases

ProteinModelPortaliP38274.
SMRiP38274. Positions 39-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32834. 35 interactions.
DIPiDIP-2762N.
IntActiP38274. 7 interactions.
MINTiMINT-399055.

PTM databases

iPTMnetiP38274.

Proteomic databases

MaxQBiP38274.
PeptideAtlasiP38274.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR133C; YBR133C; YBR133C.
GeneIDi852431.
KEGGisce:YBR133C.

Organism-specific databases

EuPathDBiFungiDB:YBR133C.
SGDiS000000337. HSL7.

Phylogenomic databases

GeneTreeiENSGT00390000001141.
HOGENOMiHOG000111188.
InParanoidiP38274.
KOiK02516.
OMAiDWAEQKK.
OrthoDBiEOG7KSXMV.

Enzyme and pathway databases

BioCyciYEAST:G3O-29088-MONOMER.
ReactomeiR-SCE-3214858. RMTs methylate histone arginines.

Miscellaneous databases

NextBioi971312.
PROiP38274.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10738. PTHR10738. 3 hits.
PfamiPF05185. PRMT5. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A search for proteins that interact genetically with histone H3 and H4 amino termini uncovers novel regulators of the Swe1 kinase in Saccharomyces cerevisiae."
    Ma X.-J., Lu Q., Grunstein M.
    Genes Dev. 10:1327-1340(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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."
    Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
    Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    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.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Hsl7p, a negative regulator of Ste20p protein kinase in the Saccharomyces cerevisiae filamentous growth-signaling pathway."
    Fujita A., Tonouchi A., Hiroko T., Inose F., Nagashima T., Satoh R., Tanaka S.
    Proc. Natl. Acad. Sci. U.S.A. 96:8522-8527(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STE20.
  6. "The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle control of Swe1p degradation by Hsl1p and Hsl7p."
    McMillan J.N., Longtine M.S., Sia R.A.L., Theesfeld C.L., Bardes E.S.G., Pringle J.R., Lew D.J.
    Mol. Cell. Biol. 19:6929-6939(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSL1 AND SWE1, PHOSPHORYLATION.
  7. "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."
    Shulewitz M.J., Inouye C.J., Thorner J.
    Mol. Cell. Biol. 19:7123-7137(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSL1 AND SWE1, SUBCELLULAR LOCATION.
  8. "Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase."
    Lee J.-H., Cook J.R., Pollack B.P., Kinzy T.G., Norris D., Pestka S.
    Biochem. Biophys. Res. Commun. 274:105-111(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A."
    Miranda T.B., Sayegh J., Frankel A., Katz J.E., Miranda M., Clarke S.
    Biochem. J. 395:563-570(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast."
    Sayegh J., Clarke S.G.
    Biochem. Biophys. Res. Commun. 372:811-815(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-387 AND GLY-389.
  13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND THR-614, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHSL7_YEAST
AccessioniPrimary (citable) accession number: P38274
Secondary accession number(s): A2NP39, D6VQD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1180 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.