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P38274 (HSL7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein arginine N-methyltransferase HSL7

EC=2.1.1.125
Gene names
Name:HSL7
Ordered Locus Names:YBR133C
ORF Names:YBR1008
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length827 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Acts as a negative regulator of the filamentous growth-signaling pathway through inhibition of STE20. Ref.5 Ref.6 Ref.7

Catalytic activity

S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. Ref.8

Subunit structure

Interacts with HSL1 and SWE1. Interacts with the amino-terminal regulatory domain of STE20. Ref.5 Ref.6 Ref.7

Subcellular location

Bud neck. Note: Associates with the septin ring of the bud neck during cell division. Ref.7

Post-translational modification

Phosphorylated in a cell cycle-dependent manner. Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.

Contains 1 SAM-dependent MTase PRMT-type domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.6. Source: SGD

cell morphogenesis

Inferred from direct assay Ref.5. Source: UniProtKB

cellular protein catabolic process

Inferred from mutant phenotype PubMed 23042131. Source: SGD

histone methylation

Inferred from direct assay Ref.8. Source: GOC

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-arginine methylation, to symmetrical-dimethyl arginine

Inferred from direct assay PubMed 18515076. Source: GOC

peptidyl-arginine omega-N-methylation

Inferred from direct assay PubMed 16426232PubMed 18515076. Source: GOC

positive regulation of mitosis

Inferred from direct assay Ref.7. Source: UniProtKB

regulation of cell cycle

Inferred from mutant phenotype Ref.1. Source: SGD

   Cellular_componentcellular bud neck

Inferred from direct assay Ref.7. Source: UniProtKB

cellular bud neck septin collar

Inferred from direct assay PubMed 23389636. Source: SGD

   Molecular_functionhistone methyltransferase activity

Inferred from direct assay Ref.8. Source: UniProtKB

histone-arginine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein-arginine omega-N monomethyltransferase activity

Inferred from direct assay PubMed 16426232PubMed 18515076. Source: SGD

protein-arginine omega-N symmetric methyltransferase activity

Inferred from direct assay PubMed 18515076. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 827827Protein arginine N-methyltransferase HSL7
PRO_0000212347

Regions

Domain329 – 675347SAM-dependent MTase PRMT-type

Amino acid modifications

Modified residue3171Phosphoserine Ref.11
Modified residue6141Phosphothreonine Ref.11

Sequences

Sequence LengthMass (Da)Tools
P38274 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 3066E300285962C9

FASTA82795,153
        10         20         30         40         50         60 
MHSNVFVGVK PGFNHKQHSK KSRFLENVSS HSPELPSNYD YVLLPITTPR YKEIVGQVFK 

        70         80         90        100        110        120 
DFQRQSIQNW KPLQIPEPQL QDICIPPFNV KKLDNDDTPS YIGLLSSWLE LESRDPNVRD 

       130        140        150        160        170        180 
LGLKVLLNEC KYARFVGINK LILAPPRDLS NLQLYGQMIY RLLQNRIVFA APALTISISL 

       190        200        210        220        230        240 
PLYEDSDPLA TWELWNTVRK QCEYHPSLTI SLALPRTRTP SYVLNRWLAE PVSCLLVSSS 

       250        260        270        280        290        300 
IFASNQYDYP VLHKFNQNLI LKFQKVNGDS QILGNELCVI LHGMEKYANN VKGGESAYLE 

       310        320        330        340        350        360 
YINYLLKKGD KVLNSNSNHQ FLLQEDSRIM PPLKPHSDNL LNSTYLTFEK DLVKYDLYES 

       370        380        390        400        410        420 
AILEALQDLA PRASAKRPLV ILVAGAGRGP LVDRTFKIIS MLFMDSKVSI IAIEKNPQAY 

       430        440        450        460        470        480 
LYLQKRNFDC WDNRVKLIKE DMTKWQINEP SEKRIQIDLC ISELLGSFGC NELSPECLWS 

       490        500        510        520        530        540 
IEKYHSHNDT IFIPRSYSSY IAPISSPLFY QKLSQTNRSL EAPWIVHRVP YCILSSRVNE 

       550        560        570        580        590        600 
VWRFEHPMAQ KDTVQDEDDF TVEFSQSSLN EFKIKHRGEI HGFIGFFSAN LYNNIFLSTL 

       610        620        630        640        650        660 
PNDSTVRLKF SEETLMNTRR EENLIKKCDH TPNMTSWSPI IFPLKQPISF IDDSELSVLM 

       670        680        690        700        710        720 
SRIHSDTEQK VWYEWSLESF IYLMLSNYTS AVTAASMTIP RSIVTDDTKT LAHNRHYSAT 

       730        740        750        760        770        780 
TNQKLDNQID LDQDIENEEE QGFLSNLETG WQSVQDIHGL SETAKPDHLD SINKPMFDLK 

       790        800        810        820 
STKALEPSNE LPRHEDLEED VPEVHVRVKT SVSTLHNVCG RAFSLPL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"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].
[11]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U65920 Genomic DNA. Translation: AAB07454.1.
X75891 Genomic DNA. Translation: CAA53492.1.
Z36002 Genomic DNA. Translation: CAA85090.1.
BK006936 Genomic DNA. Translation: DAA07250.1.
PIRS46002.
RefSeqNP_009691.1. NM_001178481.1.

3D structure databases

ProteinModelPortalP38274.
SMRP38274. Positions 39-689.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32834. 32 interactions.
DIPDIP-2762N.
IntActP38274. 7 interactions.
MINTMINT-399055.

Proteomic databases

PaxDbP38274.
PeptideAtlasP38274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR133C; YBR133C; YBR133C.
GeneID852431.
KEGGsce:YBR133C.

Organism-specific databases

CYGDYBR133c.
SGDS000000337. HSL7.

Phylogenomic databases

eggNOGNOG291156.
GeneTreeENSGT00390000001141.
HOGENOMHOG000111188.
KOK02516.
OMAMWRQTDD.
OrthoDBEOG7KSXMV.

Enzyme and pathway databases

BioCycYEAST:G3O-29088-MONOMER.

Gene expression databases

GenevestigatorP38274.

Family and domain databases

InterProIPR025799. Arg_MeTrfase.
IPR007857. Arg_MeTrfase_PRMT5.
[Graphical view]
PANTHERPTHR10738. PTHR10738. 1 hit.
PfamPF05185. PRMT5. 1 hit.
[Graphical view]
PIRSFPIRSF015894. Skb1_MeTrfase. 1 hit.
PROSITEPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971312.
PROP38274.

Entry information

Entry nameHSL7_YEAST
AccessionPrimary (citable) accession number: P38274
Secondary accession number(s): A2NP39, D6VQD0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families