Reviewed, UniProtKB/Swiss-Prot P38274 (HSL7_YEAST)

Names and origin

Protein names

Recommended name:
    Protein arginine N-methyltransferase HSL7
    EC=2.1.1.125

Gene names

Name:	HSL7
Ordered Locus Names:	YBR133C
ORF Names:	YBR1008

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	827 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.4 Ref.5 Ref.6
Catalytic activity	S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + histone-N(omega)-methyl-arginine. Ref.7
Subunit structure	Interacts with HSL1 and SWE1. Interacts with the amino-terminal regulatory domain of STE20. Ref.4 Ref.5 Ref.6
Subcellular location	Bud neck. Note: Associates with the septin ring of the bud neck during cell division. Ref.6
Post-translational modification	Phosphorylated in a cell cycle-dependent manner. Ref.5 Ref.9 Ref.10 Ref.11
Miscellaneous	Present with 1180 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the protein arginine N-methyltransferase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Ref.5 Inferred from genetic interaction. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis Ref.4 Inferred from direct assay. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of mitosis Ref.6 Inferred from direct assay. Source: UniProtKB
Cellular component	cellular bud neck Ref.6 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	histone-arginine N-methyltransferase activity Inferred from electronic annotation. Source: EC identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-21618,EBI-21618
COX4	P04037	2	EBI-21618,EBI-5039
PRP6	P19735	1	EBI-21618,EBI-227

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 827	827	Protein arginine N-methyltransferase HSL7		PRO_0000212347
Amino acid modifications
	Modified residue	317	1	Phosphoserine Ref.11
	Modified residue	614	1	Phosphothreonine Ref.11
	Modified residue	708	1	Phosphothreonine Ref.11
	Modified residue	718	1	Phosphoserine Ref.9 Ref.10 Ref.11

Sequences

	Sequence		Length	Mass (Da)
	P38274-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 3066E300285962C9	FASTA	827	95,153
	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

References

	« Hide 'large scale' referencesShow '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: 8647431] [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: 8091856] [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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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: 10411908] [Abstract] Cited for: FUNCTION, INTERACTION WITH STE20.
[5]	"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: 10490630] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSL1 AND SWE1, PHOSPHORYLATION.
[6]	"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: 10490648] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSL1 AND SWE1, SUBCELLULAR LOCATION.
[7]	"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: 10903903] [Abstract] Cited for: CATALYTIC ACTIVITY.
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-718, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317; THR-614; THR-708 AND SER-718, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U65920 Genomic DNA. Translation: AAB07454.1. X75891 Genomic DNA. Translation: CAA53492.1. Z36002 Genomic DNA. Translation: CAA85090.1.
PIR	S46002.
RefSeq	NP_009691.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2762N.
IntAct	P38274. 12 interactions.
STRING	P38274.
Proteomic databases
PeptideAtlas	P38274.
PRIDE	P38274.
Genome annotation databases
Ensembl	YBR133C; YBR133C; YBR133C; Saccharomyces cerevisiae. [Genome view]
GeneID	852431.
GenomeReviews	Gene locus YBR133C in contig Y13134_GR.
KEGG	sce:YBR133C.
NMPDR	fig|4932.3.peg.396.
Organism-specific databases
CYGD	YBR133c.
SGD	S000000337. HSL7.
Phylogenomic databases
HOGENOM	P38274.
OMA	TWELWNT.
Enzyme and pathway databases
BRENDA	2.1.1.125. 250.
Gene expression databases
ArrayExpress	P38274.
Genevestigator	P38274.
GermOnline	YBR133C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR007857. Skb1_MeTrfase. [Graphical view]
PANTHER	PTHR10738. Skb1_mtfrase. 1 hit.
Pfam	PF05185. PRMT5. 1 hit. [Graphical view]
PIRSF	PIRSF015894. Skb1_MeTrfase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	971312.

Entry information

Entry name

HSL7_YEAST

Accession

Primary (citable) accession number: P38274
Secondary accession number(s): A2NP39

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	November 3, 2009
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)