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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: -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

Miscellaneous

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

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)DescriptionActionsGraphical viewLength
Binding sitei345S-adenosyl-L-methionineBy similarity1
Sitei348Critical for specifying symmetric addition of methyl groupsBy similarity1
Binding sitei414S-adenosyl-L-methionineBy similarity1
Active sitei463Proton donor/acceptorBy similarity1
Active sitei472Proton donor/acceptorBy similarity1

GO - Molecular functioni

  • histone-arginine N-methyltransferase activity Source: GO_Central
  • 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
  • positive regulation of mitotic nuclear division Source: UniProtKB
  • regulation of cell cycle Source: SGD
  • regulation of transcription, DNA-templated Source: GO_Central

Keywordsi

Molecular functionMethyltransferase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29088-MONOMER

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi387G → A: Almost completely abolishes catalytic activity. 1 Publication1
Mutagenesisi387G → V: Completely abolishes catalytic activity; when associated with V-389. 1 Publication1
Mutagenesisi389G → V: Completely abolishes catalytic activity; when associated with V-387. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123471 – 827Protein arginine N-methyltransferase HSL7Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei317PhosphoserineCombined sources1
Modified residuei614PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38274
PaxDbiP38274
PRIDEiP38274

PTM databases

iPTMnetiP38274

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SWE1P329444EBI-21618,EBI-18607

Protein-protein interaction databases

BioGridi32834, 120 interactors
DIPiDIP-2762N
IntActiP38274, 9 interactors
MINTiP38274
STRINGi4932.YBR133C

Structurei

3D structure databases

ProteinModelPortaliP38274
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini329 – 675SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST347

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni354 – 355S-adenosyl-L-methionine bindingBy similarity2
Regioni441 – 442S-adenosyl-L-methionine bindingBy similarity2

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000001141
HOGENOMiHOG000111188
InParanoidiP38274
KOiK02516
OMAiFPMFFPT
OrthoDBiEOG092C0SQ8

Family and domain databases

InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR007857 Arg_MeTrfase_PRMT5
IPR035075 PRMT5
IPR035248 PRMT5_C
IPR035247 PRMT5_TIM
IPR029063 SAM-dependent_MTases
PANTHERiPTHR10738 PTHR10738, 1 hit
PfamiView protein in Pfam
PF05185 PRMT5, 1 hit
PF17286 PRMT5_C, 1 hit
PF17285 PRMT5_TIM, 1 hit
PIRSFiPIRSF015894 Skb1_MeTrfase, 1 hit
SUPFAMiSSF53335 SSF53335, 2 hits
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiHSL7_YEAST
AccessioniPrimary (citable) accession number: P38274
Secondary accession number(s): A2NP39, D6VQD0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 23, 2018
This is version 164 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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