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Protein

Protein arginine N-methyltransferase 1

Gene

HMT1

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 catalyzes both the mono- and asymmetric (type I) dimethylation of the guanidino nitrogens of arginine residues in a variety of RNA-binding proteins such as heterogeneous nuclear ribonucleoproteins (hnRNPs) and small nuclear ribonucleoproteins (snRNPs) (PubMed:8668183, PubMed:8647869). Methylates NAB2, NPL3, HRP1 and YRA1, shuttling hnRNPs involved in mRNA processing and export, facilitating their export out of the nucleus (PubMed:8668183, PubMed:9499403, PubMed:10652296, PubMed:11779864, PubMed:15314027). Methylation of NPL3 weakens its interaction with THO2, a component of the TREX (transcription/export) complex important for transcriptional elongation and recruitment of mRNA export factors (PubMed:15314027, PubMed:20053728). Methylates the hnRNP HRB1, but does not influence its subcellular location (PubMed:9499403). Methylates the nucleolar proteins GAR1, NOP1 and NSR1 (PubMed:12756332). Methylates the snRNP SNP1 and modulates the cotranscriptional recruitment of splicing factors (PubMed:20823272). Dimethylates free histone H4 (HHF1/HHF2) at 'Arg-4' (H4R3me2a) and plays a role in preservation and establishment of silent chromatin domains (PubMed:12097318, PubMed:17158743). Mono- and dimethylates ribosomal protein S2 (RPS2) at 'Arg-11' (PubMed:20035717). Methylates the catalytic subunit of the SWI/SNF chromatin-remodeling complex SNF2 (PubMed:22997150).14 Publications

Miscellaneous

Present with 37600 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33S-adenosyl-L-methionineBy similarity1
Binding sitei42S-adenosyl-L-methionineBy similarity1
Binding sitei66S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei88S-adenosyl-L-methionineBy similarity1
Binding sitei117S-adenosyl-L-methionineBy similarity1
Active sitei132By similarity1
Active sitei141By similarity1

GO - Molecular functioni

  • histone-arginine N-methyltransferase activity Source: GO_Central
  • identical protein binding Source: IntAct
  • protein-arginine omega-N asymmetric methyltransferase activity Source: SGD
  • protein-arginine omega-N monomethyltransferase activity Source: SGD

GO - Biological processi

  • mRNA export from nucleus Source: SGD
  • negative regulation of DNA-templated transcription, termination Source: SGD
  • peptidyl-arginine methylation Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD

Keywordsi

Molecular functionMethyltransferase, Transferase
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29011-MONOMER
ReactomeiR-SCE-3214858 RMTs methylate histone arginines
R-SCE-8876725 Protein methylation
R-SCE-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-SCE-9018519 Estrogen-dependent gene expression

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 11 Publication (EC:2.1.1.-2 Publications)
Alternative name(s):
Major type I protein arginine N-methyltransferase1 Publication
Short name:
Type I PRMT1 Publication
hnRNP arginine N-methyltransferase1 Publication
Gene namesi
Name:HMT11 Publication
Synonyms:ODP11 Publication, RMT11 Publication
Ordered Locus Names:YBR034CImported
ORF Names:YBR0320
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR034C
SGDiS000000238 HMT1

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18E → V: Cold-sensitive; reduces catalytic activity more than 20-fold at 14 degrees Celsius. 1 Publication1
Mutagenesisi68G → A: Reduces catalytic activity between 5- to 25-fold. 1 Publication1
Mutagenesisi68G → R: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002123411 – 348Protein arginine N-methyltransferase 1Add BLAST348

Proteomic databases

MaxQBiP38074
PaxDbiP38074
PRIDEiP38074

Interactioni

Subunit structurei

Homodimer. The dimers can then associate to form a ring-shaped homohexamer. Interacts with NPL3, BRE5, MTR4, SNF2, SUM1, AND SSD1.2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32735, 389 interactors
DIPiDIP-2608N
IntActiP38074, 264 interactors
MINTiP38074
STRINGi4932.YBR034C

Structurei

Secondary structure

1348
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 37Combined sources8
Helixi40 – 57Combined sources18
Beta strandi61 – 65Combined sources5
Helixi71 – 78Combined sources8
Beta strandi82 – 90Combined sources9
Helixi92 – 102Combined sources11
Turni106 – 108Combined sources3
Beta strandi109 – 114Combined sources6
Turni116 – 118Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi126 – 131Combined sources6
Helixi144 – 154Combined sources11
Beta strandi155 – 163Combined sources9
Beta strandi165 – 173Combined sources9
Helixi176 – 185Combined sources10
Helixi197 – 201Combined sources5
Beta strandi206 – 208Combined sources3
Helixi212 – 214Combined sources3
Beta strandi220 – 226Combined sources7
Turni227 – 229Combined sources3
Helixi232 – 235Combined sources4
Beta strandi236 – 245Combined sources10
Beta strandi250 – 261Combined sources12
Beta strandi272 – 274Combined sources3
Beta strandi286 – 296Combined sources11
Beta strandi302 – 312Combined sources11
Beta strandi315 – 328Combined sources14
Helixi334 – 337Combined sources4
Beta strandi339 – 347Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G6QX-ray2.901/2/3/4/5/621-348[»]
ProteinModelPortaliP38074
SMRiP38074
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38074

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 322SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST303

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00550000074406
HOGENOMiHOG000198521
InParanoidiP38074
KOiK11434
OMAiRFSTGPH
OrthoDBiEOG092C393Q

Family and domain databases

InterProiView protein in InterPro
IPR025799 Arg_MeTrfase
IPR029063 SAM-dependent_MTases
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678 SAM_MT_PRMT, 1 hit

Sequencei

Sequence statusi: Complete.

P38074-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTAVKDSA TEKTKLSESE QHYFNSYDHY GIHEEMLQDT VRTLSYRNAI
60 70 80 90 100
IQNKDLFKDK IVLDVGCGTG ILSMFAAKHG AKHVIGVDMS SIIEMAKELV
110 120 130 140 150
ELNGFSDKIT LLRGKLEDVH LPFPKVDIII SEWMGYFLLY ESMMDTVLYA
160 170 180 190 200
RDHYLVEGGL IFPDKCSIHL AGLEDSQYKD EKLNYWQDVY GFDYSPFVPL
210 220 230 240 250
VLHEPIVDTV ERNNVNTTSD KLIEFDLNTV KISDLAFKSN FKLTAKRQDM
260 270 280 290 300
INGIVTWFDI VFPAPKGKRP VEFSTGPHAP YTHWKQTIFY FPDDLDAETG
310 320 330 340
DTIEGELVCS PNEKNNRDLN IKISYKFESN GIDGNSRSRK NEGSYLMH
Length:348
Mass (Da):39,786
Last modified:October 1, 1994 - v1
Checksum:i383AF61033FB4AC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76078 Genomic DNA Translation: CAA53689.1
Z35903 Genomic DNA Translation: CAA84976.1
X76992 Genomic DNA Translation: CAA54296.1
AY557869 Genomic DNA Translation: AAS56195.1
BK006936 Genomic DNA Translation: DAA07154.1
PIRiS45890
RefSeqiNP_009590.1, NM_001178382.1

Genome annotation databases

EnsemblFungiiYBR034C; YBR034C; YBR034C
GeneIDi852322
KEGGisce:YBR034C

Similar proteinsi

Entry informationi

Entry nameiHMT1_YEAST
AccessioniPrimary (citable) accession number: P38074
Secondary accession number(s): D6VQ34
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 23, 2018
This is version 162 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

3D-structure, Complete proteome, Reference proteome

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