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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: Annotation score: 5 out of 5-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

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

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
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-29011-MONOMER.
ReactomeiR-SCE-3214858. RMTs methylate histone arginines.

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

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: GO_Central
  • nucleus Source: SGD
Complete GO annotation...

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.
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

WithEntry#Exp.IntActNotes
itself4EBI-8394,EBI-8394
BRE5P537412EBI-8394,EBI-28528
DBF2P222044EBI-8394,EBI-5569
MTR4P470472EBI-8394,EBI-11592
NAB2P325052EBI-8394,EBI-11770
NPL3Q015609EBI-8394,EBI-12114
PPH22P235953EBI-8394,EBI-12752
SNF2P220823EBI-8394,EBI-17526
SSD1P242762EBI-8394,EBI-18153
SUM1P466762EBI-8394,EBI-18547

Protein-protein interaction databases

BioGridi32735. 331 interactors.
DIPiDIP-2608N.
IntActiP38074. 265 interactors.
MINTiMINT-423994.

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
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
InParanoidiP38074.
KOiK11434.
OMAiNSMEHSE.
OrthoDBiEOG092C393Q.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi32735. 331 interactors.
DIPiDIP-2608N.
IntActiP38074. 265 interactors.
MINTiMINT-423994.

Proteomic databases

MaxQBiP38074.
PRIDEiP38074.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR034C; YBR034C; YBR034C.
GeneIDi852322.
KEGGisce:YBR034C.

Organism-specific databases

EuPathDBiFungiDB:YBR034C.
SGDiS000000238. HMT1.

Phylogenomic databases

GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
InParanoidiP38074.
KOiK11434.
OMAiNSMEHSE.
OrthoDBiEOG092C393Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-29011-MONOMER.
ReactomeiR-SCE-3214858. RMTs methylate histone arginines.

Miscellaneous databases

EvolutionaryTraceiP38074.
PROiP38074.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMT1_YEAST
AccessioniPrimary (citable) accession number: P38074
Secondary accession number(s): D6VQ34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 149 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 37600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. 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.