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P38074

- HMT1_YEAST

UniProt

P38074 - HMT1_YEAST

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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: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei33 – 331S-adenosyl-L-methionineBy similarity
Binding sitei42 – 421S-adenosyl-L-methionineBy similarity
Binding sitei66 – 661S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei88 – 881S-adenosyl-L-methionineBy similarity
Binding sitei117 – 1171S-adenosyl-L-methionineBy similarity
Active sitei132 – 1321By similarity
Active sitei141 – 1411By similarity

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. protein-arginine omega-N asymmetric methyltransferase activity Source: SGD
  3. protein-arginine omega-N monomethyltransferase activity Source: SGD

GO - Biological processi

  1. mRNA export from nucleus Source: SGD
  2. negative regulation of DNA-templated transcription, termination Source: SGD
  3. peptidyl-arginine methylation Source: SGD
  4. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: GOC
  5. peptidyl-arginine omega-N-methylation Source: GOC
  6. 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.

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
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR034c.
SGDiS000000238. HMT1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181E → V: Cold-sensitive; reduces catalytic activity more than 20-fold at 14 degrees Celsius. 1 Publication
Mutagenesisi68 – 681G → A: Reduces catalytic activity between 5- to 25-fold. 1 Publication
Mutagenesisi68 – 681G → R: Abolishes catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Protein arginine N-methyltransferase 1PRO_0000212341Add
BLAST

Proteomic databases

MaxQBiP38074.
PaxDbiP38074.
PeptideAtlasiP38074.

Expressioni

Gene expression databases

GenevestigatoriP38074.

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. 301 interactions.
DIPiDIP-2608N.
IntActiP38074. 265 interactions.
MINTiMINT-423994.
STRINGi4932.YBR034C.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 378
Helixi40 – 5718
Beta strandi61 – 655
Helixi71 – 788
Beta strandi82 – 909
Helixi92 – 10211
Turni106 – 1083
Beta strandi109 – 1146
Turni116 – 1183
Beta strandi122 – 1243
Beta strandi126 – 1316
Helixi144 – 15411
Beta strandi155 – 1639
Beta strandi165 – 1739
Helixi176 – 18510
Helixi197 – 2015
Beta strandi206 – 2083
Helixi212 – 2143
Beta strandi220 – 2267
Turni227 – 2293
Helixi232 – 2354
Beta strandi236 – 24510
Beta strandi250 – 26112
Beta strandi272 – 2743
Beta strandi286 – 29611
Beta strandi302 – 31211
Beta strandi315 – 32814
Helixi334 – 3374
Beta strandi339 – 3479

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G6QX-ray2.901/2/3/4/5/621-348[»]
ProteinModelPortaliP38074.
SMRiP38074. Positions 28-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38074.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 322303SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
InParanoidiP38074.
KOiK11434.
OMAiDIDFTAC.
OrthoDBiEOG7WDNBC.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi S45890.
RefSeqi NP_009590.1. NM_001178382.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G6Q X-ray 2.90 1/2/3/4/5/6 21-348 [» ]
ProteinModelPortali P38074.
SMRi P38074. Positions 28-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32735. 301 interactions.
DIPi DIP-2608N.
IntActi P38074. 265 interactions.
MINTi MINT-423994.
STRINGi 4932.YBR034C.

Proteomic databases

MaxQBi P38074.
PaxDbi P38074.
PeptideAtlasi P38074.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR034C ; YBR034C ; YBR034C .
GeneIDi 852322.
KEGGi sce:YBR034C.

Organism-specific databases

CYGDi YBR034c.
SGDi S000000238. HMT1.

Phylogenomic databases

eggNOGi COG0500.
GeneTreei ENSGT00550000074406.
HOGENOMi HOG000198521.
InParanoidi P38074.
KOi K11434.
OMAi DIDFTAC.
OrthoDBi EOG7WDNBC.

Enzyme and pathway databases

BioCyci YEAST:G3O-29011-MONOMER.

Miscellaneous databases

EvolutionaryTracei P38074.
NextBioi 971020.

Gene expression databases

Genevestigatori P38074.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025799. Arg_MeTrfase.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
PANTHERi PTHR11006. PTHR11006. 1 hit.
Pfami PF13847. Methyltransf_31. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51678. SAM_MT_PRMT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene."
    Smits P.H.M., de Haan M., Maat C., Grivell L.A.
    Yeast 10:S75-S80(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Sterol uptake induced by an impairment of pyridoxal phosphate synthesis in Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding pyridoxine (pyridoxamine) phosphate oxidase."
    Loubbardi A., Karst F., Guilloton M., Marcireau C.
    J. Bacteriol. 177:1817-1823(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
  6. "A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins."
    Henry M.F., Silver P.A.
    Mol. Cell. Biol. 16:3668-3678(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  7. "The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae."
    Gary J.D., Lin W.-J., Yang M.C., Herschmann H.R., Clarke S.
    J. Biol. Chem. 271:12585-12594(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  8. "Arginine methylation facilitates the nuclear export of hnRNP proteins."
    Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.
    Genes Dev. 12:679-691(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions."
    McBride A.E., Weiss V.H., Kim H.K., Hogle J.M., Silver P.A.
    J. Biol. Chem. 275:3128-3136(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-18 AND GLY-68.
  10. "Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p."
    Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H.
    J. Biol. Chem. 277:7752-7760(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase."
    Lacoste N., Utley R.T., Hunter J.M., Poirier G.G., Cote J.
    J. Biol. Chem. 277:30421-30424(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "In vivo analysis of nucleolar proteins modified by the yeast arginine methyltransferase Hmt1/Rmt1p."
    Xu C., Henry P.A., Setya A., Henry M.F.
    RNA 9:746-759(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors."
    Yu M.C., Bachand F., McBride A.E., Komili S., Casolari J.M., Silver P.A.
    Genes Dev. 18:2024-2035(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The role of protein arginine methylation in the formation of silent chromatin."
    Yu M.C., Lamming D.W., Eskin J.A., Sinclair D.A., Silver P.A.
    Genes Dev. 20:3249-3254(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae."
    Lipson R.S., Webb K.J., Clarke S.G.
    Biochem. Biophys. Res. Commun. 391:1658-1662(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors."
    Chen Y.C., Milliman E.J., Goulet I., Cote J., Jackson C.A., Vollbracht J.A., Yu M.C.
    Mol. Cell. Biol. 30:5245-5256(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Yeast arginine methyltransferase Hmt1p regulates transcription elongation and termination by methylating Npl3p."
    Wong C.M., Tang H.M., Kong K.Y., Wong G.W., Qiu H., Jin D.Y., Hinnebusch A.G.
    Nucleic Acids Res. 38:2217-2228(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Proteomic analysis of interactors for yeast protein arginine methyltransferase Hmt1 reveals novel substrate and insights into additional biological roles."
    Jackson C.A., Yadav N., Min S., Li J., Milliman E.J., Qu J., Chen Y.C., Yu M.C.
    Proteomics 12:3304-3314(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRE5; MTR4; SNF2; SUM1 AND SSD1.
  20. "The structure and oligomerization of the yeast arginine methyltransferase, Hmt1."
    Weiss V.H., McBride A.E., Soriano M.A., Filman D.J., Silver P.A., Hogle J.M.
    Nat. Struct. Biol. 7:1165-1171(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-348, FUNCTION, INTERACTION WITH NPL3, SUBUNIT.

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: October 29, 2014
This is version 132 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

External Data

Dasty 3