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Protein

Protein arginine N-methyltransferase 3

Gene

Prmt3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.By similarity

Enzyme regulationi

Inhibited by N-ethylmaleimide and high concentrations of zinc chloride.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei227S-adenosyl-L-methionineBy similarity1
Binding sitei236S-adenosyl-L-methionineBy similarity1
Binding sitei260S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei282S-adenosyl-L-methionineBy similarity1
Binding sitei311S-adenosyl-L-methionineBy similarity1
Active sitei326By similarity1
Active sitei335By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri46 – 69C2H2-typeAdd BLAST24

GO - Molecular functioni

GO - Biological processi

  • negative regulation of protein ubiquitination Source: MGI
  • protein methylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 3 (EC:2.1.1.-)
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3
Gene namesi
Name:Prmt3
Synonyms:Hrmt1l3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919224. Prmt3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002123272 – 532Protein arginine N-methyltransferase 3Add BLAST531

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylcysteineBy similarity1
Modified residuei22PhosphoserineCombined sources1
Modified residuei24PhosphoserineCombined sources1
Modified residuei169PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ922H1.
PRIDEiQ922H1.

PTM databases

iPTMnetiQ922H1.
PhosphoSitePlusiQ922H1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030505.
CleanExiMM_PRMT3.
ExpressionAtlasiQ922H1. baseline and differential.
GenevisibleiQ922H1. MM.

Interactioni

Subunit structurei

Monomer or homodimer (By similarity). Interacts with EPB41L3; this inhibits methylation of target proteins. Interacts with the 40S ribosomal protein RPS2 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ922H1. 1 interactor.
STRINGi10090.ENSMUSP00000032715.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 51Combined sources3
Beta strandi54 – 57Combined sources4
Helixi58 – 67Combined sources10
Helixi73 – 79Combined sources7
Helixi84 – 96Combined sources13
Helixi101 – 105Combined sources5
Helixi116 – 119Combined sources4
Beta strandi122 – 125Combined sources4
Helixi127 – 130Combined sources4
Helixi133 – 136Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WIRNMR-A38-145[»]
ProteinModelPortaliQ922H1.
SMRiQ922H1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922H1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini214 – 532SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST319

Domaini

The zinc-finger is responsible for substrate specificity.By similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.PROSITE-ProRule annotation
Contains 1 C2H2-type zinc finger.Curated
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri46 – 69C2H2-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ922H1.
KOiK11436.
OMAiAQDFVMH.
OrthoDBiEOG091G0ADC.
PhylomeDBiQ922H1.
TreeFamiTF323587.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 2 hits.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q922H1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF
60 70 80 90 100
CDRLFASAEE TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT
110 120 130 140 150
VEYMNSIYNP VPWEKDEYLK PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL
160 170 180 190 200
SESASVVEKL KHMEARALSA EAALARARED LQKMKQFAQD FVMNVDVRTC
210 220 230 240 250
SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY RDFIYQNPHI
260 270 280 290 300
FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE
310 320 330 340 350
DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA
360 370 380 390 400
KGGSVYPDIC TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV
410 420 430 440 450
VEVVDHKTLI SDPCDIKMDG KHIDCHTTSI SDLEFSSDFT LRTTKTAMCT
460 470 480 490 500
AVAGYFDIYF EKNCHNRVVF STGPQSTKTH WKQTVFLLEK PFPVKAGEAL
510 520 530
KGKITVHKNK KDPRSLIVTL TLNSSTQTYS LQ
Note: No experimental confirmation available.
Length:532
Mass (Da):59,902
Last modified:June 7, 2004 - v2
Checksum:i878ADDCCF4054F17
GO
Isoform 2 (identifier: Q922H1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-420: Missing.

Show »
Length:528
Mass (Da):59,471
Checksum:iE8DF5B88AB6B92FF
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010498417 – 420Missing in isoform 2. 2 Publications4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY151050 Genomic DNA. Translation: AAN84530.1.
AK031738 mRNA. Translation: BAC27531.1.
AK086646 mRNA. Translation: BAC39708.1.
BC008128 mRNA. Translation: AAH08128.1.
BC050775 mRNA. Translation: AAH50775.1.
CCDSiCCDS21307.1. [Q922H1-2]
RefSeqiNP_598501.1. NM_133740.2. [Q922H1-2]
UniGeneiMm.33202.
Mm.349442.

Genome annotation databases

EnsembliENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505. [Q922H1-2]
GeneIDi71974.
KEGGimmu:71974.
UCSCiuc009hbt.1. mouse. [Q922H1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY151050 Genomic DNA. Translation: AAN84530.1.
AK031738 mRNA. Translation: BAC27531.1.
AK086646 mRNA. Translation: BAC39708.1.
BC008128 mRNA. Translation: AAH08128.1.
BC050775 mRNA. Translation: AAH50775.1.
CCDSiCCDS21307.1. [Q922H1-2]
RefSeqiNP_598501.1. NM_133740.2. [Q922H1-2]
UniGeneiMm.33202.
Mm.349442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WIRNMR-A38-145[»]
ProteinModelPortaliQ922H1.
SMRiQ922H1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ922H1. 1 interactor.
STRINGi10090.ENSMUSP00000032715.

PTM databases

iPTMnetiQ922H1.
PhosphoSitePlusiQ922H1.

Proteomic databases

PaxDbiQ922H1.
PRIDEiQ922H1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505. [Q922H1-2]
GeneIDi71974.
KEGGimmu:71974.
UCSCiuc009hbt.1. mouse. [Q922H1-2]

Organism-specific databases

CTDi10196.
MGIiMGI:1919224. Prmt3.

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ922H1.
KOiK11436.
OMAiAQDFVMH.
OrthoDBiEOG091G0ADC.
PhylomeDBiQ922H1.
TreeFamiTF323587.

Miscellaneous databases

EvolutionaryTraceiQ922H1.
PROiQ922H1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030505.
CleanExiMM_PRMT3.
ExpressionAtlasiQ922H1. baseline and differential.
GenevisibleiQ922H1. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 2 hits.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANM3_MOUSE
AccessioniPrimary (citable) accession number: Q922H1
Secondary accession number(s): Q80VU9, Q8BFV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 7, 2004
Last modified: November 30, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.