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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei227 – 2271S-adenosyl-L-methionineBy similarity
Binding sitei236 – 2361S-adenosyl-L-methionineBy similarity
Binding sitei260 – 2601S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei282 – 2821S-adenosyl-L-methionineBy similarity
Binding sitei311 – 3111S-adenosyl-L-methionineBy similarity
Active sitei326 – 3261By similarity
Active sitei335 – 3351By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 6924C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. histone-arginine N-methyltransferase activity Source: GO_Central
  2. metal ion binding Source: UniProtKB-KW
  3. methyltransferase activity Source: MGI
  4. modified amino acid binding Source: Ensembl
  5. protein-arginine omega-N asymmetric methyltransferase activity Source: GO_Central

GO - Biological processi

  1. histone arginine methylation Source: GO_Central
  2. negative regulation of protein ubiquitination Source: MGI
  3. peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: GO_Central
  4. protein methylation Source: UniProtKB
  5. 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
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1919224. Prmt3.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 532531Protein arginine N-methyltransferase 3PRO_0000212327Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ922H1.
PaxDbiQ922H1.
PRIDEiQ922H1.

PTM databases

PhosphoSiteiQ922H1.

Expressioni

Gene expression databases

BgeeiQ922H1.
CleanExiMM_PRMT3.
ExpressionAtlasiQ922H1. baseline and differential.
GenevestigatoriQ922H1.

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 interaction.
STRINGi10090.ENSMUSP00000082373.

Structurei

Secondary structure

1
532
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 513Combined sources
Beta strandi54 – 574Combined sources
Helixi58 – 6710Combined sources
Helixi73 – 797Combined sources
Helixi84 – 9613Combined sources
Helixi101 – 1055Combined sources
Helixi116 – 1194Combined sources
Beta strandi122 – 1254Combined sources
Helixi127 – 1304Combined sources
Helixi133 – 1364Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WIRNMR-A38-145[»]
ProteinModelPortaliQ922H1.
SMRiQ922H1. Positions 38-145, 208-532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ922H1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 532319SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri46 – 6924C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ922H1.
KOiK11436.
OMAiNKCWSCG.
PhylomeDBiQ922H1.
TreeFamiTF323587.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR029063. SAM-dependent_MTases.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF06325. PrmA. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei417 – 4204Missing in isoform 2. 2 PublicationsVSP_010498

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1WIRNMR-A38-145[»]
ProteinModelPortaliQ922H1.
SMRiQ922H1. Positions 38-145, 208-532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ922H1. 1 interaction.
STRINGi10090.ENSMUSP00000082373.

PTM databases

PhosphoSiteiQ922H1.

Proteomic databases

MaxQBiQ922H1.
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

eggNOGiCOG0500.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ922H1.
KOiK11436.
OMAiNKCWSCG.
PhylomeDBiQ922H1.
TreeFamiTF323587.

Miscellaneous databases

EvolutionaryTraceiQ922H1.
NextBioi335102.
PROiQ922H1.
SOURCEiSearch...

Gene expression databases

BgeeiQ922H1.
CleanExiMM_PRMT3.
ExpressionAtlasiQ922H1. baseline and differential.
GenevestigatoriQ922H1.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025799. Arg_MeTrfase.
IPR010456. Ribosomal-L11_MeTrfase_PrmA.
IPR029063. SAM-dependent_MTases.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR11006. PTHR11006. 1 hit.
PfamiPF06325. PrmA. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51678. SAM_MT_PRMT. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization, chromosomal mapping, and expression analysis of the murine Prmt3 and Htatip2 genes."
    Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W., Johnson D.K.
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 2).
    Strain: 129/SvJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Head and Thymus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-532 (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Brain and Mammary gland.
  4. "Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 38-145.

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: February 4, 2015
This is version 111 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

External Data

Dasty 3

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 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.