Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein arginine N-methyltransferase 3

Gene

Prmt3

Organism
Rattus norvegicus (Rat)
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.1 Publication

Enzyme regulationi

Inhibited by N-ethylmaleimide and high concentrations of zinc chloride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei227 – 2271S-adenosyl-L-methionineBy similarity
Binding sitei236 – 2361S-adenosyl-L-methionine
Binding sitei260 – 2601S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei282 – 2821S-adenosyl-L-methionine
Binding sitei311 – 3111S-adenosyl-L-methionine
Active sitei326 – 32611 Publication
Active sitei335 – 33511 Publication

Regions

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

GO - Molecular functioni

  • histone-arginine N-methyltransferase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • modified amino acid binding Source: RGD
  • protein-arginine N-methyltransferase activity Source: RGD
  • protein-arginine omega-N asymmetric methyltransferase activity Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD

GO - Biological processi

  • dendritic spine morphogenesis Source: RGD
  • peptidyl-arginine methylation Source: RGD
  • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: RGD
  • 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi620413. Prmt3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 528527Protein arginine N-methyltransferase 3PRO_0000212328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei169 – 1691PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO70467.
PRIDEiO70467.

PTM databases

iPTMnetiO70467.
PhosphoSiteiO70467.

Expressioni

Gene expression databases

BgeeiENSRNOG00000014829.
ExpressionAtlasiO70467. baseline and differential.
GenevisibleiO70467. RN.

Interactioni

Subunit structurei

Monomer or homodimer. Interacts with the 40S ribosomal protein RPS2 (By similarity). Interacts with EPB41L3; this inhibits methylation of target proteins.By similarity2 Publications

Protein-protein interaction databases

IntActiO70467. 1 interaction.
STRINGi10116.ENSRNOP00000020853.

Structurei

Secondary structure

1
528
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi210 – 2123Combined sources
Helixi215 – 2206Combined sources
Beta strandi222 – 2243Combined sources
Helixi225 – 2317Combined sources
Helixi234 – 24613Combined sources
Helixi248 – 2503Combined sources
Turni251 – 2533Combined sources
Beta strandi255 – 2606Combined sources
Helixi265 – 2739Combined sources
Beta strandi276 – 2849Combined sources
Helixi286 – 29611Combined sources
Turni300 – 3023Combined sources
Beta strandi303 – 3086Combined sources
Turni310 – 3123Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi320 – 3245Combined sources
Turni333 – 3353Combined sources
Helixi337 – 34812Combined sources
Beta strandi349 – 3579Combined sources
Beta strandi359 – 3679Combined sources
Helixi370 – 3767Combined sources
Helixi378 – 3814Combined sources
Helixi389 – 3946Combined sources
Turni395 – 3973Combined sources
Beta strandi400 – 4023Combined sources
Helixi406 – 4083Combined sources
Beta strandi414 – 4207Combined sources
Turni421 – 4233Combined sources
Helixi426 – 4294Combined sources
Beta strandi430 – 43910Combined sources
Beta strandi443 – 45614Combined sources
Beta strandi464 – 4674Combined sources
Beta strandi479 – 49012Combined sources
Beta strandi495 – 50410Combined sources
Beta strandi511 – 5188Combined sources
Beta strandi521 – 5277Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3LX-ray2.03A208-528[»]
ProteinModelPortaliO70467.
SMRiO70467. Positions 35-145, 208-528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70467.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 528315SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd
BLAST

Domaini

The zinc-finger is responsible for substrate specificity.

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

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiO70467.
KOiK11436.
PhylomeDBiO70467.

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]

Sequencei

Sequence statusi: Complete.

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

O70467-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCSLAAGNGQ GAELGPEPLE LSDSGDDAGW EDEDADAEPA QGRQHTPCLF
60 70 80 90 100
CDRLFRSAEE TFSHCKLEHQ FNIDGMVHKH GLEFYGYIKL INFIRLKNPT
110 120 130 140 150
VEYMNSIYNP VPWDKDEYLK PVLEDDLLLQ FDVEDLYEPV SAPFTYPNGL
160 170 180 190 200
SENTSAVEKL KLMEARALSA EAALARARED LQKMKQFAQD FVMNVDVRTC
210 220 230 240 250
SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY RDFIYQNPHI
260 270 280 290 300
FKDKVVLDVG CGTGILSMFA AKAGAKKVIA 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 SDPCDIKHID CHTTSISDLE FSSDFTLRTT KTAMCTAVAG
460 470 480 490 500
YFDIYFEKNC HNRVVFSTGP QSTKTHWKQT IFLLEKPFPV KAGEALKGKI
510 520
TVHKNKKDPR SLIVTLTLNS STQTYSLQ
Length:528
Mass (Da):59,420
Last modified:August 1, 1998 - v1
Checksum:iB25D627902594B39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059530 mRNA. Translation: AAC40158.1.
RefSeqiNP_446009.1. NM_053557.1.
UniGeneiRn.33389.

Genome annotation databases

EnsembliENSRNOT00000020853; ENSRNOP00000020853; ENSRNOG00000014829.
GeneIDi89820.
KEGGirno:89820.
UCSCiRGD:620413. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059530 mRNA. Translation: AAC40158.1.
RefSeqiNP_446009.1. NM_053557.1.
UniGeneiRn.33389.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F3LX-ray2.03A208-528[»]
ProteinModelPortaliO70467.
SMRiO70467. Positions 35-145, 208-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70467. 1 interaction.
STRINGi10116.ENSRNOP00000020853.

PTM databases

iPTMnetiO70467.
PhosphoSiteiO70467.

Proteomic databases

PaxDbiO70467.
PRIDEiO70467.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000020853; ENSRNOP00000020853; ENSRNOG00000014829.
GeneIDi89820.
KEGGirno:89820.
UCSCiRGD:620413. rat.

Organism-specific databases

CTDi10196.
RGDi620413. Prmt3.

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiO70467.
KOiK11436.
PhylomeDBiO70467.

Miscellaneous databases

EvolutionaryTraceiO70467.
PROiO70467.

Gene expression databases

BgeeiENSRNOG00000014829.
ExpressionAtlasiO70467. baseline and differential.
GenevisibleiO70467. RN.

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_RAT
AccessioniPrimary (citable) accession number: O70467
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 133 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.