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Protein

Protein arginine N-methyltransferase 8

Gene

Prmt8

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

Functioni

Membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei86S-adenosyl-L-methionineBy similarity1
Binding sitei95S-adenosyl-L-methionineBy similarity1
Binding sitei119S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Binding sitei141S-adenosyl-L-methionineBy similarity1
Binding sitei170S-adenosyl-L-methionineBy similarity1
Active sitei185By similarity1
Active sitei194By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.125. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein arginine N-methyltransferase 8 (EC:2.1.1.-)
Alternative name(s):
Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
Gene namesi
Name:Prmt8
Synonyms:Hrmt1l4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:3043083. Prmt8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002123302 – 394Protein arginine N-methyltransferase 8Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei58Omega-N-methylarginine; by PRMT8By similarity1
Modified residuei73Asymmetric dimethylarginine; by PRMT8By similarity1

Keywords - PTMi

Lipoprotein, Methylation, Myristate

Proteomic databases

MaxQBiQ6PAK3.
PaxDbiQ6PAK3.
PeptideAtlasiQ6PAK3.
PRIDEiQ6PAK3.

PTM databases

PhosphoSitePlusiQ6PAK3.

Expressioni

Tissue specificityi

Brain-specific. Only expressed in neurons, especially in the somatosensory and limbic systems, and a part of motor system. Highly expressed in all of the regions related to general somatosensory system. Expressed in most of the relay nuclei intervening the special somatosensory system, such as the auditory, visual and vestibular systems. Also present in forebrain limbic areas and thalamic nuclei relevant to limbic areas and in areas related to the motor system, such as the caudate putamen, Purkinje cells, inferior olivary nucleus and cerebellar nuclei.1 Publication

Gene expression databases

BgeeiENSMUSG00000030350.
CleanExiMM_PRMT8.
GenevisibleiQ6PAK3. MM.

Interactioni

Subunit structurei

Homodimers and heterodimers with PRMT1 or PRMT2, recruiting PRMT1 to the cell membrane. Interacts with PRMT2 and FYN (via the SH3 domain). Interacts with EWS; independently of EWS methylation status (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032500.

Structurei

3D structure databases

ProteinModelPortaliQ6PAK3.
SMRiQ6PAK3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 394SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST322

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi29 – 42SH3-binding 1By similarityAdd BLAST14
Motifi53 – 58SH3-binding 2By similarity6

Domaini

The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein.By similarity
The N-terminal region (1-60) inhibits the enzymatic activity.By similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase PRMT-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ6PAK3.
KOiK11439.
OMAiFVIDINF.
OrthoDBiEOG091G0ADC.
PhylomeDBiQ6PAK3.
TreeFamiTF300608.

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.

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

Q6PAK3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGMKHSSRCL LLRRKMAENA VESTEVSSAP PQPPQPVIPA KPVQCVHHVS
60 70 80 90 100
TQPSCPGRGK MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR
110 120 130 140 150
NSMYHNKHVF KDKVVLDVGS GTGILSMFAA KAGAKKVFGI ECSSISDYSE
160 170 180 190 200
KIIKANHLDN VITIFKGKVE EVELPVEKVD IIISEWMGYC LFYESMLNTV
210 220 230 240 250
IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE NVYGFDMTCI
260 270 280 290 300
RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
310 320 330 340 350
NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR
360 370 380 390
GEEIYGTISM KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR
Length:394
Mass (Da):45,276
Last modified:June 7, 2005 - v2
Checksum:iA3A8B337C376D970
GO

Sequence cautioni

The sequence AAH60250 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127373 Genomic DNA. No translation available.
BC060250 mRNA. Translation: AAH60250.1. Different initiation.
BK001349 mRNA. Translation: DAA01382.1.
CCDSiCCDS57449.1.
RefSeqiNP_958759.2. NM_201371.2.
UniGeneiMm.39750.

Genome annotation databases

EnsembliENSMUST00000032500; ENSMUSP00000032500; ENSMUSG00000030350.
GeneIDi381813.
KEGGimmu:381813.
UCSCiuc009dwb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC127373 Genomic DNA. No translation available.
BC060250 mRNA. Translation: AAH60250.1. Different initiation.
BK001349 mRNA. Translation: DAA01382.1.
CCDSiCCDS57449.1.
RefSeqiNP_958759.2. NM_201371.2.
UniGeneiMm.39750.

3D structure databases

ProteinModelPortaliQ6PAK3.
SMRiQ6PAK3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000032500.

PTM databases

PhosphoSitePlusiQ6PAK3.

Proteomic databases

MaxQBiQ6PAK3.
PaxDbiQ6PAK3.
PeptideAtlasiQ6PAK3.
PRIDEiQ6PAK3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032500; ENSMUSP00000032500; ENSMUSG00000030350.
GeneIDi381813.
KEGGimmu:381813.
UCSCiuc009dwb.2. mouse.

Organism-specific databases

CTDi56341.
MGIiMGI:3043083. Prmt8.

Phylogenomic databases

eggNOGiKOG1499. Eukaryota.
ENOG410XQYH. LUCA.
GeneTreeiENSGT00550000074406.
HOGENOMiHOG000198521.
HOVERGENiHBG001793.
InParanoidiQ6PAK3.
KOiK11439.
OMAiFVIDINF.
OrthoDBiEOG091G0ADC.
PhylomeDBiQ6PAK3.
TreeFamiTF300608.

Enzyme and pathway databases

BRENDAi2.1.1.125. 3474.

Miscellaneous databases

PROiQ6PAK3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030350.
CleanExiMM_PRMT8.
GenevisibleiQ6PAK3. MM.

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 nameiANM8_MOUSE
AccessioniPrimary (citable) accession number: Q6PAK3
Secondary accession number(s): Q7M6Z2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.