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Protein

Protein arginine N-methyltransferase 8

Gene

PRMT8

Organism
Homo sapiens (Human)
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.3 Publications

Kineticsi

  1. KM=1.3 µM for GRGGFGGRGGFRGGRGG-NH21 Publication

    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

    • histone-arginine N-methyltransferase activity Source: HGNC
    • identical protein binding Source: IntAct
    • protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
    • protein-arginine omega-N monomethyltransferase activity Source: UniProtKB
    • protein heterodimerization activity Source: HGNC
    • protein homodimerization activity Source: HGNC
    • S-adenosylmethionine-dependent methyltransferase activity Source: HGNC

    GO - Biological processi

    • histone methylation Source: HGNC
    • peptidyl-arginine methylation Source: UniProtKB
    • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: HGNC
    • regulation of protein binding Source: HGNC
    • regulation of transcription, DNA-templated Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000111218-MONOMER.
    BRENDAi2.1.1.125. 2681.
    SABIO-RKQ9NR22.

    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:HRMT1L3, HRMT1L4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5188. PRMT8.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: GO_Central
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi2G → A: Loss of cell membrane localization. 1 Publication1

    Organism-specific databases

    DisGeNETi56341.
    OpenTargetsiENSG00000111218.
    PharmGKBiPA134903406.

    Chemistry databases

    ChEMBLiCHEMBL3108648.
    GuidetoPHARMACOLOGYi1259.

    Polymorphism and mutation databases

    BioMutaiPRMT8.
    DMDMi88983969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00002123292 – 394Protein arginine N-methyltransferase 8Add BLAST393

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Lipidationi2N-myristoyl glycine1 Publication1
    Modified residuei58Omega-N-methylarginine; by autocatalysis1 Publication1
    Modified residuei73Asymmetric dimethylarginine; by autocatalysis1 Publication1

    Keywords - PTMi

    Lipoprotein, Methylation, Myristate

    Proteomic databases

    EPDiQ9NR22.
    MaxQBiQ9NR22.
    PaxDbiQ9NR22.
    PeptideAtlasiQ9NR22.
    PRIDEiQ9NR22.

    PTM databases

    iPTMnetiQ9NR22.
    PhosphoSitePlusiQ9NR22.

    Expressioni

    Tissue specificityi

    Brain-specific.1 Publication

    Gene expression databases

    BgeeiENSG00000111218.
    CleanExiHS_PRMT8.
    GenevisibleiQ9NR22. HS.

    Organism-specific databases

    HPAiHPA039747.

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-745545,EBI-745545
    PRMT1Q998735EBI-10186886,EBI-78738
    PRMT1Q99873-44EBI-745545,EBI-12217323
    SYNCRIPO605063EBI-745545,EBI-1024357

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein heterodimerization activity Source: HGNC
    • protein homodimerization activity Source: HGNC

    Protein-protein interaction databases

    BioGridi121140. 39 interactors.
    IntActiQ9NR22. 11 interactors.
    MINTiMINT-3072538.
    STRINGi9606.ENSP00000372067.

    Chemistry databases

    BindingDBiQ9NR22.

    Structurei

    Secondary structure

    1394
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi83 – 91Combined sources9
    Helixi93 – 104Combined sources12
    Helixi107 – 110Combined sources4
    Beta strandi114 – 119Combined sources6
    Helixi124 – 131Combined sources8
    Beta strandi135 – 141Combined sources7
    Helixi145 – 155Combined sources11
    Turni159 – 161Combined sources3
    Beta strandi162 – 167Combined sources6
    Turni169 – 171Combined sources3
    Beta strandi175 – 177Combined sources3
    Beta strandi179 – 183Combined sources5
    Turni192 – 194Combined sources3
    Helixi197 – 207Combined sources11
    Beta strandi208 – 216Combined sources9
    Beta strandi218 – 226Combined sources9
    Helixi229 – 235Combined sources7
    Helixi237 – 240Combined sources4
    Helixi248 – 255Combined sources8
    Beta strandi259 – 261Combined sources3
    Helixi265 – 267Combined sources3
    Beta strandi273 – 279Combined sources7
    Turni280 – 282Combined sources3
    Helixi285 – 288Combined sources4
    Beta strandi289 – 298Combined sources10
    Beta strandi300 – 315Combined sources16
    Beta strandi318 – 320Combined sources3
    Beta strandi322 – 325Combined sources4
    Beta strandi337 – 348Combined sources12
    Beta strandi353 – 362Combined sources10
    Beta strandi364 – 366Combined sources3
    Beta strandi369 – 379Combined sources11
    Beta strandi384 – 393Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4X41X-ray3.50A/B61-394[»]
    5DSTX-ray2.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O68-394[»]
    ProteinModelPortaliQ9NR22.
    SMRiQ9NR22.
    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 1Add BLAST14
    Motifi53 – 58SH3-binding 26

    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.1 Publication
    The N-terminal region (1-60) inhibits the enzymatic activity.1 Publication

    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.
    InParanoidiQ9NR22.
    KOiK11439.
    OMAiFVIDINF.
    OrthoDBiEOG091G0ADC.
    PhylomeDBiQ9NR22.
    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]

    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: Q9NR22-1) [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
    MGMKHSSRCL LLRRKMAENA AESTEVNSPP SQPPQPVVPA 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 IITIFKGKVE 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):45,291
    Last modified:February 21, 2006 - v2
    Checksum:i44B55438D16394CD
    GO
    Isoform 2 (identifier: Q9NR22-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MGMKHSSRCLLLRRKMAENAAESTE → MESLASDGFKLKEVSS

    Note: No experimental confirmation available.
    Show »
    Length:385
    Mass (Da):44,169
    Checksum:i20E4A89EFD1C520D
    GO

    Sequence cautioni

    The sequence AAF91390 differs from that shown. Reason: Erroneous initiation.Curated
    The sequence BAG37987 differs from that shown. Reason: Frameshift at position 45.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti150E → Q in AAH22458 (PubMed:15489334).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0374661 – 25MGMKH…AESTE → MESLASDGFKLKEVSS in isoform 2. 1 PublicationAdd BLAST25

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK315619 mRNA. Translation: BAG37987.1. Frameshift.
    AC005831 Genomic DNA. No translation available.
    AC005908 Genomic DNA. No translation available.
    AC005925 Genomic DNA. No translation available.
    BC022458 mRNA. Translation: AAH22458.2.
    AF263539 mRNA. Translation: AAF91390.1. Different initiation.
    CCDSiCCDS58200.1. [Q9NR22-2]
    CCDS8521.2. [Q9NR22-1]
    RefSeqiNP_001243465.1. NM_001256536.1. [Q9NR22-2]
    NP_062828.3. NM_019854.4. [Q9NR22-1]
    UniGeneiHs.504530.

    Genome annotation databases

    EnsembliENST00000382622; ENSP00000372067; ENSG00000111218. [Q9NR22-1]
    ENST00000452611; ENSP00000414507; ENSG00000111218. [Q9NR22-2]
    GeneIDi56341.
    KEGGihsa:56341.
    UCSCiuc001qmf.5. human. [Q9NR22-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK315619 mRNA. Translation: BAG37987.1. Frameshift.
    AC005831 Genomic DNA. No translation available.
    AC005908 Genomic DNA. No translation available.
    AC005925 Genomic DNA. No translation available.
    BC022458 mRNA. Translation: AAH22458.2.
    AF263539 mRNA. Translation: AAF91390.1. Different initiation.
    CCDSiCCDS58200.1. [Q9NR22-2]
    CCDS8521.2. [Q9NR22-1]
    RefSeqiNP_001243465.1. NM_001256536.1. [Q9NR22-2]
    NP_062828.3. NM_019854.4. [Q9NR22-1]
    UniGeneiHs.504530.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4X41X-ray3.50A/B61-394[»]
    5DSTX-ray2.96A/B/C/D/E/F/G/H/I/J/K/L/M/N/O68-394[»]
    ProteinModelPortaliQ9NR22.
    SMRiQ9NR22.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121140. 39 interactors.
    IntActiQ9NR22. 11 interactors.
    MINTiMINT-3072538.
    STRINGi9606.ENSP00000372067.

    Chemistry databases

    BindingDBiQ9NR22.
    ChEMBLiCHEMBL3108648.
    GuidetoPHARMACOLOGYi1259.

    PTM databases

    iPTMnetiQ9NR22.
    PhosphoSitePlusiQ9NR22.

    Polymorphism and mutation databases

    BioMutaiPRMT8.
    DMDMi88983969.

    Proteomic databases

    EPDiQ9NR22.
    MaxQBiQ9NR22.
    PaxDbiQ9NR22.
    PeptideAtlasiQ9NR22.
    PRIDEiQ9NR22.

    Protocols and materials databases

    DNASUi56341.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000382622; ENSP00000372067; ENSG00000111218. [Q9NR22-1]
    ENST00000452611; ENSP00000414507; ENSG00000111218. [Q9NR22-2]
    GeneIDi56341.
    KEGGihsa:56341.
    UCSCiuc001qmf.5. human. [Q9NR22-1]

    Organism-specific databases

    CTDi56341.
    DisGeNETi56341.
    GeneCardsiPRMT8.
    H-InvDBHIX0010342.
    HGNCiHGNC:5188. PRMT8.
    HPAiHPA039747.
    MIMi610086. gene.
    neXtProtiNX_Q9NR22.
    OpenTargetsiENSG00000111218.
    PharmGKBiPA134903406.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1499. Eukaryota.
    ENOG410XQYH. LUCA.
    GeneTreeiENSGT00550000074406.
    HOGENOMiHOG000198521.
    HOVERGENiHBG001793.
    InParanoidiQ9NR22.
    KOiK11439.
    OMAiFVIDINF.
    OrthoDBiEOG091G0ADC.
    PhylomeDBiQ9NR22.
    TreeFamiTF300608.

    Enzyme and pathway databases

    BioCyciZFISH:ENSG00000111218-MONOMER.
    BRENDAi2.1.1.125. 2681.
    SABIO-RKQ9NR22.

    Miscellaneous databases

    ChiTaRSiPRMT8. human.
    GenomeRNAii56341.
    PROiQ9NR22.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000111218.
    CleanExiHS_PRMT8.
    GenevisibleiQ9NR22. HS.

    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_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR22
    Secondary accession number(s): B2RDP0, Q8TBJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 21, 2006
    Last modified: November 30, 2016
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.