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Entry version 158 (12 Aug 2020)
Sequence version 2 (21 Feb 2006)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602, PubMed:26529540). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (PubMed:18320585).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.3 µM for GRGGFGGRGGFRGGRGG-NH21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei86S-adenosyl-L-methionineBy similarity1
    Binding sitei95S-adenosyl-L-methionineCombined sources2 Publications1
    Binding sitei119S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei141S-adenosyl-L-methionineCombined sources2 Publications1
    Binding sitei170S-adenosyl-L-methionineCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei185By similarity1
    Active sitei194By similarity1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMethyltransferase, Transferase
    LigandS-adenosyl-L-methionine

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.1.125, 2681

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    Q9NR22

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9NR22

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Protein arginine N-methyltransferase 8Curated (EC:2.1.1.3193 Publications, EC:2.1.1.3213 Publications)
    Alternative name(s):
    Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:PRMT8Combined sources
    Synonyms:HRMT1L3, HRMT1L4
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000111218.11

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:5188, PRMT8

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    610086, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9NR22

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2G → A: Loss of cell membrane localization. 2 Publications1
    Mutagenesisi273C → A: No effect on homodimerization but decreased homooligomerization; when associated with A-295 and A-349. 1 Publication1
    Mutagenesisi295C → A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-349. 1 Publication1
    Mutagenesisi303Y → A: Decreases homooligomerization and cell membrane localization. No effect on homodimerization, S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-345 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-345 and A-382. 1 Publication1
    Mutagenesisi345Y → A: No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-382. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-382. 1 Publication1
    Mutagenesisi349R → A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-295. 1 Publication1
    Mutagenesisi382L → A: No effect on homooligomerization. No effect on S-adenosyl-L-methionine binding and EWS protein methylation. No effect on homodimerization but loss of homooligomerization and cell membrane localization; when associated with A-303 and A-345. No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-303 and A-345. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    56341

    Open Targets

    More...
    OpenTargetsi
    ENSG00000111218

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA134903406

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q9NR22, Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3108648

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    1259

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    PRMT8

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    88983969

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002123292 – 394Protein arginine N-methyltransferase 8Add BLAST393

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine2 Publications1
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei58Omega-N-methylarginine; by autocatalysis1 Publication1
    Modified residuei73Asymmetric dimethylarginine; by autocatalysis1 Publication1

    Keywords - PTMi

    Lipoprotein, Methylation, Myristate

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9NR22

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9NR22

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q9NR22

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q9NR22

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9NR22

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9NR22

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9NR22

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    82259 [Q9NR22-1]
    82260 [Q9NR22-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9NR22

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q9NR22

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Brain-specific.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000111218, Expressed in middle temporal gyrus and 87 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9NR22, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000111218, Tissue enriched (brain)

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer (PubMed:16051612, PubMed:26876602, PubMed:26529540). Tetramer; individual homodimers associates to form a homotetramer (PubMed:26529540). Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane (PubMed:26876602). Heterodimer with PRMT1; heterodimerization may recruit PRMT1 activity to the plasma membrane (PubMed:16051612).

    Interacts with PRMT2 (via the SH3 domain) (PubMed:17925405).

    Interacts with FYN (via the SH3 domain) (PubMed:17925405).

    Interacts with EWS; independently of EWS methylation status (PubMed:18320585).

    5 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    121140, 51 interactors

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    Q9NR22

    Protein interaction database and analysis system

    More...
    IntActi
    Q9NR22, 36 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q9NR22

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000372067

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9NR22

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    Q9NR22, protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1394
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9NR22

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini73 – 394SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST322

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni119 – 122S-adenosyl-L-methionine bindingCombined sources2 Publications4

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi29 – 42SH3-binding 11 PublicationAdd BLAST14
    Motifi53 – 58SH3-binding 21 Publication6

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 arginine N-methyltransferase activity.1 Publication

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1499, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155867

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_017375_1_1_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9NR22

    KEGG Orthology (KO)

    More...
    KOi
    K11439

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CMVKEVD

    Database of Orthologous Groups

    More...
    OrthoDBi
    840669at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9NR22

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300608

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR025799, Arg_MeTrfase
    IPR029063, SAM-dependent_MTases

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53335, SSF53335, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51678, SAM_MT_PRMT, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
    Isoform 1 (identifier: Q9NR22-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

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    Length:385
    Mass (Da):44,169
    Checksum:i20E4A89EFD1C520D
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti150E → Q in AAH22458 (PubMed:15489334).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0374661 – 25MGMKH…AESTE → MESLASDGFKLKEVSS in isoform 2. 1 PublicationAdd BLAST25

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

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    EMBLi

    GenBank nucleotide sequence database

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    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

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    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.

    The Consensus CDS (CCDS) project

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    CCDSi
    CCDS58200.1 [Q9NR22-2]
    CCDS8521.2 [Q9NR22-1]

    NCBI Reference Sequences

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    RefSeqi
    NP_001243465.1, NM_001256536.1 [Q9NR22-2]
    NP_062828.3, NM_019854.4 [Q9NR22-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

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    Ensembli
    ENST00000382622; ENSP00000372067; ENSG00000111218 [Q9NR22-1]
    ENST00000452611; ENSP00000414507; ENSG00000111218 [Q9NR22-2]

    Database of genes from NCBI RefSeq genomes

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    GeneIDi
    56341

    KEGG: Kyoto Encyclopedia of Genes and Genomes

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    KEGGi
    hsa:56341

    UCSC genome browser

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    UCSCi
    uc001qmf.5, human [Q9NR22-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

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    PDBei

    Protein Data Bank RCSB

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    RCSB PDBi

    Protein Data Bank Japan

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    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[»]
    SMRiQ9NR22
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi121140, 51 interactors
    ELMiQ9NR22
    IntActiQ9NR22, 36 interactors
    MINTiQ9NR22
    STRINGi9606.ENSP00000372067

    Chemistry databases

    BindingDBiQ9NR22
    ChEMBLiCHEMBL3108648
    GuidetoPHARMACOLOGYi1259

    PTM databases

    iPTMnetiQ9NR22
    PhosphoSitePlusiQ9NR22

    Polymorphism and mutation databases

    BioMutaiPRMT8
    DMDMi88983969

    Proteomic databases

    EPDiQ9NR22
    jPOSTiQ9NR22
    MassIVEiQ9NR22
    MaxQBiQ9NR22
    PaxDbiQ9NR22
    PeptideAtlasiQ9NR22
    PRIDEiQ9NR22
    ProteomicsDBi82259 [Q9NR22-1]
    82260 [Q9NR22-2]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

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    Antibodypediai
    10506, 164 antibodies

    The DNASU plasmid repository

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    DNASUi
    56341

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

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    CTDi
    56341
    DisGeNETi56341
    EuPathDBiHostDB:ENSG00000111218.11

    GeneCards: human genes, protein and diseases

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    GeneCardsi
    PRMT8
    HGNCiHGNC:5188, PRMT8
    HPAiENSG00000111218, Tissue enriched (brain)
    MIMi610086, gene
    neXtProtiNX_Q9NR22
    OpenTargetsiENSG00000111218
    PharmGKBiPA134903406

    GenAtlas: human gene database

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    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1499, Eukaryota
    GeneTreeiENSGT00940000155867
    HOGENOMiCLU_017375_1_1_1
    InParanoidiQ9NR22
    KOiK11439
    OMAiCMVKEVD
    OrthoDBi840669at2759
    PhylomeDBiQ9NR22
    TreeFamiTF300608

    Enzyme and pathway databases

    BRENDAi2.1.1.125, 2681
    PathwayCommonsiQ9NR22
    SABIO-RKiQ9NR22

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

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    BioGRID-ORCSi
    56341, 4 hits in 876 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    PRMT8, human

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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    GenomeRNAii
    56341
    PharosiQ9NR22, Tchem

    Protein Ontology

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    PROi
    PR:Q9NR22
    RNActiQ9NR22, protein

    The Stanford Online Universal Resource for Clones and ESTs

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    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000111218, Expressed in middle temporal gyrus and 87 other tissues
    GenevisibleiQ9NR22, HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR025799, Arg_MeTrfase
    IPR029063, SAM-dependent_MTases
    SUPFAMiSSF53335, SSF53335, 1 hit
    PROSITEiView protein in PROSITE
    PS51678, SAM_MT_PRMT, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiANM8_HUMAN
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NR22
    Secondary accession number(s): B2RDP0, Q8TBJ8
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: February 21, 2006
    Last modified: August 12, 2020
    This is version 158 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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
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