Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website on Tuesday, June 28. Please explore and share your feedback. Take me to UniProt BETA

UniProtKB - Q9NR22 (ANM8_HUMAN)

Entry version 166 (25 May 2022)
Sequence version 2 (21 Feb 2006)
Previous versions | rss
Add a publicationFeedback
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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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		2.1.1.319, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9NR22

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9NR22

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		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)
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:PRMT8Imported
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000111218

<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

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

Genetic variation 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 88 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 enhanced (brain, retina, testis)

<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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		121140, 87 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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q9NR22

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>Regioni16 – 40DisorderedSequence analysisAdd BLAST25
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

Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily.PROSITE-ProRule annotation

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

Identification of Orthologs from Complete Genome Data

More...OMAi		RNDFVHA

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

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.50.150, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

More...PANTHERi		PTHR11006, PTHR11006, 1 hit

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.<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 <p><strong>What is the canonical sequence?</strong><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

Show »
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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

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

NCBI Reference Sequences

More...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

More...Ensembli		ENST00000382622.4; ENSP00000372067.3; ENSG00000111218.12
ENST00000452611.6; ENSP00000414507.2; ENSG00000111218.12 [Q9NR22-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		56341

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:56341

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000382622.4; ENSP00000372067.3; NM_019854.5; NP_062828.3

UCSC genome browser

More...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

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
AlphaFoldDBiQ9NR22
SMRiQ9NR22
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi121140, 87 interactors
ELMiQ9NR22
IntActiQ9NR22, 36 interactors
MINTiQ9NR22
STRINGi9606.ENSP00000372067

Chemistry databases

BindingDBiQ9NR22
ChEMBLiCHEMBL3108648
GuidetoPHARMACOLOGYi1259

PTM databases

iPTMnetiQ9NR22
PhosphoSitePlusiQ9NR22

Genetic variation 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

More...Antibodypediai		10506, 169 antibodies from 27 providers

The DNASU plasmid repository

More...DNASUi		56341

Genome annotation databases

EnsembliENST00000382622.4; ENSP00000372067.3; ENSG00000111218.12
ENST00000452611.6; ENSP00000414507.2; ENSG00000111218.12 [Q9NR22-2]
GeneIDi56341
KEGGihsa:56341
MANE-SelectiENST00000382622.4; ENSP00000372067.3; NM_019854.5; NP_062828.3
UCSCiuc001qmf.5, human [Q9NR22-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		56341
DisGeNETi56341

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRMT8
HGNCiHGNC:5188, PRMT8
HPAiENSG00000111218, Tissue enhanced (brain, retina, testis)
MIMi610086, gene
neXtProtiNX_Q9NR22
OpenTargetsiENSG00000111218
PharmGKBiPA134903406
VEuPathDBiHostDB:ENSG00000111218

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1499, Eukaryota
GeneTreeiENSGT00940000155867
HOGENOMiCLU_017375_1_1_1
InParanoidiQ9NR22
OMAiRNDFVHA
OrthoDBi840669at2759
PhylomeDBiQ9NR22
TreeFamiTF300608

Enzyme and pathway databases

BRENDAi2.1.1.319, 2681
PathwayCommonsiQ9NR22
SABIO-RKiQ9NR22
SignaLinkiQ9NR22

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		56341, 8 hits in 1082 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

More...GenomeRNAii		56341
PharosiQ9NR22, Tchem

Protein Ontology

More...PROi		PR:Q9NR22
RNActiQ9NR22, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000111218, Expressed in middle temporal gyrus and 88 other tissues
GenevisibleiQ9NR22, HS

Family and domain databases

Gene3Di3.40.50.150, 1 hit
InterProiView protein in InterPro
IPR025799, Arg_MeTrfase
IPR029063, SAM-dependent_MTases
PANTHERiPTHR11006, PTHR11006, 1 hit
SUPFAMiSSF53335, SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51678, SAM_MT_PRMT, 1 hit

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: May 25, 2022
This is version 166 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again