UniProtKB - Q9NR22 (ANM8_HUMAN)
Protein arginine N-methyltransferase 8
PRMT8
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 PublicationsCatalytic activityi
- L-arginyl-[protein] + S-adenosyl-L-methionine = H+ + Nω-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine3 PublicationsThis reaction proceeds in the forward1 Publication direction.
- L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H+ + Nω,Nω-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine3 PublicationsEC:2.1.1.3193 PublicationsThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=1.3 µM for GRGGFGGRGGFRGGRGG-NH21 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 86 | S-adenosyl-L-methionineBy similarity | 1 | |
Binding sitei | 95 | S-adenosyl-L-methionineCombined sources2 Publications | 1 | |
Binding sitei | 119 | S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication | 1 | |
Binding sitei | 141 | S-adenosyl-L-methionineCombined sources2 Publications | 1 | |
Binding sitei | 170 | S-adenosyl-L-methionineCombined sources1 Publication | 1 | |
Active sitei | 185 | By similarity | 1 | |
Active sitei | 194 | By similarity | 1 |
GO - Molecular functioni
- enzyme binding Source: HGNC-UCL
- histone-arginine N-methyltransferase activity Source: HGNC-UCL
- identical protein binding Source: UniProtKB
- protein-arginine omega-N asymmetric methyltransferase activity Source: UniProtKB
- protein-arginine omega-N monomethyltransferase activity Source: UniProtKB
- protein homodimerization activity Source: HGNC-UCL
- S-adenosyl-L-methionine binding Source: UniProtKB
- S-adenosylmethionine-dependent methyltransferase activity Source: HGNC-UCL
GO - Biological processi
- histone methylation Source: UniProtKB
- peptidyl-arginine methylation Source: UniProtKB
- peptidyl-arginine methylation, to asymmetrical-dimethyl arginine Source: UniProtKB
- protein homooligomerization Source: UniProtKB
- protein methylation Source: UniProtKB
- regulation of protein binding Source: HGNC-UCL
Keywordsi
Molecular function | Methyltransferase, Transferase |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BRENDAi | 2.1.1.319, 2681 |
PathwayCommonsi | Q9NR22 |
SABIO-RKi | Q9NR22 |
SignaLinki | Q9NR22 |
Names & Taxonomyi
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 |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5188, PRMT8 |
MIMi | 610086, gene |
neXtProti | NX_Q9NR22 |
VEuPathDBi | HostDB:ENSG00000111218 |
Subcellular locationi
Plasma membrane
- Cell membrane 3 Publications; Lipid-anchor 3 Publications; Cytoplasmic side 3 Publications
Plasma Membrane
- anchored component of the cytoplasmic side of the plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 2 | G → A: Loss of cell membrane localization. 2 Publications | 1 | |
Mutagenesisi | 273 | C → A: No effect on homodimerization but decreased homooligomerization; when associated with A-295 and A-349. 1 Publication | 1 | |
Mutagenesisi | 295 | C → A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-349. 1 Publication | 1 | |
Mutagenesisi | 303 | Y → 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 Publication | 1 | |
Mutagenesisi | 345 | Y → 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 Publication | 1 | |
Mutagenesisi | 349 | R → A: No effect on homodimerization but decreased homooligomerization; when associated with A-273 and A-295. 1 Publication | 1 | |
Mutagenesisi | 382 | L → 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 Publication | 1 |
Organism-specific databases
DisGeNETi | 56341 |
OpenTargetsi | ENSG00000111218 |
PharmGKBi | PA134903406 |
Miscellaneous databases
Pharosi | Q9NR22, Tchem |
Chemistry databases
ChEMBLi | CHEMBL3108648 |
GuidetoPHARMACOLOGYi | 1259 |
Genetic variation databases
BioMutai | PRMT8 |
DMDMi | 88983969 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000212329 | 2 – 394 | Protein arginine N-methyltransferase 8Add BLAST | 393 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine2 Publications | 1 | |
Modified residuei | 58 | Omega-N-methylarginine; by autocatalysis1 Publication | 1 | |
Modified residuei | 73 | Asymmetric dimethylarginine; by autocatalysis1 Publication | 1 |
Keywords - PTMi
Lipoprotein, Methylation, MyristateProteomic databases
EPDi | Q9NR22 |
jPOSTi | Q9NR22 |
MassIVEi | Q9NR22 |
MaxQBi | Q9NR22 |
PaxDbi | Q9NR22 |
PeptideAtlasi | Q9NR22 |
PRIDEi | Q9NR22 |
ProteomicsDBi | 82259 [Q9NR22-1] 82260 [Q9NR22-2] |
PTM databases
iPTMneti | Q9NR22 |
PhosphoSitePlusi | Q9NR22 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000111218, Expressed in middle temporal gyrus and 88 other tissues |
Genevisiblei | Q9NR22, HS |
Organism-specific databases
HPAi | ENSG00000111218, Tissue enhanced (brain, retina, testis) |
Interactioni
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 PublicationsBinary interactionsi
Q9NR22
PRMT8 - isoform 2 [Q9NR22-2]
With | #Exp. | IntAct |
---|---|---|
PRMT1 [Q99873] | 5 | EBI-10186886,EBI-78738 |
itself | 3 | EBI-10186886,EBI-10186886 |
SYNCRIP [O60506] | 3 | EBI-10186886,EBI-1024357 |
GO - Molecular functioni
- enzyme binding Source: HGNC-UCL
- identical protein binding Source: UniProtKB
- protein homodimerization activity Source: HGNC-UCL
Protein-protein interaction databases
BioGRIDi | 121140, 87 interactors |
ELMi | Q9NR22 |
IntActi | Q9NR22, 36 interactors |
MINTi | Q9NR22 |
STRINGi | 9606.ENSP00000372067 |
Chemistry databases
BindingDBi | Q9NR22 |
Miscellaneous databases
RNActi | Q9NR22, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9NR22 |
SMRi | Q9NR22 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 73 – 394 | SAM-dependent MTase PRMT-typePROSITE-ProRule annotationAdd BLAST | 322 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 16 – 40 | DisorderedSequence analysisAdd BLAST | 25 | |
Regioni | 119 – 122 | S-adenosyl-L-methionine bindingCombined sources2 Publications | 4 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 29 – 42 | SH3-binding 11 PublicationAdd BLAST | 14 | |
Motifi | 53 – 58 | SH3-binding 21 Publication | 6 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG1499, Eukaryota |
GeneTreei | ENSGT00940000155867 |
HOGENOMi | CLU_017375_1_1_1 |
InParanoidi | Q9NR22 |
OMAi | RNDFVHA |
OrthoDBi | 840669at2759 |
PhylomeDBi | Q9NR22 |
TreeFami | TF300608 |
Family and domain databases
Gene3Di | 3.40.50.150, 1 hit |
InterProi | View protein in InterPro IPR025799, Arg_MeTrfase IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR11006, PTHR11006, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51678, SAM_MT_PRMT, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 150 | E → Q in AAH22458 (PubMed:15489334).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_037466 | 1 – 25 | MGMKH…AESTE → MESLASDGFKLKEVSS in isoform 2. 1 PublicationAdd BLAST | 25 |
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. |
CCDSi | CCDS58200.1 [Q9NR22-2] CCDS8521.2 [Q9NR22-1] |
RefSeqi | NP_001243465.1, NM_001256536.1 [Q9NR22-2] NP_062828.3, NM_019854.4 [Q9NR22-1] |
Genome annotation databases
Ensembli | ENST00000382622.4; ENSP00000372067.3; ENSG00000111218.12 ENST00000452611.6; ENSP00000414507.2; ENSG00000111218.12 [Q9NR22-2] |
GeneIDi | 56341 |
KEGGi | hsa:56341 |
MANE-Selecti | ENST00000382622.4; ENSP00000372067.3; NM_019854.5; NP_062828.3 |
UCSCi | uc001qmf.5, human [Q9NR22-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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. |
CCDSi | CCDS58200.1 [Q9NR22-2] CCDS8521.2 [Q9NR22-1] |
RefSeqi | NP_001243465.1, NM_001256536.1 [Q9NR22-2] NP_062828.3, NM_019854.4 [Q9NR22-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4X41 | X-ray | 3.50 | A/B | 61-394 | [»] | |
5DST | X-ray | 2.96 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O | 68-394 | [»] | |
AlphaFoldDBi | Q9NR22 | |||||
SMRi | Q9NR22 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 121140, 87 interactors |
ELMi | Q9NR22 |
IntActi | Q9NR22, 36 interactors |
MINTi | Q9NR22 |
STRINGi | 9606.ENSP00000372067 |
Chemistry databases
BindingDBi | Q9NR22 |
ChEMBLi | CHEMBL3108648 |
GuidetoPHARMACOLOGYi | 1259 |
PTM databases
iPTMneti | Q9NR22 |
PhosphoSitePlusi | Q9NR22 |
Genetic variation databases
BioMutai | PRMT8 |
DMDMi | 88983969 |
Proteomic databases
EPDi | Q9NR22 |
jPOSTi | Q9NR22 |
MassIVEi | Q9NR22 |
MaxQBi | Q9NR22 |
PaxDbi | Q9NR22 |
PeptideAtlasi | Q9NR22 |
PRIDEi | Q9NR22 |
ProteomicsDBi | 82259 [Q9NR22-1] 82260 [Q9NR22-2] |
Protocols and materials databases
Antibodypediai | 10506, 169 antibodies from 27 providers |
DNASUi | 56341 |
Genome annotation databases
Ensembli | ENST00000382622.4; ENSP00000372067.3; ENSG00000111218.12 ENST00000452611.6; ENSP00000414507.2; ENSG00000111218.12 [Q9NR22-2] |
GeneIDi | 56341 |
KEGGi | hsa:56341 |
MANE-Selecti | ENST00000382622.4; ENSP00000372067.3; NM_019854.5; NP_062828.3 |
UCSCi | uc001qmf.5, human [Q9NR22-1] |
Organism-specific databases
CTDi | 56341 |
DisGeNETi | 56341 |
GeneCardsi | PRMT8 |
HGNCi | HGNC:5188, PRMT8 |
HPAi | ENSG00000111218, Tissue enhanced (brain, retina, testis) |
MIMi | 610086, gene |
neXtProti | NX_Q9NR22 |
OpenTargetsi | ENSG00000111218 |
PharmGKBi | PA134903406 |
VEuPathDBi | HostDB:ENSG00000111218 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1499, Eukaryota |
GeneTreei | ENSGT00940000155867 |
HOGENOMi | CLU_017375_1_1_1 |
InParanoidi | Q9NR22 |
OMAi | RNDFVHA |
OrthoDBi | 840669at2759 |
PhylomeDBi | Q9NR22 |
TreeFami | TF300608 |
Enzyme and pathway databases
BRENDAi | 2.1.1.319, 2681 |
PathwayCommonsi | Q9NR22 |
SABIO-RKi | Q9NR22 |
SignaLinki | Q9NR22 |
Miscellaneous databases
BioGRID-ORCSi | 56341, 8 hits in 1082 CRISPR screens |
ChiTaRSi | PRMT8, human |
GenomeRNAii | 56341 |
Pharosi | Q9NR22, Tchem |
PROi | PR:Q9NR22 |
RNActi | Q9NR22, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000111218, Expressed in middle temporal gyrus and 88 other tissues |
Genevisiblei | Q9NR22, HS |
Family and domain databases
Gene3Di | 3.40.50.150, 1 hit |
InterProi | View protein in InterPro IPR025799, Arg_MeTrfase IPR029063, SAM-dependent_MTases |
PANTHERi | PTHR11006, PTHR11006, 1 hit |
SUPFAMi | SSF53335, SSF53335, 1 hit |
PROSITEi | View protein in PROSITE PS51678, SAM_MT_PRMT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ANM8_HUMAN | |
Accessioni | Q9NR22Primary (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: | May 25, 2022 | |
This is version 166 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families