PRMT8
Protein arginine N-methyltransferase 8
Also known as: ANM8_HUMAN, HRMT1L3, HRMT1L4
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9NR22
- Gene
- PRMT8
- Ensembl
- ENSG00000111218
- Chromosome
- 12
- Canonical length
- 394 aa
- Protein class
- Enzymes, Predicted intracellular proteins
- Quaternary structure
- Homooctamer
OverviewNCBI Gene
Arginine methylation is a widespread posttranslational modification mediated by arginine methyltransferases, such as PRMT8. Arginine methylation is involved in a number of cellular processes, including DNA repair, RNA transcription, signal transduction, protein compartmentalization, and possibly protein translation (Lee et al., 2005 [PubMed 16051612]).[supplied by OMIM, Mar 2008]
Canonical amino-acid sequenceUniProt
394 residues, UniProt reviewed canonical sequence.
>Q9NR22|PRMT8
1 MGMKHSSRCL LLRRKMAENA AESTEVNSPP SQPPQPVVPA KPVQCVHHVS TQPSCPGRGK
61 MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR NSMYHNKHVF KDKVVLDVGS
121 GTGILSMFAA KAGAKKVFGI ECSSISDYSE KIIKANHLDN IITIFKGKVE EVELPVEKVD
181 IIISEWMGYC LFYESMLNTV IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE
241 NVYGFDMTCI RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
301 NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR GEEIYGTISM
361 KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMRLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRMT8 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.32
- Highest tissue expression
- 24 nTPM
Expression across tissuesHPA
Tissue
- basal ganglia: 24 nTPM
- cerebral cortex: 18 nTPM
- cerebellum: 12 nTPM
- amygdala: 5.1 nTPM
- hippocampal formation: 4.7 nTPM
- midbrain: 4 nTPM
Single-cell type
- respiratory ciliated cells: 183 nCPM
- brain inhibitory neurons: 102 nCPM
- retinal amacrine cells: 73 nCPM
- retinal bipolar cells: 67 nCPM
- transitional alveolar cells: 63 nCPM
- brain excitatory neurons: 43 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- basal ganglia: 18 nTPM
- cerebral cortex: 16 nTPM
- thalamus: 9.7 nTPM
- white matter: 9.6 nTPM
- cerebellum: 9.5 nTPM
- midbrain: 7 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.3
- gnomAD pLI
- 0.98
- gnomAD missense Z
- 3.46
- DepMap mean gene effect
- 0.08
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- chromatin remodeling
- peptidyl-arginine methylation
- protein homooligomerization
- protein methylation
- regulation of DNA-templated transcription
- regulation of modification of postsynaptic actin cytoskeleton
Molecular functions
- enzyme binding
- histone H4 methyltransferase activity
- histone methyltransferase activity
- identical protein binding
- protein homodimerization activity
- protein-arginine omega-N asymmetric methyltransferase activity
- protein-arginine omega-N monomethyltransferase activity
- S-adenosyl-L-methionine binding
- S-adenosylmethionine-dependent methyltransferase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRMT8 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads PRMT8 as an antibody target. Whether an autoantibody or antibody against PRMT8 could matter depends on whether native PRMT8 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRMT8 is annotated at the cell surface, where native PRMT8 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label PRMT8 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
Loading the interactive Seroatlas protein explorer...