PRMT1
Protein arginine N-methyltransferase 1
Also known as: ANM1, ANM1_HUMAN, HCP1, HRMT1L2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q99873
- Gene
- PRMT1
- Ensembl
- ENSG00000126457
- Chromosome
- 19
- Canonical length
- 371 aa
- Protein class
- Enzymes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm
- Quaternary structure
- Homooctamer
OverviewNCBI Gene
This gene encodes a member of the protein arginine N-methyltransferase (PRMT) family. Post-translational modification of target proteins by PRMTs plays an important regulatory role in many biological processes, whereby PRMTs methylate arginine residues by transferring methyl groups from S-adenosyl-L-methionine to terminal guanidino nitrogen atoms. The encoded protein is a type I PRMT and is responsible for the majority of cellular arginine methylation activity. Increased expression of this gene may play a role in many types of cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 5. [provided by RefSeq, Dec 2011]
Canonical amino-acid sequenceUniProt
371 residues, UniProt reviewed canonical sequence.
>Q99873|PRMT1
1 MAAAEAANCI MENFVATLAN GMSLQPPLEE VSCGQAESSE KPNAEDMTSK DYYFDSYAHF
61 GIHEEMLKDE VRTLTYRNSM FHNRHLFKDK VVLDVGSGTG ILCMFAAKAG ARKVIGIECS
121 SISDYAVKIV KANKLDHVVT IIKGKVEEVE LPVEKVDIII SEWMGYCLFY ESMLNTVLYA
181 RDKWLAPDGL IFPDRATLYV TAIEDRQYKD YKIHWWENVY GFDMSCIKDV AIKEPLVDVV
241 DPKQLVTNAC LIKEVDIYTV KVEDLTFTSP FCLQVKRNDY VHALVAYFNI EFTRCHKRTG
301 FSTSPESPYT HWKQTVFYME DYLTVKTGEE IFGTIGMRPN AKNNRDLDFT IDLDFKGQLC
361 ELSCSTDYRM RLocalizationUniProt · AlphaFold · HPA
Whether an antibody against PRMT1 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
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.3
- Highest tissue expression
- 227 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 227 nTPM
- tongue: 152 nTPM
- heart muscle: 140 nTPM
- ovary: 113 nTPM
- endometrium: 109 nTPM
- fallopian tube: 103 nTPM
Single-cell type
- migrating cytotrophoblasts: 285 nCPM
- esophageal basal cells: 279 nCPM
- decidual stromal cells: 244 nCPM
- syncytiotrophoblasts: 241 nCPM
- cytotrophoblasts: 222 nCPM
- fallopian secretory cells: 206 nCPM
Immune cell
- memory B-cell: 200 nTPM
- naive B-cell: 173 nTPM
- NK-cell: 163 nTPM
- plasmacytoid DC: 159 nTPM
- total PBMC: 133 nTPM
- myeloid DC: 132 nTPM
Brain region
- hypothalamus: 77 nTPM
- pons: 73 nTPM
- cerebellum: 71 nTPM
- white matter: 68 nTPM
- medulla oblongata: 68 nTPM
- spinal cord: 67 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)
- 0.15
- gnomAD pLI
- 1
- gnomAD missense Z
- 3.81
- DepMap mean gene effect
- -1.25
- DepMap dependency class
- common
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cardiac muscle tissue development
- cell surface receptor signaling pathway
- cellular response to methionine
- chromatin remodeling
- DNA damage response
- in utero embryonic development
- negative regulation of apoptotic process
- negative regulation of JNK cascade
- negative regulation of megakaryocyte differentiation
- neuron projection development
- peptidyl-arginine methylation
- positive regulation of cell population proliferation
- positive regulation of double-strand break repair via homologous recombination
- positive regulation of erythrocyte differentiation
- positive regulation of hemoglobin biosynthetic process
- positive regulation of p38MAPK cascade
- positive regulation of TORC1 signaling
- positive regulation of translation
- protein homooligomerization
- protein methylation
- regulation of BMP signaling pathway
- regulation of DNA-templated transcription
- regulation of megakaryocyte differentiation
- RNA splicing
- viral protein processing
Molecular functions
- enzyme binding
- histone H4R3 methyltransferase activity
- histone methyltransferase activity
- identical protein binding
- methyl-CpG binding
- methyltransferase activity
- mitogen-activated protein kinase p38 binding
- N-methyltransferase activity
- protein methyltransferase activity
- protein-arginine N-methyltransferase activity
- protein-arginine omega-N asymmetric methyltransferase activity
- protein-arginine omega-N monomethyltransferase activity
- RNA binding
- S-adenosyl-L-methionine binding
- GATOR1 complex binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of PRMT1 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 PRMT1 as an antibody target. Whether an autoantibody or antibody against PRMT1 could matter depends on whether native PRMT1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
PRMT1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label PRMT1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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