Prmt1
entrez
15469
canonical
uniprot
Q9JIF0
canonical
ensembl
ENSMUSG00000109324
resolver
ensp
ENSMUSP00000103474
resolver
ensp
ENSMUSP00000147101
resolver
ensp
ENSMUSP00000147252
resolver
enst
ENSMUST00000207659
resolver
genesymbol
Prmt1
resolver
genesymbol_syn
Hrmt1l2
resolver
genesymbol_syn
Mrmt1
resolver
uniprot
A0A140LJ70
resolver
uniprot
F8WH01
resolver
uniprot
Q3UIG8
resolver
uniprot
Q80WV6
resolver
uniprot
Q99LS4
resolver
uniprot
Q9CX58
resolver
uniprot_entry
A0A140LJ70_MOUSE
resolver
uniprot_entry
ANM1_MOUSE
resolver
uniprot_entry
Q3UIG8_MOUSE
resolver
uniprot_entry
Q80WV6_MOUSE
resolver
uniprot_entry
Q9CX58_MOUSE
resolver
uniprot_sec
F8WH01
resolver
uniprot_sec
Q99LS4
resolver
amino_acid_sequence
MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR
uniprot
proteins
ec_number
2.1.1.319
uniprot
proteins
function
FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, FMR1, ILF3, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15, EWS, HABP4, SERBP1, RBM15, FOXO1, CHTOP, MAP3K5/ASK1, MICU1 and NPRL2 (PubMed:15327772, PubMed:19858291, PubMed:38006878). Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-3' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation (By similarity). May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway (By similarity). Methylates RBM15, promoting ubiquitination and degradation of RBM15 (By similarity). Methylates MRE11 and TP53BP1, promoting the DNA damage response (By similarity). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:19858291). Methylates MAP3K5/ASK1 at 'Arg-85' and 'Arg-87' which promotes association of MAP3K5 with thioredoxin and negatively regulates MAP3K5 association with TRAF2, inhibiting MAP3K5 stimulation and MAP3K5-induced activation of JNK (By similarity). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Plays a role in regulating alternative splicing in the heart (PubMed:30321814). Methylates NPRL2 at 'Arg-78' leading to inhibition of its GTPase activator activity and then the GATOR1 complex and consequently inducing timely mTORC1 activation under methionine-sufficient conditions (PubMed:38006878). Methylates the C-terminus of DSP, promoting its phosphorylation by GSK3B and subsequent recruitment to desmosome cell-cell junctions (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:15327772, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:30321814, ECO:0000269|PubMed:38006878}.
uniprot
proteins
mass_dalton
42436
uniprot
proteins
mutagenesis
MUTAGEN 98; /note="G->R: Inhibits methionine-stimulated mTORC1signaling pathway."; /evidence="ECO:0000269|PubMed:38006878"; MUTAGEN 145; /note="K->R: Increased stability of the protein caused by impaired ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 162; /note="E->Q: Inhibits methionine-stimulated mTORC1 signaling pathway."; /evidence="ECO:0000269|PubMed:38006878"; MUTAGEN 212; /note="K->R: Increased stability of the protein."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 227; /note="I->D: Slightly reduced degradation, probably caused by reduced ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 228; /note="K->Q: Mimicks residue acetylation; impaired interaction with FBXL17, leading to decreased ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 228; /note="K->R: Increased interaction with FBXL17, leading to increased ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 232; /note="I->D: Slightly reduced degradation, probably caused by reduced ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 233; /note="K->Q: Mimicks residue acetylation; increased interaction with FBXL17, leading to increased ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 233; /note="K->R: Impaired interaction with FBXL17, leading to decreased ubiquitination by the SCF(FBXL17) complex."; /evidence="ECO:0000269|PubMed:28883095"; MUTAGEN 356; /note="K->R: Increased stability of the protein."; /evidence="ECO:0000269|PubMed:28883095
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation (PubMed:28883095). Ubiquitination is regulated by acetylation at Lys-228 and Lys-233 (PubMed:28883095). Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:28883095}.; PTM: Acetylation at Lys-228 and Lys-233 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-233 by p300/EP300. Deacetylated at Lys-228 and Lys-233 by SIRT1. {ECO:0000269|PubMed:28883095}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Protein arginine N-methyltransferase family
uniprot
proteins
pubmed
10848611
uniprot
proteins
pubmed
15327772
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19858291
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22872859
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
28883095
uniprot
proteins
pubmed
30321814
uniprot
proteins
pubmed
38006878
uniprot
proteins
sequence_length
371
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:30321814}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm, cytosol {ECO:0000269|PubMed:19858291}. Cytoplasm {ECO:0000269|PubMed:19858291}. Lysosome membrane {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm (PubMed:19858291). Colocalizes with CHTOP within the nucleus (PubMed:19858291). Low levels detected also in the chromatin fraction (PubMed:22872859). Upon methionine stimulation, localizes to the lysosome membrane in an NPRL2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22872859}.
uniprot
proteins