Prmt1
entrez
60421
canonical
uniprot
Q63009
canonical
ensembl
ENSRNOG00000026109
resolver
ensembl
ENSRNOG00055005632
resolver
ensembl
ENSRNOG00060007875
resolver
ensembl
ENSRNOG00065028078
resolver
ensp
ENSRNOP00000078126
resolver
ensp
ENSRNOP00000084758
resolver
ensp
ENSRNOP00000100024
resolver
ensp
ENSRNOP00000105021
resolver
ensp
ENSRNOP00055006909
resolver
ensp
ENSRNOP00060009946
resolver
ensp
ENSRNOP00065039836
resolver
enst
ENSRNOT00000098850
resolver
enst
ENSRNOT00000113175
resolver
enst
ENSRNOT00000138194
resolver
enst
ENSRNOT00055009066
resolver
enst
ENSRNOT00060013117
resolver
enst
ENSRNOT00065048584
resolver
genesymbol
Prmt1
resolver
genesymbol_syn
Hrmt1l2
resolver
genesymbol_syn
Prmt1l1
resolver
uniprot
A0A8I5Y864
resolver
uniprot
A0A8I5ZYM2
resolver
uniprot_entry
A0A8I5Y864_RAT
resolver
uniprot_entry
A0A8I5ZYM2_RAT
resolver
uniprot_entry
ANM1_RAT
resolver
amino_acid_sequence
MAAAEAANCIMEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR
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 and MICU1 (PubMed:12737817, PubMed:15837430, PubMed:18492485, PubMed:19405910, PubMed:22095282). 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 (By similarity). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (By similarity). 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 (PubMed:22095282). 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 (By similarity). 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 (By similarity). 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:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:12737817, ECO:0000269|PubMed:15837430, ECO:0000269|PubMed:18492485, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:22095282}.
uniprot
proteins
mass_dalton
40522
uniprot
proteins
mutagenesis
MUTAGEN 80; /note="G->R: Abolishes catalytic activity. Disrupts interaction of MAP3K5/ASK1 with thioredoxin. Abolishes inhibition of MAP3K5 and activation of JNK1. No effect on interaction with MAP3K5."; /evidence="ECO:0000269|PubMed:22095282"; MUTAGEN 144; /note="E->D: Reduces catalytic activity 10-fold, and causes higher order oligomers of the protein."; /evidence="ECO:0000269|PubMed:12737817"; MUTAGEN 144; /note="E->Q: Reduces catalytic activity 3000-fold, and causes higher order oligomers of the protein."; /evidence="ECO:0000269|PubMed:12737817"; MUTAGEN 153; /note="E->D: Reduces catalytic activity to 0.03%, but does not affect oligomerization."; /evidence="ECO:0000269|PubMed:12737817"; MUTAGEN 153; /note="E->Q: Completely abolishes catalytic activity, but does not affect oligomerization."; /evidence="ECO:0000269|PubMed:12737817
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated at Lys-127 by the SCF(FBXL17) complex, leading to its subsequent degradation (By similarity). Ubiquitination is regulated by acetylation at Lys-210 and Lys-215 (By similarity). 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:0000250|UniProtKB:Q9JIF0}.; PTM: Acetylation at Lys-210 and Lys-215 regulates ubiquitination by the SCF(FBXL17) complex. Acetylated at Lys-215 by p300/EP300. Deacetylated at Lys-210 and Lys-215 by SIRT1. {ECO:0000250|UniProtKB:Q9JIF0}.
uniprot
proteins
protein_family
Class I-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Protein arginine N-methyltransferase family
uniprot
proteins
pubmed
12737817
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15837430
uniprot
proteins
pubmed
18492485
uniprot
proteins
pubmed
19405910
uniprot
proteins
pubmed
22095282
uniprot
proteins
pubmed
8663146
uniprot
proteins
sequence_length
353
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JIF0}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm, cytosol {ECO:0000269|PubMed:15837430}. Cytoplasm {ECO:0000250|UniProtKB:Q99873}. Lysosome membrane {ECO:0000250|UniProtKB:Q99873}. Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). Upon methionine stimulation, localizes to the lysosome in an NPRL2-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q99873, ECO:0000250|UniProtKB:Q9JIF0}.
uniprot
proteins