PRMT1
entrez
3276
canonical
uniprot
Q99873
canonical
ensembl
ENSG00000126457
resolver
ensp
ENSP00000375724
resolver
ensp
ENSP00000406162
resolver
ensp
ENSP00000433556
resolver
ensp
ENSP00000484505
resolver
genesymbol
PRMT1
resolver
genesymbol_syn
HMT2
resolver
genesymbol_syn
HRMT1L2
resolver
genesymbol_syn
IR1B4
resolver
hgnc
HGNC:5187
resolver
uniprot
A0A087X1W2
resolver
uniprot
B4E3C3
resolver
uniprot
G5E9B6
resolver
uniprot
H7C2I1
resolver
uniprot
Q15529
resolver
uniprot
Q2VP93
resolver
uniprot
Q6LEU5
resolver
uniprot
Q8WUW5
resolver
uniprot
Q99872
resolver
uniprot
Q99874
resolver
uniprot
Q9NZ04
resolver
uniprot
Q9NZ05
resolver
uniprot
Q9NZ06
resolver
uniprot_entry
ANM1_HUMAN
resolver
uniprot_sec
A0A087X1W2
resolver
uniprot_sec
B4E3C3
resolver
uniprot_sec
G5E9B6
resolver
uniprot_sec
H7C2I1
resolver
uniprot_sec
Q15529
resolver
uniprot_sec
Q2VP93
resolver
uniprot_sec
Q6LEU5
resolver
uniprot_sec
Q8WUW5
resolver
uniprot_sec
Q99872
resolver
uniprot_sec
Q99874
resolver
uniprot_sec
Q9NZ04
resolver
uniprot_sec
Q9NZ05
resolver
uniprot_sec
Q9NZ06
resolver
amino_acid_sequence
MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLYARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR
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:10749851, PubMed:15741314, PubMed:16879614, PubMed:18951090, PubMed:22095282, PubMed:25284789, PubMed:26575292, PubMed:26876602, PubMed:27642082, PubMed:30765518, PubMed:31257072, 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. 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. Methylates RBM15, promoting ubiquitination and degradation of RBM15 (PubMed:26575292). Methylates MRE11 and TP53BP1, promoting the DNA damage response (PubMed:15741314, PubMed:16294045, PubMed:29651020). Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity (PubMed:18951090). Methylates CHTOP and this methylation is critical for its 5-hydroxymethylcytosine (5hmC)-binding activity (PubMed:25284789). Methylates MAP3K5/ASK1 at 'Arg-78' and 'Arg-80' 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 (PubMed:25284789). 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 (PubMed:38006878). Methylates the C-terminus of DSP, promoting its phosphorylation by GSK3B and subsequent recruitment to desmosome cell-cell junctions (PubMed:25733715). {ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15741314, ECO:0000269|PubMed:16294045, ECO:0000269|PubMed:16879614, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:19124016, ECO:0000269|PubMed:20442406, ECO:0000269|PubMed:22095282, ECO:0000269|PubMed:25284789, ECO:0000269|PubMed:25733715, ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:26876602, ECO:0000269|PubMed:27642082, ECO:0000269|PubMed:28040436, ECO:0000269|PubMed:29651020, ECO:0000269|PubMed:30765518, ECO:0000269|PubMed:31257072, ECO:0000269|PubMed:38006878}.
uniprot
proteins
mass_dalton
42462
uniprot
proteins
mutagenesis
MUTAGEN 92; /note="V->A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity."; /evidence="ECO:0000269|PubMed:18951090"; MUTAGEN 93; /note="L->A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity."; /evidence="ECO:0000269|PubMed:18951090"; MUTAGEN 94; /note="D->A: Loss of FOXO1 methylation, its nuclear retention, and transcriptional activity."; /evidence="ECO:0000269|PubMed:18951090"; MUTAGEN 98; /note="G->R: Does not restore mTORC1 signaling pathway upon methionine or S-adenosyl-L-methionine (SAM) stimulation in PRMT1-depleted cells. Does not affect interaction with GATOR1 complex. Impairs methyltransferase activity. Inhibits methionine-stimulated mTORC1 signaling pathway. Does not affect localization at lysosome membrane."; /evidence="ECO:0000269|PubMed:38006878"; MUTAGEN 162; /note="E->Q: Does not restore mTORC1 signaling pathway upon methionine or SAM stimulation in PRMT1-depleted cells. Does not affect interaction with GATOR1 complex. Impairs methyltransferase activity. Inhibits methionine-stimulated mTORC1 signaling pathway. Does not affect localization at lysosome membrane."; /evidence="ECO:0000269|PubMed:38006878"; MUTAGEN 280; /note="Y->A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-322 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-322 and A-359."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 322; /note="Y->A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-359. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-359."; /evidence="ECO:0000269|PubMed:26876602"; MUTAGEN 359; /note="L->A: No effect on S-adenosyl-L-methionine binding but reduced EWS protein methylation; when associated with A-280 and A-322. No effect on homodimerization but loss of homooligomerization; when associated with A-280 and A-322."; /evidence="ECO:0000269|PubMed:26876602
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated at Lys-145 by the SCF(FBXL17) complex, leading to its subsequent degradation (By similarity). Ubiquitination is regulated by acetylation at Lys-228 and Lys-233 (By similarity). Polyubiquitinated by E3 ubiquitin-protein ligase TRIM48, leading to suppression of MAP3K5/ASK1 methylation and subsequent MAP3K5 activation (PubMed:29186683). {ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:29186683}.; 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: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
10749851
uniprot
proteins
pubmed
11097842
uniprot
proteins
pubmed
11101900
uniprot
proteins
pubmed
11387442
uniprot
proteins
pubmed
11448779
uniprot
proteins
pubmed
12718890
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15084609
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15741314
uniprot
proteins
pubmed
16294045
uniprot
proteins
pubmed
16879614
uniprot
proteins
pubmed
18320585
uniprot
proteins
pubmed
18657504
uniprot
proteins
pubmed
18773938
uniprot
proteins
pubmed
18951090
uniprot
proteins
pubmed
19124016
uniprot
proteins
pubmed
19136629
uniprot
proteins
pubmed
20442406
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21724836
uniprot
proteins
pubmed
22095282
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25284789
uniprot
proteins
pubmed
25733715
uniprot
proteins
pubmed
25748791
uniprot
proteins
pubmed
26575292
uniprot
proteins
pubmed
26876602
uniprot
proteins
pubmed
27642082
uniprot
proteins
pubmed
28040436
uniprot
proteins
pubmed
29186683
uniprot
proteins
pubmed
29651020
uniprot
proteins
pubmed
30765518
uniprot
proteins
pubmed
31257072
uniprot
proteins
pubmed
38006878
uniprot
proteins
pubmed
8675017
uniprot
proteins
pubmed
9545638
uniprot
proteins
sequence_length
371
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:16879614}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9JIF0}. Cytoplasm {ECO:0000269|PubMed:26876602}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JIF0}. Lysosome membrane {ECO:0000269|PubMed:38006878}. 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 membrane in an NPRL2-dependent manner (PubMed:38006878). {ECO:0000250|UniProtKB:Q9JIF0, ECO:0000269|PubMed:38006878}.
uniprot
proteins