Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PRMT1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PRMT1 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, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. 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. Homodimer and heterodimer with PRMT8. The dimer can then associate to form a homohexamer. Interacts with ILF3, BTG1, BTG2, SUPT5H and interferon-alpha/beta receptor 1. Interacts with NFATC2IP. Widely expressed. By BTG1, BTG2 and ILF3. Belongs to the protein arginine N-methyltransferase family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.1.1.125; Methyltransferase; Methyltransferase, protein arginine; EC 2.1.1.-; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol
Molecular Function: protein-arginine omega-N asymmetric methyltransferase activity; histone methyltransferase activity; methyltransferase activity; identical protein binding; protein binding; N-methyltransferase activity
Biological Process: histone methylation; peptidyl-arginine methylation; cell surface receptor linked signal transduction; protein amino acid methylation; regulation of transcription, DNA-dependent; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; negative regulation of megakaryocyte differentiation; neurite development
Reference #:  Q99873 (UniProtKB)
Alt. Names/Synonyms: ANM1; HCP1; HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 2; HMT1 hnRNP methyltransferase-like 2; HMT2; HRMT1L2; Interferon receptor 1-bound protein 4; IR1B4; PRMT1; protein arginine methyltransferase 1; Protein arginine N-methyltransferase 1
Gene Symbols: PRMT1
Molecular weight: 41,516 Da
Basal Isoelectric point: 5.24  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PRMT1

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  ENZYME  |  Source  |  NURSA  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S111-p VIGIECSsISDYAVK
0 22 K121-u DYAVKIVkANkLDHV
0 10 K124-u VKIVkANkLDHVVTI
0 1 K133-u DHVVTIIkGKVEEVE
0 1 K173-u TVLYARDkWLAPDGL
0 12 K223-u CIKDVAIkEPLVDVV
0 1 K233-u LVDVVDPkQLVTNAC
0 1 S294-p KRTGFSTsPEsPytH
0 4 S297-p GFSTsPEsPytHWkQ
1 129 Y299-p STsPEsPytHWkQTV
0 5 T300-p TsPEsPytHWkQTVF
0 6 K303-u EsPytHWkQTVFYME
0 29 K332-u IGMRPNAkNNRDLDF
  PRMT1 iso2  
S97 VIGIECSSISDYAVK
K107 DYAVKIVKANKLDHV
K110 VKIVKANKLDHVVTI
K119 DHVVTIIKGKVEEVE
K159 TVLYARDKWLAPDGL
K209 CIKDVAIKEPLVDVV
K219 LVDVVDPKQLVTNAC
S280 KRTGFSTSPESPYTH
S283 GFSTSPESPYTHWKQ
Y285 STSPESPYTHWKQTV
T286 TSPESPYTHWKQTVF
K289 ESPYTHWKQTVFYME
K318 IGMRPNAKNNRDLDF
  mouse

 
S121 VIGIECSSISDYAVK
K131 DYAVKIVKANkLDHV
K134-u VKIVKANkLDHVVTI
K143 DHVVTIIKGKVEEVE
K183 TVLHARDKWLAPDGL
K233-u CIKDVAIkEPLVDVV
K243 LVDVVDPKQLVTNAC
S304 KRTGFSTSPEsPyTH
S307-p GFSTSPEsPyTHWKQ
Y309-p STSPEsPyTHWKQTV
T310 TSPEsPyTHWKQTVF
K313 EsPyTHWKQTVFYME
K342-u IGMRPNAkNNRDLDF
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.