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Protein Page:
PRMT1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Nuclear receptor co-regulator; EC 2.1.1.125; EC 2.1.1.-; Methyltransferase; Methyltransferase, protein arginine
Cellular Component: nucleoplasm; cytoplasm; cytosol; nucleus
Molecular Function: protein-arginine omega-N asymmetric methyltransferase activity; identical protein binding; methyltransferase activity; histone methyltransferase activity; protein binding; N-methyltransferase activity
Biological Process: histone methylation; peptidyl-arginine methylation; cell surface receptor linked signal transduction; regulation of transcription, DNA-dependent; protein amino acid methylation; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; neurite development; negative regulation of megakaryocyte differentiation
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.


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Sites Implicated In
molecular association, regulation: Y299‑p

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 Y42-p EDMTSKDyyFDSYAH
0 1 Y43-p DMTSKDyyFDSYAHF
0 1 S111-p VIGIECSsISDYAVK
0 22 K121-ub DYAVKIVkANkLDHV
0 10 K124-ub VKIVkANkLDHVVTI
0 1 K133-ub DHVVTIIkGKVEEVE
0 1 K173-ub TVLYARDkWLAPDGL
0 12 K223-ub CIKDVAIkEPLVDVV
0 1 K233-ub LVDVVDPkQLVTNAC
0 1 K266-sc SPFCLQVkRNDYVHA
0 1 S294-p KRTGFSTsPEsPytH
0 4 S297-p GFSTsPEsPytHWkQ
1 133 Y299-p STsPEsPytHWkQtV
0 5 T300-p TsPEsPytHWkQtVF
0 1 K303-ac EsPytHWkQtVFYME
0 6 K303-ub EsPytHWkQtVFYME
0 1 T305-p PytHWkQtVFYMEDY
0 1 T314 FYMEDYLTVKTGEEI
0 29 K332-ub IGMRPNAkNNRDLDF
  PRMT1 iso2  
Y28 EDMTSKDYYFDSYAH
Y29 DMTSKDYYFDSYAHF
S97 VIGIECSSISDYAVK
K107 DYAVKIVKANKLDHV
K110 VKIVKANKLDHVVTI
K119 DHVVTIIKGKVEEVE
K159 TVLYARDKWLAPDGL
K209 CIKDVAIKEPLVDVV
K219 LVDVVDPKQLVTNAC
K252 SPFCLQVKRNDYVHA
S280 KRTGFSTSPESPYTH
S283 GFSTSPESPYTHWKQ
Y285 STSPESPYTHWKQTV
T286 TSPESPYTHWKQTVF
K289 ESPYTHWKQTVFYME
K289 ESPYTHWKQTVFYME
T291 PYTHWKQTVFYMEDY
T300 FYMEDYLTVKTGEEI
K318 IGMRPNAKNNRDLDF
  mouse

 
Y52 EDMTSKDYYFDSYAH
Y53 DMTSKDYYFDSYAHF
S121 VIGIECSSISDYAVK
K131 DYAVKIVKANkLDHV
K134-ub VKIVKANkLDHVVTI
K143 DHVVTIIKGKVEEVE
K183 TVLHARDKWLAPDGL
K233-ub CIKDVAIkEPLVDVV
K243 LVDVVDPKQLVTNAC
K276 SPFCLQVKRNDYVHA
S304 KRTGFSTSPEsPyTH
S307-p GFSTSPEsPyTHWKQ
Y309-p STSPEsPyTHWKQTV
T310 TSPEsPyTHWKQTVF
K313 EsPyTHWKQTVFYME
K313 EsPyTHWKQTVFYME
T315 PyTHWKQTVFYMEDY
T324-p FYMEDYLtVKTGEEI
K342-ub IGMRPNAkNNRDLDF
  rat

 
Y34 EDMTSKDYYFDSYAH
Y35 DMTSKDYYFDSYAHF
S103 VIGIECSSISDYAVK
K113 DYAVKIVKANKLDHV
K116 VKIVKANKLDHVVTI
K125 DHVVTIIKGKVEEVE
K165 TVLHARDKWLAPDGL
K215 CIKDVAIKEPLVDVV
K225 LVDVVDPKQLVTNAC
K258 SPFCLQVKRNDYVHA
S286 KRTGFSTSPESPYTH
S289 GFSTSPESPYTHWKQ
Y291 STSPESPYTHWKQTV
T292 TSPESPYTHWKQTVF
K295 ESPYTHWKQTVFYME
K295 ESPYTHWKQTVFYME
T297 PYTHWKQTVFYMEDY
T306 FYMEDYLTVKTGEEI
K324 IGMRPNAKNNRDLDF
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