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250
cold shock protein-RXR
-
at pH 8.0 and 30°C
-
0.17
FYSGFNSKPRGRVYATSWY
-
at pH 8.0 and 30°C
2.2
FYSGFNSRAKGRVYATSWY
-
at pH 8.0 and 30°C
3.6
FYSGFNSRARGRVYATSWY
-
at pH 8.0 and 30°C
12
FYSGFNSRGKGRVYATSWY
-
at pH 8.0 and 30°C
19
FYSGFNSRGRGRVYATSWY
-
at pH 8.0 and 30°C
0.15 - 7.4
FYSGFNSRPAGRVYATSWY
0.14
FYSGFNSRPKGRVYATSWY
-
at pH 8.0 and 30°C
0.54
FYSGFNSRPRGAVYATSVY
-
at pH 8.0 and 30°C
12
FYSGFNSRPRGKVYATSVY
-
at pH 8.0 and 30°C
20
FYSGFNSRPRGRVYATSWY
-
at pH 8.0 and 30°C
21
GGRGGFGARGGFGGRGGFG
-
at pH 8.0 and 30°C
4.3
GGRGGFGGRGGFGGRGGFG
-
at pH 8.0 and 30°C
49
GGRGGFGPRGGFGGRGGFG
-
at pH 8.0 and 30°C
0.934
histone H4 peptide PfH4-21-arginine
-
pH 7.5, 37°C
-
5
histone H4-arginine
-
at 30°C and pH 8.0
0.013 - 4.5
N-acetyl-GGRGGFGGRGGFGGRGGFGG
6.6
N-acetyl-SFRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.17
N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
14.3
N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
-
at 30°C and pH 8.0
21.2
N-acetyl-SGRGKGGKGLGKGGAKRHRK
-
at 30°C and pH 8.0
0.48 - 7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
9.9
N-acetyl-SGRGRGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
26.7
N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK
-
at 30°C and pH 8.0
270
nuclear poly(A)-binding protein 1-arginine
-
at pH 8.0 and 30°C
-
2.5 - 3.5
S-adenosyl-L-methionine
0.15
WGGYSmeRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
0.061
WGGYSRGGYGGW
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
additional information
additional information
-
Michaelis-Menten kinetics, kcat/Km for S-adenosyl-L-methionine is almost 2000fold higher for PRMT1 than for PRMT2, and the kcat/Km for histone H4 is nearly 600fold higher
-
0.15
FYSGFNSRPAGRVYATSWY
-
at pH 8.0 and 30°C
7.4
FYSGFNSRPAGRVYATSWY
-
at pH 8.0 and 30°C
0.013
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.46
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M155A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
1.7
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
mutant enzyme M48L, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
4.5
N-acetyl-GGRGGFGGRGGFGGRGGFGG
-
wild type enzyme, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C
0.48
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C
7.3
N-acetyl-SGRGKGGKGLGKGGAKRHRKV
-
isoform PRMT1, pH and temperature not specified in the publication
2.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
3.5
S-adenosyl-L-methionine
-
using N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0
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malfunction
-
causal role of the elevated symmetric methylation of H3R8 and H4R3 at the RBL2 promoter in transformed B-lymphocyte pathology
malfunction
-
isoform PRMT2 silencing can enhance 17beta-estradiol-induced proliferation by regulating E2F1 expression and E2F1-responsive genes in estrogen receptor alpha-positive breast cancer cells
malfunction
-
isoform PRMT7 knockdown causes a significant decrease in enzyme recruitment and hsitone H2A-arginine 3/histone H4-arginine 3 methylation
malfunction
-
knockdown of PRMT6 disrupts oestrogen-stimulated transcription of endogenous GREB1 and progesterone receptor in MCF-7 breast cancer cells. Knockdown of PRMT6 increases the exon inclusion:skipping ratio of alternatively spliced exons in endogenous vascular endothelial growth factor and spleen tyrosine kinase RNA transcripts in both the presence and absence of oestrogen
malfunction
-
mutations of protein arginine methyltransferase 10 result in a late-flowering phenotype
malfunction
-
PRMT5 deficiency is associated with late flowering. Mutation of PRMT5 leads to widespread splicing defects
malfunction
-
silencing PRMT5 expression strongly inhibits proliferation of lung adenocarcinoma cells
physiological function
-
CARM1 functions as a rather general transcriptional coactivator, much like p300/CBP. A possible scaffolding role for CARM1, that is a component of the nucleosomal methylation activator complex
physiological function
-
CARM1 is a dual functional coregulator that facilitates transcription initiation by methylation of Arg17 and Arg26 of histone H3 and also dictates the subsequent coactivator complex disassembly by methylation of the steroid receptor coactivator family coactivators and p300/cAMP-response element-binding protein-binding protein. CARM1 function is regulated by phosphorylation at Ser217
physiological function
-
involvement of protein argininemethyltransferases PRMT1 and CARM1 in p53 and p300 coactivator functions, analysis, overview. Distinct mechanisms for PRMT1 and p300, ectopic p53s. The results of recruitment of p300, PRMT1, and CARM1
physiological function
-
key role of PRMT5 and the two methylated histones in regulating rRNA promoter activity, PRMT5 functions as a transcriptional repressor of genes transcribed by RNA polymerase II
physiological function
-
methylation of Arg17 in histone H3 by CARM1 plays a role in expression of p21, a p53-responsive gene and in the tumor suppressor function promoter-specific context, overview. CARM1 also is a secondary coactivator of several nuclear receptors. And CARM1 interacts with other chromatin-modifying enzymes such as p300/CBP and PRMT1 to bring about cooperative transcriptional activation of p53-responsive genes, overview
physiological function
-
PRMT-5 negatively regulates DNA damage-induced apoptosis
physiological function
-
PRMT1 acts as a transcriptional co-activator
physiological function
-
PRMT1 functions transiently as a coactivator in thyroid hormone receptor-mediated transcription by enhancing thyroid hormone receptor-T3 responsive element binding, PRMT1 has tissue-specific roles in regulating the rate of metamorphosis, overview
physiological function
-
PRMT1 is involved as effector in DNA damage signaling and epigenetic gene expression. Role of PRMT1, the major asymmetric arginine methyltransferase, in cellular processes and its link to human diseases, overview
physiological function
-
PRMT1 is required for the transcriptional activity of the pregnane X receptor, PXR, a ligand-dependent transcription factor, regulating gene expression of enzymes and transporters involved in xenobiotic/drug metabolism. PXR has a reciprocal effect on thePRMT1 functions by regulating its cellular compartmentalization as well as its substrate specificity. The PXR ligand-binding domain is responsible for PXR-PRMT1 ligand-dependent interaction
physiological function
-
PRMT2 acts as a transcriptional co-activator
physiological function
-
PRMT5 and DNMT3A function cooperatively in gene silencing, DNMT3A binds specifically to histone H4R3me2s, overview
physiological function
-
PRMT5 is a type II protein arginine methyltransferase that, in winter-annual strains, is required for epigenetic silencing of FLC, a member of a clade of floral repressors, and for the vernalization-mediated histone modifications characteristic of the vernalized state, overview. Arginine methylation of FLC chromatin is part of the histone code that is required for mitotic stability of the vernalized state
physiological function
-
Prmt5 is required for early-gene expression but dispensable for late-gene expression. Carm1/Prmt4 is required for late- but not for early-gene expression. Prmt5 is required for skeletal muscle differentiation at the early stages of myogenesis, while Carm1/Prmt4 at late genes is required to facilitate SWI/SNF chromatin-remodeling enzyme interaction and remodeling at late-gene loci
physiological function
-
proper epigenetic modification of chromatin by protein arginine methyltransferases, PRMTs, is crucial for normal cell growth and health
physiological function
-
protein arginine methylation by PRMT5 plays a role in ZNF224-mediated transcriptional repression, overview
physiological function
-
increased PRMT1 activity is associated with breast cancer (e.g., increased estrogen receptor alpha signaling) and heart disease (e.g., decreased nitric oxide production)
physiological function
-
isoform PRMT2 and its splice variants may directly modulate estrogen receptor alpha signaling and play a role in the progression of breast cancer. Overexpression of PRMT2 variant mRNA in breast cancer is associated with estrogen receptor alpha positivity
physiological function
-
isoform PRMT7 regulates response to DNA damage and confers resistance to DNA-damaging agents. The enzyme interacts with BRG1-hSWI/SNF, targets histone H2A-arginine 3 and histone H4-arginine 3, and represses expression of POLD1. PRMT7 and BRG1 co-localize and are enriched at target DNA repair genes
physiological function
-
methylation of Kaposi sarcoma-associated herpesvirus latency-associated nuclear antigen by PRMT1 antagonizes viral reactivation
physiological function
-
PRMT6 significantly increases the activity of estrogen receptor alpha, estrogen receptor beta, glucocorticoid receptor, and progesterone receptor by about 1.5, 2.1, 1.7 and 3.7fold, respectively. PRMT6 acts as a coactivator for steroid hormone receptors rather than a general transcription enhancer. PRMT6 enhances transcriptional activation with CARM1 in the presence of SRC-1. PRMT6 mediates oestrogen-dependent proliferation and regulates alternative splicing
physiological function
-
protein arginine methyltransferase 5 is essential for growth of lung cancer cells
physiological function
-
the methyltransferase activity of PRMT10 is essential for repressing flowering locus C expression and promoting flowering in Arabidopsis
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A0A060RZ38_PLARE
401
0
47445
TrEMBL
other Location (Reliability: 2)
A0A653GZD7_9APIC
401
0
46911
TrEMBL
other Location (Reliability: 1)
A0A0K3AQ85_BABMR
Babesia microti (strain RI)
621
0
69828
TrEMBL
other Location (Reliability: 5)
A0A125YJ52_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
660
0
71627
TrEMBL
other Location (Reliability: 3)
B9RT51_RICCO
541
0
60612
TrEMBL
Mitochondrion (Reliability: 4)
Q8ILK1_PLAF7
401
0
47446
TrEMBL
other Location (Reliability: 2)
A0A0F7UTX5_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
660
0
71627
TrEMBL
other Location (Reliability: 3)
B9RKB5_RICCO
387
0
43615
TrEMBL
other Location (Reliability: 2)
A0A086JC22_TOXGO
802
0
87743
TrEMBL
other Location (Reliability: 2)
A0A086PXL7_TOXGO
277
0
30567
TrEMBL
Mitochondrion (Reliability: 5)
B7P424_IXOSC
78
0
8414
TrEMBL
other Location (Reliability: 2)
S7UQT1_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
979
0
107022
TrEMBL
other Location (Reliability: 5)
A0A086PSG8_TOXGO
660
0
71657
TrEMBL
other Location (Reliability: 3)
A0A086Q1D7_TOXGO
510
0
56519
TrEMBL
other Location (Reliability: 2)
A0A086M7N7_TOXGO
392
0
44029
TrEMBL
Mitochondrion (Reliability: 5)
A0A086LMR9_TOXGO
510
0
56469
TrEMBL
other Location (Reliability: 2)
S8ESP8_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
979
0
107092
TrEMBL
other Location (Reliability: 5)
A0A060RRA3_PLARE
928
0
110981
TrEMBL
other Location (Reliability: 1)
B0EF34_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
332
0
38164
TrEMBL
other Location (Reliability: 2)
B7P426_IXOSC
510
0
57219
TrEMBL
other Location (Reliability: 1)
A0A088RK74_9TRYP
369
0
42193
TrEMBL
Mitochondrion (Reliability: 1)
B9SEM3_RICCO
339
0
38136
TrEMBL
other Location (Reliability: 2)
B9RG70_RICCO
596
0
66616
TrEMBL
other Location (Reliability: 2)
A0A086L2V9_TOXGO
392
0
44033
TrEMBL
Mitochondrion (Reliability: 5)
A0A086KSL3_TOXGO
802
0
87665
TrEMBL
other Location (Reliability: 2)
G9I934_ICTPU
361
0
41527
TrEMBL
other Location (Reliability: 1)
E0VIG1_PEDHC
391
0
45507
TrEMBL
other Location (Reliability: 2)
D0LP56_HALO1
Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2)
345
0
37578
TrEMBL
-
A0A125YJ53_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
660
0
71627
TrEMBL
other Location (Reliability: 3)
B9QN11_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
979
0
107175
TrEMBL
other Location (Reliability: 5)
A0A1G4H4V4_PLAVI
827
0
94901
TrEMBL
other Location (Reliability: 1)
A0A1G4H4V4_PLAVI
827
0
94901
TrEMBL
other Location (Reliability: 1)
F7PIS7_9EURY
238
0
25059
TrEMBL
-
I2CP72_NANGC
Nannochloropsis gaditana (strain CCMP526)
513
0
57086
TrEMBL
other Location (Reliability: 5)
A0A086KTK3_TOXGO
392
0
44033
TrEMBL
Mitochondrion (Reliability: 5)
E0VT46_PEDHC
335
0
38370
TrEMBL
other Location (Reliability: 1)
A0A086PPU6_TOXGO
540
0
59875
TrEMBL
other Location (Reliability: 2)
A0A086PPV9_TOXGO
476
1
52059
TrEMBL
other Location (Reliability: 4)
A0A086Q1G9_TOXGO
292
0
31208
TrEMBL
other Location (Reliability: 2)
A0A086KRG7_TOXGO
660
0
71654
TrEMBL
other Location (Reliability: 3)
A0A077YFT1_PLAYE
393
0
46022
TrEMBL
other Location (Reliability: 1)
S7UNH6_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
802
0
87619
TrEMBL
other Location (Reliability: 2)
A0A8M1NCQ6_DANRE
407
0
46498
TrEMBL
other Location (Reliability: 1)
A0A086K1Y8_TOXGO
392
0
44033
TrEMBL
Mitochondrion (Reliability: 5)
A0A384LFG0_PLAKH
400
0
46945
TrEMBL
other Location (Reliability: 2)
A0A086KAF8_TOXGO
979
0
107133
TrEMBL
other Location (Reliability: 5)
B9QLS1_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
392
0
44033
TrEMBL
Mitochondrion (Reliability: 5)
A0A0D2N618_9CHLO
275
0
30312
TrEMBL
Mitochondrion (Reliability: 2)
B7P3U8_IXOSC
304
0
34580
TrEMBL
other Location (Reliability: 1)
A0A086QV63_TOXGO
979
0
107088
TrEMBL
other Location (Reliability: 5)
S8FDT9_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
802
0
87684
TrEMBL
other Location (Reliability: 2)
A0A086Q5W5_TOXGO
979
0
107050
TrEMBL
other Location (Reliability: 5)
B7QNN4_IXOSC
399
0
45212
TrEMBL
other Location (Reliability: 2)
A0A0D2MIQ2_9CHLO
414
0
43889
TrEMBL
Mitochondrion (Reliability: 5)
A0A086JYF6_TOXGO
510
0
56415
TrEMBL
other Location (Reliability: 2)
A0A1J1HD94_PLARL
400
0
47380
TrEMBL
other Location (Reliability: 1)
G2E5D1_9GAMM
2416
0
263686
TrEMBL
-
A0A0A1UH33_ENTIV
321
0
37038
TrEMBL
other Location (Reliability: 1)
A0A0A1UA73_ENTIV
332
0
38288
TrEMBL
other Location (Reliability: 2)
A0A653HIN0_9APIC
1009
0
118074
TrEMBL
other Location (Reliability: 1)
A0A1J1GTC3_PLAGA
400
0
47399
TrEMBL
other Location (Reliability: 1)
B9RGH9_RICCO
406
0
46209
TrEMBL
Chloroplast (Reliability: 5)
A0A086JIJ5_TOXGO
660
0
71654
TrEMBL
other Location (Reliability: 3)
B0EDK4_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
319
0
36521
TrEMBL
other Location (Reliability: 2)
B7QLF4_IXOSC
226
0
25410
TrEMBL
other Location (Reliability: 4)
E0VBG9_PEDHC
550
0
62733
TrEMBL
other Location (Reliability: 1)
A0A151STH2_CAJCA
492
0
55003
TrEMBL
Secretory Pathway (Reliability: 5)
A0A086LZS5_TOXGO
979
0
106999
TrEMBL
other Location (Reliability: 5)
B5DGE3_SALSA
345
0
39832
TrEMBL
other Location (Reliability: 1)
A0A086LMR1_TOXGO
292
0
31150
TrEMBL
other Location (Reliability: 2)
A0A8M1PET2_DANRE
348
0
40116
TrEMBL
other Location (Reliability: 1)
A0A5K1K956_PLAF7
912
0
108427
TrEMBL
other Location (Reliability: 1)
A0A086QSY8_TOXGO
392
0
44029
TrEMBL
Mitochondrion (Reliability: 5)
B0ECG1_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
328
0
37549
TrEMBL
other Location (Reliability: 1)
A0A086LS80_TOXGO
660
0
71698
TrEMBL
other Location (Reliability: 3)
A0A086JYC8_TOXGO
292
0
31222
TrEMBL
other Location (Reliability: 2)
A0A125YYW8_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
392
0
44029
TrEMBL
Mitochondrion (Reliability: 5)
B0EBR4_ENTDS
Entamoeba dispar (strain ATCC PRA-260 / SAW760)
367
0
42755
TrEMBL
other Location (Reliability: 1)
B9QIS1_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
802
0
87743
TrEMBL
other Location (Reliability: 2)
A0A125YYW7_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
392
0
44029
TrEMBL
Mitochondrion (Reliability: 5)
A0A086QP04_TOXGO
660
0
71627
TrEMBL
other Location (Reliability: 3)
A0A086L855_TOXGO
965
0
105848
TrEMBL
other Location (Reliability: 5)
L0ATK3_THEEQ
366
0
41739
TrEMBL
other Location (Reliability: 1)
A0A086JVH1_TOXGO
979
0
107092
TrEMBL
other Location (Reliability: 5)
A0A086JU02_TOXGO
660
0
71627
TrEMBL
other Location (Reliability: 3)
G0QJH2_ICHMG
Ichthyophthirius multifiliis (strain G5)
392
0
46516
TrEMBL
other Location (Reliability: 1)
ANM5_CAEEL
734
0
83292
Swiss-Prot
-
ANM7_MOUSE
692
0
78301
Swiss-Prot
-
ANM6_HUMAN
375
0
41938
Swiss-Prot
-
ANM5_HUMAN
637
0
72684
Swiss-Prot
-
Q3UKX1_MOUSE
445
0
50501
TrEMBL
-
ANM1_RAT
353
0
40522
Swiss-Prot
-
ANM6_MOUSE
378
0
41866
Swiss-Prot
-
A1L1Q4_DANRE
408
0
46652
TrEMBL
-
CARM1_RAT
651
0
70341
Swiss-Prot
other Location (Reliability: 2)
CARM1_HUMAN
608
0
65854
Swiss-Prot
-
ANM8_HUMAN
394
0
45291
Swiss-Prot
-
CARM1_MOUSE
608
0
65854
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
construction of PRMT1 and CARM1 single and double knockouts in siRNA-treated HeLa cells, the mutations affect the expression of diverse other genes, expression analysis and phenotypes, overview
-
in vivo PRMT5 overexpression is caused by the altered expression of the PRMT5-specific microRNAs 19a, 25, 32, 92, 92b, and 96 and results in the increased global symmetric methylation of H3R8 and H4R3
-
overall PRMT2 expression is upregulated in breast cancer tissues
-
PRMT1 expression is upregulated in the intestine during metamorphosis
-
through its interaction with the estrogen receptoralpha, peroxisome proliferator-activated receptor, progesterone receptor, and the retinoic acid receptor, PRMT2 shows a ligand-dependent increase in transcriptional activity
-
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