| Tag |
Content |
| WERAM ID |
WERAM-Mum-0051 |
| Ensembl Protein ID |
ENSMUSP00000023873.5 |
| Uniprot Accession |
Q8CIG8; ANM5_MOUSE; Q3TNN1; Q9QZS9
|
| Genbank Protein ID |
NP_001300835.1; NP_001300836.1; NP_038796.2
|
| Protein Name |
Protein arginine N-methyltransferase 5 |
| Genbank Nucleotide ID |
NM_001313906.1; NM_001313907.1; NM_013768.3
|
| Gene Name |
PRMT5 |
| Ensembl Information |
|
| Details |
| Type |
Family |
Domain |
Substrates |
AA |
References (PMIDs) |
| HMT |
PRMT |
PRMT-type |
H4R3 |
R |
23133559
|
|
| Status |
Reviewed |
| Classification |
| Type |
Family |
E-value |
Score |
Start |
End |
| HMT |
PRMT |
4.40e-111 |
372.6 |
309 |
615 |
|
| Organism |
Mus musculus |
| NCBI Taxa ID |
10090 |
Functional Description
(View)Functional Description
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:15485929, PubMed:19584108, PubMed:19858291, PubMed:21917714, PubMed:23133559). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription (PubMed:15485929). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). Methylates RPS10 (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (PubMed:23133559). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (By similarity). |
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:15485929, PubMed:19584108, PubMed:19858291, PubMed:21917714, PubMed:23133559). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H and may regulate its transcriptional elongation properties. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation (By similarity). Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription (PubMed:15485929). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:19584108). Methylates RPS10 (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (PubMed:23133559). Methylates GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (By similarity). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (By similarity).
|
| Domain Profile |
HMT PRMT
PRMT.txt 2 qqylqslselLesgvyeemlkDevrtdaYreailk...nktllkdk.....vvldvGaGtGiL...slfaakagar..kvyavekspma 77
q++lq+l+++Les++ye ++kD++++++Y++ai+k +++++++k v++++GaG+G+L sl+aak+++r ++yavek+p+a
ENSMUSP00000023873.5 309 QSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKcllDRVPEEEKetnvqVLMVLGAGRGPLvnaSLRAAKQAERriRLYAVEKNPNA 397
89************************************9999999999999*************************8889********* PP
PRMT.txt 78 kvarkvvkvnglkdrvtvikgkveelelpkekvDiivSEllgsfllnEsllpsvlhardkfLkddglslPdkatlyvapiedtklykee 166
+v++++++++++ ++vtv++++++e+ +p ek+DiivSEllgsf++nE l+p++l+++++fLkddg+s+P ++t+++api+++kly+e
ENSMUSP00000023873.5 398 VVTLENWQFEEWGSQVTVVSSDMREWVAP-EKADIIVSELLGSFADNE-LSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNE- 483
*****************************.******************.***************************************. PP
PRMT.txt 167 kaefwksvygvdlsclek.aaikeqfesplVdtldkekllsepkkiftfdiskakesdee.relslelevkrnaslhglaayFdvqfts 253
++c+ek +++++qfe+p+V++l+++++ls+pk++ftf++++++++ ++ r+++le++v++n++lhg+a+yF+++ +
ENSMUSP00000023873.5 484 -----------VRACREKdRDPEAQFEMPYVVRLHNFHQLSAPKPCFTFSHPNRDPMIDNnRYCTLEFPVEVNTVLHGFAGYFETV--L 559
...........78999999**************************************9888*************************..* PP
PRMT.txt 254 ektvvlStaPetkspath.Wkqavlyledpltvkegekisilllarkknsrdvdyel 309
+++++lS++Pet+sp+++ W+++++++++p+tv+eg++i +++++r++ns++v+ye+
ENSMUSP00000023873.5 560 YRDITLSIRPETHSPGMFsWFPIFFPIKQPITVHEGQNI-CVRFWRCSNSKKVWYEW 615
***************************************.8***************9 PP
|
Protein Sequence
(Fasta) | MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK 60
NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR RNSEAAMLQE LNFGAYLGLP 120
AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDVIEN APTTHTEEYS 180
GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK 240
KGFPVLSKVQ QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF 300
AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKETNVQV 360
LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM 420
REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL 480
YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF 540
PVEVNTVLHG FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV 600
RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL 637Protein Fasta Sequence
>ENSMUSP00000023873.5|PRMT5|Mus musculus
MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIHPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDVIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKVQQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKETNVQVLMVLGAGRGPLVNASLRAAKQAERRIRLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPKPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYRDITLSIRPETHSPGMFSWFPIFFPIKQPITVHEGQNICVRFWRCSNSKKVWYEWAVTAPVCSSIHNPTGRSYTIGL |
Nucleotide Sequence
(Fasta) | GAATTGCGGA TTGGTGGGAG CAGCGGCTTG GTCCCTCCGC CTCCGCTCTG GAGCTGTAAA 60
GACGCTCTGG TTGTTAAGGC GACTTGTCCC GCCTCCTGGG GACTCTTCAC CGCTTCGTGA 120
TTGGACTCTA GTATCAAGGA ATCCCGGCGT GGGCCGCGCG AGGGAAAAGA TGGCGGCGAT 180
GGCAGTCGGA GGTGCTGGTG GCAGCCGCGT GTCCAGCGGG AGGGACCTGA ATTGCGTCCC 240
CGAAATAGCT GACACACTGG GTGCTGTGGC CAAGCAGGGG TTTGATTTCC TCTGCATGCC 300
TGTCTTCCAC CCGCGTTTCA AGAGGGAGTT CATTCAGGAA CCTGCTAAGA ATCGGCCTGG 360
CCCCCAGACA CGATCAGACC TACTGCTGTC AGGAAGGGAC TGGAATACGC TAATTGTGGG 420
AAAGCTTTCT CCATGGATTC ATCCAGACTC AAAAGTGGAG AAGATCCGAA GGAACTCTGA 480
AGCGGCTATG TTACAGGAGT TGAATTTTGG GGCATATCTG GGTCTTCCAG CTTTCCTATT 540
GCCCCTTAAT CAGGAAGATA ACACGAATCT GGCCAGAGTT CTGACCAACC ACATCCACAC 600
TGGCCACCAC TCTTCCATGT TCTGGATGAG GGTACCCTTG GTGGCCCCAG AGGACCTGAG 660
AGATGATGTA ATTGAGAATG CCCCGACTAC ACACACAGAG GAGTACAGTG GAGAAGAGAA 720
AACATGGATG TGGTGGCATA ACTTTCGGAC TCTGTGTGAC TATAGCAAGA GAATTGCAGT 780
AGCTCTTGAA ATTGGAGCTG ACCTCCCGTC TAATCACGTC ATTGACCGCT GGCTTGGAGA 840
GCCCATCAAA GCAGCCATTC TCCCCACCAG CATTTTCCTA ACCAACAAGA AAGGATTTCC 900
TGTTCTTTCT AAGGTGCAGC AGAGGCTGAT CTTCCGGCTC CTCAAGTTGG AAGTGCAGTT 960
TATCATCACG GGAACCAACC ACCACTCAGA GAAGGAGTTC TGTTCCTACC TCCAGTACTT 1020
GGAATACTTA AGCCAAAATC GCCCTCCACC CAATGCCTAT GAGCTCTTTG CCAAAGGCTA 1080
TGAAGACTAT CTGCAGTCCC CACTCCAGCC TCTGATGGAC AATCTGGAAT CTCAGACATA 1140
TGAAGTGTTT GAAAAGGACC CCATCAAATA CTCTCAATAT CAGCAGGCTA TTTATAAATG 1200
TTTGCTAGAC CGAGTACCAG AAGAAGAAAA GGAGACCAAT GTCCAGGTAC TTATGGTGCT 1260
GGGTGCAGGC CGGGGTCCTC TTGTGAATGC GTCTCTTCGG GCAGCCAAAC AGGCCGAGCG 1320
GCGGATCAGG CTGTATGCTG TGGAGAAGAA CCCCAATGCT GTGGTGACGC TAGAGAACTG 1380
GCAGTTTGAA GAATGGGGGA GCCAGGTGAC AGTTGTCTCA TCAGACATGC GGGAATGGGT 1440
GGCTCCGGAG AAAGCTGACA TCATTGTCAG TGAGCTTCTG GGTTCCTTTG CCGACAACGA 1500
GCTGTCACCT GAGTGTCTGG ATGGAGCACA GCACTTCCTG AAAGATGATG GCGTGAGCAT 1560
CCCTGGAGAA TACACCTCCT TCCTGGCTCC CATTTCTTCC TCTAAGCTGT ACAATGAGGT 1620
CCGTGCCTGT CGGGAAAAGG ACCGCGATCC TGAGGCACAG TTTGAGATGC CTTATGTGGT 1680
TCGGTTGCAC AACTTCCACC AGCTCTCTGC TCCTAAGCCC TGCTTTACCT TCAGCCATCC 1740
CAACCGAGAT CCTATGATTG ACAACAACCG CTACTGTACC TTGGAGTTTC CTGTGGAGGT 1800
GAACACAGTG CTTCATGGCT TCGCAGGCTA CTTTGAGACT GTGCTTTACC GGGACATCAC 1860
TCTGAGTATC CGCCCAGAGA CTCACTCTCC TGGGATGTTC TCATGGTTCC CCATCTTCTT 1920
CCCCATTAAG CAGCCCATCA CGGTGCACGA AGGCCAGAAC ATCTGTGTGC GTTTCTGGCG 1980
ATGCAGCAAT TCCAAGAAAG TGTGGTACGA GTGGGCGGTG ACGGCCCCCG TCTGTTCTTC 2040
TATTCACAAC CCTACCGGCC GCTCCTATAC CATTGGCCTC TAGCCCTGCA CACAGTGTCA 2100
AAACCTTGGA AGCAGCTCTG AGTTCTCTTC CTACAGCACA GAAGGTGTAG AACATCTGCT 2160
GGTTCAGTTC CTCAGTGAGA CCCTCAGCCG CCAGAGAGGA GCGGTTCCGG CTGCTTTCCT 2220
ACCTAATGTC ATGGTGGCCA ACGGGTAGGC ATTCCCGGAC TGCCAGGCAT GGTGGTGCAT 2280
ACTCTTTATC CCAGCACTCC AGAGGCAGAG GCAGAGGCAG ATGGATCTCT TTAAGTTCAA 2340
GGCTAGCCCG GTCTACCTAG CAAGTTTCAG GCCACCTAGG GCTACATAGT GAGACCCTGT 2400
CTCCAAAAAA CGAAAAAAAA AAAAAAAAAG AACTAGAGGA CACAAGCCAG CAGCAGTCTT 2460
CAGAGCCTCT GGCTTGGGCA TGAGAACTCA GCAGCTCTGG ATGAAGCAAC CTCAGCAGAT 2520
GCTCAGCCGC CAGAGCTCCC CAGGGGTCAG GAGAGAAAGC GAAGGCTGTG GAAGAGCCCG 2580
GGCTGCGTGC ATGAACACTT GACCTGCGCT CTTCTTGCCC TACTCTGTTG TTGTTTGGGT 2640
GGTTTGTGTC TGAAGGAAAC AAATAAAGTG AAGTTACGGC CTCTGCTGCT T
2692Nucleotide Fasta Sequence
>ENSMUSP00000023873.5|PRMT|Mus musculus
GAATTGCGGATTGGTGGGAGCAGCGGCTTGGTCCCTCCGCCTCCGCTCTGGAGCTGTAAAGACGCTCTGGTTGTTAAGGCGACTTGTCCCGCCTCCTGGGGACTCTTCACCGCTTCGTGATTGGACTCTAGTATCAAGGAATCCCGGCGTGGGCCGCGCGAGGGAAAAGATGGCGGCGATGGCAGTCGGAGGTGCTGGTGGCAGCCGCGTGTCCAGCGGGAGGGACCTGAATTGCGTCCCCGAAATAGCTGACACACTGGGTGCTGTGGCCAAGCAGGGGTTTGATTTCCTCTGCATGCCTGTCTTCCACCCGCGTTTCAAGAGGGAGTTCATTCAGGAACCTGCTAAGAATCGGCCTGGCCCCCAGACACGATCAGACCTACTGCTGTCAGGAAGGGACTGGAATACGCTAATTGTGGGAAAGCTTTCTCCATGGATTCATCCAGACTCAAAAGTGGAGAAGATCCGAAGGAACTCTGAAGCGGCTATGTTACAGGAGTTGAATTTTGGGGCATATCTGGGTCTTCCAGCTTTCCTATTGCCCCTTAATCAGGAAGATAACACGAATCTGGCCAGAGTTCTGACCAACCACATCCACACTGGCCACCACTCTTCCATGTTCTGGATGAGGGTACCCTTGGTGGCCCCAGAGGACCTGAGAGATGATGTAATTGAGAATGCCCCGACTACACACACAGAGGAGTACAGTGGAGAAGAGAAAACATGGATGTGGTGGCATAACTTTCGGACTCTGTGTGACTATAGCAAGAGAATTGCAGTAGCTCTTGAAATTGGAGCTGACCTCCCGTCTAATCACGTCATTGACCGCTGGCTTGGAGAGCCCATCAAAGCAGCCATTCTCCCCACCAGCATTTTCCTAACCAACAAGAAAGGATTTCCTGTTCTTTCTAAGGTGCAGCAGAGGCTGATCTTCCGGCTCCTCAAGTTGGAAGTGCAGTTTATCATCACGGGAACCAACCACCACTCAGAGAAGGAGTTCTGTTCCTACCTCCAGTACTTGGAATACTTAAGCCAAAATCGCCCTCCACCCAATGCCTATGAGCTCTTTGCCAAAGGCTATGAAGACTATCTGCAGTCCCCACTCCAGCCTCTGATGGACAATCTGGAATCTCAGACATATGAAGTGTTTGAAAAGGACCCCATCAAATACTCTCAATATCAGCAGGCTATTTATAAATGTTTGCTAGACCGAGTACCAGAAGAAGAAAAGGAGACCAATGTCCAGGTACTTATGGTGCTGGGTGCAGGCCGGGGTCCTCTTGTGAATGCGTCTCTTCGGGCAGCCAAACAGGCCGAGCGGCGGATCAGGCTGTATGCTGTGGAGAAGAACCCCAATGCTGTGGTGACGCTAGAGAACTGGCAGTTTGAAGAATGGGGGAGCCAGGTGACAGTTGTCTCATCAGACATGCGGGAATGGGTGGCTCCGGAGAAAGCTGACATCATTGTCAGTGAGCTTCTGGGTTCCTTTGCCGACAACGAGCTGTCACCTGAGTGTCTGGATGGAGCACAGCACTTCCTGAAAGATGATGGCGTGAGCATCCCTGGAGAATACACCTCCTTCCTGGCTCCCATTTCTTCCTCTAAGCTGTACAATGAGGTCCGTGCCTGTCGGGAAAAGGACCGCGATCCTGAGGCACAGTTTGAGATGCCTTATGTGGTTCGGTTGCACAACTTCCACCAGCTCTCTGCTCCTAAGCCCTGCTTTACCTTCAGCCATCCCAACCGAGATCCTATGATTGACAACAACCGCTACTGTACCTTGGAGTTTCCTGTGGAGGTGAACACAGTGCTTCATGGCTTCGCAGGCTACTTTGAGACTGTGCTTTACCGGGACATCACTCTGAGTATCCGCCCAGAGACTCACTCTCCTGGGATGTTCTCATGGTTCCCCATCTTCTTCCCCATTAAGCAGCCCATCACGGTGCACGAAGGCCAGAACATCTGTGTGCGTTTCTGGCGATGCAGCAATTCCAAGAAAGTGTGGTACGAGTGGGCGGTGACGGCCCCCGTCTGTTCTTCTATTCACAACCCTACCGGCCGCTCCTATACCATTGGCCTCTAGCCCTGCACACAGTGTCAAAACCTTGGAAGCAGCTCTGAGTTCTCTTCCTACAGCACAGAAGGTGTAGAACATCTGCTGGTTCAGTTCCTCAGTGAGACCCTCAGCCGCCAGAGAGGAGCGGTTCCGGCTGCTTTCCTACCTAATGTCATGGTGGCCAACGGGTAGGCATTCCCGGACTGCCAGGCATGGTGGTGCATACTCTTTATCCCAGCACTCCAGAGGCAGAGGCAGAGGCAGATGGATCTCTTTAAGTTCAAGGCTAGCCCGGTCTACCTAGCAAGTTTCAGGCCACCTAGGGCTACATAGTGAGACCCTGTCTCCAAAAAACGAAAAAAAAAAAAAAAAAGAACTAGAGGACACAAGCCAGCAGCAGTCTTCAGAGCCTCTGGCTTGGGCATGAGAACTCAGCAGCTCTGGATGAAGCAACCTCAGCAGATGCTCAGCCGCCAGAGCTCCCCAGGGGTCAGGAGAGAAAGCGAAGGCTGTGGAAGAGCCCGGGCTGCGTGCATGAACACTTGACCTGCGCTCTTCTTGCCCTACTCTGTTGTTGTTTGGGTGGTTTGTGTCTGAAGGAAACAAATAAAGTGAAGTTACGGCCTCTGCTGCTT
|
| Sequence Source |
Ensembl |
| Keyword |
KW-0007--Acetylation
KW-0090--Biological rhythms
KW-0156--Chromatin regulator
KW-0181--Complete proteome
KW-0963--Cytoplasm
KW-0333--Golgi apparatus
KW-0489--Methyltransferase
KW-0539--Nucleus
KW-1185--Reference proteome
KW-0678--Repressor
KW-0949--S-adenosyl-L-methionine
KW-0804--Transcription
KW-0805--Transcription regulation
KW-0808--Transferase
--
|
| Interpro |
IPR025799--Arg_MeTrfase
IPR007857--Arg_MeTrfase_PRMT5
IPR029063--SAM-dependent_MTases
|
| PROSITE |
PS51678--SAM_MT_PRMT
|
| Pfam |
PF05185--PRMT5
|
| Gene Ontology |
GO:0005737--C:cytoplasm
GO:0005829--C:cytosol
GO:0005794--C:Golgi apparatus
GO:0035097--C:histone methyltransferase complex
GO:0034709--C:methylosome
GO:0005634--C:nucleus
GO:0003682--F:chromatin binding
GO:0001046--F:core promoter sequence-specific DNA binding
GO:0044020--F:histone methyltransferase activity (H4-R3 specific)
GO:0008327--F:methyl-CpG binding
GO:0008168--F:methyltransferase activity
GO:0046982--F:protein heterodimerization activity
GO:0016274--F:protein-arginine N-methyltransferase activity
GO:0035243--F:protein-arginine omega-N symmetric methyltransferase activity
GO:0043021--F:ribonucleoprotein complex binding
GO:0003714--F:transcription corepressor activity
GO:0032922--P:circadian regulation of gene expression
GO:0006353--P:DNA-templated transcription, termination
GO:0042118--P:endothelial cell activation
GO:0090161--P:Golgi ribbon formation
GO:0043985--P:histone H4-R3 methylation
GO:0000122--P:negative regulation of transcription from RNA polymerase II promoter
GO:0018216--P:peptidyl-arginine methylation
GO:0019918--P:peptidyl-arginine methylation, to symmetrical-dimethyl arginine
GO:0035246--P:peptidyl-arginine N-methylation
GO:1904992--P:positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway
GO:0000387--P:spliceosomal snRNP assembly
|
| Orthology |
|
| Created Date |
25-Jun-2016 |
