ID ANM5_MOUSE Reviewed; 637 AA. AC Q8CIG8; Q3TNN1; Q9QZS9; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 169. DE RecName: Full=Protein arginine N-methyltransferase 5; DE Short=Prmt5; DE EC=2.1.1.320 {ECO:0000269|PubMed:28263986}; DE AltName: Full=Histone-arginine N-methyltransferase PRMT5; DE AltName: Full=Jak-binding protein 1; DE AltName: Full=Shk1 kinase-binding protein 1 homolog; DE Short=SKB1 homolog; GN Name=Prmt5; Synonyms=Jbp1, Skb1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Skin; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-637. RX PubMed=10531356; DOI=10.1074/jbc.274.44.31531; RA Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.; RT "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with RT Jak kinases and contains protein methyltransferase activity."; RL J. Biol. Chem. 274:31531-31542(1999). RN [4] RP FUNCTION IN METHYLATION OF HISTONE H3. RX PubMed=15485929; DOI=10.1128/mcb.24.21.9630-9645.2004; RA Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.; RT "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and RT negatively regulates expression of ST7 and NM23 tumor suppressor genes."; RL Mol. Cell. Biol. 24:9630-9645(2004). RN [5] RP FUNCTION, AND INTERACTION WITH PRDM1. RX PubMed=16699504; DOI=10.1038/ncb1413; RA Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J., RA Kouzarides T., Surani M.A.; RT "Blimp1 associates with Prmt5 and directs histone arginine methylation in RT mouse germ cells."; RL Nat. Cell Biol. 8:623-630(2006). RN [6] RP FUNCTION IN METHYLATION OF PIWI PROTEINS. RX PubMed=19584108; DOI=10.1101/gad.1814809; RA Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S., RA Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.; RT "Proteomic analysis of murine Piwi proteins reveals a role for arginine RT methylation in specifying interaction with Tudor family members."; RL Genes Dev. 23:1749-1762(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP FUNCTION, AND INTERACTION WITH CHTOP. RX PubMed=19858291; DOI=10.1128/mcb.00645-09; RA van Dijk T.B., Gillemans N., Stein C., Fanis P., Demmers J., RA van de Corput M., Essers J., Grosveld F., Bauer U.M., Philipsen S.; RT "Friend of Prmt1, a novel chromatin target of protein arginine RT methyltransferases."; RL Mol. Cell. Biol. 30:260-272(2010). RN [9] RP FUNCTION IN THE REGULATION OF MAPK1/MAPK3 SIGNALING PATHWAY, AND RAF1 RP METHYLATION. RX PubMed=21917714; DOI=10.1126/scisignal.2001936; RA Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., RA Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., RA Avila M.A., Recio J.A.; RT "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction RT amplitude and cell fate through CRAF."; RL Sci. Signal. 4:RA58-RA58(2011). RN [10] RP INTERACTION WITH CHTOP, AND SUBCELLULAR LOCATION. RX PubMed=22872859; DOI=10.1074/mcp.m112.017194; RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J., RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.; RT "Five friends of methylated chromatin target of protein-arginine- RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation RT to desumoylation."; RL Mol. Cell. Proteomics 11:1263-1273(2012). RN [11] RP INTERACTION WITH COPRS, AND IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 RP AND CBFB. RX PubMed=22193545; DOI=10.1038/cdd.2011.193; RA Paul C., Sardet C., Fabbrizio E.; RT "The histone- and PRMT5-associated protein COPR5 is required for myogenic RT differentiation."; RL Cell Death Differ. 19:900-908(2012). RN [12] RP FUNCTION, AND INTERACTION WITH CRY1. RX PubMed=23133559; DOI=10.1371/journal.pone.0048152; RA Na J., Lee K., Kim H.G., Shin J.Y., Na W., Jeong H., Lee J.W., Cho S., RA Kim W.S., Ju B.G.; RT "Role of type II protein arginine methyltransferase 5 in the regulation of RT Circadian Per1 gene."; RL PLoS ONE 7:E48152-E48152(2012). RN [13] RP FUNCTION, INTERACTION WITH TDRD6, AND CATALYTIC ACTIVITY. RX PubMed=28263986; DOI=10.1371/journal.pgen.1006660; RA Akpinar M., Lesche M., Fanourgakis G., Fu J., Anastassiadis K., Dahl A., RA Jessberger R.; RT "TDRD6 mediates early steps of spliceosome maturation in primary RT spermatocytes."; RL PLoS Genet. 13:E1006660-E1006660(2017). CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the CC formation of omega-N monomethylarginine (MMA) and symmetrical CC dimethylarginine (sDMA), with a preference for the formation of MMA CC (PubMed:15485929, PubMed:19584108, PubMed:19858291, PubMed:21917714, CC PubMed:23133559, PubMed:28263986). Specifically mediates the CC symmetrical dimethylation of arginine residues in the small nuclear CC ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation CC being required for the assembly and biogenesis of snRNP core particles. CC Methylates SUPT5H and may regulate its transcriptional elongation CC properties (By similarity). May methylate the N-terminal region of MBD2 CC (By similarity). Mono- and dimethylates arginine residues of myelin CC basic protein (MBP) in vitro. May play a role in cytokine-activated CC transduction pathways. Negatively regulates cyclin E1 promoter activity CC and cellular proliferation (By similarity). Methylates histone H2A and CC H4 'Arg-3' during germ cell development (PubMed:16699504). Methylates CC histone H3 'Arg-8', which may repress transcription (PubMed:15485929). CC Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation CC of Piwi proteins being required for the interaction with Tudor domain- CC containing proteins and subsequent localization to the meiotic nuage CC (PubMed:19584108). Methylates RPS10 (By similarity). Attenuates EGF CC signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, CC monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and CC PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. CC Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 CC signaling proteins and reducing their catalytic activity CC (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on CC the endothelial cells surface at sites of inflammation. Methylates CC HOXA9. Methylates and regulates SRGAP2 which is involved in cell CC migration and differentiation (By similarity). Acts as a CC transcriptional corepressor in CRY1-mediated repression of the core CC circadian component PER1 by regulating the H4R3 dimethylation at the CC PER1 promoter (PubMed:23133559). Methylates GM130/GOLGA2, regulating CC Golgi ribbon formation. Methylates H4R3 in genes involved in CC glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. CC Symmetrically methylates POLR2A, a modification that allows the CC recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is CC required for resolving RNA-DNA hybrids created by RNA polymerase II, CC that form R-loop in transcription terminal regions, an important step CC in proper transcription termination. Along with LYAR, binds the CC promoter of gamma-globin HBG1/HBG2 and represses its expression. CC Symmetrically methylates NCL. Methylates p53/TP53; methylation might CC possibly affect p53/TP53 target gene specificity (By similarity). CC Involved in spliceosome maturation and mRNA splicing in prophase I CC spermatocytes through the catalysis of the symmetrical arginine CC dimethylation of SNRPB (small nuclear ribonucleoprotein-associated CC protein) and the interaction with tudor domain-containing protein TDRD6 CC (PubMed:28263986). {ECO:0000250|UniProtKB:O14744, CC ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:16699504, CC ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19858291, CC ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:23133559, CC ECO:0000269|PubMed:28263986}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA- CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320; CC Evidence={ECO:0000269|PubMed:28263986}; CC -!- ACTIVITY REGULATION: Activity is increased by EGF, HGF, FGF1 or FGF2 CC treatments, and slightly decreased by NGF treatment. {ECO:0000250}. CC -!- SUBUNIT: Forms, at least, homodimers and homotetramers. Component of CC the methylosome complex, composed of PRMT5, WDR77 and CLNS1A. Found in CC a complex composed of PRMT5, WDR77 and RIOK1. RIOK1 and CLNS1A CC associate with PRMT5 in a mutually exclusive fashion, which allows the CC recruitment of distinct methylation substrates, such as nucleolin/NCL CC and Sm proteins, respectively (By similarity). Interacts with PRDM1 CC (PubMed:16699504). Identified in a complex composed of methylosome and CC PRMT1 and ERH. Interacts with EGFR; methylates EGFR and stimulates CC EGFR-mediated ERK activation. Interacts with HOXA9. Interacts with CC SRGAP2 (By similarity). Found in a complex with COPRS, RUNX1 and CBFB CC (PubMed:22193545). Interacts with CHTOP; the interaction symmetrically CC methylates CHTOP, but seems to require the presence of PRMT1 CC (PubMed:19858291, PubMed:22872859). Interacts with EPB41L3; this CC modulates methylation of target proteins. Component of a high molecular CC weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). CC Associates with SWI/SNF remodeling complexes containing SMARCA2 and CC SMARCA4. Interacts with JAK2, SSTR1, SUPT5H, BRAF and with active RAF1. CC Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting CC its recruitment on histone H4. Interacts with CLNS1A/pICln. Identified CC in a complex with CLNS1A/pICln and Sm proteins. Interacts with RPS10. CC Interacts with WDR77 (By similarity). Interacts with IWS1. Interacts CC with CRY1 (PubMed:23133559). Interacts with POLR2A. Interacts with CC SMN1/SMN2. Interacts with LYAR; this interaction is direct. Interacts CC with TTC5/STRAP; this interaction is DNA damage-dependent and promotes CC PRMT5 interaction with p53/TP53. Interacts with p53/TP53 in response to CC DNA damage; the interaction is TTC5/STRAP dependent. Interacts with CC FAM47E; the interaction is direct, promotes PRMT5 localization to CC chromatin, and does not disrupt its association with WDR77 or STUB1 (By CC similarity). Interacts with TDRD6 (PubMed:28263986). Interacts with CC STUB1 (By similarity). Interacts with MBD2 (By similarity). Does not CC interact with MBD3 (By similarity). {ECO:0000250|UniProtKB:O14744, CC ECO:0000269|PubMed:16699504, ECO:0000269|PubMed:19858291, CC ECO:0000269|PubMed:22193545, ECO:0000269|PubMed:22872859, CC ECO:0000269|PubMed:23133559, ECO:0000269|PubMed:28263986}. CC -!- INTERACTION: CC Q8CIG8; P25322: Ccnd1; NbExp=5; IntAct=EBI-2527009, EBI-847243; CC Q8CIG8; Q9CY57: Chtop; NbExp=4; IntAct=EBI-2527009, EBI-6393116; CC Q8CIG8; P97784: Cry1; NbExp=2; IntAct=EBI-2527009, EBI-1266607; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14744}. Nucleus CC {ECO:0000269|PubMed:22872859}. Golgi apparatus CC {ECO:0000250|UniProtKB:O14744}. Note=Localizes to promoter regions of CC target genes on chromosomes (By similarity). Localizes to methylated CC chromatin (By similarity). {ECO:0000250|UniProtKB:O14744}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Protein arginine N-methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU01015}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK132414; BAE21155.1; -; mRNA. DR EMBL; AK165165; BAE38057.1; -; mRNA. DR EMBL; BC023905; AAH23905.1; -; mRNA. DR EMBL; AF167573; AAF04503.1; -; mRNA. DR CCDS; CCDS27091.1; -. DR RefSeq; NP_001300835.1; NM_001313906.1. DR RefSeq; NP_001300836.1; NM_001313907.1. DR RefSeq; NP_038796.2; NM_013768.3. DR AlphaFoldDB; Q8CIG8; -. DR SMR; Q8CIG8; -. DR BioGRID; 205181; 50. DR ComplexPortal; CPX-1023; Methylosome. DR IntAct; Q8CIG8; 20. DR MINT; Q8CIG8; -. DR STRING; 10090.ENSMUSP00000023873; -. DR iPTMnet; Q8CIG8; -. DR PhosphoSitePlus; Q8CIG8; -. DR SwissPalm; Q8CIG8; -. DR EPD; Q8CIG8; -. DR MaxQB; Q8CIG8; -. DR PaxDb; 10090-ENSMUSP00000023873; -. DR PeptideAtlas; Q8CIG8; -. DR ProteomicsDB; 281870; -. DR Pumba; Q8CIG8; -. DR DNASU; 27374; -. DR GeneID; 27374; -. DR KEGG; mmu:27374; -. DR UCSC; uc007twf.2; mouse. DR AGR; MGI:1351645; -. DR CTD; 10419; -. DR MGI; MGI:1351645; Prmt5. DR eggNOG; KOG0822; Eukaryota. DR InParanoid; Q8CIG8; -. DR OrthoDB; 5489665at2759; -. DR PhylomeDB; Q8CIG8; -. DR TreeFam; TF300626; -. DR BRENDA; 2.1.1.320; 3474. DR Reactome; R-MMU-191859; snRNP Assembly. DR Reactome; R-MMU-3214858; RMTs methylate histone arginines. DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation. DR BioGRID-ORCS; 27374; 29 hits in 83 CRISPR screens. DR ChiTaRS; Prmt5; mouse. DR PRO; PR:Q8CIG8; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q8CIG8; Protein. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0035097; C:histone methyltransferase complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI. DR GO; GO:0034709; C:methylosome; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IMP:MGI. DR GO; GO:0070888; F:E-box binding; IDA:UniProtKB. DR GO; GO:0008469; F:histone arginine N-methyltransferase activity; IBA:GO_Central. DR GO; GO:0070612; F:histone H2AR3 methyltransferase activity; IDA:MGI. DR GO; GO:0044020; F:histone H4R3 methyltransferase activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0008327; F:methyl-CpG binding; ISS:UniProtKB. DR GO; GO:0008168; F:methyltransferase activity; ISO:MGI. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; ISS:UniProtKB. DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI. DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI. DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB. DR GO; GO:0006353; P:DNA-templated transcription termination; ISS:UniProtKB. DR GO; GO:0042118; P:endothelial cell activation; ISO:MGI. DR GO; GO:0010467; P:gene expression; IDA:MGI. DR GO; GO:0090161; P:Golgi ribbon formation; ISS:UniProtKB. DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0018216; P:peptidyl-arginine methylation; ISS:UniProtKB. DR GO; GO:1904992; P:positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway; ISO:MGI. DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI. DR GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI. DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR Gene3D; 2.70.160.11; Hnrnp arginine n-methyltransferase1; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR025799; Arg_MeTrfase. DR InterPro; IPR007857; Arg_MeTrfase_PRMT5. DR InterPro; IPR035075; PRMT5. DR InterPro; IPR035248; PRMT5_C. DR InterPro; IPR035247; PRMT5_TIM. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR10738; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1. DR PANTHER; PTHR10738:SF0; PROTEIN ARGININE N-METHYLTRANSFERASE 5; 1. DR Pfam; PF05185; PRMT5; 1. DR Pfam; PF17286; PRMT5_C; 1. DR Pfam; PF17285; PRMT5_TIM; 1. DR PIRSF; PIRSF015894; Skb1_MeTrfase; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51678; SAM_MT_PRMT; 1. PE 1: Evidence at protein level; KW Acetylation; Biological rhythms; Chromatin regulator; Cytoplasm; KW Golgi apparatus; Methyltransferase; Nucleus; Reference proteome; Repressor; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O14744" FT CHAIN 2..637 FT /note="Protein arginine N-methyltransferase 5" FT /id="PRO_0000212344" FT DOMAIN 308..615 FT /note="SAM-dependent MTase PRMT-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015" FT REGION 13..292 FT /note="TIM barrel" FT /evidence="ECO:0000250|UniProtKB:O14744" FT REGION 465..637 FT /note="Beta barrel" FT /evidence="ECO:0000250|UniProtKB:O14744" FT REGION 488..494 FT /note="Dimerization" FT /evidence="ECO:0000250|UniProtKB:O14744" FT ACT_SITE 435 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:O14744" FT ACT_SITE 444 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 324 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 327 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_note="substrate" FT /ligand_part="L-arginine residue" FT /ligand_part_id="ChEBI:CHEBI:29965" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 333..334 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 392 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 419..420 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 435 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_note="substrate" FT /ligand_part="L-arginine residue" FT /ligand_part_id="ChEBI:CHEBI:29965" FT /evidence="ECO:0000250|UniProtKB:O14744" FT BINDING 444 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_note="substrate" FT /ligand_part="L-arginine residue" FT /ligand_part_id="ChEBI:CHEBI:29965" FT /evidence="ECO:0000250|UniProtKB:O14744" FT SITE 327 FT /note="Critical for specifying symmetric addition of methyl FT groups" FT /evidence="ECO:0000250|UniProtKB:P46580" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:O14744" FT CONFLICT 169 FT /note="A -> E (in Ref. 1; BAE21155/BAE38057)" FT /evidence="ECO:0000305" FT CONFLICT 376 FT /note="L -> F (in Ref. 3; AAF04503)" FT /evidence="ECO:0000305" SQ SEQUENCE 637 AA; 72680 MW; E8014CA172B30543 CRC64; MAAMAVGGAG GSRVSSGRDL NCVPEIADTL GAVAKQGFDF LCMPVFHPRF KREFIQEPAK NRPGPQTRSD LLLSGRDWNT LIVGKLSPWI HPDSKVEKIR RNSEAAMLQE LNFGAYLGLP AFLLPLNQED NTNLARVLTN HIHTGHHSSM FWMRVPLVAP EDLRDDVIAN APTTHTEEYS GEEKTWMWWH NFRTLCDYSK RIAVALEIGA DLPSNHVIDR WLGEPIKAAI LPTSIFLTNK KGFPVLSKVQ QRLIFRLLKL EVQFIITGTN HHSEKEFCSY LQYLEYLSQN RPPPNAYELF AKGYEDYLQS PLQPLMDNLE SQTYEVFEKD PIKYSQYQQA IYKCLLDRVP EEEKETNVQV LMVLGAGRGP LVNASLRAAK QAERRIRLYA VEKNPNAVVT LENWQFEEWG SQVTVVSSDM REWVAPEKAD IIVSELLGSF ADNELSPECL DGAQHFLKDD GVSIPGEYTS FLAPISSSKL YNEVRACREK DRDPEAQFEM PYVVRLHNFH QLSAPKPCFT FSHPNRDPMI DNNRYCTLEF PVEVNTVLHG FAGYFETVLY RDITLSIRPE THSPGMFSWF PIFFPIKQPI TVHEGQNICV RFWRCSNSKK VWYEWAVTAP VCSSIHNPTG RSYTIGL //