ANM5_MOUSE
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 03-AUG-2022, entry version 160.
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, Pancreas,
RC 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). Mono- and dimethylates arginine residues of
CC myelin basic protein (MBP) in vitro. May play a role in cytokine-
CC activated transduction pathways. Negatively regulates cyclin E1
CC promoter activity and cellular proliferation (By similarity).
CC Methylates histone H2A and H4 'Arg-3' during germ cell development
CC (PubMed:16699504). Methylates histone H3 'Arg-8', which may repress
CC transcription (PubMed:15485929). Methylates the Piwi proteins (PIWIL1,
CC PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the
CC interaction with Tudor domain-containing proteins and subsequent
CC localization to the meiotic nuage (PubMed:19584108). Methylates RPS10
CC (By similarity). Attenuates EGF signaling through the MAPK1/MAPK3
CC pathway acting at 2 levels. First, monomethylates EGFR; this enhances
CC EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually
CC leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and
CC probably BRAF, hence destabilizing these 2 signaling proteins and
CC reducing their catalytic activity (PubMed:21917714). Required for
CC induction of E-selectin and VCAM-1, on the endothelial cells surface at
CC sites of inflammation. Methylates HOXA9. Methylates and regulates
CC SRGAP2 which is involved in cell migration and differentiation (By
CC similarity). Acts as a transcriptional corepressor in CRY1-mediated
CC repression of the core circadian component PER1 by regulating the H4R3
CC dimethylation at the PER1 promoter (PubMed:23133559). Methylates
CC GM130/GOLGA2, regulating Golgi ribbon formation. Methylates H4R3 in
CC genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent
CC manner. 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). {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}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01015}.
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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; 48.
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; Q8CIG8; -.
DR PeptideAtlas; Q8CIG8; -.
DR PRIDE; Q8CIG8; -.
DR ProteomicsDB; 281870; -.
DR DNASU; 27374; -.
DR GeneID; 27374; -.
DR KEGG; mmu:27374; -.
DR UCSC; uc007twf.2; mouse.
DR CTD; 10419; -.
DR MGI; MGI:1351645; Prmt5.
DR eggNOG; KOG0822; Eukaryota.
DR InParanoid; Q8CIG8; -.
DR OrthoDB; 475852at2759; -.
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 77 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:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0034969; P:histone arginine methylation; IDA:MGI.
DR GO; GO:0043985; P:histone H4-R3 methylation; IMP: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:0035246; P:peptidyl-arginine N-methylation; ISO:MGI.
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; IC:ComplexPortal.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:MGI.
DR GO; GO:0006479; P:protein methylation; ISO:MGI.
DR GO; GO:0044030; P:regulation of DNA methylation; ISO:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 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; PTHR10738; 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; SSF53335; 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
