ANM3_HUMAN
ID ANM3_HUMAN Reviewed; 531 AA.
AC O60678; A0A0A0MSN7; B4DUC7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Protein arginine N-methyltransferase 3 {ECO:0000305|PubMed:33495566};
DE EC=2.1.1.319 {ECO:0000305|PubMed:33495566};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3 {ECO:0000312|HGNC:HGNC:30163};
GN Name=PRMT3 {ECO:0000312|HGNC:HGNC:30163};
GN Synonyms=HRMT1L3 {ECO:0000312|HGNC:HGNC:30163};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-531 (ISOFORM 1).
RX PubMed=9642256; DOI=10.1074/jbc.273.27.16935;
RA Tang J., Gary J.D., Clarke S., Herschman H.R.;
RT "PRMT 3, a type I protein arginine N-methyltransferase that differs from
RT PRMT1 in its oligomerization, subcellular localization, substrate
RT specificity, and regulation.";
RL J. Biol. Chem. 273:16935-16945(1998).
RN [5]
RP INTERACTION WITH EPB41L3.
RX PubMed=15334060; DOI=10.1038/sj.onc.1208057;
RA Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A.,
RA Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.;
RT "DAL-1/4.1B tumor suppressor interacts with protein arginine N-
RT methyltransferase 3 (PRMT3) and inhibits its ability to methylate
RT substrates in vitro and in vivo.";
RL Oncogene 23:7761-7771(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION AT SER-25 AND SER-27, MUTAGENESIS OF TYR-87, ABSENCE OF
RP PHOSPHORYLATION AT TYR-87, AND INTERACTION WITH RPS2.
RX PubMed=21059412; DOI=10.1016/j.bbapap.2010.10.011;
RA Handrkova H., Petrak J., Halada P., Pospisilova D., Cmejla R.;
RT "Tyrosine 87 is vital for the activity of human protein arginine
RT methyltransferase 3 (PRMT3).";
RL Biochim. Biophys. Acta 1814:277-282(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-27, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-27 AND SER-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ALDH1A1, SUBCELLULAR
RP LOCATION, REGION, AND MUTAGENESIS OF GLU-338; HIS-464; ASN-465; ARG-466 AND
RP VAL-468.
RX PubMed=33495566; DOI=10.1038/s42003-020-01644-3;
RA Verma M., Khan M.I.K., Kadumuri R.V., Chakrapani B., Awasthi S., Mahesh A.,
RA Govindaraju G., Chavali P.L., Rajavelu A., Chavali S., Dhayalan A.;
RT "PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting
RT retinoic acid signaling.";
RL Commun. Biol. 4:109-109(2021).
RN [17] {ECO:0007744|PDB:2FYT}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 211-531 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in
RT complex with SAH.";
RL Submitted (MAR-2006) to the PDB data bank.
RN [18]
RP INTERACTION WITH RPS2.
RX PubMed=30530495; DOI=10.1074/jbc.ra118.004928;
RA Dionne K.L., Bergeron D., Landry-Voyer A.M., Bachand F.;
RT "The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal
RT complex with human ZNF277 that competes with the PRMT3-uS5 interaction.";
RL J. Biol. Chem. 294:1944-1955(2019).
CC -!- FUNCTION: Protein-arginine N-methyltransferase that catalyzes both the
CC monomethylation and asymmetric dimethylation of the guanidino nitrogens
CC of arginine residues in target proteins, and therefore falls into the
CC group of type I methyltransferases (Probable). May regulate retinoic
CC acid synthesis and signaling by inhibiting ALDH1A1 retinal
CC dehydrogenase activity (PubMed:33495566). {ECO:0000269|PubMed:33495566,
CC ECO:0000305|PubMed:33495566}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280;
CC Evidence={ECO:0000305|PubMed:33495566};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000305|PubMed:33495566};
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:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61897; EC=2.1.1.319;
CC Evidence={ECO:0000305|PubMed:33495566};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000305|PubMed:33495566};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide and high
CC concentrations of zinc chloride. {ECO:0000250|UniProtKB:O70467}.
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with EPB41L3
CC (via FERM domain); the interaction is direct and inhibits the protein-
CC arginine N-methyltransferase activity of PRMT3 (PubMed:15334060).
CC Interacts with the 40S ribosomal protein RPS2 (PubMed:21059412,
CC PubMed:30530495). Interacts with ALDH1A1; the interaction is direct,
CC inhibits ALDH1A1 aldehyde dehydrogenase activity and is independent of
CC the methyltransferase activity of PRMT3 (PubMed:33495566).
CC {ECO:0000250|UniProtKB:O70467, ECO:0000269|PubMed:15334060,
CC ECO:0000269|PubMed:21059412, ECO:0000269|PubMed:30530495,
CC ECO:0000269|PubMed:33495566}.
CC -!- INTERACTION:
CC O60678; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-2809009, EBI-10181188;
CC O60678; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2809009, EBI-16439278;
CC O60678; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-2809009, EBI-10232538;
CC O60678; P15880: RPS2; NbExp=5; IntAct=EBI-2809009, EBI-443446;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9642256}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60678-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60678-2; Sequence=VSP_040330;
CC -!- DOMAIN: The C2H2-type zinc-finger is responsible for substrate
CC specificity. {ECO:0000250|UniProtKB:O70467}.
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; AK300591; BAG62289.1; -; mRNA.
DR EMBL; AC025972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037544; AAH37544.1; -; mRNA.
DR EMBL; BC064831; AAH64831.1; -; mRNA.
DR EMBL; AF059531; AAC39837.1; -; mRNA.
DR CCDS; CCDS44554.1; -. [O60678-2]
DR CCDS; CCDS7853.1; -. [O60678-1]
DR RefSeq; NP_005779.1; NM_005788.3. [O60678-1]
DR PDB; 2FYT; X-ray; 2.00 A; A=211-531.
DR PDB; 3SMQ; X-ray; 2.00 A; A=211-531.
DR PDB; 4HSG; X-ray; 2.30 A; A=211-531.
DR PDB; 4QQN; X-ray; 2.08 A; A=211-531.
DR PDB; 4RYL; X-ray; 2.10 A; A=211-531.
DR PDBsum; 2FYT; -.
DR PDBsum; 3SMQ; -.
DR PDBsum; 4HSG; -.
DR PDBsum; 4QQN; -.
DR PDBsum; 4RYL; -.
DR AlphaFoldDB; O60678; -.
DR SMR; O60678; -.
DR BioGRID; 115491; 94.
DR IntAct; O60678; 32.
DR MINT; O60678; -.
DR STRING; 9606.ENSP00000331879; -.
DR BindingDB; O60678; -.
DR ChEMBL; CHEMBL5891; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR GuidetoPHARMACOLOGY; 1254; -.
DR GlyGen; O60678; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60678; -.
DR PhosphoSitePlus; O60678; -.
DR BioMuta; PRMT3; -.
DR EPD; O60678; -.
DR jPOST; O60678; -.
DR MassIVE; O60678; -.
DR PaxDb; O60678; -.
DR PeptideAtlas; O60678; -.
DR PRIDE; O60678; -.
DR ProteomicsDB; 49522; -. [O60678-1]
DR ProteomicsDB; 49523; -. [O60678-2]
DR ABCD; O60678; 2 sequenced antibodies.
DR Antibodypedia; 1605; 345 antibodies from 33 providers.
DR DNASU; 10196; -.
DR Ensembl; ENST00000331079.11; ENSP00000331879.6; ENSG00000185238.13. [O60678-1]
DR Ensembl; ENST00000437750.2; ENSP00000397766.2; ENSG00000185238.13. [O60678-2]
DR GeneID; 10196; -.
DR KEGG; hsa:10196; -.
DR MANE-Select; ENST00000331079.11; ENSP00000331879.6; NM_005788.4; NP_005779.1.
DR UCSC; uc001mqb.4; human. [O60678-1]
DR CTD; 10196; -.
DR DisGeNET; 10196; -.
DR GeneCards; PRMT3; -.
DR HGNC; HGNC:30163; PRMT3.
DR HPA; ENSG00000185238; Low tissue specificity.
DR MIM; 603190; gene.
DR neXtProt; NX_O60678; -.
DR OpenTargets; ENSG00000185238; -.
DR PharmGKB; PA29462; -.
DR VEuPathDB; HostDB:ENSG00000185238; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000156825; -.
DR HOGENOM; CLU_017375_6_2_1; -.
DR InParanoid; O60678; -.
DR OMA; ETHWQQG; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; O60678; -.
DR TreeFam; TF323587; -.
DR BioCyc; MetaCyc:MON66-43216; -.
DR BRENDA; 2.1.1.319; 2681.
DR PathwayCommons; O60678; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SABIO-RK; O60678; -.
DR SignaLink; O60678; -.
DR BioGRID-ORCS; 10196; 15 hits in 1092 CRISPR screens.
DR ChiTaRS; PRMT3; human.
DR EvolutionaryTrace; O60678; -.
DR GeneWiki; PRMT3; -.
DR GenomeRNAi; 10196; -.
DR Pharos; O60678; Tchem.
DR PRO; PR:O60678; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O60678; protein.
DR Bgee; ENSG00000185238; Expressed in ventricular zone and 188 other tissues.
DR ExpressionAtlas; O60678; baseline and differential.
DR Genevisible; O60678; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0072341; F:modified amino acid binding; IEA:Ensembl.
DR GO; GO:0016274; F:protein-arginine N-methyltransferase activity; TAS:Reactome.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IEA:Ensembl.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IEA:RHEA.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:1900053; P:negative regulation of retinoic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IEA:Ensembl.
DR GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW Methyltransferase; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..531
FT /note="Protein arginine N-methyltransferase 3"
FT /id="PRO_0000212326"
FT DOMAIN 217..531
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ZN_FING 48..71
FT /note="C2H2-type"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..531
FT /note="Mediates interaction with ALDH1A1"
FT /evidence="ECO:0000269|PubMed:33495566"
FT REGION 285..287
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT"
FT REGION 313..314
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT"
FT COMPBIAS 20..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:O70467"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT"
FT SITE 87
FT /note="Not phosphorylated"
FT /evidence="ECO:0000269|PubMed:21059412"
FT MOD_RES 2
FT /note="N-acetylcysteine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21059412,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21059412,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 11..99
FT /note="GRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEE
FT TFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLK -> YSHLLKKHFHTVSLSISL
FT ILTAWFINM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040330"
FT VARIANT 440
FT /note="L -> V (in dbSNP:rs3758805)"
FT /id="VAR_024584"
FT VARIANT 470
FT /note="S -> C (in dbSNP:rs11025585)"
FT /id="VAR_030943"
FT VARIANT 508
FT /note="N -> S (in dbSNP:rs6483700)"
FT /id="VAR_024585"
FT MUTAGEN 87
FT /note="Y->C: Markedly reduced affinity for RPS2."
FT /evidence="ECO:0000269|PubMed:21059412"
FT MUTAGEN 87
FT /note="Y->E: Markedly reduced affinity for RPS2."
FT /evidence="ECO:0000269|PubMed:21059412"
FT MUTAGEN 87
FT /note="Y->F: No effect on interaction with RPS2."
FT /evidence="ECO:0000269|PubMed:21059412"
FT MUTAGEN 338
FT /note="E->Q: No effect on ALDH1A1 activity regulation."
FT /evidence="ECO:0000269|PubMed:33495566"
FT MUTAGEN 464
FT /note="H->A: Loss of interaction with ALDH1A1."
FT /evidence="ECO:0000269|PubMed:33495566"
FT MUTAGEN 465
FT /note="N->A: Loss of interaction with ALDH1A1."
FT /evidence="ECO:0000269|PubMed:33495566"
FT MUTAGEN 466
FT /note="R->A: Loss of interaction with ALDH1A1."
FT /evidence="ECO:0000269|PubMed:33495566"
FT MUTAGEN 468
FT /note="V->A: Loss of interaction with ALDH1A1."
FT /evidence="ECO:0000269|PubMed:33495566"
FT CONFLICT 21
FT /note="L -> E (in Ref. 4; AAC39837)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="V -> F (in Ref. 1; BAG62289)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="K -> R (in Ref. 1; BAG62289)"
FT /evidence="ECO:0000305"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2FYT"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:2FYT"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:2FYT"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3SMQ"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:2FYT"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 362..370
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2FYT"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:2FYT"
FT HELIX 429..432
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 433..442
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 446..459
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 482..493
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 498..507
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:2FYT"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:2FYT"
SQ SEQUENCE 531 AA; 59903 MW; 71EC59E2BEDBE7AC CRC64;
MCSLASGATG GRGAVENEED LPELSDSGDE AAWEDEDDAD LPHGKQQTPC LFCNRLFTSA
EETFSHCKSE HQFNIDSMVH KHGLEFYGYI KLINFIRLKN PTVEYMNSIY NPVPWEKEEY
LKPVLEDDLL LQFDVEDLYE PVSVPFSYPN GLSENTSVVE KLKHMEARAL SAEAALARAR
EDLQKMKQFA QDFVMHTDVR TCSSSTSVIA DLQEDEDGVY FSSYGHYGIH EEMLKDKIRT
ESYRDFIYQN PHIFKDKVVL DVGCGTGILS MFAAKAGAKK VLGVDQSEIL YQAMDIIRLN
KLEDTITLIK GKIEEVHLPV EKVDVIISEW MGYFLLFESM LDSVLYAKNK YLAKGGSVYP
DICTISLVAV SDVNKHADRI AFWDDVYGFK MSCMKKAVIP EAVVEVLDPK TLISEPCGIK
HIDCHTTSIS DLEFSSDFTL KITRTSMCTA IAGYFDIYFE KNCHNRVVFS TGPQSTKTHW
KQTVFLLEKP FSVKAGEALK GKVTVHKNKK DPRSLTVTLT LNNSTQTYGL Q
