ANM8_HUMAN
ID ANM8_HUMAN Reviewed; 394 AA.
AC Q9NR22; B2RDP0; Q8TBJ8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein arginine N-methyltransferase 8 {ECO:0000305};
DE EC=2.1.1.319 {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:18320585};
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
GN Name=PRMT8 {ECO:0000312|HGNC:HGNC:5188}; Synonyms=HRMT1L3, HRMT1L4;
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).
RC TISSUE=Neuroepithelioma;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(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 37-394 (ISOFORM 1).
RC TISSUE=Brain;
RA Lorenz B., Strom T.M.;
RT "Transcripts in human map region 12p13.3.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=16051612; DOI=10.1074/jbc.m506944200;
RA Lee J., Sayegh J., Daniel J., Clarke S., Bedford M.T.;
RT "PRMT8, a new membrane-bound tissue-specific member of the protein arginine
RT methyltransferase family.";
RL J. Biol. Chem. 280:32890-32896(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, N-TERMINAL REGION DOMAIN, DOMAIN SH3-BINDING
RP MOTIF, METHYLATION AT ARG-58 AND ARG-73, AND INTERACTION WITH PRMT2 AND
RP FYN.
RX PubMed=17925405; DOI=10.1074/jbc.m704650200;
RA Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
RT "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its
RT N-terminal domain.";
RL J. Biol. Chem. 282:36444-36453(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH EWS.
RX PubMed=18320585; DOI=10.1002/prot.22004;
RA Pahlich S., Zakaryan R.P., Gehring H.;
RT "Identification of proteins interacting with protein arginine
RT methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of
RT its methylation state.";
RL Proteins 72:1125-1137(2008).
RN [8] {ECO:0007744|PDB:5DST}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 68-394 OF HOMODIMER IN COMPLEX
RP WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, SUBUNIT,
RP S-ADENOSYL-L-METHIONINE-BINDING, SUBCELLULAR LOCATION, MYRISTOYLATION AT
RP GLY-2, AND MUTAGENESIS OF GLY-2; CYS-273; CYS-295; TYR-303; TYR-345;
RP ARG-349 AND LEU-382.
RX PubMed=26876602; DOI=10.1016/j.jmb.2016.02.007;
RA Toma-Fukai S., Kim J.D., Park K.E., Kuwabara N., Shimizu N., Krayukhina E.,
RA Uchiyama S., Fukamizu A., Shimizu T.;
RT "Novel helical assembly in arginine methyltransferase 8.";
RL J. Mol. Biol. 428:1197-1208(2016).
RN [9] {ECO:0007744|PDB:4X41}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 61-394 OF HOMODIMER IN COMPLEX IN
RP COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, AND SUBUNIT.
RX PubMed=26529540; DOI=10.1021/acs.biochem.5b00995;
RA Lee W.C., Lin W.L., Matsui T., Chen E.S., Wei T.Y., Lin W.H., Hu H.,
RA Zheng Y.G., Tsai M.D., Ho M.C.;
RT "Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein
RT Substrate Specificity.";
RL Biochemistry 54:7514-7523(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent and membrane-associated
CC arginine methyltransferase that can both catalyze the formation of
CC omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine
CC (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A
CC and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602,
CC PubMed:26529540). Able to mono- and dimethylate EWS protein; however
CC its precise role toward EWS remains unclear as it still interacts with
CC fully methylated EWS (PubMed:18320585). {ECO:0000269|PubMed:16051612,
CC ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:18320585,
CC ECO:0000269|PubMed:26529540, ECO:0000269|PubMed:26876602}.
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:0000269|PubMed:16051612, ECO:0000269|PubMed:17925405,
CC ECO:0000269|PubMed:18320585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48101;
CC Evidence={ECO:0000305|PubMed:16051612};
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:0000269|PubMed:16051612, ECO:0000269|PubMed:17925405,
CC ECO:0000269|PubMed:18320585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48097;
CC Evidence={ECO:0000305|PubMed:16051612};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for GRGGFGGRGGFRGGRGG-NH2 {ECO:0000269|PubMed:18320585};
CC -!- SUBUNIT: Homodimer (PubMed:16051612, PubMed:26876602, PubMed:26529540).
CC Tetramer; individual homodimers associates to form a homotetramer
CC (PubMed:26529540). Homooctamer; individual homodimers associates to
CC form a homooctamer and homooligomerization is required for proper
CC localization to the cell membrane (PubMed:26876602). Heterodimer with
CC PRMT1; heterodimerization may recruit PRMT1 activity to the plasma
CC membrane (PubMed:16051612). Interacts with PRMT2 (via the SH3 domain)
CC (PubMed:17925405). Interacts with FYN (via the SH3 domain)
CC (PubMed:17925405). Interacts with EWS; independently of EWS methylation
CC status (PubMed:18320585). {ECO:0000269|PubMed:16051612,
CC ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:18320585,
CC ECO:0000269|PubMed:26529540, ECO:0000269|PubMed:26876602}.
CC -!- INTERACTION:
CC Q9NR22; Q99873: PRMT1; NbExp=3; IntAct=EBI-745545, EBI-78738;
CC Q9NR22; Q99873-3: PRMT1; NbExp=10; IntAct=EBI-745545, EBI-17165527;
CC Q9NR22; Q9NR22: PRMT8; NbExp=9; IntAct=EBI-745545, EBI-745545;
CC Q9NR22; O60506: SYNCRIP; NbExp=4; IntAct=EBI-745545, EBI-1024357;
CC Q9NR22; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-745545, EBI-11123832;
CC Q9NR22; O14787-2: TNPO2; NbExp=3; IntAct=EBI-745545, EBI-12076664;
CC Q9NR22; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-745545, EBI-607755;
CC Q9NR22-2; Q99873: PRMT1; NbExp=5; IntAct=EBI-10186886, EBI-78738;
CC Q9NR22-2; Q9NR22-2: PRMT8; NbExp=3; IntAct=EBI-10186886, EBI-10186886;
CC Q9NR22-2; O60506: SYNCRIP; NbExp=3; IntAct=EBI-10186886, EBI-1024357;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16051612,
CC ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:26876602}; Lipid-anchor
CC {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:18320585,
CC ECO:0000269|PubMed:26876602}; Cytoplasmic side
CC {ECO:0000269|PubMed:16051612, ECO:0000269|PubMed:18320585,
CC ECO:0000269|PubMed:26876602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR22-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR22-2; Sequence=VSP_037466;
CC -!- TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:16051612}.
CC -!- DOMAIN: The SH3-binding motifs mediate the interaction with SH3 domain-
CC containing proteins such as PRMT2 and FYN, possibly leading to displace
CC the N-terminal domain and activate the protein.
CC {ECO:0000269|PubMed:17925405}.
CC -!- DOMAIN: The N-terminal region (1-60) inhibits the arginine N-
CC methyltransferase activity. {ECO:0000269|PubMed:17925405}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT8
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF91390.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG37987.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK315619; BAG37987.1; ALT_FRAME; mRNA.
DR EMBL; AC005831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022458; AAH22458.2; -; mRNA.
DR EMBL; AF263539; AAF91390.1; ALT_INIT; mRNA.
DR CCDS; CCDS58200.1; -. [Q9NR22-2]
DR CCDS; CCDS8521.2; -. [Q9NR22-1]
DR RefSeq; NP_001243465.1; NM_001256536.1. [Q9NR22-2]
DR RefSeq; NP_062828.3; NM_019854.4. [Q9NR22-1]
DR PDB; 4X41; X-ray; 3.50 A; A/B=61-394.
DR PDB; 5DST; X-ray; 2.96 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=68-394.
DR PDBsum; 4X41; -.
DR PDBsum; 5DST; -.
DR AlphaFoldDB; Q9NR22; -.
DR SMR; Q9NR22; -.
DR BioGRID; 121140; 87.
DR ELM; Q9NR22; -.
DR IntAct; Q9NR22; 36.
DR MINT; Q9NR22; -.
DR STRING; 9606.ENSP00000372067; -.
DR BindingDB; Q9NR22; -.
DR ChEMBL; CHEMBL3108648; -.
DR GuidetoPHARMACOLOGY; 1259; -.
DR iPTMnet; Q9NR22; -.
DR PhosphoSitePlus; Q9NR22; -.
DR BioMuta; PRMT8; -.
DR DMDM; 88983969; -.
DR EPD; Q9NR22; -.
DR jPOST; Q9NR22; -.
DR MassIVE; Q9NR22; -.
DR MaxQB; Q9NR22; -.
DR PaxDb; Q9NR22; -.
DR PeptideAtlas; Q9NR22; -.
DR PRIDE; Q9NR22; -.
DR ProteomicsDB; 82259; -. [Q9NR22-1]
DR ProteomicsDB; 82260; -. [Q9NR22-2]
DR Antibodypedia; 10506; 171 antibodies from 27 providers.
DR DNASU; 56341; -.
DR Ensembl; ENST00000382622.4; ENSP00000372067.3; ENSG00000111218.12. [Q9NR22-1]
DR Ensembl; ENST00000452611.6; ENSP00000414507.2; ENSG00000111218.12. [Q9NR22-2]
DR GeneID; 56341; -.
DR KEGG; hsa:56341; -.
DR MANE-Select; ENST00000382622.4; ENSP00000372067.3; NM_019854.5; NP_062828.3.
DR UCSC; uc001qmf.5; human. [Q9NR22-1]
DR CTD; 56341; -.
DR DisGeNET; 56341; -.
DR GeneCards; PRMT8; -.
DR HGNC; HGNC:5188; PRMT8.
DR HPA; ENSG00000111218; Tissue enhanced (brain, retina, testis).
DR MIM; 610086; gene.
DR neXtProt; NX_Q9NR22; -.
DR OpenTargets; ENSG00000111218; -.
DR PharmGKB; PA134903406; -.
DR VEuPathDB; HostDB:ENSG00000111218; -.
DR eggNOG; KOG1499; Eukaryota.
DR GeneTree; ENSGT00940000155867; -.
DR HOGENOM; CLU_017375_1_1_1; -.
DR InParanoid; Q9NR22; -.
DR OMA; RNDFVHA; -.
DR OrthoDB; 840669at2759; -.
DR PhylomeDB; Q9NR22; -.
DR TreeFam; TF300608; -.
DR BioCyc; MetaCyc:ENSG00000111218-MON; -.
DR BRENDA; 2.1.1.319; 2681.
DR PathwayCommons; Q9NR22; -.
DR SABIO-RK; Q9NR22; -.
DR SignaLink; Q9NR22; -.
DR BioGRID-ORCS; 56341; 8 hits in 1082 CRISPR screens.
DR ChiTaRS; PRMT8; human.
DR GenomeRNAi; 56341; -.
DR Pharos; Q9NR22; Tchem.
DR PRO; PR:Q9NR22; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NR22; protein.
DR Bgee; ENSG00000111218; Expressed in middle temporal gyrus and 65 other tissues.
DR Genevisible; Q9NR22; HS.
DR GO; GO:0098753; C:anchored component of the cytoplasmic side of the plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IDA:HGNC-UCL.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:HGNC-UCL.
DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:UniProtKB.
DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; TAS:HGNC-UCL.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51678; SAM_MT_PRMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Lipoprotein; Membrane;
KW Methylation; Methyltransferase; Myristate; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16051612,
FT ECO:0000269|PubMed:26876602"
FT CHAIN 2..394
FT /note="Protein arginine N-methyltransferase 8"
FT /id="PRO_0000212329"
FT DOMAIN 73..394
FT /note="SAM-dependent MTase PRMT-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT REGION 16..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 29..42
FT /note="SH3-binding 1"
FT /evidence="ECO:0000269|PubMed:17925405"
FT MOTIF 53..58
FT /note="SH3-binding 2"
FT /evidence="ECO:0000269|PubMed:17925405"
FT ACT_SITE 185
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT ACT_SITE 194
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q63009"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26529540,
FT ECO:0000305|PubMed:26876602, ECO:0007744|PDB:4X41,
FT ECO:0007744|PDB:5DST"
FT BINDING 119..122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26529540,
FT ECO:0000305|PubMed:26876602, ECO:0007744|PDB:4X41,
FT ECO:0007744|PDB:5DST"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26876602,
FT ECO:0007744|PDB:5DST"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26529540,
FT ECO:0000305|PubMed:26876602, ECO:0007744|PDB:4X41,
FT ECO:0007744|PDB:5DST"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:26876602,
FT ECO:0007744|PDB:5DST"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17925405"
FT MOD_RES 73
FT /note="Asymmetric dimethylarginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17925405"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:16051612,
FT ECO:0000269|PubMed:26876602"
FT VAR_SEQ 1..25
FT /note="MGMKHSSRCLLLRRKMAENAAESTE -> MESLASDGFKLKEVSS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037466"
FT MUTAGEN 2
FT /note="G->A: Loss of cell membrane localization."
FT /evidence="ECO:0000269|PubMed:17925405,
FT ECO:0000269|PubMed:26876602"
FT MUTAGEN 273
FT /note="C->A: No effect on homodimerization but decreased
FT homooligomerization; when associated with A-295 and A-349."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 295
FT /note="C->A: No effect on homodimerization but decreased
FT homooligomerization; when associated with A-273 and A-349."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 303
FT /note="Y->A: Decreases homooligomerization and cell
FT membrane localization. No effect on homodimerization, S-
FT adenosyl-L-methionine binding and EWS protein methylation.
FT No effect on homodimerization but loss of
FT homooligomerization and cell membrane localization; when
FT associated with A-345 and A-382. No effect on S-adenosyl-L-
FT methionine binding but reduced EWS protein methylation;
FT when associated with A-345 and A-382."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 345
FT /note="Y->A: No effect on homooligomerization. No effect on
FT S-adenosyl-L-methionine binding and EWS protein
FT methylation. No effect on homodimerization but loss of
FT homooligomerization and cell membrane localization; when
FT associated with A-303 and A-382. No effect on S-adenosyl-L-
FT methionine binding but reduced EWS protein methylation;
FT when associated with A-303 and A-382."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 349
FT /note="R->A: No effect on homodimerization but decreased
FT homooligomerization; when associated with A-273 and A-295."
FT /evidence="ECO:0000269|PubMed:26876602"
FT MUTAGEN 382
FT /note="L->A: No effect on homooligomerization. No effect on
FT S-adenosyl-L-methionine binding and EWS protein
FT methylation. No effect on homodimerization but loss of
FT homooligomerization and cell membrane localization; when
FT associated with A-303 and A-345. No effect on S-adenosyl-L-
FT methionine binding but reduced EWS protein methylation;
FT when associated with A-303 and A-345."
FT /evidence="ECO:0000269|PubMed:26876602"
FT CONFLICT 150
FT /note="E -> Q (in Ref. 3; AAH22458)"
FT /evidence="ECO:0000305"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:5DST"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5DST"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5DST"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:5DST"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5DST"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 289..298
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 300..315
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 337..348
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 353..362
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4X41"
FT STRAND 369..379
FT /evidence="ECO:0007829|PDB:5DST"
FT STRAND 384..393
FT /evidence="ECO:0007829|PDB:5DST"
SQ SEQUENCE 394 AA; 45291 MW; 44B55438D16394CD CRC64;
MGMKHSSRCL LLRRKMAENA AESTEVNSPP SQPPQPVVPA KPVQCVHHVS TQPSCPGRGK
MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR NSMYHNKHVF KDKVVLDVGS
GTGILSMFAA KAGAKKVFGI ECSSISDYSE KIIKANHLDN IITIFKGKVE EVELPVEKVD
IIISEWMGYC LFYESMLNTV IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE
NVYGFDMTCI RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR GEEIYGTISM
KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR
