DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220484X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions mouse Mus musculus Mouse anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220479X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220485X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220486X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220482X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220483X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220481X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. Only protein-protein interactions in vitro In vitro fps fluorescence polarization spectroscopy Fluorescence anisotropy FPS FPS Fluorescence anisotropy fps predetermined predetermined participant predetermined Liu K., Chen C., Guo Y., Lam R., Bian C., Xu C., Zhao DY., Jin J., MacKenzie F., Pawson T., Min J. DIP original experiment: DIP-220480X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain. piwl1_mouse Piwi-like protein 1 Piwil1 Miwi protein protein mouse Mus musculus Mouse MTGRARARARGRARGQETVQHVGAAASQQPGYIPPRPQQSPTEGDLVGRGRQRGMVVGATSKSQELQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVKLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGRCHAFDGTILFLPKRLQHKVTEVFSQTRNGEHVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPSDPIDIPNHRLVIWPGFTTSILQYENNIMLCTDVSHKVLRSETVLDFMFNLYQQTEEHKFQEQVSKELIGLIVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKDDNVQRELRDWGLSFDSNLLSFSGRILQSEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGIQMKKAIMIEVDDRTEAYLRALQQKVTSDTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDMPLKLAMIVGIDCYHDTTAGRRSIAGFVASINEGMTRWFSRCVFQDRGQELVDGLKVCLQAALRAWSGCNEYMPSRVIVYRDGVGDGQLKTLVNYEVPQFLDCLKSVGRGYNPRLTVIVVKKRVNARFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDSSGLKPDHIQRLTYKLCHVYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL DIP protein Q9JMB7 original sequence version: 95 DIP protein Q9JMB7 original sequence version: 69 mint Probable component of some RISC complex (RNA-induced silencing), which plays a role in spermatogenesis and in germ cell production, proliferation and maintenance. RISC complexes mediate RNA cleavage and translational silencing. Overexpression may cause malignant germline development. May be associated with proliferating activity of cancer cells. When suppressed, inhibits the growth of gastric cancer cells and induced cell cycle arrest in G2/M phase. Inhibits endoribonuclease DICER1 activity 45588D13284CCC4C snd1_mouse Staphylococcal nuclease domain-containing protein 1 p100 co-activator 100 kDa coactivator Snd1 protein protein mouse Mus musculus Mouse MASSAQSSGSSGGPAVPTVQRGIVKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDGKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKASKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPGHHLVTVMLSGIKCPTFRRETDGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNLLGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVPPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGDNIQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHMDGANLSVLLVEQALSKVHFTAERSAYYKPLLSAEEAAKQRKEKVWAHYEERPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDISSHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKVHVFYIDYGNREILPSTRLGTLPPAFSTRVLPAQATEYAFAFIQVPQDEDARTDAVDSVVRDIQNTQCLLNVEHLSASCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR DIP protein Q78PY7 original sequence version: 75 7A31459E9274D0B6 h3-11 Histone H3 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) ARTKQTARSKY h4-4 Histone 4 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) SGRGKGGK q9y2w6-2 Tudor and KH domain-containing protein TDRKH TDRD2 Tudor domain-containing protein 2 protein protein human Homo sapiens Human MSTERTSWTSLSTIQKIALGLGIPASATVAYILYRRYRESREERLTFVGEDDIEIEMRVPQEAVKLIIGRQGANIKQLRKQTGARIDVDTEDVGDERVLLISGFPVQVCKAKAAIHQILTENTPVSEQLSVPQRSVGRIIGRGGETIRSICKASGAKITCDKESEGTLLLSRLIKISGTQKEVAAAKHLILEKVSEDEELRKRIAHSAETRVPRKQPISVRREDMTEPGGAGEPALWKNTSSSMEPTAPLVTPPPKGGGDMAVVVSKEGSWEKPSDDSFQKSEAQAIPEMPMFEIPSPDFSFHADEYLEVYVSASEHPNHFWIQIVGSRSLQLDKLVNEMTQHYENSVPEDLTVHVGDIVAAPLPTNGSWYRARVLGTLENGNLDLYFVDFGDNGDCPLKDLRALRSDFLSLPFQAIECSLARIAPSGDQWEEEALDEFDRLTHCADWKPLVAKISSYVQTGISTWPKIYLYDTSNGKKLDIGLELVHKGYAIELPEDIEENRAVPDMLKDMATETDASLSTLLTETKKSSGEITHTLSCLSLSEAASMSGDDNLEDDYLL DIP protein Q9Y2W6-2 original sequence version: 86 snd1_human Staphylococcal nuclease domain-containing protein 1 100 kDa coactivator EBNA2 coactivator p100 Tudor domain-containing protein 11 SND1 p100 co-activator TDRD11 protein protein human Homo sapiens Human MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR DIP protein Q7KZF4 original sequence version: 43 DIP protein Q7KZF4 original sequence version: 88 D58BF200F3F3D628 piwl1_human Piwi-like protein 1 PIWIL1 HIWI protein protein human Homo sapiens Human MTGRARARARGRARGQETAQLVGSTASQQPGYIQPRPQPPPAEGELFGRGRQRGTAGGTAKSQGLQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVRLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGKCHAFDGTILFLPKRLQQKVTEVFSKTRNGEDVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPNDPIDIPSHRLVIWPGFTTSILQYENSIMLCTDVSHKVLRSETVLDFMFNFYHQTEEHKFQEQVSKELIGLVVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKNDNVQRELRDWGLSFDSNLLSFSGRILQTEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGMQMRKAIMIEVDDRTEAYLRVLQQKVTADTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDIPLKLVMIVGIDCYHDMTAGRRSIAGFVASINEGMTRWFSRCIFQDRGQELVDGLKVCLQAALRAWNSCNEYMPSRIIVYRDGVGDGQLKTLVNYEVPQFLDCLKSIGRGYNPRLTVIVVKKRVNTRFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDNSGLKPDHIQRLTYKLCHIYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL DIP protein Q96J94 original sequence version: 70 58D7F6C7321DEFA4 snd1-piwil1-1 2 9 unspecified role unspecified role prey prey mouse Mus musculus Mouse 10 unspecified role unspecified role bait bait mouse Mus musculus Mouse physical association physical association piwil1-snd1-1 3 15 unspecified role unspecified role unspecified role unspecified role Region 10-17 Region 10-17 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction piwil1-snd1-2 6 15 unspecified role unspecified role unspecified role unspecified role Region 2-9 Region 2-9 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h3-snd1-1 7 11 unspecified role unspecified role unspecified role unspecified role R2me2 R2me2 nnme2arg dimethylated L-arginine Dimethyl NNMe2Arg dimethylr certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction piwil1-snd1-3 8 15 unspecified role unspecified role unspecified role unspecified role Region 2-17 Region 2-17 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q7KZF4:p.Asn768Arg N768R mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N R This feature has been corrected as a result of our quality control procedures. The original label was 'N768R'. Wed May 02 19:19:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn768arg' Tue Jun 30 17:23:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn768Arg' Q7KZF4:p.Asn768Gln N768Q mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N Q This feature has been corrected as a result of our quality control procedures. The original label was 'N768Q'. Wed May 02 17:12:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn768gln' Tue Jun 30 16:22:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn768Gln' Q7KZF4:p.Phe740Leu F740L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F L This feature has been corrected as a result of our quality control procedures. The original label was 'F740L'. Wed May 02 20:23:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe740leu' Tue Jun 30 16:12:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe740Leu' Q7KZF4:p.Tyr746Leu F746L mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y L Wed May 02 16:42:40 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr746leu' Tue Jun 30 17:31:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr746Leu' Q7KZF4:p.Tyr763Leu F763L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y L Wed May 02 17:08:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr763leu' Tue Jun 30 15:59:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr763Leu' Q7KZF4:p.Tyr766Leu F766L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y L Wed May 02 15:38:26 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr766leu' Tue Jun 30 19:52:23 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr766Leu' region Δ650-699 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain This feature has been corrected as a result of our quality control procedures. The original label was 'Δ650-699'. ecolx Escherichia coli direct interaction direct interaction Deletion of region 801-910 decreased the interaction rate/strength. piwil1-tdrkh-1 4 15 unspecified role unspecified role unspecified role unspecified role Region 2-17 Region 2-17 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 13 unspecified role unspecified role unspecified role unspecified role Region 290-530 Region 290-530 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction piwil1-snd1-4 1 15 unspecified role unspecified role unspecified role unspecified role Region 2-17 Region 2-17 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction h4-snd1-1 5 12 unspecified role unspecified role unspecified role unspecified role R3me2 R3me2 nnme2arg dimethylated L-arginine Dimethyl NNMe2Arg dimethylr certain certain sequence position certain certain certain sequence position certain in vitro In vitro 14 unspecified role unspecified role unspecified role unspecified role Tudor domain Region 650-910 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction