ID B0YJ53_HUMAN Unreviewed; 264 AA. AC B0YJ53; A0A024R3J0; Q6FH49; DT 28-JUN-2023, integrated into UniProtKB/TrEMBL. DT 28-JUN-2023, sequence version 1. DT 13-SEP-2023, entry version 2. DE SubName: Full=NNMT protein {ECO:0000313|EMBL:CAG46705.1}; DE SubName: Full=Nicotinamide N-methyltransferase {ECO:0000313|EMBL:ACA06031.1}; DE SubName: Full=Nicotinamide N-methyltransferase, isoform CRA_a {ECO:0000313|EMBL:EAW67243.1}; GN Name=NNMT {ECO:0000313|EMBL:ACA06031.1}; GN ORFNames=hCG_39357 {ECO:0000313|EMBL:EAW67243.1}; 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 {ECO:0000313|EMBL:ACA06031.1}; RN [1] {ECO:0000313|EMBL:EAW67243.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|EMBL:CAG46705.1} RP NUCLEOTIDE SEQUENCE. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:EAW67243.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:EAW67244.1} RP NUCLEOTIDE SEQUENCE. RA Tsai W.S., Green S.K., Behjatnia S.A.A., Rezaian A., Iram S., Mansoor; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ACA06031.1} RP NUCLEOTIDE SEQUENCE. RA Chin K.-J., Sharma M.L., Russell L.A., O'Neill K.R., Lovley D.R.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0007829|PDB:7SOK} RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS). RA Iyamu I., Vilseck J.Z., Yadav R., Noinaj N., Huang R.; RT "Structure of Nicotinamide N-Methyltransferase (NNMT) in complex with RT inhibitor II329."; RL Submitted (OCT-2021) to the PDB data bank. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000256|ARBA:ARBA00007996}. 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; EF445002; ACA06031.1; -; Genomic_DNA. DR EMBL; CR541907; CAG46705.1; -; mRNA. DR EMBL; CH471065; EAW67243.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67244.1; -; Genomic_DNA. DR RefSeq; NP_006160.1; NM_006169.2. DR PDB; 7SOK; X-ray; 2.08 A; A/B/C/D=1-264. DR DNASU; 4837; -. DR GeneID; 4837; -. DR UCSC; uc001por.2; human. DR HOGENOM; CLU_082526_1_1_1; -. DR OMA; FRCHRLK; -. DR OrthoDB; 5297821at2759; -. DR BioGRID-ORCS; 4837; 7 hits in 1162 CRISPR screens. DR ChiTaRS; NNMT; human. DR GenomeRNAi; 4837; -. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR025820; NNMT/PNMT/TEMT_CS. DR InterPro; IPR000940; NNMT_TEMT_trans. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; NF041360; GntF_guanitoxin; 1. DR PANTHER; PTHR10867:SF32; NICOTINAMIDE N-METHYLTRANSFERASE; 1. DR PANTHER; PTHR10867; NNMT/PNMT/TEMT FAMILY MEMBER; 1. DR Pfam; PF01234; NNMT_PNMT_TEMT; 1. DR PIRSF; PIRSF000384; PNMTase; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS01100; NNMT_PNMT_TEMT; 1. DR PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7SOK}; KW Methyltransferase {ECO:0000313|EMBL:ACA06031.1}; KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR000384-1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACA06031.1}. FT BINDING 20 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 25 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 63..64 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 69 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 85 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" FT BINDING 142..143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|PIRSR:PIRSR000384-1" SQ SEQUENCE 264 AA; 29574 MW; 280B12748F4488AC CRC64; MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQ LLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNE GLFSLVARKL SRPL //