NMT1_HUMAN
ID NMT1_HUMAN Reviewed; 496 AA.
AC P30419; A8K7C1; Q9UE09;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1 {ECO:0000305};
DE EC=2.3.1.97 {ECO:0000269|PubMed:22865860, ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 1;
DE Short=HsNMT1 {ECO:0000303|PubMed:32111831};
DE Short=NMT 1;
DE Short=Type I N-myristoyltransferase;
DE AltName: Full=Peptide N-myristoyltransferase 1;
DE AltName: Full=Protein-lysine myristoyltransferase NMT1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831};
GN Name=NMT1 {ECO:0000303|PubMed:9506952, ECO:0000312|HGNC:HGNC:7857};
GN Synonyms=NMT {ECO:0000303|PubMed:9353336};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9353336; DOI=10.1074/jbc.272.45.28680;
RA Glover C.J., Hartman K.D., Felsted R.L.;
RT "Human N-myristoyltransferase amino-terminal domain involved in targeting
RT the enzyme to the ribosomal subcellular fraction.";
RL J. Biol. Chem. 272:28680-28689(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=9506952; DOI=10.1074/jbc.273.12.6595;
RA Giang D.K., Cravatt B.F.;
RT "A second mammalian N-myristoyltransferase.";
RL J. Biol. Chem. 273:6595-6598(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Muscle, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-496, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLY-492.
RX PubMed=1570339; DOI=10.1073/pnas.89.9.4129;
RA Duronio R.J., Reed S.I., Gordon J.I.;
RT "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause
RT temperature-sensitive myristic acid auxotrophy in Saccharomyces
RT cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4129-4133(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-89.
RX PubMed=9677304; DOI=10.1042/bj3330491;
RA Mcilhinney R.A.J., Young K., Egerton M., Camble R., White A., Soloviev M.;
RT "Characterization of human and rat brain myristoyl-CoA:protein N-
RT myristoyltransferase: evidence for an alternative splice variant of the
RT enzyme.";
RL Biochem. J. 333:491-495(1998).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP 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 CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=22865860; DOI=10.1074/jbc.m112.393231;
RA Montgomery C., Pei Z., Watkins P.A., Miziorko H.M.;
RT "Identification and characterization of an extramitochondrial human 3-
RT Hydroxy-3-methylglutaryl-CoA lyase.";
RL J. Biol. Chem. 287:33227-33236(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [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-47 AND SER-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 115-496 IN COMPLEX WITH
RP TETRADECANOYL-COA.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human type-I N-myristoyltransferase with bound
RT myristoyl-CoA and inhibitor DDD90055.";
RL Submitted (SEP-2009) to the PDB data bank.
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 109-496 IN COMPLEX WITH
RP TETRADECANOYL-COA, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [19] {ECO:0007744|PDB:6PAV}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 109-496 IN COMPLEX WITH
RP TETRADECANOYL-COA, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32103017; DOI=10.1038/s41467-020-14893-x;
RA Kosciuk T., Price I.R., Zhang X., Zhu C., Johnson K.N., Zhang S.,
RA Halaby S.L., Komaniecki G.P., Yang M., DeHart C.J., Thomas P.M.,
RA Kelleher N.L., Fromme J.C., Lin H.;
RT "NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase
RT cycle.";
RL Nat. Commun. 11:1067-1067(2020).
RN [20] {ECO:0007744|PDB:6EHJ, ECO:0007744|PDB:6QRM, ECO:0007744|PDB:6SJZ, ECO:0007744|PDB:6SK2, ECO:0007744|PDB:6SK3, ECO:0007744|PDB:6SK8, ECO:0007744|PDB:6SKJ}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 99-493 IN COMPLEX WITH
RP TETRADECANOYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF TYR-180; VAL-181 AND TYR-192.
RX PubMed=32111831; DOI=10.1038/s41467-020-14847-3;
RA Dian C., Perez-Dorado I., Riviere F., Asensio T., Legrand P., Ritzefeld M.,
RA Shen M., Cota E., Meinnel T., Tate E.W., Giglione C.;
RT "High-resolution snapshots of human N-myristoyltransferase in action
RT illuminate a mechanism promoting N-terminal Lys and Gly myristoylation.";
RL Nat. Commun. 11:1132-1132(2020).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular and viral proteins (PubMed:22865860, PubMed:25255805,
CC PubMed:9353336, PubMed:9506952). Also able to mediate N-terminal lysine
CC myristoylation of proteins: catalyzes myristoylation of ARF6 on both
CC 'Gly-2' and 'Lys-3' (PubMed:32103017, PubMed:32111831). Lysine
CC myristoylation is required to maintain ARF6 on membranes during the
CC GTPase cycle (PubMed:32103017). {ECO:0000269|PubMed:22865860,
CC ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:32111831, ECO:0000269|PubMed:9353336,
CC ECO:0000269|PubMed:9506952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC Evidence={ECO:0000269|PubMed:22865860, ECO:0000269|PubMed:25255805,
CC ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
CC ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-L-lysyl-[protein] + tetradecanoyl-CoA = CoA
CC + H(+) + N-terminal glycyl-(N(6)-tetradecanoyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:70671, Rhea:RHEA-COMP:17947, Rhea:RHEA-COMP:17948,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:189855, ChEBI:CHEBI:189856;
CC Evidence={ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672;
CC Evidence={ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:32111831};
CC Note=kcat is 0.41 sec(-1) with tetradecanoyl-CoA as substrate.
CC {ECO:0000269|PubMed:32111831};
CC -!- INTERACTION:
CC P30419; Q9BR61: ACBD6; NbExp=5; IntAct=EBI-5280164, EBI-2848793;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9353336,
CC ECO:0000269|PubMed:9506952}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:9353336}. Membrane {ECO:0000269|PubMed:9506952};
CC Peripheral membrane protein {ECO:0000269|PubMed:9506952}.
CC Note=Copurifies with ribosomes. {ECO:0000269|PubMed:9353336}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P30419-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P30419-2; Sequence=VSP_003570;
CC -!- TISSUE SPECIFICITY: Heart, gut, kidney, liver and placenta.
CC {ECO:0000269|PubMed:1570339}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NMT1ID43604ch17q21.html";
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; AF043324; AAC09294.1; ALT_INIT; mRNA.
DR EMBL; AF020500; AAB95316.1; -; mRNA.
DR EMBL; AK291936; BAF84625.1; -; mRNA.
DR EMBL; CH471178; EAW51554.1; -; Genomic_DNA.
DR EMBL; BC006538; AAH06538.1; -; mRNA.
DR EMBL; BC006569; AAH06569.1; -; mRNA.
DR EMBL; BC007258; AAH07258.2; -; mRNA.
DR EMBL; BC008312; AAH08312.2; -; mRNA.
DR EMBL; M86707; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; Y17208; CAA76685.1; -; mRNA.
DR EMBL; Y17209; CAA76686.1; -; mRNA.
DR CCDS; CCDS11494.1; -. [P30419-1]
DR PIR; JC1343; JC1343.
DR RefSeq; NP_066565.1; NM_021079.4. [P30419-1]
DR PDB; 1RXT; X-ray; 3.00 A; A/B/C/D=1-496.
DR PDB; 3IU1; X-ray; 1.42 A; A/B=115-496.
DR PDB; 3IU2; X-ray; 1.73 A; A/B=115-496.
DR PDB; 3IWE; X-ray; 1.79 A; A/B=115-496.
DR PDB; 3JTK; X-ray; 1.61 A; A/B=115-496.
DR PDB; 4C2Y; X-ray; 1.64 A; A/B=109-496.
DR PDB; 4C2Z; X-ray; 2.08 A; A/B=109-496.
DR PDB; 5MU6; X-ray; 1.88 A; A/B=109-496.
DR PDB; 5NPQ; X-ray; 2.37 A; A/B=109-496.
DR PDB; 5O6H; X-ray; 1.29 A; A/B=109-496.
DR PDB; 5O6J; X-ray; 1.45 A; A/B=109-496.
DR PDB; 5O9S; X-ray; 2.70 A; A/B=99-496.
DR PDB; 5O9T; X-ray; 2.15 A; A/B=99-496.
DR PDB; 5O9U; X-ray; 1.85 A; A/B=99-496.
DR PDB; 5O9V; X-ray; 2.20 A; A/B=99-496.
DR PDB; 5UUT; X-ray; 2.25 A; A/B=109-496.
DR PDB; 6EHJ; X-ray; 2.10 A; A/B=109-496.
DR PDB; 6F56; X-ray; 1.94 A; A/B/C/D=109-496.
DR PDB; 6FZ2; X-ray; 2.05 A; A/B=115-496.
DR PDB; 6FZ3; X-ray; 2.00 A; A/B=115-496.
DR PDB; 6FZ5; X-ray; 1.89 A; A/B=115-496.
DR PDB; 6PAV; X-ray; 2.52 A; A/B=109-496.
DR PDB; 6QRM; X-ray; 2.30 A; A/B=99-496.
DR PDB; 6SJZ; X-ray; 2.00 A; A/B=99-496.
DR PDB; 6SK2; X-ray; 1.90 A; A/B=99-496.
DR PDB; 6SK3; X-ray; 2.70 A; A/B=99-493.
DR PDB; 6SK8; X-ray; 1.87 A; A/B=99-493.
DR PDB; 6SKJ; X-ray; 2.80 A; A/B=99-494.
DR PDBsum; 1RXT; -.
DR PDBsum; 3IU1; -.
DR PDBsum; 3IU2; -.
DR PDBsum; 3IWE; -.
DR PDBsum; 3JTK; -.
DR PDBsum; 4C2Y; -.
DR PDBsum; 4C2Z; -.
DR PDBsum; 5MU6; -.
DR PDBsum; 5NPQ; -.
DR PDBsum; 5O6H; -.
DR PDBsum; 5O6J; -.
DR PDBsum; 5O9S; -.
DR PDBsum; 5O9T; -.
DR PDBsum; 5O9U; -.
DR PDBsum; 5O9V; -.
DR PDBsum; 5UUT; -.
DR PDBsum; 6EHJ; -.
DR PDBsum; 6F56; -.
DR PDBsum; 6FZ2; -.
DR PDBsum; 6FZ3; -.
DR PDBsum; 6FZ5; -.
DR PDBsum; 6PAV; -.
DR PDBsum; 6QRM; -.
DR PDBsum; 6SJZ; -.
DR PDBsum; 6SK2; -.
DR PDBsum; 6SK3; -.
DR PDBsum; 6SK8; -.
DR PDBsum; 6SKJ; -.
DR AlphaFoldDB; P30419; -.
DR SMR; P30419; -.
DR BioGRID; 110899; 131.
DR IntAct; P30419; 44.
DR MINT; P30419; -.
DR STRING; 9606.ENSP00000468424; -.
DR BindingDB; P30419; -.
DR ChEMBL; CHEMBL2593; -.
DR DrugBank; DB03062; (1-Methyl-1h-Imidazol-2-Yl)-(3-Methyl-4-{3-[(Pyridin-3-Ylmethyl)-Amino]-Propoxy}-Benzofuran-2-Yl)-Methanone.
DR SwissLipids; SLP:000001287; -.
DR GlyGen; P30419; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30419; -.
DR MetOSite; P30419; -.
DR PhosphoSitePlus; P30419; -.
DR SwissPalm; P30419; -.
DR BioMuta; NMT1; -.
DR DMDM; 12231020; -.
DR EPD; P30419; -.
DR jPOST; P30419; -.
DR MassIVE; P30419; -.
DR MaxQB; P30419; -.
DR PaxDb; P30419; -.
DR PeptideAtlas; P30419; -.
DR PRIDE; P30419; -.
DR ProteomicsDB; 54667; -. [P30419-1]
DR ProteomicsDB; 54668; -. [P30419-2]
DR TopDownProteomics; P30419-2; -. [P30419-2]
DR Antibodypedia; 17578; 204 antibodies from 25 providers.
DR DNASU; 4836; -.
DR Ensembl; ENST00000258960.7; ENSP00000258960.2; ENSG00000136448.13. [P30419-1]
DR Ensembl; ENST00000592654.3; ENSP00000466827.2; ENSG00000136448.13. [P30419-2]
DR Ensembl; ENST00000592782.5; ENSP00000468424.1; ENSG00000136448.13. [P30419-1]
DR Ensembl; ENST00000676828.1; ENSP00000504192.1; ENSG00000136448.13. [P30419-1]
DR Ensembl; ENST00000678938.1; ENSP00000503621.1; ENSG00000136448.13. [P30419-2]
DR GeneID; 4836; -.
DR KEGG; hsa:4836; -.
DR MANE-Select; ENST00000258960.7; ENSP00000258960.2; NM_021079.5; NP_066565.1.
DR UCSC; uc002ihz.4; human. [P30419-1]
DR CTD; 4836; -.
DR DisGeNET; 4836; -.
DR GeneCards; NMT1; -.
DR HGNC; HGNC:7857; NMT1.
DR HPA; ENSG00000136448; Low tissue specificity.
DR MIM; 160993; gene.
DR neXtProt; NX_P30419; -.
DR OpenTargets; ENSG00000136448; -.
DR PharmGKB; PA31661; -.
DR VEuPathDB; HostDB:ENSG00000136448; -.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; P30419; -.
DR OMA; EHDVEHW; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; P30419; -.
DR BRENDA; 2.3.1.97; 2681.
DR PathwayCommons; P30419; -.
DR Reactome; R-HSA-162599; Late Phase of HIV Life Cycle.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-75108; Activation, myristolyation of BID and translocation to mitochondria.
DR SignaLink; P30419; -.
DR SIGNOR; P30419; -.
DR BioGRID-ORCS; 4836; 464 hits in 1082 CRISPR screens.
DR ChiTaRS; NMT1; human.
DR EvolutionaryTrace; P30419; -.
DR GeneWiki; N-myristoyltransferase_1; -.
DR GenomeRNAi; 4836; -.
DR Pharos; P30419; Tchem.
DR PRO; PR:P30419; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P30419; protein.
DR Bgee; ENSG00000136448; Expressed in monocyte and 207 other tissues.
DR ExpressionAtlas; P30419; baseline and differential.
DR Genevisible; P30419; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019107; F:myristoyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042180; P:cellular ketone metabolic process; IDA:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IDA:UniProtKB.
DR GO; GO:0006499; P:N-terminal protein myristoylation; TAS:Reactome.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000903; NMT.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR PANTHER; PTHR11377; PTHR11377; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR PIRSF; PIRSF015892; N-myristl_transf; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..496
FT /note="Glycylpeptide N-tetradecanoyltransferase 1"
FT /id="PRO_0000064221"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32111831, ECO:0000269|Ref.17"
FT BINDING 119
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
FT ECO:0000269|Ref.17"
FT BINDING 120
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
FT ECO:0000269|Ref.17"
FT BINDING 247
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:32103017"
FT BINDING 248
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
FT ECO:0000269|Ref.17"
FT BINDING 249
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805, ECO:0000269|Ref.17"
FT BINDING 250
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
FT ECO:0000269|Ref.17"
FT BINDING 256
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:32111831,
FT ECO:0000269|Ref.17"
FT BINDING 258
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32111831, ECO:0000269|Ref.17"
FT BINDING 259
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32111831, ECO:0000269|Ref.17"
FT BINDING 260
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:32111831, ECO:0000269|Ref.17"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70310"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003570"
FT VARIANT 61
FT /note="Q -> K (in dbSNP:rs3087878)"
FT /id="VAR_050286"
FT MUTAGEN 180
FT /note="Y->P: Abolished glycine- and lysine-
FT myristoyltransferase activites."
FT /evidence="ECO:0000269|PubMed:32111831"
FT MUTAGEN 181
FT /note="V->L: Reduced glycine N-myristoyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32111831"
FT MUTAGEN 192
FT /note="Y->A: Reduced glycine N-myristoyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:32111831"
FT MUTAGEN 492
FT /note="G->D,K: Reduced activity."
FT /evidence="ECO:0000269|PubMed:1570339"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5O9V"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:5O9U"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6SK2"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:5O6H"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 222..235
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 238..250
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5O9S"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:5O6H"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 291..302
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:5O6H"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1RXT"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:5O6H"
FT TURN 461..466
FT /evidence="ECO:0007829|PDB:5O6H"
FT STRAND 468..480
FT /evidence="ECO:0007829|PDB:5O6H"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:5O6H"
SQ SEQUENCE 496 AA; 56806 MW; 7661140D3837BE7A CRC64;
MADESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN DTGAKKKKKK
QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW
DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY
VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK
KMVEINFLCV HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP METKDIPVVH QLLTRYLKQF
HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY
SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN
WKCPSMGAEK VGLVLQ
