Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycylpeptide N-tetradecanoyltransferase 1

Gene

NMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins.3 Publications

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.97. 2681.
ReactomeiR-HSA-162599. Late Phase of HIV Life Cycle.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-75108. Activation, myristolyation of BID and translocation to mitochondria.

Chemistry

SwissLipidsiSLP:000001287.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferase 1 (EC:2.3.1.973 Publications)
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase 1
Short name:
NMT 1
Short name:
Type I N-myristoyltransferase
Peptide N-myristoyltransferase 1
Gene namesi
Name:NMT1
Synonyms:NMT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7857. NMT1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cell junction Source: HPA
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extrinsic component of membrane Source: UniProtKB
  • mitochondrion Source: GOC
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi492 – 4921G → D or K: Reduced activity. 1 Publication

Organism-specific databases

PharmGKBiPA31661.

Chemistry

ChEMBLiCHEMBL2096973.

Polymorphism and mutation databases

BioMutaiNMT1.
DMDMi12231020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Glycylpeptide N-tetradecanoyltransferase 1PRO_0000064221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei83 – 831PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP30419.
MaxQBiP30419.
PaxDbiP30419.
PeptideAtlasiP30419.
PRIDEiP30419.
TopDownProteomicsiP30419-2. [P30419-2]

PTM databases

iPTMnetiP30419.
PhosphoSiteiP30419.
SwissPalmiP30419.

Expressioni

Tissue specificityi

Heart, gut, kidney, liver and placenta.

Gene expression databases

BgeeiP30419.
CleanExiHS_NMT1.
ExpressionAtlasiP30419. baseline and differential.
GenevisibleiP30419. HS.

Organism-specific databases

HPAiHPA022949.
HPA022963.

Interactioni

Protein-protein interaction databases

BioGridi110899. 81 interactions.
IntActiP30419. 19 interactions.
MINTiMINT-5004170.
STRINGi9606.ENSP00000258960.

Chemistry

BindingDBiP30419.

Structurei

Secondary structure

1
496
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi120 – 1223Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi156 – 1605Combined sources
Helixi166 – 17914Combined sources
Beta strandi188 – 1903Combined sources
Helixi194 – 2018Combined sources
Helixi208 – 2103Combined sources
Beta strandi211 – 2166Combined sources
Turni217 – 2193Combined sources
Beta strandi222 – 23514Combined sources
Beta strandi238 – 25013Combined sources
Helixi252 – 2543Combined sources
Helixi259 – 27214Combined sources
Turni273 – 2753Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi291 – 30212Combined sources
Helixi303 – 3086Combined sources
Helixi320 – 3278Combined sources
Beta strandi338 – 3403Combined sources
Helixi343 – 3453Combined sources
Helixi346 – 35611Combined sources
Helixi357 – 3593Combined sources
Beta strandi360 – 3656Combined sources
Helixi368 – 3758Combined sources
Turni379 – 3813Combined sources
Beta strandi382 – 3887Combined sources
Beta strandi390 – 3923Combined sources
Beta strandi394 – 4029Combined sources
Beta strandi405 – 4073Combined sources
Beta strandi418 – 4214Combined sources
Beta strandi427 – 4293Combined sources
Helixi431 – 44414Combined sources
Beta strandi448 – 4547Combined sources
Helixi458 – 4603Combined sources
Turni461 – 4666Combined sources
Beta strandi468 – 48013Combined sources
Helixi488 – 4903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RXTX-ray3.00A/B/C/D1-496[»]
3IU1X-ray1.42A/B115-496[»]
3IU2X-ray1.73A/B115-496[»]
3IWEX-ray1.79A/B115-496[»]
3JTKX-ray1.61A/B115-496[»]
4C2YX-ray1.64A/B109-496[»]
4C2ZX-ray2.08A/B109-496[»]
ProteinModelPortaliP30419.
SMRiP30419. Positions 115-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30419.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 1203Myristoyl-CoA binding2 Publications
Regioni248 – 2503Myristoyl-CoA binding2 Publications
Regioni256 – 2605Myristoyl-CoA binding2 Publications

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 6713Poly-LysAdd
BLAST

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiP30419.
KOiK00671.
OMAiTIMNHPV.
OrthoDBiEOG76DTS3.
PhylomeDBiP30419.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P30419-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADESETAVK PPAPPLPQMM EGNGNGHEHC SDCENEEDNS YNRGGLSPAN
60 70 80 90 100
DTGAKKKKKK QKKKKEKGSE TDSAQDQPVK MNSLPAERIQ EIQKAIELFS
110 120 130 140 150
VGQGPAKTME EASKRSYQFW DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY
160 170 180 190 200
TLPQGFTWDA LDLGDRGVLK ELYTLLNENY VEDDDNMFRF DYSPEFLLWA
210 220 230 240 250
LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK KMVEINFLCV
260 270 280 290 300
HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS
310 320 330 340 350
LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP METKDIPVVH
360 370 380 390 400
QLLTRYLKQF HLTPVMSQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF
410 420 430 440 450
YTLPSTIMNH PTHKSLKAAY SFYNVHTQTP LLDLMSDALV LAKMKGFDVF
460 470 480 490
NALDLMENKT FLEKLKFGIG DGNLQYYLYN WKCPSMGAEK VGLVLQ
Length:496
Mass (Da):56,806
Last modified:January 11, 2001 - v2
Checksum:i7661140D3837BE7A
GO
Isoform Short (identifier: P30419-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.

Show »
Length:416
Mass (Da):48,141
Checksum:iCF08D233B6DD9383
GO

Sequence cautioni

The sequence AAC09294.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611Q → K.
Corresponds to variant rs3087878 [ dbSNP | Ensembl ].
VAR_050286

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8080Missing in isoform Short. 1 PublicationVSP_003570Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043324 mRNA. Translation: AAC09294.1. Different initiation.
AF020500 mRNA. Translation: AAB95316.1.
AK291936 mRNA. Translation: BAF84625.1.
CH471178 Genomic DNA. Translation: EAW51554.1.
BC006538 mRNA. Translation: AAH06538.1.
BC006569 mRNA. Translation: AAH06569.1.
BC007258 mRNA. Translation: AAH07258.2.
BC008312 mRNA. Translation: AAH08312.2.
M86707 mRNA. No translation available.
Y17208 mRNA. Translation: CAA76685.1.
Y17209 mRNA. Translation: CAA76686.1.
CCDSiCCDS11494.1. [P30419-1]
PIRiJC1343.
RefSeqiNP_066565.1. NM_021079.4. [P30419-1]
UniGeneiHs.532790.

Genome annotation databases

EnsembliENST00000258960; ENSP00000258960; ENSG00000136448. [P30419-1]
ENST00000592782; ENSP00000468424; ENSG00000136448. [P30419-1]
GeneIDi4836.
KEGGihsa:4836.
UCSCiuc002ihz.4. human. [P30419-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043324 mRNA. Translation: AAC09294.1. Different initiation.
AF020500 mRNA. Translation: AAB95316.1.
AK291936 mRNA. Translation: BAF84625.1.
CH471178 Genomic DNA. Translation: EAW51554.1.
BC006538 mRNA. Translation: AAH06538.1.
BC006569 mRNA. Translation: AAH06569.1.
BC007258 mRNA. Translation: AAH07258.2.
BC008312 mRNA. Translation: AAH08312.2.
M86707 mRNA. No translation available.
Y17208 mRNA. Translation: CAA76685.1.
Y17209 mRNA. Translation: CAA76686.1.
CCDSiCCDS11494.1. [P30419-1]
PIRiJC1343.
RefSeqiNP_066565.1. NM_021079.4. [P30419-1]
UniGeneiHs.532790.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RXTX-ray3.00A/B/C/D1-496[»]
3IU1X-ray1.42A/B115-496[»]
3IU2X-ray1.73A/B115-496[»]
3IWEX-ray1.79A/B115-496[»]
3JTKX-ray1.61A/B115-496[»]
4C2YX-ray1.64A/B109-496[»]
4C2ZX-ray2.08A/B109-496[»]
ProteinModelPortaliP30419.
SMRiP30419. Positions 115-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110899. 81 interactions.
IntActiP30419. 19 interactions.
MINTiMINT-5004170.
STRINGi9606.ENSP00000258960.

Chemistry

BindingDBiP30419.
ChEMBLiCHEMBL2096973.
SwissLipidsiSLP:000001287.

PTM databases

iPTMnetiP30419.
PhosphoSiteiP30419.
SwissPalmiP30419.

Polymorphism and mutation databases

BioMutaiNMT1.
DMDMi12231020.

Proteomic databases

EPDiP30419.
MaxQBiP30419.
PaxDbiP30419.
PeptideAtlasiP30419.
PRIDEiP30419.
TopDownProteomicsiP30419-2. [P30419-2]

Protocols and materials databases

DNASUi4836.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258960; ENSP00000258960; ENSG00000136448. [P30419-1]
ENST00000592782; ENSP00000468424; ENSG00000136448. [P30419-1]
GeneIDi4836.
KEGGihsa:4836.
UCSCiuc002ihz.4. human. [P30419-1]

Organism-specific databases

CTDi4836.
GeneCardsiNMT1.
HGNCiHGNC:7857. NMT1.
HPAiHPA022949.
HPA022963.
MIMi160993. gene.
neXtProtiNX_P30419.
PharmGKBiPA31661.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2779. Eukaryota.
COG5092. LUCA.
GeneTreeiENSGT00390000017837.
HOGENOMiHOG000189123.
HOVERGENiHBG003404.
InParanoidiP30419.
KOiK00671.
OMAiTIMNHPV.
OrthoDBiEOG76DTS3.
PhylomeDBiP30419.

Enzyme and pathway databases

BRENDAi2.3.1.97. 2681.
ReactomeiR-HSA-162599. Late Phase of HIV Life Cycle.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
R-HSA-75108. Activation, myristolyation of BID and translocation to mitochondria.

Miscellaneous databases

ChiTaRSiNMT1. human.
EvolutionaryTraceiP30419.
GeneWikiiN-myristoyltransferase_1.
GenomeRNAii4836.
PROiP30419.
SOURCEiSearch...

Gene expression databases

BgeeiP30419.
CleanExiHS_NMT1.
ExpressionAtlasiP30419. baseline and differential.
GenevisibleiP30419. HS.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction."
    Glover C.J., Hartman K.D., Felsted R.L.
    J. Biol. Chem. 272:28680-28689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  2. "A second mammalian N-myristoyltransferase."
    Giang D.K., Cravatt B.F.
    J. Biol. Chem. 273:6595-6598(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
    Tissue: Brain.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT).
    Tissue: Muscle and Skin.
  6. "Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae."
    Duronio R.J., Reed S.I., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 89:4129-4133(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 58-496, MUTAGENESIS OF GLY-492.
  7. "Characterization of human and rat brain myristoyl-CoA:protein N-myristoyltransferase: evidence for an alternative splice variant of the enzyme."
    Mcilhinney R.A.J., Young K., Egerton M., Camble R., White A., Soloviev M.
    Biochem. J. 333:491-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 81-89.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Crystal structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055."
    Structural genomics consortium (SGC)
    Submitted (SEP-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 115-496 IN COMPLEX WITH MYRISTOYL-COA.
  17. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 109-496 IN COMPLEX WITH MYRISTOYL-COA, CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiNMT1_HUMAN
AccessioniPrimary (citable) accession number: P30419
Secondary accession number(s): A8K7C1, Q9UE09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 11, 2001
Last modified: July 6, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.