Protein detail

NMT2

Glycylpeptide N-tetradecanoyltransferase 2 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 2) (NMT 2) (Peptide N-myristoyltransferase 2) (Protein-lysine myristoyltransferase NMT2) (EC 2.3.1.-) (Type II N-myristoyltransferase)

Entry name
NMT2
UniProt ID
EVMP confidence score
0.38
Supporting publications (n)
1
Transmembrane count
Protein classification
EnzymesMetabolic proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information10
Protein Names
Glycylpeptide N-tetradecanoyltransferase 2 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 2) (NMT 2) (Peptide N-myristoyltransferase 2) (Protein-lysine myristoyltransferase NMT2) (EC 2.3.1.-) (Type II N-myristoyltransferase)
Protein Class (3)
EnzymesMetabolic proteinsPredicted intracellular proteins
Protein Function (3)
  • ENZYME proteins:Transferases
  • Enzymes
  • Predicted intracellular proteins
Entrez Gene Symbol
Gene Description
N-myristoyltransferase 2
Chromosome
10
Position
15102584-15168693
Supporting publications (n)
1
EVMP confidence score
0.38
Fluorescence & Localization4
NMT2 fluorescence
Cell SpecificEsophageal apical cellsBlood Cell Specificintermediate monocyteBlood Lineage Specificdendritic cells
Function & Pathway7
Relations & Evidence10

Ligand-Receptor Signaling (5)

5 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Protein Complex Composition (4)

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass Spectrometry138037300
Sequence, Structure & Domains11

Sequences

Length
498
Mass
56,980
Sequence
MAEDSESAASQQSLELDDQDTCGIDGDNEEETEHAKGSPGGYLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQPSKNPSVPMQKLQDIQRAMELLSACQGPARNIDEAAKHRYQFWDTQPVPKLDEVITSHGAIEPDKDNVRQEPYSLPQGFMWDTLDLSDAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKKMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPIATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIKSVRELINTYLKQFHLAPVMDEEEVAHWFLPREHIIDTFVVESPNGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMSDALILAKSKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ

3D Structural Models

Turn
219..221; 275..277; 381..383; 463..468
Helix
122..124; 168..181; 196..203; 210..212; 254..256; 261..274; 305..310; 322..328; 345..347; 348..358; 359..361; 370..377; 433..446; 460..462; 490..492
Beta Strand
125..127; 158..162; 188..192; 213..218; 224..237; 240..252; 281..287; 293..304; 318..320; 340..342; 362..366; 384..390; 392..394; 396..404; 407..409; 416..418; 420..423; 427..431; 450..456; 470..482
3D Structure
Electron microscopy (1); X-ray crystallography (2)

Domain & Motif Annotations

Compositional Bias
15..32; Acidic residues; 45..57; Basic residues; 61..86; Polar residues
Region
1..88; Disordered
Protein Families
NMT family
Sequence Similarities
Belongs to the NMT family.
Clinical Relevance4
Antibody
Interaction Protein (3)
ENSG00000101266ENSG00000204435ENSG00000230124
Interaction Count
3
Interaction Dataset (3)
biogrid_opencellintact_biogrid_opencellintact_biogrid
Supporting Publications1
PMIDTitleAbstract
30550287Label-Free Proteomic Analysis of Exosomes Secreted from THP-1-Derived Macrophages Treated with IFN-α Identifies Antiviral Proteins Enriched in Exosomes.No abstract available