Q8N183 · NDUF2_HUMAN

  • Protein
    NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2
  • Gene
    NDUFAF2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a molecular chaperone for mitochondrial complex I assembly (PubMed:16200211, PubMed:19384974).
Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:16200211, PubMed:27626371).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrion
Molecular Functionprotein-containing complex binding
Biological Processmitochondrial respiratory chain complex I assembly
Biological Processnegative regulation of insulin secretion involved in cellular response to glucose stimulus

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2
  • Alternative names
    • B17.2-like (B17.2L)
    • Mimitin
    • Myc-induced mitochondrial protein
      (MMTN
      )
    • NDUFA12-like protein

Gene names

    • Name
      NDUFAF2
    • Synonyms
      NDUFA12L

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8N183
  • Secondary accessions
    • A8K5I1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Involvement in disease

Mitochondrial complex I deficiency, nuclear type 10 (MC1DN10)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of mitochondrial complex I deficiency, the most common biochemical signature of mitochondrial disorders, a group of highly heterogeneous conditions characterized by defective oxidative phosphorylation, which collectively affects 1 in 5-10000 live births. Clinical disorders have variable severity, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease. MC1DN10 transmission pattern is consistent with autosomal recessive inheritance.
  • See also
    MIM:618233
Natural variants in MC1DN10
Variant IDPosition(s)ChangeDescription
VAR_0814223-169missingin MC1DN10
VAR_08142338-169missingin MC1DN10; patient cells homozygous for the variant do not express detectable amounts of protein; complex I assembly is altered and activity is severely reduced in patient cells compared to control
VAR_08142447-169missingin MC1DN10

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_0814223-169in MC1DN10
Natural variantVAR_08142338-169in MC1DN10; patient cells homozygous for the variant do not express detectable amounts of protein; complex I assembly is altered and activity is severely reduced in patient cells compared to control
Natural variantVAR_08142447-169in MC1DN10

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 221 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, transit peptide, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_0000020054?-169UniProtNADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2
Transit peptide1-?UniProtMitochondrion
Modified residue (large scale data)116PRIDEPhosphothreonine
Modified residue134UniProtPhosphoserine
Modified residue (large scale data)134PRIDEPhosphoserine
Modified residue (large scale data)137PRIDEPhosphotyrosine
Modified residue (large scale data)149PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in ESCC cells. Also expressed in heart, skeletal muscle, liver, and in fibroblasts.

Induction

By MYC. Direct transcriptional target of MYC.

Gene expression databases

Organism-specific databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region116-169Disordered
Compositional bias146-169Polar residues

Sequence similarities

Belongs to the complex I NDUFA12 subunit family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    169
  • Mass (Da)
    19,856
  • Last updated
    2002-10-01 v1
  • Checksum
    3D72AE8B5942E0FA
MGWSQDLFRALWRSLSREVKEHVGTDQFGNKYYYIPQYKNWRGQTIREKRIVEAANKKEVDYEAGDIPTEWEAWIRRTRKTPPTMEEILKNEKHREEIKIKSQDFYEKEKLLSKETSEELLPPPVQTQIKGHASAPYFGKEEPSVAPSSTGKTFQPGSWMPRDGKSHNQ

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D6RA56D6RA56_HUMANNDUFAF260
H0YA50H0YA50_HUMANNDUFAF251
A0A7I2YQX2A0A7I2YQX2_HUMANNDUFAF2177
A0A7I2V3X5A0A7I2V3X5_HUMANNDUFAF267
A0A7I2V4Z7A0A7I2V4Z7_HUMANNDUFAF271

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias146-169Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB183433
EMBL· GenBank· DDBJ
BAD91205.1
EMBL· GenBank· DDBJ
mRNA
AK291296
EMBL· GenBank· DDBJ
BAF83985.1
EMBL· GenBank· DDBJ
mRNA
CH471123
EMBL· GenBank· DDBJ
EAW55008.1
EMBL· GenBank· DDBJ
Genomic DNA
BC001753
EMBL· GenBank· DDBJ
AAH01753.2
EMBL· GenBank· DDBJ
mRNA
BC033965
EMBL· GenBank· DDBJ
AAH33965.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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