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Protein

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

Gene

NDUFA9

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

Functioni

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. 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.2 Publications

Cofactori

FADNote: Binds 1 FAD per subunit.

GO - Molecular functioni

  • coenzyme binding Source: InterPro
  • NADH dehydrogenase (ubiquinone) activity Source: UniProtKB
  • NADH dehydrogenase activity Source: UniProtKB
  • protein complex binding Source: MGI

GO - Biological processi

  • mitochondrial electron transport, NADH to ubiquinone Source: Reactome
  • mitochondrial respiratory chain complex I assembly Source: UniProtKB
  • sodium ion transport Source: UniProtKB
  • ubiquinone-6 biosynthetic process Source: GO_Central

Keywordsi

Biological processElectron transport, Respiratory chain, Transport
LigandFAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-HSA-611105. Respiratory electron transport.
R-HSA-6799198. Complex I biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Alternative name(s):
Complex I-39kD
Short name:
CI-39kD
NADH-ubiquinone oxidoreductase 39 kDa subunit
Gene namesi
Name:NDUFA9
Synonyms:NDUFS2L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000139180.10.
HGNCiHGNC:7693. NDUFA9.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Leigh syndrome (LS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum and spinal cord. Clinical features depend on which areas of the central nervous system are involved and include subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, and dysphagia.
See also OMIM:256000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078936321R → P in LS. 1 PublicationCorresponds to variant dbSNP:rs199592341Ensembl.1

Keywords - Diseasei

Disease mutation, Leigh syndrome, Primary mitochondrial disease

Organism-specific databases

DisGeNETi4704.
MalaCardsiNDUFA9.
MIMi256000. phenotype.
OpenTargetsiENSG00000139180.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA31499.

Chemistry databases

ChEMBLiCHEMBL2363065.
DrugBankiDB00157. NADH.

Polymorphism and mutation databases

BioMutaiNDUFA9.
DMDMi2833280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 35MitochondrionBy similarityAdd BLAST35
ChainiPRO_000001999236 – 377NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrialAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei175N6-succinyllysineBy similarity1
Modified residuei189N6-acetyllysineBy similarity1
Modified residuei370N6-acetyllysineBy similarity1

Post-translational modificationi

Acetylated on lysine residues. BLOC1S1 is required for acetylation.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ16795.
MaxQBiQ16795.
PaxDbiQ16795.
PeptideAtlasiQ16795.
PRIDEiQ16795.
TopDownProteomicsiQ16795.

PTM databases

iPTMnetiQ16795.
PhosphoSitePlusiQ16795.
SwissPalmiQ16795.

Expressioni

Gene expression databases

BgeeiENSG00000139180.
CleanExiHS_NDUFA9.
ExpressionAtlasiQ16795. baseline and differential.
GenevisibleiQ16795. HS.

Organism-specific databases

HPAiHPA042268.
HPA073212.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction (PubMed:12611891, PubMed:27626371). Interacts with BLOC1S1 (PubMed:22309213). Interacts with SLC2A4 (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi110784. 95 interactors.
CORUMiQ16795.
DIPiDIP-38526N.
IntActiQ16795. 57 interactors.
MINTiMINT-3033599.
STRINGi9606.ENSP00000266544.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi43 – 51Combined sources9
Beta strandi55 – 57Combined sources3
Turni59 – 62Combined sources4
Helixi64 – 75Combined sources12
Beta strandi79 – 84Combined sources6
Helixi89 – 97Combined sources9
Helixi100 – 102Combined sources3
Beta strandi103 – 107Combined sources5
Helixi114 – 119Combined sources6
Turni120 – 122Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi137 – 139Combined sources3
Helixi141 – 144Combined sources4
Helixi147 – 159Combined sources13
Beta strandi162 – 167Combined sources6
Helixi179 – 194Combined sources16
Beta strandi199 – 201Combined sources3
Helixi212 – 223Combined sources12
Beta strandi225 – 229Combined sources5
Turni230 – 233Combined sources4
Helixi242 – 254Combined sources13
Helixi273 – 284Combined sources12
Beta strandi290 – 293Combined sources4
Helixi295 – 305Combined sources11
Helixi316 – 323Combined sources8
Helixi335 – 337Combined sources3
Helixi345 – 347Combined sources3
Helixi349 – 353Combined sources5
Turni354 – 356Combined sources3
Helixi359 – 362Combined sources4
Helixi367 – 369Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XTBelectron microscopy3.40J40-376[»]
5XTDelectron microscopy3.70J40-376[»]
5XTHelectron microscopy3.90J40-376[»]
5XTIelectron microscopy17.40BJ/J40-376[»]
ProteinModelPortaliQ16795.
SMRiQ16795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I NDUFA9 subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2865. Eukaryota.
COG0702. LUCA.
GeneTreeiENSGT00390000006865.
HOGENOMiHOG000168008.
HOVERGENiHBG006546.
InParanoidiQ16795.
KOiK03953.
OMAiKFIHVSH.
OrthoDBiEOG091G07EJ.
PhylomeDBiQ16795.
TreeFamiTF105961.

Family and domain databases

InterProiView protein in InterPro
IPR001509. Epimerase_deHydtase.
IPR036291. NAD(P)-bd_dom_sf.
PfamiView protein in Pfam
PF01370. Epimerase. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q16795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAQSRVV RVLSMSRSAI TAIATSVCHG PPCRQLHHAL MPHGKGGRSS
60 70 80 90 100
VSGIVATVFG ATGFLGRYVV NHLGRMGSQV IIPYRCDKYD IMHLRPMGDL
110 120 130 140 150
GQLLFLEWDA RDKDSIRRVV QHSNVVINLI GRDWETKNFD FEDVFVKIPQ
160 170 180 190 200
AIAQLSKEAG VEKFIHVSHL NANIKSSSRY LRNKAVGEKV VRDAFPEAII
210 220 230 240 250
VKPSDIFGRE DRFLNSFASM HRFGPIPLGS LGWKTVKQPV YVVDVSKGIV
260 270 280 290 300
NAVKDPDANG KSFAFVGPSR YLLFHLVKYI FAVAHRLFLP FPLPLFAYRW
310 320 330 340 350
VARVFEISPF EPWITRDKVE RMHITDMKLP HLPGLEDLGI QATPLELKAI
360 370
EVLRRHRTYR WLSAEIEDVK PAKTVNI
Length:377
Mass (Da):42,510
Last modified:November 1, 1997 - v2
Checksum:i66A1CC7FCE86DD0E
GO

Sequence cautioni

The sequence CAA54099 differs from that shown. Reason: Frameshift at position 18.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078936321R → P in LS. 1 PublicationCorresponds to variant dbSNP:rs199592341Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050641 mRNA. Translation: AAD42055.1.
BC009311 mRNA. Translation: AAH09311.1.
BC015837 mRNA. Translation: AAH15837.1.
BC111546 mRNA. Translation: AAI11547.1.
X76665 Genomic DNA. Translation: CAA54099.1. Frameshift.
L04490 mRNA. Translation: AAA36350.1.
CCDSiCCDS8532.1.
PIRiI37258.
RefSeqiNP_004993.1. NM_005002.4.
UniGeneiHs.75227.

Genome annotation databases

EnsembliENST00000266544; ENSP00000266544; ENSG00000139180.
GeneIDi4704.
KEGGihsa:4704.
UCSCiuc001qnc.4. human.

Similar proteinsi

Entry informationi

Entry nameiNDUA9_HUMAN
AccessioniPrimary (citable) accession number: Q16795
Secondary accession number(s): Q14076, Q2NKX0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 22, 2017
This is version 158 of the entry and version 2 of the sequence. See 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 12
    Human chromosome 12: 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