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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial

Gene

NDUFS8

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

Functioni

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for 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 (By similarity). May donate electrons to ubiquinone.By similarity

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).
NADH + acceptor = NAD+ + reduced acceptor.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi111Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi114Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi117Iron-sulfur 1 (4Fe-4S)By similarity1
Metal bindingi121Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi150Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi153Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi156Iron-sulfur 2 (4Fe-4S)By similarity1
Metal bindingi160Iron-sulfur 1 (4Fe-4S)By similarity1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • NADH dehydrogenase (ubiquinone) activity Source: UniProtKB

GO - Biological processi

  • mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  • mitochondrial respiratory chain complex I assembly Source: UniProtKB
  • response to oxidative stress Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Respiratory chain, Transport
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

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] iron-sulfur protein 8, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-23kD
Short name:
CI-23kD
NADH-ubiquinone oxidoreductase 23 kDa subunit
TYKY subunit
Gene namesi
Name:NDUFS8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000110717.10
HGNCiHGNC:7715 NDUFS8
MIMi602141 gene
neXtProtiNX_O00217

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_01953879P → L in LS. 1 PublicationCorresponds to variant dbSNP:rs28939679EnsemblClinVar.1
Natural variantiVAR_019539102R → H in LS. 1 PublicationCorresponds to variant dbSNP:rs121912638EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Leigh syndrome, Primary mitochondrial disease

Organism-specific databases

DisGeNETi4728
MalaCardsiNDUFS8
MIMi256000 phenotype
OpenTargetsiENSG00000110717
Orphaneti2609 Isolated NADH-CoQ reductase deficiency
255241 Leigh syndrome with leukodystrophy
PharmGKBiPA31525

Chemistry databases

ChEMBLiCHEMBL2363065
DrugBankiDB00157 NADH

Polymorphism and mutation databases

BioMutaiNDUFS8

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionBy similarityAdd BLAST34
ChainiPRO_000002001235 – 210NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrialAdd BLAST176

Proteomic databases

EPDiO00217
MaxQBiO00217
PaxDbiO00217
PeptideAtlasiO00217
PRIDEiO00217
ProteomicsDBi47787
TopDownProteomicsiO00217

2D gel databases

OGPiO00217

PTM databases

CarbonylDBiO00217
iPTMnetiO00217
PhosphoSitePlusiO00217
SwissPalmiO00217

Expressioni

Gene expression databases

BgeeiENSG00000110717
CleanExiHS_NDUFS8
ExpressionAtlasiO00217 baseline and differential
GenevisibleiO00217 HS

Organism-specific databases

HPAiHPA018524

Interactioni

Subunit structurei

Mammalian complex I is composed of 45 different subunits.1 Publication

Protein-protein interaction databases

BioGridi110806, 61 interactors
ComplexPortaliCPX-577 Mitochondrial respiratory chain complex I
CORUMiO00217
IntActiO00217, 30 interactors
MINTiO00217
STRINGi9606.ENSP00000315774

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Helixi48 – 60Combined sources13
Helixi63 – 76Combined sources14
Turni84 – 86Combined sources3
Beta strandi98 – 101Combined sources4
Helixi117 – 120Combined sources4
Beta strandi130 – 132Combined sources3
Beta strandi138 – 141Combined sources4
Beta strandi144 – 146Combined sources3
Turni147 – 149Combined sources3
Helixi155 – 159Combined sources5
Beta strandi165 – 167Combined sources3
Beta strandi175 – 177Combined sources3
Helixi178 – 181Combined sources4
Beta strandi182 – 184Combined sources3
Helixi185 – 194Combined sources10
Helixi196 – 206Combined sources11
Helixi207 – 209Combined sources3

3D structure databases

ProteinModelPortaliO00217
SMRiO00217
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini102 – 1314Fe-4S ferredoxin-type 1Add BLAST30
Domaini141 – 1704Fe-4S ferredoxin-type 2Add BLAST30

Sequence similaritiesi

Belongs to the complex I 23 kDa subunit family.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiKOG3256 Eukaryota
COG1143 LUCA
GeneTreeiENSGT00390000003049
HOGENOMiHOG000228289
HOVERGENiHBG006547
InParanoidiO00217
KOiK03941
OMAiEIARGMY
OrthoDBiEOG091G0OQD
PhylomeDBiO00217
TreeFamiTF105610

Family and domain databases

HAMAPiMF_01351 NDH1_NuoI, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR010226 NADH_quinone_OxRdtase_chainI
PfamiView protein in Pfam
PF12838 Fer4_7, 1 hit
TIGRFAMsiTIGR01971 NuoI, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 2 hits
PS51379 4FE4S_FER_2, 2 hits

Sequencei

Sequence statusi: Complete.

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

O00217-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS
60 70 80 90 100
VTDRAARTLL WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA
110 120 130 140 150
LRRYPSGEER CIACKLCEAI CPAQAITIEA EPRADGSRRT TRYDIDMTKC
160 170 180 190 200
IYCGFCQEAC PVDAIVEGPN FEFSTETHEE LLYNKEKLLN NGDKWEAEIA
210
ANIQADYLYR
Length:210
Mass (Da):23,705
Last modified:July 1, 1997 - v1
Checksum:i8C3EBD205BFA0112
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01953879P → L in LS. 1 PublicationCorresponds to variant dbSNP:rs28939679EnsemblClinVar.1
Natural variantiVAR_019539102R → H in LS. 1 PublicationCorresponds to variant dbSNP:rs121912638EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65579 mRNA Translation: AAB51776.1
AF038406 Genomic DNA Translation: AAC34273.1
AK314546 mRNA Translation: BAG37133.1
BC119754 mRNA Translation: AAI19755.1
CCDSiCCDS8176.1
RefSeqiNP_002487.1, NM_002496.3
XP_005274070.1, XM_005274013.1
XP_005274071.1, XM_005274014.2
XP_011543355.1, XM_011545053.2
UniGeneiHs.90443

Genome annotation databases

EnsembliENST00000313468; ENSP00000315774; ENSG00000110717
GeneIDi4728
KEGGihsa:4728
UCSCiuc001onc.4 human

Similar proteinsi

Entry informationi

Entry nameiNDUS8_HUMAN
AccessioniPrimary (citable) accession number: O00217
Secondary accession number(s): B2RB86, Q0VDA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 20, 2018
This is version 177 of the entry and version 1 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 11
    Human chromosome 11: 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

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