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Protein

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

Gene

NDUFS8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi114 – 1141Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi117 – 1171Iron-sulfur 1 (4Fe-4S)By similarity
Metal bindingi121 – 1211Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi150 – 1501Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi153 – 1531Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi156 – 1561Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi160 – 1601Iron-sulfur 1 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  3. mitochondrial respiratory chain complex I assembly Source: UniProtKB
  4. respiratory electron transport chain Source: Reactome
  5. response to oxidative stress Source: UniProtKB
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.

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
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7715. NDUFS8.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial respiratory chain complex I Source: UniProtKB
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791P → L in LS. 1 Publication
Corresponds to variant rs28939679 [ dbSNP | Ensembl ].
VAR_019538
Natural varianti102 – 1021R → H in LS. 1 Publication
VAR_019539

Keywords - Diseasei

Disease mutation, Leigh syndrome

Organism-specific databases

MIMi256000. phenotype.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBiPA31525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434MitochondrionBy similarityAdd
BLAST
Chaini35 – 210176NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrialPRO_0000020012Add
BLAST

Proteomic databases

MaxQBiO00217.
PaxDbiO00217.
PeptideAtlasiO00217.
PRIDEiO00217.

2D gel databases

OGPiO00217.

PTM databases

PhosphoSiteiO00217.

Expressioni

Gene expression databases

BgeeiO00217.
CleanExiHS_NDUFS8.
ExpressionAtlasiO00217. baseline and differential.
GenevestigatoriO00217.

Organism-specific databases

HPAiHPA018524.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110806. 29 interactions.
IntActiO00217. 5 interactions.
MINTiMINT-2997478.
STRINGi9606.ENSP00000315774.

Structurei

3D structure databases

ProteinModelPortaliO00217.
SMRiO00217. Positions 64-189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini102 – 131304Fe-4S ferredoxin-type 1Add
BLAST
Domaini141 – 170304Fe-4S ferredoxin-type 2Add
BLAST

Sequence similaritiesi

Belongs to the complex I 23 kDa subunit family.Curated
Contains 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG1143.
GeneTreeiENSGT00390000003049.
HOGENOMiHOG000228289.
HOVERGENiHBG006547.
InParanoidiO00217.
KOiK03941.
OMAiFVITLKY.
OrthoDBiEOG7J9VQT.
PhylomeDBiO00217.
TreeFamiTF105610.

Family and domain databases

HAMAPiMF_01351. NDH1_NuoI.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR010226. NADH_quinone_OxRdtase_chainI.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01971. NuoI. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

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:June 30, 1997 - v1
Checksum:i8C3EBD205BFA0112
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791P → L in LS. 1 Publication
Corresponds to variant rs28939679 [ dbSNP | Ensembl ].
VAR_019538
Natural varianti102 – 1021R → H in LS. 1 Publication
VAR_019539

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_005274014.1.
UniGeneiHs.90443.

Genome annotation databases

EnsembliENST00000313468; ENSP00000315774; ENSG00000110717.
GeneIDi4728.
KEGGihsa:4728.
UCSCiuc001onc.3. human.

Cross-referencesi

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_005274014.1.
UniGeneiHs.90443.

3D structure databases

ProteinModelPortaliO00217.
SMRiO00217. Positions 64-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110806. 29 interactions.
IntActiO00217. 5 interactions.
MINTiMINT-2997478.
STRINGi9606.ENSP00000315774.

Chemistry

ChEMBLiCHEMBL2363065.

PTM databases

PhosphoSiteiO00217.

2D gel databases

OGPiO00217.

Proteomic databases

MaxQBiO00217.
PaxDbiO00217.
PeptideAtlasiO00217.
PRIDEiO00217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313468; ENSP00000315774; ENSG00000110717.
GeneIDi4728.
KEGGihsa:4728.
UCSCiuc001onc.3. human.

Organism-specific databases

CTDi4728.
GeneCardsiGC11P067798.
HGNCiHGNC:7715. NDUFS8.
HPAiHPA018524.
MIMi256000. phenotype.
602141. gene.
neXtProtiNX_O00217.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBiPA31525.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1143.
GeneTreeiENSGT00390000003049.
HOGENOMiHOG000228289.
HOVERGENiHBG006547.
InParanoidiO00217.
KOiK03941.
OMAiFVITLKY.
OrthoDBiEOG7J9VQT.
PhylomeDBiO00217.
TreeFamiTF105610.

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.

Miscellaneous databases

GeneWikiiNDUFS8.
GenomeRNAii4728.
NextBioi18230.
PROiO00217.
SOURCEiSearch...

Gene expression databases

BgeeiO00217.
CleanExiHS_NDUFS8.
ExpressionAtlasiO00217. baseline and differential.
GenevestigatoriO00217.

Family and domain databases

HAMAPiMF_01351. NDH1_NuoI.
InterProiIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR010226. NADH_quinone_OxRdtase_chainI.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01971. NuoI. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and chromosomal localization of the NDUFS8 human gene coding for the 23 kDa subunit of the mitochondrial complex I."
    Procaccio V., Depetris D., Soularue P., Mattei M.-G., Lunardi J., Issartel J.-P.
    Biochim. Biophys. Acta 1351:37-41(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase."
    de Sury R., Martinez P., Procaccio V., Lunardi J., Issartel J.-P.
    Gene 215:1-10(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification."
    Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A.
    J. Biol. Chem. 278:13619-13622(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: VARIANTS LS LEU-79 AND HIS-102.

Entry informationi

Entry nameiNDUS8_HUMAN
AccessioniPrimary (citable) accession number: O00217
Secondary accession number(s): B2RB86, Q0VDA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: June 30, 1997
Last modified: March 3, 2015
This is version 147 of the entry and version 1 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.