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UniProtKB/Swiss-Prot entry O00217


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NDUS8_HUMAN
Primary accession number O00217
Secondary accession numbers B2RB86 Q0VDA8
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 81)
Name and origin of the protein
Protein name NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial [Precursor]
Synonyms EC 1.6.5.3
EC 1.6.99.3
NADH-ubiquinone oxidoreductase 23 kDa subunit
Complex I-23kD
CI-23kD
TYKY subunit
Gene name
Name: NDUFS8
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1016/S0167-4781(97)00020-1; PubMed=9116042 [NCBI, ExPASy, EBI, Israel, Japan]
Procaccio V., Depetris D., Soularue P., Mattei M.-G., Lunardi J., Issartel J.-P.;
"cDNA sequence and chromosomal localization of the NDUFS8 human gene coding for the 23 kDa subunit of the mitochondrial complex I.";
Biochim. Biophys. Acta 1351:37-41(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0378-1119(98)00275-3; PubMed=9666055 [NCBI, ExPASy, EBI, Israel, Japan]
de Sury R., Martinez P., Procaccio V., Lunardi J., Issartel J.-P.;
"Genomic structure of the human NDUFS8 gene coding for the iron-sulfur TYKY subunit of the mitochondrial NADH:ubiquinone oxidoreductase.";
Gene 215:1-10(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
VARIANTS LS LEU-79 AND HIS-102.
DOI=10.1086/302154; PubMed=9837812 [NCBI, ExPASy, EBI, Israel, Japan]
Loeffen J., Smeitink J., Triepels R., Smeets R., Schuelke M., Sengers R., Trijbels F., Hamel B.C.J., Mullaart R., van den Heuvel L.;
"The first nuclear-encoded complex I mutation in a patient with Leigh syndrome.";
Am. J. Hum. Genet. 63:1598-1608(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U65579; AAB51776.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF038406; AAC34273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314546; BAG37133.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119754; AAI19755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_002487.1; -.
UniGene Hs.90443
3D structure databases
HSSP P00198; 2FDN. [HSSP ENTRY / PDB]
ModBase O00217.
PTM databases
PhosphoSite O00217; -.
Enzyme and pathway databases
Reactome REACT_6305; Electron Transport Chain.
2D gel databases
OGP O00217; -.
Organism-specific databases
GeneCards GC11P067554; -.
H-InvDB HIX0023060; -.
HGNC HGNC:7715; NDUFS8.
GenAtlas NDUFS8.
HPA HPA018524; -.
MIM 256000; phenotype. [NCBI / EBI]
602141; gene. [NCBI / EBI]
Orphanet 506; Leigh syndrome.
2609; NADH-CoQ reductase deficiency.
PharmGKB PA31525; -.
GeneCards O00217.
Gene expression databases
ArrayExpress O00217; -.
CleanEx HS_NDUFS8; -.
GermOnline ENSG00000110717; Homo sapiens.
Ontologies
GO
GO:0005747; Cellular component: mitochondrial respiratory chain complex I (inferred from mutant phenotype from UniProtKB).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137; Molecular function: NADH dehydrogenase (ubiquinone) activity (non-traceable author statement from UniProtKB).
GO:0006120; Biological process: mitochondrial electron transport, NADH to ubiquinone (non-traceable author statement from UniProtKB).
GO:0032981; Biological process: mitochondrial respiratory chain complex I assembly (inferred from mutant phenotype from UniProtKB).
GO:0006979; Biological process: response to oxidative stress (inferred from direct assay from UniProtKB).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001450; 4Fe4S_Fe_S_bd.
IPR010226; NADH_quinone_OxRdtase_I.
Graphical view of domain structure.
Pfam PF00037; Fer4; 2.
Pfam graphical view of domain structure.
PRINTS PR00353; 4FE4SFRDOXIN.
TIGRFAMs TIGR01971; NuoI; 1.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas O00217; -.
Proteomics databases
PRIDE O00217; -.
Genome annotation databases
Ensembl ENSG00000110717; Homo sapiens. [Contig view]
GeneID 4728; -.
KEGG hsa:4728; -.
NMPDR fig|9606.3.peg.6162; -.
Phylogenomic databases
HOVERGEN O00217; -.
Other
DrugBank DB00157; NADH.
NextBio 18230; -.
SOURCE NDUFS8; Homo sapiens.
ProtoNet O00217.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Disease mutation; Electron transport; Iron; Iron-sulfur; Leigh syndrome; Metal-binding; Mitochondrion; NAD; Oxidoreductase; Repeat; Respiratory chain; Transit peptide; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    34  34     Mitochondrion (By similarity). 
CHAIN   35   210  176     NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial. PRO_0000020012
DOMAIN   102   131  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   141   170  30     4Fe-4S ferredoxin-type 2. 
METAL   111   111        Iron-sulfur 1 (4Fe-4S) (By similarity). 
METAL   114   114        Iron-sulfur 1 (4Fe-4S) (By similarity). 
METAL   117   117        Iron-sulfur 1 (4Fe-4S) (By similarity). 
METAL   121   121        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   150   150        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   153   153        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   156   156        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   160   160        Iron-sulfur 1 (4Fe-4S) (By similarity). 
VARIANT   79    79  1     P -> L (in LS). VAR_019538 
VARIANT   102   102  1     R -> H (in LS). VAR_019539 
Sequence information
Length: 210 AA [This is the length of the unprocessed precursor] Molecular weight: 23705 Da [This is the MW of the unprocessed precursor] CRC64: 8C3EBD205BFA0112 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRCLTTPMLL RALAQAARAG PPGGRSLHSS AVAATYKYVN MQDPEMDMKS VTDRAARTLL 

        70         80         90        100        110        120 
WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI 

       130        140        150        160        170        180 
CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE 

       190        200        210 
LLYNKEKLLN NGDKWEAEIA ANIQADYLYR 

O00217 in FASTA format

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