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UniProtKB/Swiss-Prot entry O75306


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

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Entry information
Entry name NDUS2_HUMAN
Primary accession number O75306
Secondary accession numbers Q5VTW0 Q969P3 Q9UEV3
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on April 16, 2002 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 81)
Name and origin of the protein
Protein name NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial [Precursor]
Synonyms EC 1.6.5.3
EC 1.6.99.3
NADH-ubiquinone oxidoreductase 49 kDa subunit
Complex I-49kD
CI-49kD
Gene name
Name: NDUFS2
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 [MRNA].
DOI=10.1006/bbrc.1998.8882; PubMed=9647766 [NCBI, ExPASy, EBI, Israel, Japan]
Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R., Trijbels F., Smeitink J.;
"cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed.";
Biochem. Biophys. Res. Commun. 247:751-758(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/s003359900803; PubMed=9585441 [NCBI, ExPASy, EBI, Israel, Japan]
Procaccio V., de Sury R., Martinez P., Depetris D., Rabilloud T., Soularue P., Lunardi J., Issartel J.-P.;
"Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory complex I and immunodetection of the mature protein in mitochondria.";
Mamm. Genome 9:482-484(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Placenta;
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).
[6]
VARIANTS COMPLEX I DEFICIENCY GLN-228; GLN-229 AND PRO-413.
DOI=10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M; PubMed=11220739 [NCBI, ExPASy, EBI, Israel, Japan]
Loeffen J., Elpeleg O., Smeitink J., Smeets R., Stoeckler-Ipsiroglu S., Mandel H., Sengers R., Trijbels F., van den Heuvel L.;
"Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy.";
Ann. Neurol. 49:195-201(2001).
Comments
  • FUNCTION: 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).
  • CATALYTIC ACTIVITY: NADH + ubiquinone = NAD+ + ubiquinol.
  • CATALYTIC ACTIVITY: NADH + acceptor = NAD+ + reduced acceptor.
  • COFACTOR: Binds 1 4Fe-4S cluster.
  • SUBUNIT: Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme.
  • SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
  • DISEASE: Defects in NDUFS2 are a cause of complex I mitochondrial respiratory chain deficiency [MIM:252010]. Complex I (NADH-ubiquinone oxidoreductase), the largest complex of the mitochondrial respiratory chain, contains more than 40 subunits. It is embedded in the inner mitochondrial membrane and is partly protruding in the matrix. Complex I deficiency is the most common cause of mitochondrial disorders. It represents largely one-third of all cases of respiratory chain deficiency and is responsible for a variety of clinical symptoms, ranging from neurological disorders to cardiomyopathy, liver failure, and myopathy.
  • SIMILARITY: Belongs to the complex I 49 kDa subunit family.
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
AF050640; AAC27453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF013160; AAC34362.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590714; CAH72148.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471121; EAW52625.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000170; AAH00170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001456; AAH01456.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008868; AAH08868.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JE0193; JE0193.
RefSeq NP_004541.1; -.
UniGene Hs.173611
3D structure databases
ModBase O75306.
Protein-protein interaction databases
IntAct O75306; -.
PTM databases
PhosphoSite O75306; -.
Enzyme and pathway databases
Reactome REACT_6305; Electron Transport Chain.
Organism-specific databases
HGNC HGNC:7708; NDUFS2.
GenAtlas NDUFS2.
MIM 252010; phenotype. [NCBI / EBI]
602985; gene. [NCBI / EBI]
Orphanet 2597; Mitochondrial myopathy - lactic acidosis.
2609; NADH-CoQ reductase deficiency.
PharmGKB PA31519; -.
GeneCards O75306.
Gene expression databases
ArrayExpress O75306; -.
CleanEx HS_NDUFS2; -.
GermOnline ENSG00000158864; Homo sapiens.
Ontologies
GO
GO:0005747; Cellular component: mitochondrial respiratory chain complex I (inferred from direct assay from UniProtKB).
GO:0009055; Molecular function: electron carrier activity (non-traceable author statement from UniProtKB).
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:0006979; Biological process: response to oxidative stress (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR014029; NADH-UbQ_OxRdtase_49kDa_CS.
IPR010219; NADH_DH_1_dsu.
IPR001135; NADH_UbQ_OxRdtase_49kDa.
Graphical view of domain structure.
Pfam PF00346; Complex1_49kDa; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01962; NuoD; 1.
PROSITE PS00535; COMPLEX1_49K; 1.
BLOCKS O75306.
Proteomic databases
PeptideAtlas O75306; -.
Genome annotation databases
Ensembl ENSG00000158864; Homo sapiens. [Contig view]
GeneID 4720; -.
KEGG hsa:4720; -.
Phylogenomic databases
HOVERGEN O75306; -.
Other
DrugBank DB00157; NADH.
SOURCE NDUFS2; Homo sapiens.
ProtoNet O75306.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Disease mutation; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase; Polymorphism; Respiratory chain; Transit peptide; Transport; Ubiquinone.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    33  33     Mitochondrion (By similarity). 
CHAIN   34   463  430     NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial. PRO_0000019981
METAL   326   326        Iron-sulfur (4Fe-4S) (Potential). 
METAL   332   332        Iron-sulfur (4Fe-4S) (Potential). 
METAL   347   347        Iron-sulfur (4Fe-4S) (Potential). 
VARIANT   20    20  1     P -> T (in dbSNP:rs11538340 [NCBI]). VAR_034150 
VARIANT   228   228  1     R -> Q (in complex I deficiency). VAR_019535 
VARIANT   229   229  1     P -> A (in dbSNP:rs16827493 [NCBI]). VAR_034151 
VARIANT   229   229  1     P -> Q (in complex I deficiency). VAR_019536 
VARIANT   352   352  1     P -> A (in dbSNP:rs11576415 [NCBI]). VAR_034152 
VARIANT   413   413  1     S -> P (in complex I deficiency). VAR_019537 
CONFLICT   24    24        V -> G (in Ref. 2; AAC34362). 
Sequence information
Length: 463 AA [This is the length of the unprocessed precursor] Molecular weight: 52546 Da [This is the MW of the unprocessed precursor] CRC64: A2BF56F008B6312C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA VMYPSKETAH 

        70         80         90        100        110        120 
WKPPPWNDVD PPKDTIVKNI TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT 

       130        140        150        160        170        180 
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IRPPPRAQWI RVLFGEITRL 

       190        200        210        220        230        240 
LNHIMAVTTH ALDLGAMTPF FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL 

       250        260        270        280        290        300 
MDDIYQFSKN FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW 

       310        320        330        340        350        360 
DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK MPPGEIKVDD 

       370        380        390        400        410        420 
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY 

       430        440        450        460 
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE VDR 

O75306 in FASTA format

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