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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

Gene

NDUFS2

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).By similarity

Catalytic activityi

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

Cofactori

[4Fe-4S] clusterNote: Binds 1 [4Fe-4S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Iron-sulfur (4Fe-4S)Sequence Analysis
Metal bindingi332 – 3321Iron-sulfur (4Fe-4S)Sequence Analysis
Metal bindingi347 – 3471Iron-sulfur (4Fe-4S)Sequence Analysis

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB
  6. quinone binding Source: InterPro

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  3. respiratory electron transport chain Source: Reactome
  4. response to oxidative stress Source: UniProtKB
  5. 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 2, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-49kD
Short name:
CI-49kD
NADH-ubiquinone oxidoreductase 49 kDa subunit
Gene namesi
Name:NDUFS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7708. NDUFS2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Mitochondrial complex I deficiency (MT-C1D)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.

See also OMIM:252010
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
VAR_019535
Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
VAR_019536
Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
VAR_019537

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi252010. phenotype.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA31519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 463430NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrialPRO_0000019981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621N6-acetyllysineBy similarity
Modified residuei118 – 1181Symmetric dimethylarginineBy similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiO75306.
PaxDbiO75306.
PeptideAtlasiO75306.
PRIDEiO75306.

PTM databases

PhosphoSiteiO75306.

Expressioni

Gene expression databases

BgeeiO75306.
CleanExiHS_NDUFS2.
ExpressionAtlasiO75306. baseline and differential.
GenevestigatoriO75306.

Organism-specific databases

HPAiHPA055140.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3 and NDUFAF7.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NDUFS3O754895EBI-1224806,EBI-1224896

Protein-protein interaction databases

BioGridi110800. 33 interactions.
IntActiO75306. 16 interactions.
STRINGi9606.ENSP00000356972.

Structurei

3D structure databases

ProteinModelPortaliO75306.
SMRiO75306. Positions 80-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I 49 kDa subunit family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0649.
GeneTreeiENSGT00390000009529.
HOGENOMiHOG000228264.
HOVERGENiHBG000760.
InParanoidiO75306.
KOiK03935.
OMAiEYRTWTQ.
OrthoDBiEOG7WT411.
PhylomeDBiO75306.
TreeFamiTF300370.

Family and domain databases

Gene3Di1.10.645.10. 1 hit.
HAMAPiMF_01358. NDH1_NuoD.
InterProiIPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
IPR029014. NiFe_Hase-like.
[Graphical view]
PfamiPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
SUPFAMiSSF56762. SSF56762. 1 hit.
TIGRFAMsiTIGR01962. NuoD. 1 hit.
PROSITEiPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75306-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA
60 70 80 90 100
VMYPSKETAH WKPPPWNDVD PPKDTIVKNI TLNFGPQHPA AHGVLRLVME
110 120 130 140 150
LSGEMVRKCD PHIGLLHRGT EKLIEYKTYL QALPYFDRLD YVSMMCNEQA
160 170 180 190 200
YSLAVEKLLN IRPPPRAQWI RVLFGEITRL LNHIMAVTTH ALDLGAMTPF
210 220 230 240 250
FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL MDDIYQFSKN
260 270 280 290 300
FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW
310 320 330 340 350
DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK
360 370 380 390 400
MPPGEIKVDD AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI
410 420 430 440 450
EAPKGEFGVY LVSDGSSRPY RCKIKAPGFA HLAGLDKMSK GHMLADVVAI
460
IGTQDIVFGE VDR
Length:463
Mass (Da):52,546
Last modified:April 16, 2002 - v2
Checksum:iA2BF56F008B6312C
GO
Isoform 2 (identifier: O75306-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-463: QDIVFGEVDR → RPIV

Note: No experimental confirmation available.

Show »
Length:457
Mass (Da):51,852
Checksum:i312C97A91028FF66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241V → G in AAC34362 (PubMed:9585441).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201P → T.
Corresponds to variant rs11538340 [ dbSNP | Ensembl ].
VAR_034150
Natural varianti224 – 2241A → V.1 Publication
VAR_071891
Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
VAR_019535
Natural varianti229 – 2291P → A.
Corresponds to variant rs16827493 [ dbSNP | Ensembl ].
VAR_034151
Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
VAR_019536
Natural varianti352 – 3521P → A.
Corresponds to variant rs11576415 [ dbSNP | Ensembl ].
VAR_034152
Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
VAR_019537

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 46310QDIVFGEVDR → RPIV in isoform 2. CuratedVSP_046466

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050640 mRNA. Translation: AAC27453.1.
AF013160 mRNA. Translation: AAC34362.1.
AK314807 mRNA. No translation available.
AL590714 Genomic DNA. Translation: CAH72148.1.
CH471121 Genomic DNA. Translation: EAW52625.1.
CH471121 Genomic DNA. Translation: EAW52626.1.
BC000170 mRNA. Translation: AAH00170.1.
BC001456 mRNA. Translation: AAH01456.1.
BC008868 mRNA. Translation: AAH08868.1.
CCDSiCCDS1224.1. [O75306-1]
CCDS53404.1. [O75306-2]
PIRiJE0193.
RefSeqiNP_001159631.1. NM_001166159.1. [O75306-2]
NP_004541.1. NM_004550.4. [O75306-1]
XP_005245265.1. XM_005245208.1. [O75306-1]
UniGeneiHs.173611.

Genome annotation databases

EnsembliENST00000367993; ENSP00000356972; ENSG00000158864. [O75306-1]
ENST00000392179; ENSP00000376018; ENSG00000158864. [O75306-2]
GeneIDi4720.
KEGGihsa:4720.
UCSCiuc001fyv.3. human. [O75306-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF050640 mRNA. Translation: AAC27453.1.
AF013160 mRNA. Translation: AAC34362.1.
AK314807 mRNA. No translation available.
AL590714 Genomic DNA. Translation: CAH72148.1.
CH471121 Genomic DNA. Translation: EAW52625.1.
CH471121 Genomic DNA. Translation: EAW52626.1.
BC000170 mRNA. Translation: AAH00170.1.
BC001456 mRNA. Translation: AAH01456.1.
BC008868 mRNA. Translation: AAH08868.1.
CCDSiCCDS1224.1. [O75306-1]
CCDS53404.1. [O75306-2]
PIRiJE0193.
RefSeqiNP_001159631.1. NM_001166159.1. [O75306-2]
NP_004541.1. NM_004550.4. [O75306-1]
XP_005245265.1. XM_005245208.1. [O75306-1]
UniGeneiHs.173611.

3D structure databases

ProteinModelPortaliO75306.
SMRiO75306. Positions 80-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110800. 33 interactions.
IntActiO75306. 16 interactions.
STRINGi9606.ENSP00000356972.

Chemistry

ChEMBLiCHEMBL2363065.
DrugBankiDB00997. Doxorubicin.

PTM databases

PhosphoSiteiO75306.

Proteomic databases

MaxQBiO75306.
PaxDbiO75306.
PeptideAtlasiO75306.
PRIDEiO75306.

Protocols and materials databases

DNASUi4720.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367993; ENSP00000356972; ENSG00000158864. [O75306-1]
ENST00000392179; ENSP00000376018; ENSG00000158864. [O75306-2]
GeneIDi4720.
KEGGihsa:4720.
UCSCiuc001fyv.3. human. [O75306-1]

Organism-specific databases

CTDi4720.
GeneCardsiGC01P161166.
HGNCiHGNC:7708. NDUFS2.
HPAiHPA055140.
MIMi252010. phenotype.
602985. gene.
neXtProtiNX_O75306.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA31519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0649.
GeneTreeiENSGT00390000009529.
HOGENOMiHOG000228264.
HOVERGENiHBG000760.
InParanoidiO75306.
KOiK03935.
OMAiEYRTWTQ.
OrthoDBiEOG7WT411.
PhylomeDBiO75306.
TreeFamiTF300370.

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.

Miscellaneous databases

ChiTaRSiNDUFS2. human.
GeneWikiiNDUFS2.
GenomeRNAii4720.
NextBioi18206.
PROiO75306.
SOURCEiSearch...

Gene expression databases

BgeeiO75306.
CleanExiHS_NDUFS2.
ExpressionAtlasiO75306. baseline and differential.
GenevestigatoriO75306.

Family and domain databases

Gene3Di1.10.645.10. 1 hit.
HAMAPiMF_01358. NDH1_NuoD.
InterProiIPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
IPR029014. NiFe_Hase-like.
[Graphical view]
PfamiPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
SUPFAMiSSF56762. SSF56762. 1 hit.
TIGRFAMsiTIGR01962. NuoD. 1 hit.
PROSITEiPS00535. COMPLEX1_49K. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R., Trijbels F., Smeitink J.
    Biochem. Biophys. Res. Commun. 247:751-758(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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."
    Procaccio V., de Sury R., Martinez P., Depetris D., Rabilloud T., Soularue P., Lunardi J., Issartel J.-P.
    Mamm. Genome 9:482-484(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Muscle and Placenta.
  7. "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.
  8. "Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease."
    Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J., Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O., Shohat M., Huynen M.A., Smeitink J.A.M., van den Heuvel L.P., Nijtmans L.G.
    Am. J. Hum. Genet. 84:718-727(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDUFAF3.
  9. Cited for: INTERACTION WITH NDUFAF7.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.
  12. "Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy."
    Loeffen J., Elpeleg O., Smeitink J., Smeets R., Stoeckler-Ipsiroglu S., Mandel H., Sengers R., Trijbels F., van den Heuvel L.
    Ann. Neurol. 49:195-201(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MT-C1D GLN-228; GLN-229 AND PRO-413.
  13. Cited for: VARIANT VAL-224.

Entry informationi

Entry nameiNDUS2_HUMAN
AccessioniPrimary (citable) accession number: O75306
Secondary accession number(s): D3DVG7
, J3KPM7, Q5VTW0, Q969P3, Q9UEV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 16, 2002
Last modified: March 4, 2015
This is version 155 of the entry and version 2 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 1
    Human chromosome 1: 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.