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Protein

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial

Gene

NDUFS1

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). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi131 – 1311Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi179 – 1791Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S)By similarity

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • electron carrier activity Source: UniProtKB
  • iron-sulfur cluster binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • NADH dehydrogenase (ubiquinone) activity Source: UniProtKB

GO - Biological processi

  • apoptotic mitochondrial changes Source: UniProtKB
  • ATP metabolic process Source: UniProtKB
  • cellular metabolic process Source: Reactome
  • cellular respiration Source: UniProtKB
  • mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of mitochondrial membrane potential Source: UniProtKB
  • respiratory electron transport chain Source: Reactome
  • small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, 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-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-75kD
Short name:
CI-75kD
Gene namesi
Name:NDUFS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7707. NDUFS1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrial respiratory chain complex I Source: UniProtKB
  • mitochondrion Source: HPA
  • myelin sheath Source: Ensembl
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 varianti241 – 2411R → W in MT-C1D. 1 Publication
VAR_019532
Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
VAR_019533

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi252010. phenotype.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBiPA31518.

Polymorphism and mutation databases

BioMutaiNDUFS1.
DMDMi92090799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrialPRO_0000019968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-acetyllysineBy similarity
Modified residuei467 – 4671N6-acetyllysineBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei709 – 7091N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP28331.
PaxDbiP28331.
PeptideAtlasiP28331.
PRIDEiP28331.

2D gel databases

REPRODUCTION-2DPAGEIPI00604664.
P28331.
UCD-2DPAGEP28331.

PTM databases

PhosphoSiteiP28331.

Miscellaneous databases

PMAP-CutDBP28331.

Expressioni

Gene expression databases

BgeeiP28331.
CleanExiHS_NDUFS1.
ExpressionAtlasiP28331. baseline and differential.
GenevisibleiP28331. HS.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits.1 Publication

Protein-protein interaction databases

BioGridi110799. 45 interactions.
IntActiP28331. 27 interactions.
MINTiMINT-3011123.
STRINGi9606.ENSP00000392709.

Structurei

3D structure databases

ProteinModelPortaliP28331.
SMRiP28331. Positions 31-636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 108792Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini245 – 301574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1034.
GeneTreeiENSGT00390000018768.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiP28331.
KOiK03934.
OMAiADCESMF.
OrthoDBiEOG783MTP.
PhylomeDBiP28331.
TreeFamiTF105756.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P28331-1) [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
MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL
60 70 80 90 100
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW
110 120 130 140 150
NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR
160 170 180 190 200
SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR
210 220 230 240 250
GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES
260 270 280 290 300
IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ
310 320 330 340 350
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA
360 370 380 390 400
LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV
410 420 430 440 450
LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK
460 470 480 490 500
ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI
510 520 530 540 550
RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA
560 570 580 590 600
DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE
610 620 630 640 650
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS
660 670 680 690 700
PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI
710 720
SRASQTMAKC VKAVTEGAQA VEEPSIC
Length:727
Mass (Da):79,468
Last modified:March 7, 2006 - v3
Checksum:i9C35F4B8294771FB
GO
Isoform 2 (identifier: P28331-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRIRGSSGTLSRINM

Note: No experimental confirmation available.
Show »
Length:741
Mass (Da):80,997
Checksum:iEB7CA8F41E3DF6E2
GO
Isoform 3 (identifier: P28331-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ML → MW
     3-113: Missing.

Note: No experimental confirmation available.
Show »
Length:616
Mass (Da):67,524
Checksum:i16CA2EF571877D03
GO
Isoform 4 (identifier: P28331-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Note: No experimental confirmation available.
Show »
Length:670
Mass (Da):73,527
Checksum:iC8B37BF8C954187F
GO
Isoform 5 (identifier: P28331-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-87: Missing.

Note: No experimental confirmation available.
Show »
Length:691
Mass (Da):75,375
Checksum:i522872E0D6EB9E09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81K → R in CAA43412 (PubMed:1935949).Curated
Sequence conflicti417 – 4171R → W in CAA43412 (PubMed:1935949).Curated
Sequence conflicti572 – 5721H → L in BAG58551 (PubMed:14702039).Curated
Sequence conflicti691 – 6911I → L in CAA43412 (PubMed:1935949).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti241 – 2411R → Q.1 Publication
Corresponds to variant rs17856901 [ dbSNP | Ensembl ].
VAR_025511
Natural varianti241 – 2411R → W in MT-C1D. 1 Publication
VAR_019532
Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
VAR_019533
Natural varianti253 – 2531V → G.1 Publication
VAR_069506
Natural varianti649 – 6491V → F.1 Publication
Corresponds to variant rs1044049 [ dbSNP | Ensembl ].
VAR_018463

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform 4. 1 PublicationVSP_043727Add
BLAST
Alternative sequencei1 – 22ML → MW in isoform 3. 1 PublicationVSP_043728
Alternative sequencei1 – 11M → MRIRGSSGTLSRINM in isoform 2. CuratedVSP_042682
Alternative sequencei3 – 113111Missing in isoform 3. 1 PublicationVSP_043729Add
BLAST
Alternative sequencei52 – 8736Missing in isoform 5. 1 PublicationVSP_045864Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61100 mRNA. Translation: CAA43412.1.
AK295705 mRNA. Translation: BAG58551.1.
AK295987 mRNA. Translation: BAG58762.1.
AK298320 mRNA. Translation: BAG60573.1.
AK300585 mRNA. Translation: BAG62283.1.
AC007383 Genomic DNA. Translation: AAY15061.1.
CH471063 Genomic DNA. Translation: EAW70379.1.
BC022368 mRNA. Translation: AAH22368.1.
BC030833 mRNA. Translation: AAH30833.1.
CCDSiCCDS2366.1. [P28331-1]
CCDS56162.1. [P28331-4]
CCDS56163.1. [P28331-3]
CCDS56164.1. [P28331-5]
CCDS56165.1. [P28331-2]
PIRiS17854.
RefSeqiNP_001186910.1. NM_001199981.1. [P28331-5]
NP_001186911.1. NM_001199982.1. [P28331-3]
NP_001186912.1. NM_001199983.1. [P28331-4]
NP_001186913.1. NM_001199984.1. [P28331-2]
NP_004997.4. NM_005006.6. [P28331-1]
UniGeneiHs.471207.
Hs.598436.

Genome annotation databases

EnsembliENST00000233190; ENSP00000233190; ENSG00000023228.
ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
ENST00000449699; ENSP00000399912; ENSG00000023228.
ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
GeneIDi4719.
KEGGihsa:4719.
UCSCiuc002vbe.3. human. [P28331-1]
uc010ziq.2. human. [P28331-2]
uc010zit.2. human. [P28331-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61100 mRNA. Translation: CAA43412.1.
AK295705 mRNA. Translation: BAG58551.1.
AK295987 mRNA. Translation: BAG58762.1.
AK298320 mRNA. Translation: BAG60573.1.
AK300585 mRNA. Translation: BAG62283.1.
AC007383 Genomic DNA. Translation: AAY15061.1.
CH471063 Genomic DNA. Translation: EAW70379.1.
BC022368 mRNA. Translation: AAH22368.1.
BC030833 mRNA. Translation: AAH30833.1.
CCDSiCCDS2366.1. [P28331-1]
CCDS56162.1. [P28331-4]
CCDS56163.1. [P28331-3]
CCDS56164.1. [P28331-5]
CCDS56165.1. [P28331-2]
PIRiS17854.
RefSeqiNP_001186910.1. NM_001199981.1. [P28331-5]
NP_001186911.1. NM_001199982.1. [P28331-3]
NP_001186912.1. NM_001199983.1. [P28331-4]
NP_001186913.1. NM_001199984.1. [P28331-2]
NP_004997.4. NM_005006.6. [P28331-1]
UniGeneiHs.471207.
Hs.598436.

3D structure databases

ProteinModelPortaliP28331.
SMRiP28331. Positions 31-636.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110799. 45 interactions.
IntActiP28331. 27 interactions.
MINTiMINT-3011123.
STRINGi9606.ENSP00000392709.

Chemistry

ChEMBLiCHEMBL2363065.

PTM databases

PhosphoSiteiP28331.

Polymorphism and mutation databases

BioMutaiNDUFS1.
DMDMi92090799.

2D gel databases

REPRODUCTION-2DPAGEIPI00604664.
P28331.
UCD-2DPAGEP28331.

Proteomic databases

MaxQBiP28331.
PaxDbiP28331.
PeptideAtlasiP28331.
PRIDEiP28331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233190; ENSP00000233190; ENSG00000023228.
ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
ENST00000449699; ENSP00000399912; ENSG00000023228.
ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
GeneIDi4719.
KEGGihsa:4719.
UCSCiuc002vbe.3. human. [P28331-1]
uc010ziq.2. human. [P28331-2]
uc010zit.2. human. [P28331-3]

Organism-specific databases

CTDi4719.
GeneCardsiGC02M206986.
HGNCiHGNC:7707. NDUFS1.
MIMi157655. gene.
252010. phenotype.
neXtProtiNX_P28331.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBiPA31518.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1034.
GeneTreeiENSGT00390000018768.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiP28331.
KOiK03934.
OMAiADCESMF.
OrthoDBiEOG783MTP.
PhylomeDBiP28331.
TreeFamiTF105756.

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.

Miscellaneous databases

ChiTaRSiNDUFS1. human.
GeneWikiiNDUFS1.
GenomeRNAii4719.
NextBioi18202.
PMAP-CutDBP28331.
PROiP28331.
SOURCEiSearch...

Gene expression databases

BgeeiP28331.
CleanExiHS_NDUFS1.
ExpressionAtlasiP28331. baseline and differential.
GenevisibleiP28331. HS.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase."
    Chow W., Ragan I., Robinson B.H.
    Eur. J. Biochem. 201:547-550(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-649.
  2. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
    Tissue: Hippocampus, Kidney and Substantia nigra.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-241.
    Tissue: Brain and Liver.
  6. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 185-200; 247-266; 277-289; 312-325; 361-382; 451-467; 471-499; 519-538; 544-557 AND 625-655, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency."
    Benit P., Chretien D., Kadhom N., de Lonlay-Debeney P., Cormier-Daire V., Cabral A., Peudenier S., Rustin P., Munnich A., Roetig A.
    Am. J. Hum. Genet. 68:1344-1352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MT-C1D TRP-241 AND GLY-252.
  11. "Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes."
    Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.
    J. Med. Genet. 49:234-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-253.

Entry informationi

Entry nameiNDUS1_HUMAN
AccessioniPrimary (citable) accession number: P28331
Secondary accession number(s): B4DIN9
, B4DJA0, B4DPG1, B4DUC1, E7ENF3, Q53TR8, Q8N1C4, Q8TCC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 7, 2006
Last modified: July 22, 2015
This is version 171 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.