Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28331 (NDUS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NDUFS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length727 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. 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.

Catalytic activity

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

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Binds 2 4Fe-4S clusters per subunit By similarity.

Subunit structure

Complex I is composed of 45 different subunits. Ref.7

Subcellular location

Mitochondrion inner membrane.

Involvement in disease

Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Ligand2Fe-2S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP metabolic process

Inferred from mutant phenotype PubMed 15186778. Source: UniProtKB

apoptotic mitochondrial changes

Inferred from direct assay PubMed 15186778. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

cellular respiration

Inferred from mutant phenotype PubMed 15186778PubMed 16478720. Source: UniProtKB

mitochondrial electron transport, NADH to ubiquinone

Non-traceable author statement PubMed 9878551. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 15186778PubMed 16478720PubMed 16870178. Source: UniProtKB

regulation of mitochondrial membrane potential

Inferred from mutant phenotype PubMed 15186778PubMed 16478720. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial intermembrane space

Inferred from direct assay PubMed 15186778. Source: UniProtKB

mitochondrial respiratory chain complex I

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Non-traceable author statement PubMed 9878551. Source: UniProtKB

electron carrier activity

Non-traceable author statement Ref.1. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28331-1)

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.
Isoform 2 (identifier: P28331-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRIRGSSGTLSRINM
Note: No experimental confirmation available.
Isoform 3 (identifier: P28331-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ML → MW
     3-113: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P28331-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P28331-5)

The sequence of this isoform differs from the canonical sequence as follows:
     52-87: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
PRO_0000019968

Regions

Domain30 – 108792Fe-2S ferredoxin-type
Domain245 – 301574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding641Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding751Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding781Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding921Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1241Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1281Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1311Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1371Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1761Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1791Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2261Iron-sulfur 3 (4Fe-4S) By similarity

Amino acid modifications

Modified residue841N6-acetyllysine By similarity
Modified residue4671N6-acetyllysine By similarity
Modified residue4991N6-acetyllysine By similarity
Modified residue7091N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 5757Missing in isoform 4.
VSP_043727
Alternative sequence1 – 22ML → MW in isoform 3.
VSP_043728
Alternative sequence11M → MRIRGSSGTLSRINM in isoform 2.
VSP_042682
Alternative sequence3 – 113111Missing in isoform 3.
VSP_043729
Alternative sequence52 – 8736Missing in isoform 5.
VSP_045864
Natural variant2411R → Q. Ref.5
Corresponds to variant rs17856901 [ dbSNP | Ensembl ].
VAR_025511
Natural variant2411R → W in MT-C1D. Ref.9
VAR_019532
Natural variant2521D → G in MT-C1D. Ref.9
VAR_019533
Natural variant2531V → G. Ref.10
VAR_069506
Natural variant6491V → F. Ref.1
Corresponds to variant rs1044049 [ dbSNP | Ensembl ].
VAR_018463

Experimental info

Sequence conflict81K → R in CAA43412. Ref.1
Sequence conflict4171R → W in CAA43412. Ref.1
Sequence conflict5721H → L in BAG58551. Ref.2
Sequence conflict6911I → L in CAA43412. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 9C35F4B8294771FB

FASTA72779,468
        10         20         30         40         50         60 
MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 

        70         80         90        100        110        120 
PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 

       130        140        150        160        170        180 
LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 

       190        200        210        220        230        240 
RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA 

       250        260        270        280        290        300 
RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 

       310        320        330        340        350        360 
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR 

       370        380        390        400        410        420 
VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 

       430        440        450        460        470        480 
SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 

       490        500        510        520        530        540 
LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 

       550        560        570        580        590        600 
PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 

       610        620        630        640        650        660 
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 

       670        680        690        700        710        720 
GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA 


VEEPSIC 

« Hide

Isoform 2 [UniParc].

Checksum: EB7CA8F41E3DF6E2
Show »

FASTA74180,997
Isoform 3 [UniParc].

Checksum: 16CA2EF571877D03
Show »

FASTA61667,524
Isoform 4 [UniParc].

Checksum: C8B37BF8C954187F
Show »

FASTA67073,527
Isoform 5 [UniParc].

Checksum: 522872E0D6EB9E09
Show »

FASTA69175,375

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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.
[10]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS17854.
RefSeqNP_001186910.1. NM_001199981.1.
NP_001186911.1. NM_001199982.1.
NP_001186912.1. NM_001199983.1.
NP_001186913.1. NM_001199984.1.
NP_004997.4. NM_005006.6.
UniGeneHs.471207.
Hs.598436.

3D structure databases

ProteinModelPortalP28331.
SMRP28331. Positions 31-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110799. 36 interactions.
IntActP28331. 12 interactions.
MINTMINT-3011123.
STRING9606.ENSP00000233190.

Chemistry

ChEMBLCHEMBL2363065.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP28331.

Polymorphism databases

DMDM92090799.

2D gel databases

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

Proteomic databases

PaxDbP28331.
PeptideAtlasP28331.
PRIDEP28331.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233190; ENSP00000233190; ENSG00000023228. [P28331-1]
ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
ENST00000449699; ENSP00000399912; ENSG00000023228. [P28331-1]
ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
GeneID4719.
KEGGhsa:4719.
UCSCuc002vbe.3. human. [P28331-1]
uc010ziq.2. human. [P28331-2]
uc010zit.2. human. [P28331-3]

Organism-specific databases

CTD4719.
GeneCardsGC02M206986.
HGNCHGNC:7707. NDUFS1.
MIM157655. gene.
252010. phenotype.
neXtProtNX_P28331.
Orphanet2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBPA31518.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1034.
HOGENOMHOG000031442.
HOVERGENHBG003482.
InParanoidP28331.
KOK03934.
OMAMPVMKGM.
OrthoDBEOG783MTP.
PhylomeDBP28331.
TreeFamTF105756.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP28331.
BgeeP28331.
CleanExHS_NDUFS1.
GenevestigatorP28331.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 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]
PfamPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 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]
ProtoNetSearch...

Other

ChiTaRSNDUFS1. human.
GeneWikiNDUFS1.
GenomeRNAi4719.
NextBio18202.
PMAP-CutDBP28331.
PROP28331.
SOURCESearch...

Entry information

Entry nameNDUS1_HUMAN
AccessionPrimary (citable) accession number: P28331
Secondary accession number(s): B4DIN9 expand/collapse secondary AC list , B4DJA0, B4DPG1, B4DUC1, E7ENF3, Q53TR8, Q8N1C4, Q8TCC9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM