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O43920 (NDUS5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
Alternative name(s):
Complex I-15 kDa
Short name=CI-15 kDa
NADH-ubiquinone oxidoreductase 15 kDa subunit
Gene names
Name:NDUFS5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length106 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in 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.

Subunit structure

Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme. Ref.4

Subcellular location

Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein Probable. Mitochondrion intermembrane space Potential.

Domain

Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds. Ref.6

Sequence similarities

Belongs to the complex I NDUFS5 subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 106105NADH dehydrogenase [ubiquinone] iron-sulfur protein 5
PRO_0000118786

Regions

Motif33 – 4311C-X9-C motif 1
Motif56 – 6611C-X9-C motif 2

Amino acid modifications

Disulfide bond33 ↔ 66 Potential
Disulfide bond43 ↔ 56 Potential

Natural variations

Natural variant961P → S Detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance. Ref.8
VAR_064569

Sequences

Sequence LengthMass (Da)Tools
O43920 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3D55402837DD99EE

FASTA10612,518
        10         20         30         40         50         60 
MPFLDIQKRF GLNIDRWLTI QSGEQPYKMA GRCHAFEKEW IECAHGIGYT RAEKECKIEY 

        70         80         90        100 
DDFVECLLRQ KTMRRAGTIR KQRDKLIKEG KYTPPPHHIG KGEPRP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[2]"The human NADH:ubiquinone oxidoreductase NDUFS5 (15 kDa) subunit: cDNA cloning, chromosomal localization, tissue distribution and the absence of mutations in isolated complex I-deficient patients."
Loeffen J., Smeets R., Smeitink J., Triepels R., Sengers R., Trijbels F., van den Heuvel L.
J. Inherit. Metab. Dis. 22:19-28(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Kidney.
[4]"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.
[5]"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].
[6]"NDUFB7 and NDUFA8 are located at the intermembrane surface of complex I."
Szklarczyk R., Wanschers B.F., Nabuurs S.B., Nouws J., Nijtmans L.G., Huynen M.A.
FEBS Lett. 585:737-743(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, MOTIF.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"High-throughput, pooled sequencing identifies mutations in NUBPL and FOXRED1 in human complex I deficiency."
Calvo S.E., Tucker E.J., Compton A.G., Kirby D.M., Crawford G., Burtt N.P., Rivas M., Guiducci C., Bruno D.L., Goldberger O.A., Redman M.C., Wiltshire E., Wilson C.J., Altshuler D., Gabriel S.B., Daly M.J., Thorburn D.R., Mootha V.K.
Nat. Genet. 42:851-858(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-96.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047434 mRNA. Translation: AAC39878.1.
AF020352 mRNA. Translation: AAB87866.1.
BC001884 mRNA. Translation: AAH01884.1.
RefSeqNP_001171908.1. NM_001184979.1.
NP_004543.1. NM_004552.2.
UniGeneHs.632385.

3D structure databases

ProteinModelPortalO43920.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110804. 2 interactions.
IntActO43920. 4 interactions.
MINTMINT-2796423.
STRING9606.ENSP00000362058.

Chemistry

ChEMBLCHEMBL2363065.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteO43920.

Proteomic databases

PaxDbO43920.
PeptideAtlasO43920.
PRIDEO43920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372967; ENSP00000362058; ENSG00000168653.
ENST00000372969; ENSP00000362060; ENSG00000168653.
GeneID4725.
KEGGhsa:4725.
UCSCuc001ccx.3. human.

Organism-specific databases

CTD4725.
GeneCardsGC01P039491.
HGNCHGNC:7712. NDUFS5.
HPAHPA042582.
MIM603847. gene.
neXtProtNX_O43920.
PharmGKBPA31522.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313534.
HOGENOMHOG000264236.
HOVERGENHBG001646.
InParanoidO43920.
KOK03938.
OMALRQKTMK.
OrthoDBEOG7C8GKB.
PhylomeDBO43920.
TreeFamTF332111.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO43920.
BgeeO43920.
CleanExHS_NDUFS5.
GenevestigatorO43920.

Family and domain databases

InterProIPR019342. NADH_UbQ_OxRdtase_FeS-su5.
[Graphical view]
PfamPF10200. Ndufs5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNDUFS5. human.
GeneWikiNDUFS5.
GenomeRNAi4725.
NextBio18222.
PROO43920.
SOURCESearch...

Entry information

Entry nameNDUS5_HUMAN
AccessionPrimary (citable) accession number: O43920
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 114 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 1

Human chromosome 1: entries, gene names and cross-references to MIM