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Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 5

Gene

NDUFS5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • NADH dehydrogenase (ubiquinone) activity Source: UniProtKB

GO - Biological processi

  • mitochondrial electron transport, NADH to ubiquinone Source: Reactome
  • mitochondrial respiratory chain complex I assembly Source: UniProtKB

Keywordsi

Biological processElectron transport, Respiratory chain, Transport

Enzyme and pathway databases

ReactomeiR-HSA-611105. Respiratory electron transport.
R-HSA-6799198. Complex I biogenesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NDUFS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000168653.10.
HGNCiHGNC:7712. NDUFS5.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi4725.
OpenTargetsiENSG00000168653.
PharmGKBiPA31522.

Chemistry databases

ChEMBLiCHEMBL2363065.
DrugBankiDB00157. NADH.

Polymorphism and mutation databases

BioMutaiNDUFS5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001187861 – 106NADH dehydrogenase [ubiquinone] iron-sulfur protein 5Add BLAST106

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 66PROSITE-ProRule annotation
Disulfide bondi43 ↔ 56PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiO43920.
PaxDbiO43920.
PeptideAtlasiO43920.
PRIDEiO43920.
TopDownProteomicsiO43920.

PTM databases

iPTMnetiO43920.
PhosphoSitePlusiO43920.

Expressioni

Gene expression databases

BgeeiENSG00000168653.
CleanExiHS_NDUFS5.
ExpressionAtlasiO43920. baseline and differential.
GenevisibleiO43920. HS.

Organism-specific databases

HPAiHPA042582.

Interactioni

Subunit structurei

Mammalian complex I is composed of 45 different subunits. This is a component of the iron-sulfur (IP) fragment of the enzyme.2 Publications

Protein-protein interaction databases

BioGridi110804. 81 interactors.
CORUMiO43920.
IntActiO43920. 56 interactors.
MINTiMINT-2796423.
STRINGi9606.ENSP00000362058.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5XTCelectron microscopy3.70h2-105[»]
5XTDelectron microscopy3.70h2-105[»]
5XTHelectron microscopy3.90h2-105[»]
5XTIelectron microscopy17.40Bh/h2-105[»]
ProteinModelPortaliO43920.
SMRiO43920.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 74CHCHPROSITE-ProRule annotationAdd BLAST45

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi33 – 43Cx9C motif 1PROSITE-ProRule annotationAdd BLAST11
Motifi56 – 66Cx9C motif 2PROSITE-ProRule annotationAdd BLAST11

Domaini

Contains two C-X9-C motifs that are predicted to form a helix-coil-helix structure, permitting the formation of intramolecular disulfide bonds.1 Publication

Sequence similaritiesi

Belongs to the complex I NDUFS5 subunit family.Curated

Phylogenomic databases

eggNOGiKOG4110. Eukaryota.
ENOG41123TD. LUCA.
GeneTreeiENSGT00390000002919.
HOGENOMiHOG000264236.
HOVERGENiHBG001646.
InParanoidiO43920.
KOiK03938.
OMAiFEDFYEC.
OrthoDBiEOG091G1CDO.
PhylomeDBiO43920.
TreeFamiTF332111.

Family and domain databases

InterProiView protein in InterPro
IPR019342. NADH_UbQ_OxRdtase_FeS-su5.
PfamiView protein in Pfam
PF10200. Ndufs5. 1 hit.
PROSITEiView protein in PROSITE
PS51808. CHCH. 1 hit.

Sequencei

Sequence statusi: Complete.

O43920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFLDIQKRF GLNIDRWLTI QSGEQPYKMA GRCHAFEKEW IECAHGIGYT
60 70 80 90 100
RAEKECKIEY DDFVECLLRQ KTMRRAGTIR KQRDKLIKEG KYTPPPHHIG

KGEPRP
Length:106
Mass (Da):12,518
Last modified:January 23, 2007 - v3
Checksum:i3D55402837DD99EE
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06456996P → S Detected in a patient with mitochondrial complex I deficiency; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201212110Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047434 mRNA. Translation: AAC39878.1.
AF020352 mRNA. Translation: AAB87866.1.
BC001884 mRNA. Translation: AAH01884.1.
CCDSiCCDS434.1.
RefSeqiNP_001171908.1. NM_001184979.1.
NP_004543.1. NM_004552.2.
UniGeneiHs.632385.

Genome annotation databases

EnsembliENST00000372967; ENSP00000362058; ENSG00000168653.
ENST00000372969; ENSP00000362060; ENSG00000168653.
GeneIDi4725.
KEGGihsa:4725.

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiNDUS5_HUMAN
AccessioniPrimary (citable) accession number: O43920
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 146 of the entry and version 3 of the sequence. See 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families