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

P19404 (NDUV2_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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial

EC=1.6.5.3
EC=1.6.99.3
Alternative name(s):
NADH-ubiquinone oxidoreductase 24 kDa subunit
Gene names
Name:NDUFV2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 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.

Catalytic activity

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

NADH + acceptor = NAD+ + reduced acceptor.

Cofactor

Binds 1 2Fe-2S cluster Potential.

Subunit structure

Complex I is composed of 45 different subunits. This is a component of the flavoprotein-sulfur (FP) fragment of the enzyme. Ref.3

Subcellular location

Mitochondrion inner membrane.

Sequence similarities

Belongs to the complex I 24 kDa subunit family.

Ontologies

Keywords
   Biological processElectron transport
Respiratory chain
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Ligand2Fe-2S
Iron
Iron-sulfur
Metal-binding
NAD
Ubiquinone
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle tissue development

Inferred from mutant phenotype PubMed 12754703. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial electron transport, NADH to ubiquinone

Inferred from mutant phenotype PubMed 12754703. Source: UniProtKB

nervous system development

Inferred from mutant phenotype PubMed 9570948. 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 respiratory chain complex I

Inferred from direct assay Ref.3. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 12754703. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

NADH dehydrogenase (ubiquinone) activity

Inferred from mutant phenotype PubMed 12754703. Source: UniProtKB

electron carrier activity

Non-traceable author statement PubMed 7488192. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3232Mitochondrion
Chain33 – 249217NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial
PRO_0000020003

Sites

Metal binding1351Iron-sulfur (2Fe-2S) Potential
Metal binding1401Iron-sulfur (2Fe-2S) Potential
Metal binding1761Iron-sulfur (2Fe-2S) Potential
Metal binding1801Iron-sulfur (2Fe-2S) Potential

Amino acid modifications

Modified residue611N6-acetyllysine By similarity
Modified residue1931Phosphotyrosine; by SRC Ref.5

Natural variations

Natural variant291V → A. Ref.1
Corresponds to variant rs906807 [ dbSNP | Ensembl ].
VAR_016167

Sequences

Sequence LengthMass (Da)Tools
P19404 [UniParc].

Last modified May 2, 2002. Version 2.
Checksum: AAF46ABB0908B177

FASTA24927,392
        10         20         30         40         50         60 
MFFSAALRAR AAGLTAHWGR HVRNLHKTVM QNGAGGALFV HRDTPENNPD TPFDFTPENY 

        70         80         90        100        110        120 
KRIEAIVKNY PEGHKAAAVL PVLDLAQRQN GWLPISAMNK VAEVLQVPPM RVYEVATFYT 

       130        140        150        160        170        180 
MYNRKPVGKY HIQVCTTTPC MLRNSDSILE AIQKKLGIKV GETTPDKLFT LIEVECLGAC 

       190        200        210        220        230        240 
VNAPMVQIND NYYEDLTAKD IEEIIDELKA GKIPKPGPRS GRFSCEPAGG LTSLTEPPKG 


PGFGVQAGL 

« Hide

References

« Hide 'large scale' references
[1]"Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit."
Pilkington S.J., Walker J.E.
Biochemistry 28:3257-3264(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-29.
[2]"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: Lung.
[3]"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.
[4]"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].
[5]"Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components."
Ogura M., Yamaki J., Homma M.K., Homma Y.
Biochem. J. 447:281-289(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-193.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22538 mRNA. Translation: AAA75390.1.
BC001632 mRNA. Translation: AAH01632.1.
BC017487 mRNA. Translation: AAH17487.1.
PIRA30113.
RefSeqNP_066552.2. NM_021074.4.
UniGeneHs.464572.

3D structure databases

ProteinModelPortalP19404.
SMRP19404. Positions 63-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110807. 30 interactions.
IntActP19404. 8 interactions.
MINTMINT-4991740.
STRING9606.ENSP00000327268.

Chemistry

ChEMBLCHEMBL2363065.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP19404.

Polymorphism databases

DMDM20455499.

2D gel databases

SWISS-2DPAGEP19404.
UCD-2DPAGEP19404.

Proteomic databases

PaxDbP19404.
PRIDEP19404.

Protocols and materials databases

DNASU4729.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318388; ENSP00000327268; ENSG00000178127.
GeneID4729.
KEGGhsa:4729.
UCSCuc002knu.3. human.

Organism-specific databases

CTD4729.
GeneCardsGC18P009092.
HGNCHGNC:7717. NDUFV2.
HPAHPA003404.
MIM600532. gene.
neXtProtNX_P19404.
Orphanet2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBPA31527.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1905.
HOGENOMHOG000257748.
HOVERGENHBG029601.
KOK03943.
PhylomeDBP19404.
TreeFamTF300004.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeP19404.
CleanExHS_NDUFV2.
GenevestigatorP19404.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR002023. NuoE-like.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERPTHR10371. PTHR10371. 1 hit.
PfamPF01257. 2Fe-2S_thioredx. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR01958. nuoE_fam. 1 hit.
PROSITEPS01099. COMPLEX1_24K. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNDUFV2. human.
GeneWikiNDUFV2.
GenomeRNAi4729.
NextBio18234.
PROP19404.
SOURCESearch...

Entry information

Entry nameNDUV2_HUMAN
AccessionPrimary (citable) accession number: P19404
Secondary accession number(s): Q9BV41
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 2, 2002
Last modified: April 16, 2014
This is version 157 of the entry and version 2 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 18

Human chromosome 18: entries, gene names and cross-references to MIM