NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial precursor

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Q16795 (NDUA9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

Alternative name(s):
Complex I-39kD
Short name=CI-39kD
NADH-ubiquinone oxidoreductase 39 kDa subunit

Gene names

Name:	NDUFA9
Synonyms:	NDUFS2L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Cofactor	Binds 1 FAD per subunit.
Subunit structure	Complex I is composed of 45 different subunits. This a component of the hydrophobic protein fraction. Interacts with BLOC1S1. Interacts with SLC2A4 By similarity. Ref.5 Ref.7
Subcellular location	Mitochondrion matrix.
Post-translational modification	Acetylated on lysine residues. BLOC1S1 is required for acetylation.
Sequence similarities	Belongs to the complex I NDUFA9 subunit family.
Sequence caution	The sequence CAA54099.1 differs from that shown. Reason: Frameshift at position 18.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, NADH to ubiquinone Non-traceable author statement PubMed 9878551. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome sodium ion transport Non-traceable author statement Ref.4. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from direct assay Ref.4. Source: UniProtKB mitochondrial respiratory chain complex I Inferred from direct assay Ref.5 PubMed 17209039 PubMed 9878551. Source: UniProtKB
Molecular_function	NADH dehydrogenase (ubiquinone) activity Non-traceable author statement Ref.4 PubMed 9878551. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLOC1S1	P78537	3	EBI-1045087,EBI-348630
NOA1	Q8NC60	2	EBI-1045087,EBI-717871

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

Mitochondrion By similarity

Chain

36 – 377

342

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

PRO_0000019992

Amino acid modifications

Modified residue

370

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q16795 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 66A1CC7FCE86DD0E
Show »

FASTA

377

42,510

        10         20         30         40         50         60 
MAAAAQSRVV RVLSMSRSAI TAIATSVCHG PPCRQLHHAL MPHGKGGRSS VSGIVATVFG 

        70         80         90        100        110        120 
ATGFLGRYVV NHLGRMGSQV IIPYRCDKYD IMHLRPMGDL GQLLFLEWDA RDKDSIRRVV 

       130        140        150        160        170        180 
QHSNVVINLI GRDWETKNFD FEDVFVKIPQ AIAQLSKEAG VEKFIHVSHL NANIKSSSRY 

       190        200        210        220        230        240 
LRNKAVGEKV VRDAFPEAII VKPSDIFGRE DRFLNSFASM HRFGPIPLGS LGWKTVKQPV 

       250        260        270        280        290        300 
YVVDVSKGIV NAVKDPDANG KSFAFVGPSR YLLFHLVKYI FAVAHRLFLP FPLPLFAYRW 

       310        320        330        340        350        360 
VARVFEISPF EPWITRDKVE RMHITDMKLP HLPGLEDLGI QATPLELKAI EVLRRHRTYR 

       370 
WLSAEIEDVK PAKTVNI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"39 kDa subunit of NADH-ubiquinone oxidoreductase." Loeffen J.L.C.M., Smeets R.J.P., Triepels R., Ruitenbeek W., Smeitink J.A.M., van den Heuvel L. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Colon, Muscle and Skeletal muscle.
[3]	"Purification of CpG islands using a methylated DNA binding column." Cross S.H., Charlton J.A., Nan X., Bird A.P. Nat. Genet. 6:236-244(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33. Tissue: Blood.
[4]	"Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid." Baens M., Chaffanet M., Cassiman J.-J., van den Berghe H., Marynen P. Genomics 16:214-218(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-377. Tissue: Liver.
[5]	"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: MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
[6]	"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].
[7]	"Identification of a molecular component of the mitochondrial acetyl transferase program; a novel role for GCN5L1." Scott I., Webster B.R., Li J.H., Sack M.N. Biochem. J. 443:655-661(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BLOC1S1, ACETYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF050641 mRNA. Translation: AAD42055.1. BC009311 mRNA. Translation: AAH09311.1. BC015837 mRNA. Translation: AAH15837.1. BC111546 mRNA. Translation: AAI11547.1. X76665 Genomic DNA. Translation: CAA54099.1. Frameshift. L04490 mRNA. Translation: AAA36350.1.
IPI	IPI00003968.
PIR	I37258.
RefSeq	NP_004993.1. NM_005002.4.
UniGene	Hs.75227.
3D structure databases
ProteinModelPortal	Q16795.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-38526N.
IntAct	Q16795. 10 interactions.
STRING	9606.ENSP00000266544.
PTM databases
PhosphoSite	Q16795.
Polymorphism databases
DMDM	2833280.
Proteomic databases
PaxDb	Q16795.
PRIDE	Q16795.
Protocols and materials databases
DNASU	4704.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266544; ENSP00000266544; ENSG00000139180.
GeneID	4704.
KEGG	hsa:4704.
UCSC	uc001qnc.3. human.
Organism-specific databases
CTD	4704.
GeneCards	GC12P004714.
HGNC	HGNC:7693. NDUFA9.
HPA	HPA042268.
MIM	603834. gene.
neXtProt	NX_Q16795.
Orphanet	2609. Isolated NADH-CoQ reductase deficiency.
PharmGKB	PA31499.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0702.
HOGENOM	HOG000168008.
HOVERGEN	HBG006546.
InParanoid	Q16795.
KO	K03953.
OMA	YIYAVAH.
OrthoDB	EOG4RJG1Z.
PhylomeDB	Q16795.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q16795.
Bgee	Q16795.
CleanEx	HS_NDUFA9.
Genevestigator	Q16795.
GermOnline	ENSG00000139180. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00157. NADH.
GenomeRNAi	4704.
NextBio	18140.
SOURCE	Search...

Entry information

Entry name

NDUA9_HUMAN

Accession

Primary (citable) accession number: Q16795
Secondary accession number(s): Q14076, Q2NKX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

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Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents