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Protein

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9

Gene

Ndufb9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9
Alternative name(s):
Complex I-B22
Short name:
CI-B22
NADH-ubiquinone oxidoreductase B22 subunit
Gene namesi
Name:Ndufb9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1913468. Ndufb9.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial respiratory chain complex I Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 179178NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9PRO_0000174307Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei85 – 851PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQJ8.
MaxQBiQ9CQJ8.
PaxDbiQ9CQJ8.
PRIDEiQ9CQJ8.

PTM databases

iPTMnetiQ9CQJ8.
PhosphoSiteiQ9CQJ8.

Expressioni

Gene expression databases

BgeeiQ9CQJ8.
GenevisibleiQ9CQJ8. MM.

Interactioni

Subunit structurei

Mammalian complex I is composed of 45 different subunits.By similarity

Protein-protein interaction databases

BioGridi211305. 1 interaction.
IntActiQ9CQJ8. 2 interactions.
MINTiMINT-1844117.
STRINGi10090.ENSMUSP00000022980.

Family & Domainsi

Sequence similaritiesi

Belongs to the complex I LYR family.Curated

Phylogenomic databases

eggNOGiKOG3466. Eukaryota.
ENOG4111PES. LUCA.
GeneTreeiENSGT00390000005809.
HOGENOMiHOG000021684.
HOVERGENiHBG000418.
InParanoidiQ9CQJ8.
KOiK03965.
OMAiDYWHPSE.
OrthoDBiEOG7CNZH0.
PhylomeDBiQ9CQJ8.
TreeFamiTF315148.

Family and domain databases

InterProiIPR008011. Complex1_LYR.
IPR033034. NDUFB9.
[Graphical view]
PANTHERiPTHR12868:SF0. PTHR12868:SF0. 1 hit.
PfamiPF05347. Complex1_LYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFCAPPAYL THQQKVLRLY KRALRHLESW CIHRDKYRYF ACLMRARFEE
60 70 80 90 100
HKNEKDMMRA TQLLREAEEE FWQNQHPQPY IFPDSPGGTS FERYECYKVP
110 120 130 140 150
EWCLDYWHPS EKAMYPDYFS KREQWKKLRM ESWDREVKQL QEETSPDGIM
160 170
TEALPPARRE GDLPPLWWHI VTRPRERPT
Length:179
Mass (Da):21,984
Last modified:January 23, 2007 - v3
Checksum:i826692A25D5B9B78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002254 mRNA. Translation: BAB21968.1.
AK003540 mRNA. Translation: BAB22846.1.
AK004522 mRNA. Translation: BAB23345.1.
BC031539 mRNA. Translation: AAH31539.1.
CCDSiCCDS27495.1.
RefSeqiNP_075661.1. NM_023172.3.
UniGeneiMm.322294.

Genome annotation databases

EnsembliENSMUST00000022980; ENSMUSP00000022980; ENSMUSG00000022354.
GeneIDi66218.
KEGGimmu:66218.
UCSCiuc007vtw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002254 mRNA. Translation: BAB21968.1.
AK003540 mRNA. Translation: BAB22846.1.
AK004522 mRNA. Translation: BAB23345.1.
BC031539 mRNA. Translation: AAH31539.1.
CCDSiCCDS27495.1.
RefSeqiNP_075661.1. NM_023172.3.
UniGeneiMm.322294.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211305. 1 interaction.
IntActiQ9CQJ8. 2 interactions.
MINTiMINT-1844117.
STRINGi10090.ENSMUSP00000022980.

PTM databases

iPTMnetiQ9CQJ8.
PhosphoSiteiQ9CQJ8.

Proteomic databases

EPDiQ9CQJ8.
MaxQBiQ9CQJ8.
PaxDbiQ9CQJ8.
PRIDEiQ9CQJ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022980; ENSMUSP00000022980; ENSMUSG00000022354.
GeneIDi66218.
KEGGimmu:66218.
UCSCiuc007vtw.1. mouse.

Organism-specific databases

CTDi4715.
MGIiMGI:1913468. Ndufb9.

Phylogenomic databases

eggNOGiKOG3466. Eukaryota.
ENOG4111PES. LUCA.
GeneTreeiENSGT00390000005809.
HOGENOMiHOG000021684.
HOVERGENiHBG000418.
InParanoidiQ9CQJ8.
KOiK03965.
OMAiDYWHPSE.
OrthoDBiEOG7CNZH0.
PhylomeDBiQ9CQJ8.
TreeFamiTF315148.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiNdufb9. mouse.
PROiQ9CQJ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQJ8.
GenevisibleiQ9CQJ8. MM.

Family and domain databases

InterProiIPR008011. Complex1_LYR.
IPR033034. NDUFB9.
[Graphical view]
PANTHERiPTHR12868:SF0. PTHR12868:SF0. 1 hit.
PfamiPF05347. Complex1_LYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Kidney.
  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].
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 26-34; 39-45; 48-55; 99-121; 139-158 AND 160-175, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiNDUB9_MOUSE
AccessioniPrimary (citable) accession number: Q9CQJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.