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Protein

Acyl-CoA dehydrogenase family member 9, mitochondrial

Gene

ACAD9

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

Functioni

Required for mitochondrial complex I assembly (PubMed:20816094, PubMed:24158852). Has a dehydrogenase activity on palmitoyl-CoA (C16:0) and stearoyl-CoA (C18:0). It is three times more active on palmitoyl-CoA than on stearoyl-CoA. However, it does not play a primary role in long-chain fatty acid oxidation in vivo (PubMed:20816094, PubMed:24158852). Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0).2 Publications

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei426 – 4261Proton acceptorBy similarity

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro

GO - Biological processi

  1. mitochondrial respiratory chain complex I assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKQ9H845.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA dehydrogenase family member 9, mitochondrial (EC:1.3.99.-)
Short name:
ACAD-9
Gene namesi
Name:ACAD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:21497. ACAD9.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. dendrite Source: UniProtKB
  2. mitochondrion Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase family, member 9, deficiency (ACAD9 deficiency)7 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive metabolic disorder associated with mitochondrial complex I deficiency, resulting in multisystemic and variable manifestations. Clinical features include infantile onset of acute metabolic acidosis, Reye-like episodes (brain edema and vomiting that may rapidly progress to seizures, coma and death), exercise intolerance, hypertrophic cardiomyopathy, liver failure, muscle weakness, and neurologic dysfunction.

See also OMIM:611126
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441F → I in ACAD9 deficiency. 1 Publication
Corresponds to variant rs387907041 [ dbSNP | Ensembl ].
VAR_071892
Natural varianti127 – 1271R → K in ACAD9 deficiency. 1 Publication
VAR_071893
Natural varianti193 – 1931R → W in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs377547811 [ dbSNP | Ensembl ].
VAR_071894
Natural varianti220 – 2201A → V in ACAD9 deficiency. 1 Publication
VAR_071895
Natural varianti234 – 2341S → F in ACAD9 deficiency; unknown pathological significance. 1 Publication
VAR_071896
Natural varianti266 – 2661R → Q in ACAD9 deficiency. 1 Publication
Corresponds to variant rs387907042 [ dbSNP | Ensembl ].
VAR_071897
Natural varianti303 – 3031G → S in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs143383023 [ dbSNP | Ensembl ].
VAR_071898
Natural varianti326 – 3261A → T in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs115532916 [ dbSNP | Ensembl ].
VAR_071899
Natural varianti413 – 4131E → K in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs149753643 [ dbSNP | Ensembl ].
VAR_071900
Natural varianti414 – 4141R → C in ACAD9 deficiency. 1 Publication
VAR_071901
Natural varianti417 – 4171R → C in ACAD9 deficiency. 1 Publication
Corresponds to variant rs368949613 [ dbSNP | Ensembl ].
VAR_071902
Natural varianti469 – 4691R → W in ACAD9 deficiency. 1 Publication
Corresponds to variant rs139145143 [ dbSNP | Ensembl ].
VAR_071903
Natural varianti518 – 5181R → H in ACAD9 deficiency. 1 Publication
VAR_071904
Natural varianti532 – 5321R → W in ACAD9 deficiency. 3 Publications
Corresponds to variant rs377022708 [ dbSNP | Ensembl ].
VAR_071905

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi426 – 4261E → Q: Catalytically inactive. Does not affect mitochondrial complex I assembly. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi611126. phenotype.
Orphaneti99901. Acyl-CoA dehydrogenase 9 deficiency.
2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA134900655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 621Acyl-CoA dehydrogenase family member 9, mitochondrialPRO_0000000524
Transit peptidei1 – ?MitochondrionSequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-acetyllysine1 Publication
Modified residuei92 – 921N6-succinyllysineBy similarity
Modified residuei521 – 5211N6-acetyllysine; alternateBy similarity
Modified residuei521 – 5211N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9H845.
PaxDbiQ9H845.
PeptideAtlasiQ9H845.
PRIDEiQ9H845.

PTM databases

PhosphoSiteiQ9H845.

Expressioni

Tissue specificityi

Ubiquitously expressed in most normal human tissues and cancer cell lines with high level of expression in heart, skeletal muscles, brain, kidney and liver.1 Publication

Gene expression databases

BgeeiQ9H845.
CleanExiHS_ACAD9.
ExpressionAtlasiQ9H845. baseline and differential.
GenevestigatoriQ9H845.

Organism-specific databases

HPAiHPA037716.
HPA046720.

Interactioni

Subunit structurei

Part of the mitochondrial complex I assembly (MCIA) complex. The complex comprises at least TMEM126B, NDUFAF1, ECSIT, and ACAD9 (By similarity). Interacts with NDUFAF1 and ECSIT (PubMed:20816094).By similarity1 Publication

Protein-protein interaction databases

BioGridi118799. 19 interactions.
DIPiDIP-53699N.
IntActiQ9H845. 16 interactions.
STRINGi9606.ENSP00000312618.

Structurei

3D structure databases

ProteinModelPortaliQ9H845.
SMRiQ9H845. Positions 38-617.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131665.
HOVERGENiHBG050448.
InParanoidiQ9H845.
KOiK15980.
OMAiVPASEGH.
OrthoDBiEOG712TVX.
PhylomeDBiQ9H845.
TreeFamiTF105053.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H845-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGCGLFLRT TAAARACRGL VVSTANRRLL RTSPPVRAFA KELFLGKIKK
60 70 80 90 100
KEVFPFPEVS QDELNEINQF LGPVEKFFTE EVDSRKIDQE GKIPDETLEK
110 120 130 140 150
LKSLGLFGLQ VPEEYGGLGF SNTMYSRLGE IISMDGSITV TLAAHQAIGL
160 170 180 190 200
KGIILAGTEE QKAKYLPKLA SGEHIAAFCL TEPASGSDAA SIRSRATLSE
210 220 230 240 250
DKKHYILNGS KVWITNGGLA NIFTVFAKTE VVDSDGSVKD KITAFIVERD
260 270 280 290 300
FGGVTNGKPE DKLGIRGSNT CEVHFENTKI PVENILGEVG DGFKVAMNIL
310 320 330 340 350
NSGRFSMGSV VAGLLKRLIE MTAEYACTRK QFNKRLSEFG LIQEKFALMA
360 370 380 390 400
QKAYVMESMT YLTAGMLDQP GFPDCSIEAA MVKVFSSEAA WQCVSEALQI
410 420 430 440 450
LGGLGYTRDY PYERILRDTR ILLIFEGTNE ILRMYIALTG LQHAGRILTT
460 470 480 490 500
RIHELKQAKV STVMDTVGRR LRDSLGRTVD LGLTGNHGVV HPSLADSANK
510 520 530 540 550
FEENTYCFGR TVETLLLRFG KTIMEEQLVL KRVANILINL YGMTAVLSRA
560 570 580 590 600
SRSIRIGLRN HDHEVLLANT FCVEAYLQNL FSLSQLDKYA PENLDEQIKK
610 620
VSQQILEKRA YICAHPLDRT C
Length:621
Mass (Da):68,760
Last modified:February 28, 2001 - v1
Checksum:i064BCE0378877F54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971A → V in AAL56011 (PubMed:12359260).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441F → I in ACAD9 deficiency. 1 Publication
Corresponds to variant rs387907041 [ dbSNP | Ensembl ].
VAR_071892
Natural varianti127 – 1271R → K in ACAD9 deficiency. 1 Publication
VAR_071893
Natural varianti193 – 1931R → W in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs377547811 [ dbSNP | Ensembl ].
VAR_071894
Natural varianti220 – 2201A → V in ACAD9 deficiency. 1 Publication
VAR_071895
Natural varianti234 – 2341S → F in ACAD9 deficiency; unknown pathological significance. 1 Publication
VAR_071896
Natural varianti266 – 2661R → Q in ACAD9 deficiency. 1 Publication
Corresponds to variant rs387907042 [ dbSNP | Ensembl ].
VAR_071897
Natural varianti303 – 3031G → S in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs143383023 [ dbSNP | Ensembl ].
VAR_071898
Natural varianti326 – 3261A → T in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs115532916 [ dbSNP | Ensembl ].
VAR_071899
Natural varianti413 – 4131E → K in ACAD9 deficiency; unknown pathological significance. 1 Publication
Corresponds to variant rs149753643 [ dbSNP | Ensembl ].
VAR_071900
Natural varianti414 – 4141R → C in ACAD9 deficiency. 1 Publication
VAR_071901
Natural varianti417 – 4171R → C in ACAD9 deficiency. 1 Publication
Corresponds to variant rs368949613 [ dbSNP | Ensembl ].
VAR_071902
Natural varianti469 – 4691R → W in ACAD9 deficiency. 1 Publication
Corresponds to variant rs139145143 [ dbSNP | Ensembl ].
VAR_071903
Natural varianti477 – 4771R → Q.
Corresponds to variant rs4494951 [ dbSNP | Ensembl ].
VAR_033459
Natural varianti518 – 5181R → H in ACAD9 deficiency. 1 Publication
VAR_071904
Natural varianti532 – 5321R → W in ACAD9 deficiency. 3 Publications
Corresponds to variant rs377022708 [ dbSNP | Ensembl ].
VAR_071905

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327351 mRNA. Translation: AAL56011.1.
AK024012 mRNA. Translation: BAB14775.1.
CH471052 Genomic DNA. Translation: EAW79295.1.
CH471052 Genomic DNA. Translation: EAW79296.1.
BC013354 mRNA. Translation: AAH13354.1.
BC007970 mRNA. Translation: AAH07970.1.
CCDSiCCDS3053.1.
PIRiJC7892.
RefSeqiNP_054768.2. NM_014049.4.
UniGeneiHs.567482.

Genome annotation databases

EnsembliENST00000308982; ENSP00000312618; ENSG00000177646.
GeneIDi28976.
KEGGihsa:28976.
UCSCiuc003ela.4. human.

Polymorphism databases

DMDMi32469596.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF327351 mRNA. Translation: AAL56011.1.
AK024012 mRNA. Translation: BAB14775.1.
CH471052 Genomic DNA. Translation: EAW79295.1.
CH471052 Genomic DNA. Translation: EAW79296.1.
BC013354 mRNA. Translation: AAH13354.1.
BC007970 mRNA. Translation: AAH07970.1.
CCDSiCCDS3053.1.
PIRiJC7892.
RefSeqiNP_054768.2. NM_014049.4.
UniGeneiHs.567482.

3D structure databases

ProteinModelPortaliQ9H845.
SMRiQ9H845. Positions 38-617.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118799. 19 interactions.
DIPiDIP-53699N.
IntActiQ9H845. 16 interactions.
STRINGi9606.ENSP00000312618.

PTM databases

PhosphoSiteiQ9H845.

Polymorphism databases

DMDMi32469596.

Proteomic databases

MaxQBiQ9H845.
PaxDbiQ9H845.
PeptideAtlasiQ9H845.
PRIDEiQ9H845.

Protocols and materials databases

DNASUi28976.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308982; ENSP00000312618; ENSG00000177646.
GeneIDi28976.
KEGGihsa:28976.
UCSCiuc003ela.4. human.

Organism-specific databases

CTDi28976.
GeneCardsiGC03P129047.
H-InvDBHIX0003659.
HGNCiHGNC:21497. ACAD9.
HPAiHPA037716.
HPA046720.
MIMi611103. gene.
611126. phenotype.
neXtProtiNX_Q9H845.
Orphaneti99901. Acyl-CoA dehydrogenase 9 deficiency.
2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA134900655.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131665.
HOVERGENiHBG050448.
InParanoidiQ9H845.
KOiK15980.
OMAiVPASEGH.
OrthoDBiEOG712TVX.
PhylomeDBiQ9H845.
TreeFamiTF105053.

Enzyme and pathway databases

SABIO-RKQ9H845.

Miscellaneous databases

GeneWikiiACAD9.
GenomeRNAii28976.
NextBioi51851.
PROiQ9H845.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H845.
CleanExiHS_ACAD9.
ExpressionAtlasiQ9H845. baseline and differential.
GenevestigatoriQ9H845.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional characterization of ACAD-9, a novel member of human acyl-CoA dehydrogenase family."
    Zhang J., Zhang W., Zou D., Chen G., Wan T., Zhang M., Cao X.
    Biochem. Biophys. Res. Commun. 297:1033-1042(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.
    Tissue: Dendritic cell.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Uterus.
  5. "A new genetic disorder in mitochondrial fatty acid beta-oxidation: ACAD9 deficiency."
    He M., Rutledge S.L., Kelly D.R., Palmer C.A., Murdoch G., Majumder N., Nicholls R.D., Pei Z., Watkins P.A., Vockley J.
    Am. J. Hum. Genet. 81:87-103(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NDUFAF1 AND ECSIT, INVOLVEMENT IN ACAD9 DEFICIENCY, VARIANTS ACAD9 DEFICIENCY LYS-413 AND HIS-518.
  8. Cited for: INVOLVEMENT IN ACAD9 DEFICIENCY, VARIANTS ACAD9 DEFICIENCY ILE-44; TRP-193; PHE-234; GLN-266; SER-303; THR-326; CYS-417 AND TRP-532.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "ACAD9, a complex I assembly factor with a moonlighting function in fatty acid oxidation deficiencies."
    Nouws J., Te Brinke H., Nijtmans L.G., Houten S.M.
    Hum. Mol. Genet. 23:1311-1319(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-426.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Riboflavin-responsive oxidative phosphorylation complex I deficiency caused by defective ACAD9: new function for an old gene."
    Gerards M., van den Bosch B.J., Danhauser K., Serre V., van Weeghel M., Wanders R.J., Nicolaes G.A., Sluiter W., Schoonderwoerd K., Scholte H.R., Prokisch H., Rotig A., de Coo I.F., Smeets H.J.
    Brain 134:210-219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ACAD9 DEFICIENCY LYS-127; TRP-469 AND TRP-532.
  13. Cited for: VARIANT ACAD9 DEFICIENCY TRP-532.
  14. Cited for: VARIANT ACAD9 DEFICIENCY CYS-414.
  15. "A patient with complex I deficiency caused by a novel ACAD9 mutation not responding to riboflavin treatment."
    Nouws J., Wibrand F., van den Brand M., Venselaar H., Duno M., Lund A.M., Trautner S., Nijtmans L., Ostergard E.
    JIMD Rep. 12:37-45(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACAD9 DEFICIENCY VAL-220.

Entry informationi

Entry nameiACAD9_HUMAN
AccessioniPrimary (citable) accession number: Q9H845
Secondary accession number(s): D3DNB8, Q8WXX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 2, 2003
Last sequence update: February 28, 2001
Last modified: March 3, 2015
This is version 127 of the entry and version 1 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.