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Q9H845

- ACAD9_HUMAN

UniProt

Q9H845 - ACAD9_HUMAN

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Protein

Acyl-CoA dehydrogenase family member 9, mitochondrial

Gene

ACAD9

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

Functioni

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. Has little activity on octanoyl-CoA (C8:0), butyryl-CoA (C4:0) or isovaleryl-CoA (5:0).

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
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: Chromosome 3

Organism-specific databases

HGNCiHGNC:21497. ACAD9.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. dendrite Source: UniProtKB
  2. mitochondrion Source: LIFEdb
  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) [MIM:611126]: A metabolic disorder with variable manifestations that include dilated cardiomyopathy, liver failure, muscle weakness, neurologic dysfunction, hypoglycemia and Reye-like episodes (brain edema and vomiting that may rapidly progress to seizures, coma and death).1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

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).By similarity

Protein-protein interaction databases

BioGridi118799. 20 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.
OMAiHYLINGS.
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:March 1, 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 varianti477 – 4771R → Q.
Corresponds to variant rs4494951 [ dbSNP | Ensembl ].
VAR_033459

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 .
CCDSi CCDS3053.1.
PIRi JC7892.
RefSeqi NP_054768.2. NM_014049.4.
UniGenei Hs.567482.

3D structure databases

ProteinModelPortali Q9H845.
SMRi Q9H845. Positions 38-617.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118799. 20 interactions.
DIPi DIP-53699N.
IntActi Q9H845. 16 interactions.
STRINGi 9606.ENSP00000312618.

PTM databases

PhosphoSitei Q9H845.

Polymorphism databases

DMDMi 32469596.

Proteomic databases

MaxQBi Q9H845.
PaxDbi Q9H845.
PeptideAtlasi Q9H845.
PRIDEi Q9H845.

Protocols and materials databases

DNASUi 28976.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308982 ; ENSP00000312618 ; ENSG00000177646 .
GeneIDi 28976.
KEGGi hsa:28976.
UCSCi uc003ela.4. human.

Organism-specific databases

CTDi 28976.
GeneCardsi GC03P129047.
H-InvDB HIX0003659.
HGNCi HGNC:21497. ACAD9.
HPAi HPA037716.
HPA046720.
MIMi 611103. gene.
611126. phenotype.
neXtProti NX_Q9H845.
Orphaneti 99901. Acyl-CoA dehydrogenase 9 deficiency.
2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBi PA134900655.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00760000119007.
HOGENOMi HOG000131665.
HOVERGENi HBG050448.
InParanoidi Q9H845.
KOi K15980.
OMAi HYLINGS.
OrthoDBi EOG712TVX.
PhylomeDBi Q9H845.
TreeFami TF105053.

Enzyme and pathway databases

SABIO-RK Q9H845.

Miscellaneous databases

GeneWikii ACAD9.
GenomeRNAii 28976.
NextBioi 51851.
PROi Q9H845.
SOURCEi Search...

Gene expression databases

Bgeei Q9H845.
CleanExi HS_ACAD9.
ExpressionAtlasi Q9H845. baseline and differential.
Genevestigatori Q9H845.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. 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 ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(2002) [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(2004) [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(2004) [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(2007) [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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACAD9_HUMAN
AccessioniPrimary (citable) accession number: Q9H845
Secondary accession number(s): D3DNB8, Q8WXX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 125 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