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Q9UKU7

- ACAD8_HUMAN

UniProt

Q9UKU7 - ACAD8_HUMAN

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Protein

Isobutyryl-CoA dehydrogenase, mitochondrial

Gene

ACAD8

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

Functioni

Has very high activity toward isobutyryl-CoA. Is an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Plays a role in transcriptional coactivation within the ARC complex.1 Publication

Catalytic activityi

Isobutyryl-CoA + ETF = methylacrylyl-CoA + reduced ETF.

Cofactori

FAD.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygen
Binding sitei302 – 3021FAD; shared with dimeric partner1 Publication
Active sitei398 – 3981Proton acceptor
Binding sitei399 – 3991Substrate; via amide nitrogen
Binding sitei410 – 4101Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD1 Publication
Nucleotide bindingi191 – 1933FAD1 Publication
Nucleotide bindingi312 – 3132FAD; shared with dimeric partner1 Publication
Nucleotide bindingi371 – 3755FAD; shared with dimeric partner1 Publication
Nucleotide bindingi400 – 4023FAD1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. lipid metabolic process Source: ProtInc
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. small molecule metabolic process Source: Reactome
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. valine catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Activator, Oxidoreductase

Keywords - Biological processi

Branched-chain amino acid catabolism, Transcription, Transcription regulation

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_197. Branched-chain amino acid catabolism.
UniPathwayiUPA00362.

Names & Taxonomyi

Protein namesi
Recommended name:
Isobutyryl-CoA dehydrogenase, mitochondrial (EC:1.3.99.-)
Alternative name(s):
Activator-recruited cofactor 42 kDa component
Short name:
ARC42
Acyl-CoA dehydrogenase family member 8
Short name:
ACAD-8
Gene namesi
Name:ACAD8
Synonyms:ARC42, IBD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:87. ACAD8.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Isobutyryl-CoA dehydrogenase deficiency (IBDD) [MIM:611283]: The symptoms of IBDD generally appear until late in infancy or in childhood and can include poor feeding and growth (failure to thrive), a weakened and enlarged heart (dilated cardiomyopathy), seizures, and low numbers of red blood cells (anemia).3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281M → I in IBDD. 1 Publication
VAR_035071
Natural varianti134 – 1341D → Y in IBDD. 1 Publication
VAR_035072
Natural varianti137 – 1371G → R in IBDD; complete loss of activity. 1 Publication
VAR_035073
Natural varianti152 – 1521M → T in IBDD. 1 Publication
VAR_035074
Natural varianti203 – 2031V → I in IBDD. 1 Publication
VAR_035075
Natural varianti302 – 3021R → Q in IBDD; complete loss of activity. 2 Publications
VAR_035076
Natural varianti320 – 3201A → T in IBDD; <20% of wild-type activity. 1 Publication
VAR_035077
Natural varianti334 – 3341R → C in IBDD. 1 Publication
VAR_035078
Natural varianti385 – 3851Q → R in IBDD. 1 Publication
VAR_035079

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi611283. phenotype.
Orphaneti79159. Isobutyryl-CoA dehydrogenase deficiency.
PharmGKBiPA24423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2222MitochondrionSequence AnalysisAdd
BLAST
Chaini23 – 415393Isobutyryl-CoA dehydrogenase, mitochondrialPRO_0000000522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6-acetyllysine; alternateBy similarity
Modified residuei50 – 501N6-succinyllysine; alternateBy similarity
Modified residuei213 – 2131N6-succinyllysineBy similarity
Modified residuei231 – 2311N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UKU7.
PaxDbiQ9UKU7.
PRIDEiQ9UKU7.

2D gel databases

UCD-2DPAGEQ9UKU7.

PTM databases

PhosphoSiteiQ9UKU7.

Expressioni

Tissue specificityi

Detected at comparable levels in all tissues examined (heart, lung, brain, skeletal muscle, pancreas and placenta). Weakly expressed in liver and kidney.

Gene expression databases

BgeeiQ9UKU7.
CleanExiHS_ACAD8.
ExpressionAtlasiQ9UKU7. baseline and differential.
GenevestigatoriQ9UKU7.

Organism-specific databases

HPAiHPA040689.
HPA043903.

Interactioni

Subunit structurei

Homotetramer, formed by a dimer of dimers. Subunit of the large multiprotein complex ARC/DRIP.3 Publications

Protein-protein interaction databases

BioGridi117965. 6 interactions.
IntActiQ9UKU7. 3 interactions.
STRINGi9606.ENSP00000281182.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni37 – 404Combined sources
Helixi43 – 5917Combined sources
Turni60 – 634Combined sources
Helixi64 – 707Combined sources
Helixi75 – 839Combined sources
Helixi93 – 953Combined sources
Helixi102 – 11312Combined sources
Helixi117 – 13620Combined sources
Helixi139 – 15012Combined sources
Beta strandi156 – 1594Combined sources
Beta strandi165 – 1684Combined sources
Helixi169 – 1713Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi182 – 19312Combined sources
Turni194 – 1974Combined sources
Beta strandi199 – 21113Combined sources
Helixi212 – 2143Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi227 – 2293Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi243 – 25412Combined sources
Helixi255 – 2573Combined sources
Beta strandi258 – 2614Combined sources
Helixi265 – 30137Combined sources
Helixi309 – 3113Combined sources
Helixi313 – 34129Combined sources
Helixi347 – 37226Combined sources
Helixi373 – 3786Combined sources
Helixi384 – 39310Combined sources
Turni394 – 3963Combined sources
Beta strandi397 – 3993Combined sources
Helixi401 – 41414Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RX0X-ray1.77A/B/C/D24-415[»]
ProteinModelPortaliQ9UKU7.
SMRiQ9UKU7. Positions 32-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UKU7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 2774Substrate binding

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiQ9UKU7.
KOiK11538.
OMAiWRAQETR.
OrthoDBiEOG74FF0S.
PhylomeDBiQ9UKU7.
TreeFamiTF105052.

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. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UKU7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLWSGCRRFG ARLGCLPGGL RVLVQTGHRS LTSCIDPSMG LNEEQKEFQK
60 70 80 90 100
VAFDFAAREM APNMAEWDQK ELFPVDVMRK AAQLGFGGVY IQTDVGGSGL
110 120 130 140 150
SRLDTSVIFE ALATGCTSTT AYISIHNMCA WMIDSFGNEE QRHKFCPPLC
160 170 180 190 200
TMEKFASYCL TEPGSGSDAA SLLTSAKKQG DHYILNGSKA FISGAGESDI
210 220 230 240 250
YVVMCRTGGP GPKGISCIVV EKGTPGLSFG KKEKKVGWNS QPTRAVIFED
260 270 280 290 300
CAVPVANRIG SEGQGFLIAV RGLNGGRINI ASCSLGAAHA SVILTRDHLN
310 320 330 340 350
VRKQFGEPLA SNQYLQFTLA DMATRLVAAR LMVRNAAVAL QEERKDAVAL
360 370 380 390 400
CSMAKLFATD ECFAICNQAL QMHGGYGYLK DYAVQQYVRD SRVHQILEGS
410
NEVMRILISR SLLQE
Length:415
Mass (Da):45,070
Last modified:May 1, 2000 - v1
Checksum:iCAFFE91B74E2362D
GO
Isoform 2 (identifier: Q9UKU7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: P → R
     38-164: Missing.

Note: No experimental confirmation available.

Show »
Length:288
Mass (Da):31,024
Checksum:i731C090A54E4BCAB
GO
Isoform 3 (identifier: Q9UKU7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
     399-415: GSNEVMRILISRSLLQE → ELFWQGPGVQSRSFVPFGGPQIALLLPFSSGDLREG

Note: No experimental confirmation available.

Show »
Length:357
Mass (Da):38,359
Checksum:iFFFBC112FA06E2FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101P → L in AAH01964. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281M → I in IBDD. 1 Publication
VAR_035071
Natural varianti134 – 1341D → Y in IBDD. 1 Publication
VAR_035072
Natural varianti137 – 1371G → R in IBDD; complete loss of activity. 1 Publication
VAR_035073
Natural varianti152 – 1521M → T in IBDD. 1 Publication
VAR_035074
Natural varianti203 – 2031V → I in IBDD. 1 Publication
VAR_035075
Natural varianti302 – 3021R → Q in IBDD; complete loss of activity. 2 Publications
VAR_035076
Natural varianti320 – 3201A → T in IBDD; <20% of wild-type activity. 1 Publication
VAR_035077
Natural varianti334 – 3341R → C in IBDD. 1 Publication
VAR_035078
Natural varianti385 – 3851Q → R in IBDD. 1 Publication
VAR_035079

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 3. 1 PublicationVSP_055779Add
BLAST
Alternative sequencei37 – 371P → R in isoform 2. 1 PublicationVSP_055780
Alternative sequencei38 – 164127Missing in isoform 2. 1 PublicationVSP_055781Add
BLAST
Alternative sequencei399 – 41517GSNEV…SLLQE → ELFWQGPGVQSRSFVPFGGP QIALLLPFSSGDLREG in isoform 3. 1 PublicationVSP_055782Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF126245 mRNA. Translation: AAF12736.1.
AF260689
, AF260679, AF260680, AF260681, AF260682, AF260683, AF260684, AF260685, AF260686, AF260687, AF260688 Genomic DNA. Translation: AAF97922.1.
AK000359 mRNA. Translation: BAA91109.1.
AK074640 mRNA. Translation: BAC11107.1.
AK299492 mRNA. Translation: BAH13050.1.
AP000859 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67833.1.
BC001964 mRNA. Translation: AAH01964.1.
CCDSiCCDS8498.1. [Q9UKU7-1]
RefSeqiNP_055199.1. NM_014384.2. [Q9UKU7-1]
UniGeneiHs.14791.

Genome annotation databases

EnsembliENST00000281182; ENSP00000281182; ENSG00000151498. [Q9UKU7-1]
ENST00000374752; ENSP00000363884; ENSG00000151498. [Q9UKU7-2]
GeneIDi27034.
KEGGihsa:27034.
UCSCiuc001qhk.3. human. [Q9UKU7-1]

Polymorphism databases

DMDMi26006699.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF126245 mRNA. Translation: AAF12736.1 .
AF260689
, AF260679 , AF260680 , AF260681 , AF260682 , AF260683 , AF260684 , AF260685 , AF260686 , AF260687 , AF260688 Genomic DNA. Translation: AAF97922.1 .
AK000359 mRNA. Translation: BAA91109.1 .
AK074640 mRNA. Translation: BAC11107.1 .
AK299492 mRNA. Translation: BAH13050.1 .
AP000859 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67833.1 .
BC001964 mRNA. Translation: AAH01964.1 .
CCDSi CCDS8498.1. [Q9UKU7-1 ]
RefSeqi NP_055199.1. NM_014384.2. [Q9UKU7-1 ]
UniGenei Hs.14791.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RX0 X-ray 1.77 A/B/C/D 24-415 [» ]
ProteinModelPortali Q9UKU7.
SMRi Q9UKU7. Positions 32-415.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117965. 6 interactions.
IntActi Q9UKU7. 3 interactions.
STRINGi 9606.ENSP00000281182.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSitei Q9UKU7.

Polymorphism databases

DMDMi 26006699.

2D gel databases

UCD-2DPAGE Q9UKU7.

Proteomic databases

MaxQBi Q9UKU7.
PaxDbi Q9UKU7.
PRIDEi Q9UKU7.

Protocols and materials databases

DNASUi 27034.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281182 ; ENSP00000281182 ; ENSG00000151498 . [Q9UKU7-1 ]
ENST00000374752 ; ENSP00000363884 ; ENSG00000151498 . [Q9UKU7-2 ]
GeneIDi 27034.
KEGGi hsa:27034.
UCSCi uc001qhk.3. human. [Q9UKU7-1 ]

Organism-specific databases

CTDi 27034.
GeneCardsi GC11P134123.
HGNCi HGNC:87. ACAD8.
HPAi HPA040689.
HPA043903.
MIMi 604773. gene.
611283. phenotype.
neXtProti NX_Q9UKU7.
Orphaneti 79159. Isobutyryl-CoA dehydrogenase deficiency.
PharmGKBi PA24423.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00760000119007.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi Q9UKU7.
KOi K11538.
OMAi WRAQETR.
OrthoDBi EOG74FF0S.
PhylomeDBi Q9UKU7.
TreeFami TF105052.

Enzyme and pathway databases

UniPathwayi UPA00362 .
Reactomei REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

EvolutionaryTracei Q9UKU7.
GeneWikii ACAD8.
GenomeRNAii 27034.
NextBioi 35479818.
PROi Q9UKU7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKU7.
CleanExi HS_ACAD8.
ExpressionAtlasi Q9UKU7. baseline and differential.
Genevestigatori Q9UKU7.

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. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterisation of a cDNA encoding the precursor for a novel member of the acyl-CoA dehydrogenase gene family."
    Telford E.A.R., Moynihan L.M., Markham A.F., Lench N.J.
    Biochim. Biophys. Acta 1446:371-376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Skin fibroblast.
  2. "Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism."
    Andresen B.S., Christensen E., Corydon T.J., Bross P., Pilgaard B., Wanders R.J.A., Ruiter J.P.N., Simonsen H., Winter V., Knudsen I., Schroeder L.D., Gregersen N., Skovby F.
    Am. J. Hum. Genet. 67:1095-1103(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  3. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Brain and Embryo.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 1).
    Tissue: Cervix.
  7. "Composite co-activator ARC mediates chromatin-directed transcriptional activation."
    Naeaer A.M., Beaurang P.A., Zhou S., Abraham S., Solomon W.B., Tjian R.
    Nature 398:828-832(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN ARC COMPLEX, PROTEIN SEQUENCE OF 50-61; 70-80 AND 345-355.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Structures of isobutyryl-CoA dehydrogenase and enzyme-product complex: comparison with isovaleryl- and short-chain acyl-CoA dehydrogenases."
    Battaile K.P., Nguyen T.V., Vockley J., Kim J.-J.P.
    J. Biol. Chem. 279:16526-16534(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 24-415 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, COFACTOR, SUBUNIT.
  10. Cited for: VARIANT IBDD GLN-302, FUNCTION.
  11. "Isobutyryl-CoA dehydrogenase deficiency: isobutyrylglycinuria and ACAD8 gene mutations in two infants."
    Sass J.O., Sander S., Zschocke J.
    J. Inherit. Metab. Dis. 27:741-745(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS IBDD ILE-128 AND ILE-203.
  12. Cited for: VARIANTS IBDD TYR-134; ARG-137; THR-152; GLN-302; THR-320; CYS-334 AND ARG-385, CHARACTERIZATION OF VARIANTS IBDD ARG-137; GLN-302 AND THR-320.

Entry informationi

Entry nameiACAD8_HUMAN
AccessioniPrimary (citable) accession number: Q9UKU7
Secondary accession number(s): B7Z5W4, Q6ZWP6, Q9BUS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 139 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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