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P45954

- ACDSB_HUMAN

UniProt

P45954 - ACDSB_HUMAN

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Protein

Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

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

Functioni

Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent.

Catalytic activityi

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+.

Cofactori

FAD.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831Substrate; via carbonyl oxygen
Binding sitei283 – 2831Substrate
Binding sitei319 – 3191FAD; shared with dimeric partner
Binding sitei330 – 3301FAD; shared with dimeric partner
Active sitei414 – 4141Proton acceptor By similarity
Binding sitei415 – 4151Substrate; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi174 – 18310FAD
Nucleotide bindingi207 – 2093FAD
Nucleotide bindingi387 – 3915FAD; shared with dimeric partner
Nucleotide bindingi416 – 4183FAD

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. fatty acid metabolic process Source: ProtInc
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_197. Branched-chain amino acid catabolism.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.5)
Short name:
SBCAD
Alternative name(s):
2-methyl branched chain acyl-CoA dehydrogenase
Short name:
2-MEBCAD
2-methylbutyryl-coenzyme A dehydrogenase
Short name:
2-methylbutyryl-CoA dehydrogenase
Gene namesi
Name:ACADSB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:91. ACADSB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD) [MIM:610006]: Autosomal recessive disorder and consists of a defect in catabolism of L-isoleucine which is characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine. Affected individuals have seizures and psychomotor delay as the main clinical features.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti255 – 2551L → F in SBCADD. 2 Publications
VAR_013010

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610006. phenotype.
Orphaneti79157. 2-methylbutyryl-CoA dehydrogenase deficiency.
PharmGKBiPA24427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionAdd
BLAST
Chaini34 – 432399Short/branched chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000519Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701N6-acetyllysine; alternate By similarity
Modified residuei70 – 701N6-succinyllysine; alternate By similarity
Modified residuei284 – 2841N6-acetyllysine; alternate1 Publication
Modified residuei284 – 2841N6-succinyllysine; alternate By similarity
Modified residuei426 – 4261N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP45954.
PaxDbiP45954.
PeptideAtlasiP45954.
PRIDEiP45954.

PTM databases

PhosphoSiteiP45954.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiP45954.
BgeeiP45954.
CleanExiHS_ACADSB.
GenevestigatoriP45954.

Organism-specific databases

HPAiHPA041458.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi106554. 3 interactions.
IntActiP45954. 1 interaction.
STRINGi9606.ENSP00000357873.

Structurei

Secondary structure

1
432
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 7517
Helixi77 – 793
Helixi80 – 867
Helixi91 – 999
Turni100 – 1034
Beta strandi104 – 1074
Helixi109 – 1113
Helixi118 – 12912
Helixi133 – 14412
Helixi146 – 1538
Helixi156 – 16813
Beta strandi172 – 1754
Beta strandi181 – 1844
Helixi185 – 1873
Beta strandi191 – 1955
Beta strandi198 – 20912
Turni210 – 2134
Beta strandi215 – 2239
Helixi225 – 2317
Beta strandi232 – 2387
Beta strandi244 – 2463
Beta strandi252 – 2543
Beta strandi260 – 27112
Helixi272 – 2743
Beta strandi275 – 2784
Helixi282 – 31837
Helixi326 – 3283
Helixi330 – 35829
Helixi364 – 38926
Helixi390 – 3945
Helixi400 – 4078
Helixi408 – 4114
Turni412 – 4143
Helixi417 – 43115

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JIFX-ray2.00A/B/C/D52-432[»]
ProteinModelPortaliP45954.
SMRiP45954. Positions 52-432.

Miscellaneous databases

EvolutionaryTraceiP45954.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 2302Substrate binding
Regioni291 – 2944Substrate binding

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP45954.
KOiK09478.
OMAiFLIFANV.
PhylomeDBiP45954.
TreeFamiTF105055.

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.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P45954-1) [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

MEGLAVRLLR GSRLLRRNFL TCLSSWKIPP HVSKSSQSEA LLNITNNGIH    50
FAPLQTFTDE EMMIKSSVKK FAQEQIAPLV STMDENSKME KSVIQGLFQQ 100
GLMGIEVDPE YGGTGASFLS TVLVIEELAK VDASVAVFCE IQNTLINTLI 150
RKHGTEEQKA TYLPQLTTEK VGSFCLSEAG AGSDSFALKT RADKEGDYYV 200
LNGSKMWISS AEHAGLFLVM ANVDPTIGYK GITSFLVDRD TPGLHIGKPE 250
NKLGLRASST CPLTFENVKV PEANILGQIG HGYKYAIGSL NEGRIGIAAQ 300
MLGLAQGCFD YTIPYIKERI QFGKRLFDFQ GLQHQVAHVA TQLEAARLLT 350
YNAARLLEAG KPFIKEASMA KYYASEIAGQ TTSKCIEWMG GVGYTKDYPV 400
EKYFRDAKIG TIYEGASNIQ LNTIAKHIDA EY 432
Length:432
Mass (Da):47,485
Last modified:November 1, 1995 - v1
Checksum:i1EB5F894B1944E99
GO
Isoform 2 (identifier: P45954-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.

Note: No experimental confirmation available.

Show »
Length:330
Mass (Da):36,025
Checksum:i1BFB4E4C8E0F3615
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131R → K.2 Publications
Corresponds to variant rs12263012 [ dbSNP | Ensembl ].
VAR_048177
Natural varianti209 – 2091S → G.
Corresponds to variant rs1799823 [ dbSNP | Ensembl ].
VAR_014749
Natural varianti255 – 2551L → F in SBCADD. 2 Publications
VAR_013010
Natural varianti316 – 3161I → V.1 Publication
Corresponds to variant rs1131430 [ dbSNP | Ensembl ].
VAR_048178
Natural varianti376 – 3761E → G.
Corresponds to variant rs12357783 [ dbSNP | Ensembl ].
VAR_048179

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 102102Missing in isoform 2. VSP_055778Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12778 mRNA. Translation: AAA74424.1.
AF260678
, AF260668, AF260669, AF260670, AF260671, AF260672, AF260673, AF260674, AF260675, AF260676, AF260677 Genomic DNA. Translation: AAF97921.1.
AK298638 mRNA. Translation: BAG60813.1.
AK314241 mRNA. Translation: BAG36909.1.
AL731666, AC012391, AC073585 Genomic DNA. Translation: CAI10847.1.
CH471066 Genomic DNA. Translation: EAW49291.1.
BC013756 mRNA. Translation: AAH13756.1.
AL831821 mRNA. Translation: CAD38535.2.
CCDSiCCDS7634.1.
PIRiA55680.
RefSeqiNP_001600.1. NM_001609.3.
UniGeneiHs.81934.

Genome annotation databases

EnsembliENST00000358776; ENSP00000357873; ENSG00000196177.
ENST00000368869; ENSP00000357862; ENSG00000196177.
GeneIDi36.
KEGGihsa:36.
UCSCiuc001lhb.3. human.

Polymorphism databases

DMDMi1168283.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12778 mRNA. Translation: AAA74424.1 .
AF260678
, AF260668 , AF260669 , AF260670 , AF260671 , AF260672 , AF260673 , AF260674 , AF260675 , AF260676 , AF260677 Genomic DNA. Translation: AAF97921.1 .
AK298638 mRNA. Translation: BAG60813.1 .
AK314241 mRNA. Translation: BAG36909.1 .
AL731666 , AC012391 , AC073585 Genomic DNA. Translation: CAI10847.1 .
CH471066 Genomic DNA. Translation: EAW49291.1 .
BC013756 mRNA. Translation: AAH13756.1 .
AL831821 mRNA. Translation: CAD38535.2 .
CCDSi CCDS7634.1.
PIRi A55680.
RefSeqi NP_001600.1. NM_001609.3.
UniGenei Hs.81934.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JIF X-ray 2.00 A/B/C/D 52-432 [» ]
ProteinModelPortali P45954.
SMRi P45954. Positions 52-432.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106554. 3 interactions.
IntActi P45954. 1 interaction.
STRINGi 9606.ENSP00000357873.

Chemistry

DrugBanki DB00167. L-Isoleucine.

PTM databases

PhosphoSitei P45954.

Polymorphism databases

DMDMi 1168283.

Proteomic databases

MaxQBi P45954.
PaxDbi P45954.
PeptideAtlasi P45954.
PRIDEi P45954.

Protocols and materials databases

DNASUi 36.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358776 ; ENSP00000357873 ; ENSG00000196177 .
ENST00000368869 ; ENSP00000357862 ; ENSG00000196177 .
GeneIDi 36.
KEGGi hsa:36.
UCSCi uc001lhb.3. human.

Organism-specific databases

CTDi 36.
GeneCardsi GC10P124758.
HGNCi HGNC:91. ACADSB.
HPAi HPA041458.
MIMi 600301. gene.
610006. phenotype.
neXtProti NX_P45954.
Orphaneti 79157. 2-methylbutyryl-CoA dehydrogenase deficiency.
PharmGKBi PA24427.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
HOGENOMi HOG000131659.
HOVERGENi HBG000224.
InParanoidi P45954.
KOi K09478.
OMAi FLIFANV.
PhylomeDBi P45954.
TreeFami TF105055.

Enzyme and pathway databases

UniPathwayi UPA00660 .
Reactomei REACT_197. Branched-chain amino acid catabolism.

Miscellaneous databases

ChiTaRSi ACADSB. human.
EvolutionaryTracei P45954.
GenomeRNAii 36.
NextBioi 139.
PROi P45954.
SOURCEi Search...

Gene expression databases

ArrayExpressi P45954.
Bgeei P45954.
CleanExi HS_ACADSB.
Genevestigatori P45954.

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.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family."
    Rozen R., Vockley J., Zhou L., Milos R., Willard J., Fu K., Vicanek C., Low-Nang L., Torban E., Fournier B.
    Genomics 24:280-287(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  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].
  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 AND 2).
    Tissue: Esophagus and Mammary gland.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    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), VARIANT LYS-13.
    Tissue: Mammary gland.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-432 (ISOFORM 1), VARIANTS LYS-13 AND VAL-316.
    Tissue: Skeletal muscle.
  8. "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-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human short-branched chain acyl-CoA dehydrogenase."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-432 IN COMPLEX WITH FAD AND SUBSTRATE ANALOG, SUBUNIT.
  11. Cited for: VARIANT SBCADD PHE-255.
  12. "Short/branched-chain acyl-CoA dehydrogenase deficiency due to an IVS3+3A>G mutation that causes exon skipping."
    Madsen P.P., Kibaek M., Roca X., Sachidanandam R., Krainer A.R., Christensen E., Steiner R.D., Gibson K.M., Corydon T.J., Knudsen I., Wanders R.J., Ruiter J.P.N., Gregersen N., Andresen B.S.
    Hum. Genet. 118:680-690(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SBCADD PHE-255.

Entry informationi

Entry nameiACDSB_HUMAN
AccessioniPrimary (citable) accession number: P45954
Secondary accession number(s): B4DQ51, Q5SQN6, Q96CX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 154 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

Dasty 3

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