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Protein

Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

ACADM

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

Functioni

Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).1 Publication

Catalytic activityi

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FAD1 Publication

Pathwayi: mitochondrial fatty acid beta-oxidation

This protein is involved in the pathway mitochondrial fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mitochondrial fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei167 – 1671Substrate; via carbonyl oxygen
Binding sitei216 – 2161Substrate
Active sitei401 – 4011Proton acceptor
Binding sitei402 – 4021Substrate; via amide nitrogen
Binding sitei413 – 4131Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 16710FAD1 Publication
Nucleotide bindingi191 – 1933FAD1 Publication
Nucleotide bindingi306 – 3083FAD1 Publication
Nucleotide bindingi316 – 3172FAD1 Publication
Nucleotide bindingi374 – 3785FAD1 Publication
Nucleotide bindingi403 – 4053FAD1 Publication

GO - Molecular functioni

GO - Biological processi

  • carnitine biosynthetic process Source: BHF-UCL
  • carnitine metabolic process, CoA-linked Source: BHF-UCL
  • fatty acid beta-oxidation Source: UniProtKB
  • fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: UniProtKB
  • lipid homeostasis Source: GO_Central
  • medium-chain fatty acid catabolic process Source: BHF-UCL
  • medium-chain fatty acid metabolic process Source: BHF-UCL
  • oxidation-reduction process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS04089-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP11310.
UniPathwayiUPA00660.

Chemistry

SwissLipidsiSLP:000001334.

Names & Taxonomyi

Protein namesi
Recommended name:
Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.7)
Short name:
MCAD
Gene namesi
Name:ACADM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:89. ACADM.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: LIFEdb
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn inborn error of mitochondrial fatty acid beta-oxidation which causes fasting hypoglycemia, hepatic dysfunction and encephalopathy, often resulting in death in infancy.
See also OMIM:201450
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531R → C in ACADMD.
Corresponds to variant rs398123072 [ dbSNP | Ensembl ].
VAR_000317
Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
Corresponds to variant rs121434280 [ dbSNP | Ensembl ].
VAR_013698
Natural varianti78 – 781I → T in ACADMD. 1 Publication
Corresponds to variant rs398123074 [ dbSNP | Ensembl ].
VAR_015954
Natural varianti115 – 1162Missing in ACADMD. 1 Publication
VAR_000318
Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
VAR_015955
Natural varianti121 – 1211T → I in ACADMD. 1 Publication
Corresponds to variant rs121434283 [ dbSNP | Ensembl ].
VAR_015956
Natural varianti149 – 1491M → I in ACADMD. 1 Publication
Corresponds to variant rs121434277 [ dbSNP | Ensembl ].
VAR_000319
Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 2 Publications
Corresponds to variant rs121434279 [ dbSNP | Ensembl ].
VAR_000320
Natural varianti195 – 1951G → R in ACADMD. 1 Publication
Corresponds to variant rs121434278 [ dbSNP | Ensembl ].
VAR_000321
Natural varianti206 – 2061R → L in ACADMD. 1 Publication
VAR_015957
Natural varianti244 – 2441C → R in ACADMD. 1 Publication
Corresponds to variant rs121434276 [ dbSNP | Ensembl ].
VAR_000322
Natural varianti245 – 2451S → L in ACADMD. 1 Publication
Corresponds to variant rs121434281 [ dbSNP | Ensembl ].
VAR_013699
Natural varianti267 – 2671G → R in ACADMD. 1 Publication
Corresponds to variant rs121434274 [ dbSNP | Ensembl ].
VAR_000323
Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
Corresponds to variant rs121434282 [ dbSNP | Ensembl ].
VAR_013700
Natural varianti310 – 3101G → R in ACADMD. 1 Publication
Corresponds to variant rs747268471 [ dbSNP | Ensembl ].
VAR_015958
Natural varianti326 – 3261M → T in ACADMD. 1 Publication
Corresponds to variant rs786204631 [ dbSNP | Ensembl ].
VAR_000324
Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
VAR_000325
Natural varianti336 – 3361S → R in ACADMD. 1 Publication
VAR_000326
Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
VAR_015959
Natural varianti375 – 3751I → T in ACADMD. 1 Publication
Corresponds to variant rs121434275 [ dbSNP | Ensembl ].
VAR_000327

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861L → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi98 – 981L → W: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi100 – 1001L → Y: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi108 – 1081I → M: Strongly reduced rate of electron transfer to ETF. 1 Publication
Mutagenesisi191 – 1911W → A: Loss of electron transfer to ETF. 1 Publication
Mutagenesisi191 – 1911W → F: Reduces rate of electron transfer to ETF about six-fold. 1 Publication
Mutagenesisi237 – 2371E → A: Strongly reduced rate of electron transfer to ETF. 2 Publications
Mutagenesisi384 – 3841E → A: Reduces rate of electron transfer to ETF three-fold. 2 Publications
Mutagenesisi384 – 3841E → Q: Reduces rate of electron transfer to ETF two-fold. 2 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiACADM.
MIMi201450. phenotype.
Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24425.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Polymorphism and mutation databases

BioMutaiACADM.
DMDMi113017.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionAdd
BLAST
Chaini26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000502Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
Modified residuei69 – 691N6-succinyllysine; alternateBy similarity
Modified residuei179 – 1791N6-succinyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
Modified residuei212 – 2121N6-succinyllysine; alternateBy similarity
Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity
Modified residuei259 – 2591N6-acetyllysine; alternateBy similarity
Modified residuei259 – 2591N6-succinyllysine; alternateBy similarity
Modified residuei271 – 2711N6-acetyllysine; alternateBy similarity
Modified residuei271 – 2711N6-succinyllysine; alternateBy similarity
Modified residuei279 – 2791N6-acetyllysineCombined sources
Modified residuei301 – 3011N6-acetyllysineCombined sources
Modified residuei351 – 3511PhosphothreonineBy similarity

Post-translational modificationi

Acetylation at Lys-307 and Lys-311 in proximity of the cofactor-binding sites reduces catalytic activity (By similarity). These sites are deacetylated by SIRT3.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11310.
MaxQBiP11310.
PaxDbiP11310.
PeptideAtlasiP11310.
PRIDEiP11310.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

PTM databases

iPTMnetiP11310.
PhosphoSiteiP11310.
SwissPalmiP11310.

Expressioni

Gene expression databases

BgeeiENSG00000117054.
CleanExiHS_ACADM.
ExpressionAtlasiP11310. baseline and differential.
GenevisibleiP11310. HS.

Organism-specific databases

HPAiHPA006198.
HPA026542.

Interactioni

Subunit structurei

Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.3 Publications

GO - Molecular functioni

  • identical protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106552. 50 interactions.
DIPiDIP-34281N.
IntActiP11310. 9 interactions.
MINTiMINT-3007693.
STRINGi9606.ENSP00000409612.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Helixi43 – 5816Combined sources
Helixi61 – 7010Combined sources
Helixi75 – 839Combined sources
Helixi93 – 953Combined sources
Helixi102 – 11514Combined sources
Helixi117 – 13620Combined sources
Helixi139 – 1457Combined sources
Helixi147 – 1515Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 1713Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi182 – 19312Combined sources
Turni194 – 1974Combined sources
Beta strandi198 – 2069Combined sources
Helixi215 – 2184Combined sources
Beta strandi219 – 2257Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi239 – 2413Combined sources
Beta strandi247 – 25812Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2654Combined sources
Turni266 – 2683Combined sources
Helixi269 – 30335Combined sources
Beta strandi309 – 3124Combined sources
Helixi313 – 3153Combined sources
Helixi317 – 34529Combined sources
Helixi351 – 37626Combined sources
Helixi377 – 3815Combined sources
Helixi387 – 3948Combined sources
Helixi395 – 3984Combined sources
Beta strandi400 – 4023Combined sources
Helixi404 – 41714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGCX-ray2.60A/B/C/D26-421[»]
1EGDX-ray2.40A/B/C/D26-421[»]
1EGEX-ray2.75A/B/C/D26-421[»]
1T9GX-ray2.90A/B/C/D26-421[»]
2A1TX-ray2.80A/B/C/D1-421[»]
4P13X-ray1.73A/B/C/D35-421[»]
ProteinModelPortaliP11310.
SMRiP11310. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11310.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 2814Substrate binding

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP11310.
KOiK00249.
PhylomeDBiP11310.
TreeFamiTF105020.

Family and domain databases

Gene3Di1.10.540.10. 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. AlignAdd to basket

Isoform 1 (identifier: P11310-1) [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
MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA
60 70 80 90 100
TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL
110 120 130 140 150
GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT
160 170 180 190 200
EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW
210 220 230 240 250
YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI
260 270 280 290 300
VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT
310 320 330 340 350
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN
360 370 380 390 400
TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY
410 420
EGTSQIQRLI VAREHIDKYK N
Length:421
Mass (Da):46,588
Last modified:July 1, 1989 - v1
Checksum:i7CD0B5832410581B
GO
Isoform 2 (identifier: P11310-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: R → RCSLQ

Show »
Length:425
Mass (Da):47,020
Checksum:iC6A133404E1B6E70
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti356 – 3561I → T in AAF63626 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531R → C in ACADMD.
Corresponds to variant rs398123072 [ dbSNP | Ensembl ].
VAR_000317
Natural varianti67 – 671Y → H in ACADMD; mild. 1 Publication
Corresponds to variant rs121434280 [ dbSNP | Ensembl ].
VAR_013698
Natural varianti78 – 781I → T in ACADMD. 1 Publication
Corresponds to variant rs398123074 [ dbSNP | Ensembl ].
VAR_015954
Natural varianti115 – 1162Missing in ACADMD. 1 Publication
VAR_000318
Natural varianti116 – 1161C → Y in ACADMD. 1 Publication
VAR_015955
Natural varianti121 – 1211T → I in ACADMD. 1 Publication
Corresponds to variant rs121434283 [ dbSNP | Ensembl ].
VAR_015956
Natural varianti132 – 1321P → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_035716
Natural varianti149 – 1491M → I in ACADMD. 1 Publication
Corresponds to variant rs121434277 [ dbSNP | Ensembl ].
VAR_000319
Natural varianti193 – 1931T → A in ACADMD; the thermostability is markedly decreased. 2 Publications
Corresponds to variant rs121434279 [ dbSNP | Ensembl ].
VAR_000320
Natural varianti195 – 1951G → R in ACADMD. 1 Publication
Corresponds to variant rs121434278 [ dbSNP | Ensembl ].
VAR_000321
Natural varianti206 – 2061R → L in ACADMD. 1 Publication
VAR_015957
Natural varianti244 – 2441C → R in ACADMD. 1 Publication
Corresponds to variant rs121434276 [ dbSNP | Ensembl ].
VAR_000322
Natural varianti245 – 2451S → L in ACADMD. 1 Publication
Corresponds to variant rs121434281 [ dbSNP | Ensembl ].
VAR_013699
Natural varianti267 – 2671G → R in ACADMD. 1 Publication
Corresponds to variant rs121434274 [ dbSNP | Ensembl ].
VAR_000323
Natural varianti281 – 2811R → T in ACADMD; mild or benign clinical phenotype. 1 Publication
Corresponds to variant rs121434282 [ dbSNP | Ensembl ].
VAR_013700
Natural varianti310 – 3101G → R in ACADMD. 1 Publication
Corresponds to variant rs747268471 [ dbSNP | Ensembl ].
VAR_015958
Natural varianti326 – 3261M → T in ACADMD. 1 Publication
Corresponds to variant rs786204631 [ dbSNP | Ensembl ].
VAR_000324
Natural varianti329 – 3291K → E in ACADMD; most common variant. 6 Publications
Corresponds to variant rs77931234 [ dbSNP | Ensembl ].
VAR_000325
Natural varianti336 – 3361S → R in ACADMD. 1 Publication
VAR_000326
Natural varianti352 – 3521Y → C in ACADMD. 1 Publication
VAR_015959
Natural varianti375 – 3751I → T in ACADMD. 1 Publication
Corresponds to variant rs121434275 [ dbSNP | Ensembl ].
VAR_000327

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei10 – 101R → RCSLQ in isoform 2. 1 PublicationVSP_038420

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16827 mRNA. Translation: AAA51566.1.
M91432
, M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
AK312629 mRNA. Translation: BAG35514.1.
AL357314 Genomic DNA. Translation: CAI22390.1.
CH471059 Genomic DNA. Translation: EAX06401.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.
CCDSiCCDS44165.1. [P11310-2]
CCDS668.1. [P11310-1]
PIRiA29031. DEHUCM.
RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
NP_001120800.1. NM_001127328.2. [P11310-2]
UniGeneiHs.445040.

Genome annotation databases

EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneIDi34.
KEGGihsa:34.
UCSCiuc001dgw.6. human. [P11310-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16827 mRNA. Translation: AAA51566.1.
M91432
, M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
AK312629 mRNA. Translation: BAG35514.1.
AL357314 Genomic DNA. Translation: CAI22390.1.
CH471059 Genomic DNA. Translation: EAX06401.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.
CCDSiCCDS44165.1. [P11310-2]
CCDS668.1. [P11310-1]
PIRiA29031. DEHUCM.
RefSeqiNP_000007.1. NM_000016.5. [P11310-1]
NP_001120800.1. NM_001127328.2. [P11310-2]
UniGeneiHs.445040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGCX-ray2.60A/B/C/D26-421[»]
1EGDX-ray2.40A/B/C/D26-421[»]
1EGEX-ray2.75A/B/C/D26-421[»]
1T9GX-ray2.90A/B/C/D26-421[»]
2A1TX-ray2.80A/B/C/D1-421[»]
4P13X-ray1.73A/B/C/D35-421[»]
ProteinModelPortaliP11310.
SMRiP11310. Positions 35-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106552. 50 interactions.
DIPiDIP-34281N.
IntActiP11310. 9 interactions.
MINTiMINT-3007693.
STRINGi9606.ENSP00000409612.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.
SwissLipidsiSLP:000001334.

PTM databases

iPTMnetiP11310.
PhosphoSiteiP11310.
SwissPalmiP11310.

Polymorphism and mutation databases

BioMutaiACADM.
DMDMi113017.

2D gel databases

REPRODUCTION-2DPAGEIPI00005040.
UCD-2DPAGEP11310.

Proteomic databases

EPDiP11310.
MaxQBiP11310.
PaxDbiP11310.
PeptideAtlasiP11310.
PRIDEiP11310.

Protocols and materials databases

DNASUi34.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1]
ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2]
GeneIDi34.
KEGGihsa:34.
UCSCiuc001dgw.6. human. [P11310-1]

Organism-specific databases

CTDi34.
GeneCardsiACADM.
GeneReviewsiACADM.
HGNCiHGNC:89. ACADM.
HPAiHPA006198.
HPA026542.
MalaCardsiACADM.
MIMi201450. phenotype.
607008. gene.
neXtProtiNX_P11310.
Orphaneti42. Medium chain acyl-CoA dehydrogenase deficiency.
PharmGKBiPA24425.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0140. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131659.
HOVERGENiHBG000224.
InParanoidiP11310.
KOiK00249.
PhylomeDBiP11310.
TreeFamiTF105020.

Enzyme and pathway databases

UniPathwayiUPA00660.
BioCyciMetaCyc:HS04089-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-77288. mitochondrial fatty acid beta-oxidation of unsaturated fatty acids.
R-HSA-77346. Beta oxidation of decanoyl-CoA to octanoyl-CoA-CoA.
R-HSA-77348. Beta oxidation of octanoyl-CoA to hexanoyl-CoA.
SABIO-RKP11310.

Miscellaneous databases

EvolutionaryTraceiP11310.
GenomeRNAii34.
PROiP11310.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000117054.
CleanExiHS_ACADM.
ExpressionAtlasiP11310. baseline and differential.
GenevisibleiP11310. HS.

Family and domain databases

Gene3Di1.10.540.10. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiACADM_HUMAN
AccessioniPrimary (citable) accession number: P11310
Secondary accession number(s): Q5T4U4, Q9NYF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 195 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

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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.