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Reviewed, UniProtKB/Swiss-Prot P11310 (ACADM_HUMAN)

Last modified October 13, 2009. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
      Short name=MCAD
    EC=1.3.99.3
Gene names
Name: ACADM
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This enzyme is specific for acyl chain lengths of 4 to 16.

Catalytic activity

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

Cofactor

FAD.

Pathway

Lipid metabolism; mitochondrial fatty acid beta-oxidation.

Subunit structure

Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF. Ref.9 Ref.10 Ref.11

Subcellular location

Mitochondrion matrix.

Involvement in disease

Defects in ACADM are the cause of medium-chain acyl-CoA dehydrogenase deficiency (MCAD deficiency) [MIM:201450]. It is an autosomal recessive disease which causes fasting hypoglycemia, hepatic dysfunction, and encephalopathy, often resulting in death in infancy. The disease frequency is one in 13000.

Miscellaneous

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

Utilizes the electron transfer flavoprotein (ETF) as electron acceptor that transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).

Sequence similarities

Belongs to the acyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processfatty acid beta-oxidation Ref.6

Inferred from mutant phenotype. Source: UniProtKB

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

acyl-CoA dehydrogenase activity Ref.6

Inferred from mutant phenotype. Source: UniProtKB

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2525Mitochondrion
Chain26 – 421396Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
PRO_0000000502

Regions

Nucleotide binding158 – 16710FAD
Nucleotide binding191 – 1933FAD
Nucleotide binding306 – 3083FAD
Nucleotide binding316 – 3172FAD
Nucleotide binding374 – 3785FAD
Nucleotide binding403 – 4053FAD
Region278 – 2814Substrate binding

Sites

Active site4011Proton acceptor
Binding site1671Substrate; via carbonyl oxygen
Binding site4021Substrate; via amide nitrogen

Amino acid modifications

Modified residue2121N6-acetyllysine Ref.8
Modified residue2791N6-acetyllysine Ref.8
Modified residue3011N6-acetyllysine Ref.8

Natural variations

Natural variant531R → C in MCAD deficiency.
VAR_000317
Natural variant671Y → H in MCAD deficiency; mild. Ref.24
VAR_013698
Natural variant781I → T in MCAD deficiency. Ref.24
VAR_015954
Natural variant115 – 1162Missing in MCAD deficiency.
VAR_000318
Natural variant1161C → Y in MCAD deficiency. Ref.21
VAR_015955
Natural variant1211T → I in MCAD deficiency. Ref.24
VAR_015956
Natural variant1321P → R in a breast cancer sample; somatic mutation. Ref.27
VAR_035716
Natural variant1491M → I in MCAD deficiency. Ref.15
VAR_000319
Natural variant1931T → A in MCAD deficiency; the thermostability is markedly decreased. Ref.21 Ref.22
VAR_000320
Natural variant1951G → R in MCAD deficiency. Ref.20
VAR_000321
Natural variant2061R → L in MCAD deficiency. Ref.23
VAR_015957
Natural variant2441C → R in MCAD deficiency. Ref.15
VAR_000322
Natural variant2451S → L in MCAD deficiency. Ref.25
VAR_013699
Natural variant2671G → R in MCAD deficiency. Ref.15
VAR_000323
Natural variant2811R → T in MCAD deficiency; mild or benign clinical phenotype. Ref.26
VAR_013700
Natural variant3101G → R in MCAD deficiency. Ref.24
VAR_015958
Natural variant3261M → T in MCAD deficiency. Ref.18
VAR_000324
Natural variant3291K → E in MCAD deficiency; most common variant. Ref.23 Ref.26 Ref.6 Ref.13 Ref.14 Ref.16 Ref.17
VAR_000325
Natural variant3361S → R in MCAD deficiency. Ref.18
VAR_000326
Natural variant3521Y → C in MCAD deficiency. Ref.21
VAR_015959
Natural variant3751I → T in MCAD deficiency. Ref.15
VAR_000327

Experimental info

Mutagenesis861L → M: Strongly reduced rate of electron transfer to ETF. Ref.10
Mutagenesis981L → W: Strongly reduced rate of electron transfer to ETF. Ref.10
Mutagenesis1001L → Y: Strongly reduced rate of electron transfer to ETF. Ref.10
Mutagenesis1081I → M: Strongly reduced rate of electron transfer to ETF. Ref.10
Mutagenesis1911W → A: Loss of electron transfer to ETF. Ref.11
Mutagenesis1911W → F: Reduces rate of electron transfer to ETF about six-fold. Ref.11
Mutagenesis2371E → A: Strongly reduced rate of electron transfer to ETF. Ref.10 Ref.11
Mutagenesis3841E → A: Reduces rate of electron transfer to ETF three-fold. Ref.10 Ref.11
Mutagenesis3841E → Q: Reduces rate of electron transfer to ETF two-fold. Ref.10 Ref.11
Sequence conflict101R → RCSLQ in AAF63626. Ref.3
Sequence conflict3561I → T in AAF63626. Ref.3

Secondary structure

.......................................................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11310-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7CD0B5832410581B

FASTA42146,588
        10         20         30         40         50         60 
MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI 

        70         80         90        100        110        120 
IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ 

       130        140        150        160        170        180 
TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG 

       190        200        210        220        230        240 
DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM 

       250        260        270        280        290        300 
GQRCSDTRGI VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT 

       310        320        330        340        350        360 
KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF 

       370        380        390        400        410        420 
AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK 


N 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue."
Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W., Strauss A.W.
Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987) [PubMed: 3035565] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene."
Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L., Whelan A.J., Strauss A.W.
Biochemistry 31:81-89(1992) [PubMed: 1731887] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Medium-chain acyl-CoA dehydrogenase."
Sun F., Wang Y., Block G.D.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[5]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 218-235, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[6]"Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M., Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R.
Biochem. Biophys. Res. Commun. 171:498-505(1990) [PubMed: 2393404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, VARIANT MCAD DEFICIENCY GLU-329.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-279 AND LYS-301, MASS SPECTROMETRY.
[9]"Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity."
Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P.
Biochemistry 35:12412-12420(1996) [PubMed: 8823176] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND OCTANOYL-COENZYME A, SUBUNIT.
[10]"Extensive domain motion and electron transfer in the human electron transferring flavoprotein-medium chain acyl-CoA dehydrogenase complex."
Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., Leys D.
J. Biol. Chem. 279:32904-32912(2004) [PubMed: 15159392] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100; ILE-108; GLU-237 AND GLU-384, SUBUNIT.
[11]"Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein."
Toogood H.S., van Thiel A., Scrutton N.S., Leys D.
J. Biol. Chem. 280:30361-30366(2005) [PubMed: 15975918] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384, SUBUNIT.
[12]"Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene."
Tanaka K., Yokota I., Coates P.M., Strauss A.W., Kelly D.P., Zhang Z.F., Gregersen N., Andresen B.S., Matsubara Y., Curtis D., Chen Y.-T.
Hum. Mutat. 1:271-279(1992) [PubMed: 1363805] [Abstract]
Cited for: REVIEW ON VARIANTS MCAD DEFICIENCY.
[13]"Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation."
Yokota I., Indo Y., Coates P.M., Tanaka K.
J. Clin. Invest. 86:1000-1003(1990) [PubMed: 2394825] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[14]"Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency."
Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G., Gregersen N., Dorland L., Strauss A.W.
Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990) [PubMed: 2251268] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[15]"Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency."
Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K.
Am. J. Hum. Genet. 49:1280-1291(1991) [PubMed: 1684086] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY ILE-149; ARG-244; ARG-267 AND THR-375.
[16]"Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli."
Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N., Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S., Bolund L., Ghisla S.
Hum. Genet. 86:545-551(1991) [PubMed: 1902818] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY GLU-329.
[17]"Frequency of the G985 MCAD mutation in the general population."
Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S., Gregersen N., Curtis D.
Lancet 337:298-299(1991) [PubMed: 1671131] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY GLU-329 FREQUENCY.
[18]"Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene."
Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V., Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K., Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N.
Am. J. Hum. Genet. 54:975-988(1994) [PubMed: 8198141] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY THR-326 AND ARG-336.
[19]"Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies."
Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C., Strauss A.W., Naylor E.W.
Pediatr. Res. 37:675-678(1995) [PubMed: 7603790] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY 115-GLY-CYS-116 DEL.
[20]"A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death."
Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M., Demartinville B., Rinaldo P., Slaugh R., Strauss A.W.
J. Clin. Invest. 94:1477-1483(1994) [PubMed: 7929823] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY ARG-195.
[21]"The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype?"
Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S., Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K., Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L., Koelvraa S., Gregersen N.
Hum. Mol. Genet. 6:695-707(1997) [PubMed: 9158144] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY TYR-116; ALA-193 AND CYS-352.
[22]"Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site."
Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I., Ghisla S.
Biochem. J. 337:225-230(1999) [PubMed: 9882619] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT MCAD DEFICIENCY ALA-193.
[23]"Identification of a novel mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency."
Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L., Dasouki M.J., Wilkinson J., Roe C.R.
Mol. Genet. Metab. 69:259-262(2000) [PubMed: 10767181] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY LEU-206 AND GLU-329.
[24]"Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by MS/MS-based prospective screening of newborns differ from those observed in patients with clinical symptoms: identification and characterization of a new, prevalent mutation that results in mild MCAD deficiency."
Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J., McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I., Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N.
Am. J. Hum. Genet. 68:1408-1418(2001) [PubMed: 11349232] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY HIS-67; THR-78; ILE-121 AND ARG-310.
[25]"Molecular and functional characterization of mild MCAD deficiency."
Zschocke J., Schulze A., Lindner M., Fiesel S., Olgemoller K., Hoffmann G.F., Penzien J., Ruiter J.P.N., Wanders R.J.A., Mayatepek E.
Hum. Genet. 108:404-408(2001) [PubMed: 11409868] [Abstract]
Cited for: VARIANT MCAD DEFICIENCY LEU-245.
[26]"Compound heterozygosity in four asymptomatic siblings with medium-chain acyl-CoA dehydrogenase deficiency."
Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D.
J. Inherit. Metab. Dis. 24:417-418(2001) [PubMed: 11486912] [Abstract]
Cited for: VARIANTS MCAD DEFICIENCY THR-281 AND GLU-329.
[27]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-132.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

M16827 mRNA. Translation: AAA51566.1.
M91432 expand/collapse EMBL AC list , M91421, M91422, M91423, M91425, M91426, M91427, M91428, M91429, M91430, M91431 Genomic DNA. Translation: AAA59567.1.
AF251043 mRNA. Translation: AAF63626.1.
BC005377 mRNA. Translation: AAH05377.1.
M60505 Genomic DNA. Translation: AAB59625.1.
IPIIPI00005040.
PIRDEHUCM. A29031.
RefSeqNP_000007.1.
NP_001120800.1.
UniGeneHs.445040

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP11310.

2-D gel databases

REPRODUCTION-2DPAGEIPI00005040.

Proteomic databases

PRIDEP11310.

Genome annotation databases

EnsemblENST00000370834; ENSP00000359871; ENSG00000117054; Homo sapiens. [Genome view]
ENST00000370841; ENSP00000359878; ENSG00000117054; Homo sapiens. [Genome view]
ENST00000420607; ENSP00000409612; ENSG00000117054; Homo sapiens. [Genome view]
GeneID34.
KEGGhsa:34.
UCSCuc001dgw.2. human.

Organism-specific databases

CTD34.
GeneCardsGC01P075902.
H-InvDBHIX0000706.
HGNCHGNC:89. ACADM.
HPAHPA006198.
HPA026542.
MIM201450. phenotype.
607008. gene.
Orphanet42. Acyl-CoA dehydrogenase, medium chain, deficiency of.
PharmGKBPA24425.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP11310.

Enzyme and pathway databases

BRENDA1.3.99.3. 247.
Pathway_Interaction_DBhnf3bpathway. FOXA2 and FOXA3 transcription factor networks.
ReactomeREACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpressP11310.
BgeeP11310.
CleanExHS_ACADM.
GenevestigatorP11310.
GermOnlineENSG00000117054. Homo sapiens.

Family and domain databases

InterProIPR006089. Acyl-CoA_DH_CS.
IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_M.
IPR013786. AcylCoA_DH/ox_N.
IPR013764. AcylCoA_oxidase/DH_1/2_C.
[Graphical view]
Gene3DG3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.
PfamPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
PROSITEPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio131.
SOURCESearch...

Entry information

Entry nameACADM_HUMAN
AccessionPrimary (citable) accession number: P11310
Secondary accession number(s): Q9NYF1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 13, 2009
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents