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B4DJE7

- B4DJE7_HUMAN

UniProt

B4DJE7 - B4DJE7_HUMAN

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Protein
Submitted name: Medium-chain-specific acyl-CoA dehydrogenase, mitochondrial
Gene
ACADM
Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. medium-chain-acyl-CoA dehydrogenase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. cardiac muscle cell differentiation Source: Ensembl
  2. carnitine metabolic process, CoA-linked Source: Ensembl
  3. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: Ensembl
  4. glycogen biosynthetic process Source: Ensembl
  5. liver development Source: Ensembl
  6. medium-chain fatty acid metabolic process Source: Ensembl
  7. post-embryonic development Source: Ensembl
  8. regulation of gluconeogenesis Source: Ensembl
  9. response to cold Source: Ensembl
  10. response to starvation Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Medium-chain-specific acyl-CoA dehydrogenase, mitochondrialImported
Submitted name:
cDNA FLJ52595, highly similar to Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.99.3)Imported
Gene namesi
Name:ACADMImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:89. ACADM.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Family & Domainsi

Phylogenomic databases

HOVERGENiHBG000224.
KOiK00249.

Family and domain databases

Gene3Di2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B4DJE7-1 [UniParc]FASTAAdd to Basket

« Hide

MWITNGGKAN WYFLLARSDP DPKAPANKAF TGFIVEADTP GIQIGRKELN    50
MGQRCSDTRG IVFEDVKVPK ENVLIGDGAG FKVAMGAFDK TRPVVAAGAV 100
GLAQRALDEA TKYALERKTF GKLLVEHQAI SFMLAEMAMK VELARMSYQR 150
AAWEVDSGRR NTYYASIAKA FAGDIANQLA TDAVQILGGN GFNTEYPVEK 200
LMRDAKIYQI YEGTSQIQRL IVAREHIDKY KN 232
Length:232
Mass (Da):25,663
Last modified:September 23, 2008 - v1
Checksum:iB903551ACCD1B68B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL357314 Genomic DNA. No translation available.
AK296045 mRNA. Translation: BAG58809.1.
RefSeqiNP_001272973.1. NM_001286044.1.
UniGeneiHs.445040.

Genome annotation databases

EnsembliENST00000543667; ENSP00000446176; ENSG00000117054.
GeneIDi34.
KEGGihsa:34.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL357314 Genomic DNA. No translation available.
AK296045 mRNA. Translation: BAG58809.1 .
RefSeqi NP_001272973.1. NM_001286044.1.
UniGenei Hs.445040.

3D structure databases

ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000543667 ; ENSP00000446176 ; ENSG00000117054 .
GeneIDi 34.
KEGGi hsa:34.

Organism-specific databases

CTDi 34.
HGNCi HGNC:89. ACADM.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG000224.
KOi K00249.

Miscellaneous databases

NextBioi 35472513.

Family and domain databases

Gene3Di 2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "NEDO human cDNA sequencing project focused on splicing variants."
    Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.
    , Sugano S., Nomura N., Isogai T.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Subthalamic nucleusImported.
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiB4DJE7_HUMAN
AccessioniPrimary (citable) accession number: B4DJE7
Entry historyi
Integrated into UniProtKB/TrEMBL: September 23, 2008
Last sequence update: September 23, 2008
Last modified: September 3, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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

External Data

Dasty 3

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