CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acyl-CoA dehydrogenase family member 11 
Protein Synonyms/Alias
 ACAD-11 
Gene Name
 ACAD11 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
683ESRIAIEKIRLLTLKacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. 
Sequence Annotation
 NP_BIND 504 514 FAD.
 NP_BIND 504 507 FAD.
 NP_BIND 512 514 FAD.
 NP_BIND 538 540 FAD.
 NP_BIND 727 731 FAD; shared with dimeric partner.
 NP_BIND 756 758 FAD.
 REGION 629 632 Substrate binding (By similarity).
 BINDING 514 514 Substrate; via carbonyl oxygen (By
 BINDING 657 657 FAD.
 BINDING 657 657 FAD; shared with dimeric partner.
 BINDING 727 727 FAD.
 BINDING 755 755 Substrate; via amide nitrogen.
 MOD_RES 324 324 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 780 AA 
Protein Sequence
MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR AGKSNPTFYL 60
QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP VPKPILYCSD TSVIGTEFYV 120
MEHVQGRIFR DLTIPGLSPA ERSAIYVATV ETLAQLRSLN IQSLQLEGYG IGAGYCKRQV 180
STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV 240
LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS 300
ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET GLQLSKRTFS 360
TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE VTEFYVQNEN SVDKWGKPLV 420
IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA LIAEETGKCF FAPDVFNCQA PDTGNMEVLH 480
LYGSEEQKKQ WLEPLLQGNI TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS 540
GAGNPKCKIA IVLGRTQNTS LSRHKQHSMI LVPMNTPGVK IIRPLSVFGY TDNFHGGHFE 600
IHFNQVRVPA TNLILGEGRG FEISQGRLGP GRIHHCMRTV GLAERALQIM CERATQRIAF 660
KKKLYAHEVV AHWIAESRIA IEKIRLLTLK AAHSMDTLGS AGAKKEIAMI KVAAPRAVSK 720
IVDWAIQVCG GAGVSQDYPL ANMYAITRVL RLADGPDEVH LSAIATMELR DQAKRLTAKI 780 
Gene Ontology
 GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005777; C:peroxisome; ISS:HGNC.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IDA:UniProtKB.
 GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
 GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IDA:UniProtKB.
 GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:UniProtKB. 
Interpro
 IPR006092; Acyl-CoA_DH_N.
 IPR006090; Acyl-CoA_Oxase/DH_1.
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase.
 IPR002575; Aminoglycoside_PTrfase.
 IPR011009; Kinase-like_dom. 
Pfam
 PF00441; Acyl-CoA_dh_1
 PF02770; Acyl-CoA_dh_M
 PF02771; Acyl-CoA_dh_N
 PF01636; APH 
SMART
  
PROSITE
  
PRINTS