UniProt Accession

 ECI2_HUMAN; O75521; Q5JYK5; Q5JYK7; Q7L124; Q8N0X0; Q9BUE9; Q9H0T9; Q9NQH1; Q9NYH7; Q9UN55 

Genbank Protein ID

 AF069301; AL136642; AK075108; AL033383; AL033383; BC002668; BC016781; BC017474; BC033841; BC034702; AF153612; AF244138 

Genbank Nucleotide ID

 AAC19317.1; CAB66577.1; BAG52068.1; CAI42125.1; CAI42127.1; AAH02668.3; AAH16781.1; AAH17474.1; AAH33841.3; AAH34702.1; AAD34173.1; AAF66247.1 

Protein Name

 Enoyl-CoA delta isomerase 2, mitochondrial 

Protein Synonyms/Alias

 DRS-1; Delta(3),delta(2)-enoyl-CoA isomerase; D3,D2-enoyl-CoA isomerase; Diazepam-binding inhibitor-related protein 1; DBI-related protein 1; Dodecenoyl-CoA isomerase; Hepatocellular carcinoma-associated antigen 88; Peroxisomal 3,2-trans-enoyl-CoA isomerase; pECI; Renal carcinoma antigen NY-REN-1 

Gene Name

 ECI2 

Gene Synonyms/Alias

 DRS1; HCA88; PECI 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
51	ENSMNQVKLLKKDPG	acetylation	[1]
90	GVFDLINKAKWDAWN	ubiquitination	[2, 3]
92	FDLINKAKWDAWNAL	acetylation	[1]
92	FDLINKAKWDAWNAL	ubiquitination	[2, 3, 4]
104	NALGSLPKEAARQNY	acetylation	[5]
349	PNALRISKEVIRKRE	ubiquitination	[4]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] 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

 Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity). 

Sequence Annotation

 DOMAIN 39 124 ACB.
 REGION 66 70 Acyl-CoA binding (By similarity).
 REGION 151 322 ECH-like.
 MOTIF 392 394 Microbody targeting signal (Potential).
 BINDING 92 92 Acyl-CoA (By similarity).
 BINDING 111 111 Acyl-CoA (By similarity).
 MOD_RES 51 51 N6-acetyllysine.
 MOD_RES 62 62 N6-acetyllysine (By similarity).
 MOD_RES 92 92 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Isomerase; Mitochondrion; Peroxisome; Polymorphism; Reference proteome; Transit peptide. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 394 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:LIFEdb.
 GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
 GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IDA:UniProtKB.
 GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
 GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB. 

Interpro

 IPR022408; Acyl-CoA-binding_prot_CS.
 IPR000582; Acyl-CoA-binding_protein.
 IPR001753; Crotonase_core_superfam.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. 

Pfam

 PF00887; ACBP
 PF00378; ECH 

SMART

  

PROSITE

 PS00880; ACB_1
 PS51228; ACB_2 

PRINTS

 PR00689; ACOABINDINGP.