Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Acyl-CoA-binding protein  

UniProtKB / Swiss-Prot ID :  ACBP_HUMAN

Gene Name (Synonyms) : 
DBI  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. 

Protein Sequence MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWNELKGTSKEDA...
Predicted Secondary Structure CCHHHHHHHHHHHHCCCCCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCCCHHHH...
Protein Variant
LocationDescription
39D -> N (in dbSNP:rs8192504). VAR_048160
71M -> V (in dbSNP:rs8192506). VAR_048161
86G -> R (in dbSNP:rs8192507). VAR_048162
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylserine---MSQAEF
---CCHHHH
37.79HPRD
Link
2N-acetylserine.---MSQAEF
---CCHHHH
37.79UniProtKB
Link
8N6-acetyllysineAEFEKAAEE
HHHHHHHHH
59.21HPRD
Link
8N6-acetyllysineAEFEKAAEE
HHHHHHHHH
59.21Phosphositeplus
Link
8N6-acetyllysine.AEFEKAAEE
HHHHHHHHH
59.21UniProtKB
Link
17N6-acetyllysineVRHLKTKPS
HHCCCCCCC
48.67HPRD
Link
17N6-acetyllysineVRHLKTKPS
HHCCCCCCC
48.67Phosphositeplus
Link
19N6-acetyllysineHLKTKPSDE
CCCCCCCHH
40.72HPRD
Link
19N6-acetyllysineHLKTKPSDE
CCCCCCCHH
40.72Phosphositeplus
Link
19N6-acetyllysine.HLKTKPSDE
CCCCCCCHH
40.72UniProtKB
Link
29PhosphotyrosineMLFIYGHYK
HHHHHHHHH
7.19HPRD
Link
29PhosphotyrosineMLFIYGHYK
HHHHHHHHH
7.19PhosphoELM
Link
29PhosphotyrosineMLFIYGHYK
HHHHHHHHH
7.19Phosphositeplus
Link
29Phosphotyrosine.MLFIYGHYK
HHHHHHHHH
7.19UniProtKB
Link
32PhosphotyrosineIYGHYKQAT
HHHHHHHCC
10.63Phosphositeplus
Link
51PhosphothreonineMLDFTGKAK
CCCHHHHHH
37.12HPRD
Link
51PhosphothreonineMLDFTGKAK
CCCHHHHHH
37.12Phosphositeplus
Link
55Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TGKAKWDAW
HHHHHHHHH
49.44Phosphositeplus
Link
55N6-acetyllysineTGKAKWDAW
HHHHHHHHH
49.44HPRD
Link
55N6-acetyllysineTGKAKWDAW
HHHHHHHHH
49.44Phosphositeplus
Link
55N6-acetyllysine; alternate.TGKAKWDAW
HHHHHHHHH
49.44UniProtKB
Link
55N6-malonyllysine; alternate.TGKAKWDAW
HHHHHHHHH
49.44UniProtKB
Link
72N6-acetyllysineEDAMKAYIN
HHHHHHHHH
39.49HPRD
Link
77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AYINKVEEL
HHHHHHHHH
41.27Phosphositeplus
Link
77N6-acetyllysineAYINKVEEL
HHHHHHHHH
41.27HPRD
Link
77N6-acetyllysineAYINKVEEL
HHHHHHHHH
41.27Phosphositeplus
Link
77N6-acetyllysine.AYINKVEEL
HHHHHHHHH
41.27UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
COAC_HUMANphysical interactionMINT-63420MINT16169070
COAC_HUMANphysical interactionEBI-736535
intact16169070
COAC_HUMANyeast 2-hybridHPRD:08832HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-19; LYS-55 ANDLYS-77, AND MASS SPECTROMETRY.
"Complete amino acid sequences of bovine and human endozepines.Homology with rat diazepam binding inhibitor.";
Marquardt H., Todaro G.J., Shoyab M.;
J. Biol. Chem. 261:9727-9731(1986).
Cited for: PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), AND ACETYLATION AT SER-2.
N6-malonyllysine
ReferencePubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme.";
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.;
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
Cited for: MALONYLATION AT LYS-55.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures