ACBP_RAT - dbPTM
ACBP_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACBP_RAT
UniProt AC P11030
Protein Name Acyl-CoA-binding protein
Gene Name Dbi
Organism Rattus norvegicus (Rat).
Sequence Length 87
Subcellular Localization Endoplasmic reticulum . Golgi apparatus . Golgi localization is dependent on ligand binding.
Protein Description 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 MSQADFDKAAEEVKRLKTQPTDEEMLFIYSHFKQATVGDVNTDRPGLLDLKGKAKWDSWNKLKGTSKENAMKTYVEKVEELKKKYGI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSQADFDKA
------CCHHHHHHH
33.7918455725
2Acetylation------MSQADFDKA
------CCHHHHHHH
33.792803267
8SuccinylationMSQADFDKAAEEVKR
CCHHHHHHHHHHHHH
49.87-
8SuccinylationMSQADFDKAAEEVKR
CCHHHHHHHHHHHHH
49.87-
8AcetylationMSQADFDKAAEEVKR
CCHHHHHHHHHHHHH
49.8722902405
14AcetylationDKAAEEVKRLKTQPT
HHHHHHHHHHCCCCC
56.1222902405
17AcetylationAEEVKRLKTQPTDEE
HHHHHHHCCCCCCHH
49.5022902405
17SuccinylationAEEVKRLKTQPTDEE
HHHHHHHCCCCCCHH
49.50-
17SuccinylationAEEVKRLKTQPTDEE
HHHHHHHCCCCCCHH
49.50-
29PhosphorylationDEEMLFIYSHFKQAT
CHHHHHHHHHHCCCC
6.6922108457
30PhosphorylationEEMLFIYSHFKQATV
HHHHHHHHHHCCCCC
20.0325403869
33AcetylationLFIYSHFKQATVGDV
HHHHHHHCCCCCCCC
33.3322902405
51AcetylationRPGLLDLKGKAKWDS
CCCCCCCCCCCCHHC
59.0225786129
51UbiquitinationRPGLLDLKGKAKWDS
CCCCCCCCCCCCHHC
59.02-
53AcetylationGLLDLKGKAKWDSWN
CCCCCCCCCCHHCHH
45.2522902405
55N6-malonyllysineLDLKGKAKWDSWNKL
CCCCCCCCHHCHHHC
55.83-
55MalonylationLDLKGKAKWDSWNKL
CCCCCCCCHHCHHHC
55.83-
55SuccinylationLDLKGKAKWDSWNKL
CCCCCCCCHHCHHHC
55.83-
55AcetylationLDLKGKAKWDSWNKL
CCCCCCCCHHCHHHC
55.8325786129
58PhosphorylationKGKAKWDSWNKLKGT
CCCCCHHCHHHCCCC
31.2829779826
61AcetylationAKWDSWNKLKGTSKE
CCHHCHHHCCCCCHH
45.3722902405
63AcetylationWDSWNKLKGTSKENA
HHCHHHCCCCCHHHH
62.8526302492
67AcetylationNKLKGTSKENAMKTY
HHCCCCCHHHHHHHH
55.6222902405
72AcetylationTSKENAMKTYVEKVE
CCHHHHHHHHHHHHH
34.0022902405
77UbiquitinationAMKTYVEKVEELKKK
HHHHHHHHHHHHHHH
44.92-
77SuccinylationAMKTYVEKVEELKKK
HHHHHHHHHHHHHHH
44.92-
77AcetylationAMKTYVEKVEELKKK
HHHHHHHHHHHHHHH
44.9222902405
77SuccinylationAMKTYVEKVEELKKK
HHHHHHHHHHHHHHH
44.92-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of ACBP_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACBP_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ACBP_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACBP_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACBP_RAT

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Acyl-CoA-binding protein in the rat. Purification, bindingcharacteristics, tissue concentrations and amino acid sequence.";
Knudsen J., Hoejrup P., Hansen H.O., Hansen H.F., Roepstorff P.;
Biochem. J. 262:513-519(1989).
Cited for: PROTEIN SEQUENCE OF 2-87, AND ACETYLATION AT SER-2.

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