ACBP_HUMAN - dbPTM
ACBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACBP_HUMAN
UniProt AC P07108
Protein Name Acyl-CoA-binding protein
Gene Name DBI
Organism Homo sapiens (Human).
Sequence Length 87
Subcellular Localization Endoplasmic reticulum . Golgi apparatus . Golgi localization is dependent on ligand binding (PubMed:17953517).
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 MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKKKYGI
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------MSQAEFEKA
------CCHHHHHHH
37.7929255136
2Acetylation------MSQAEFEKA
------CCHHHHHHH
37.7919413330
8SuccinylationMSQAEFEKAAEEVRH
CCHHHHHHHHHHHHH
59.21-
8SuccinylationMSQAEFEKAAEEVRH
CCHHHHHHHHHHHHH
59.2123954790
8AcetylationMSQAEFEKAAEEVRH
CCHHHHHHHHHHHHH
59.2119608861
17SuccinylationAEEVRHLKTKPSDEE
HHHHHHCCCCCCCHH
48.67-
17AcetylationAEEVRHLKTKPSDEE
HHHHHHCCCCCCCHH
48.6723954790
17SuccinylationAEEVRHLKTKPSDEE
HHHHHHCCCCCCCHH
48.67-
17MalonylationAEEVRHLKTKPSDEE
HHHHHHCCCCCCCHH
48.6726320211
18AcetylationEEVRHLKTKPSDEEM
HHHHHCCCCCCCHHH
55.3219608861
18PhosphorylationEEVRHLKTKPSDEEM
HHHHHCCCCCCCHHH
55.3223403867
19MalonylationEVRHLKTKPSDEEML
HHHHCCCCCCCHHHH
40.7226320211
19AcetylationEVRHLKTKPSDEEML
HHHHCCCCCCCHHHH
40.7219608861
20AcetylationVRHLKTKPSDEEMLF
HHHCCCCCCCHHHHH
52.8519608861
21PhosphorylationRHLKTKPSDEEMLFI
HHCCCCCCCHHHHHE
60.2423403867
25SulfoxidationTKPSDEEMLFIYGHY
CCCCCHHHHHEEEEC
3.3130846556
28 (in isoform 4)Phosphorylation-3.38-
29PhosphorylationDEEMLFIYGHYKQAT
CHHHHHEEEECEEEE
7.1927155012
32PhosphorylationMLFIYGHYKQATVGD
HHHEEEECEEEEECC
10.6327155012
33 (in isoform 4)Phosphorylation-27.99-
36PhosphorylationYGHYKQATVGDINTE
EEECEEEEECCCCCC
23.6420068231
37 (in isoform 4)Phosphorylation-7.90-
42PhosphorylationATVGDINTERPGMLD
EEECCCCCCCCCCCC
33.4328555341
47 (in isoform 5)Phosphorylation-3.44-
47SulfoxidationINTERPGMLDFTGKA
CCCCCCCCCCCCCCC
3.4428465586
51PhosphorylationRPGMLDFTGKAKWDA
CCCCCCCCCCCCHHH
37.1220068231
52 (in isoform 5)Phosphorylation-28.11-
53AcetylationGMLDFTGKAKWDAWN
CCCCCCCCCCHHHHH
43.6723236377
53MalonylationGMLDFTGKAKWDAWN
CCCCCCCCCCHHHHH
43.6726320211
53UbiquitinationGMLDFTGKAKWDAWN
CCCCCCCCCCHHHHH
43.67-
53 (in isoform 1)Ubiquitination-43.6721890473
53UbiquitinationGMLDFTGKAKWDAWN
CCCCCCCCCCHHHHH
43.6722053931
55UbiquitinationLDFTGKAKWDAWNEL
CCCCCCCCHHHHHHC
49.4419608861
55AcetylationLDFTGKAKWDAWNEL
CCCCCCCCHHHHHHC
49.4419608861
55N6-malonyllysineLDFTGKAKWDAWNEL
CCCCCCCCHHHHHHC
49.44-
55MalonylationLDFTGKAKWDAWNEL
CCCCCCCCHHHHHHC
49.4421908771
55 (in isoform 1)Ubiquitination-49.4421890473
55SuccinylationLDFTGKAKWDAWNEL
CCCCCCCCHHHHHHC
49.44-
56AcetylationDFTGKAKWDAWNELK
CCCCCCCHHHHHHCC
12.8619608861
56 (in isoform 5)Phosphorylation-12.86-
56UbiquitinationDFTGKAKWDAWNELK
CCCCCCCHHHHHHCC
12.8619608861
59AcetylationGKAKWDAWNELKGTS
CCCCHHHHHHCCCCC
9.0719608861
61AcetylationAKWDAWNELKGTSKE
CCHHHHHHCCCCCHH
40.9519608861
63SuccinylationWDAWNELKGTSKEDA
HHHHHHCCCCCHHHH
54.7023954790
63UbiquitinationWDAWNELKGTSKEDA
HHHHHHCCCCCHHHH
54.70-
63 (in isoform 1)Ubiquitination-54.7021890473
63UbiquitinationWDAWNELKGTSKEDA
HHHHHHCCCCCHHHH
54.7021890473
65PhosphorylationAWNELKGTSKEDAMK
HHHHCCCCCHHHHHH
34.73-
65UbiquitinationAWNELKGTSKEDAMK
HHHHCCCCCHHHHHH
34.7321890473
66PhosphorylationWNELKGTSKEDAMKA
HHHCCCCCHHHHHHH
42.5930576142
67SuccinylationNELKGTSKEDAMKAY
HHCCCCCHHHHHHHH
60.4923954790
70 (in isoform 2)Ubiquitination-11.4921890473
70UbiquitinationKGTSKEDAMKAYINK
CCCCHHHHHHHHHHH
11.4921890473
72 (in isoform 2)Ubiquitination-39.4921890473
72UbiquitinationTSKEDAMKAYINKVE
CCHHHHHHHHHHHHH
39.4921890473
72AcetylationTSKEDAMKAYINKVE
CCHHHHHHHHHHHHH
39.4921339330
73UbiquitinationSKEDAMKAYINKVEE
CHHHHHHHHHHHHHH
9.4321890473
74PhosphorylationKEDAMKAYINKVEEL
HHHHHHHHHHHHHHH
10.2528152594
77SuccinylationAMKAYINKVEELKKK
HHHHHHHHHHHHHHH
41.27-
77UbiquitinationAMKAYINKVEELKKK
HHHHHHHHHHHHHHH
41.2722053931
77 (in isoform 1)Ubiquitination-41.2721890473
77AcetylationAMKAYINKVEELKKK
HHHHHHHHHHHHHHH
41.2719608861
77SuccinylationAMKAYINKVEELKKK
HHHHHHHHHHHHHHH
41.2723954790
77UbiquitinationAMKAYINKVEELKKK
HHHHHHHHHHHHHHH
41.2719608861
78UbiquitinationMKAYINKVEELKKKY
HHHHHHHHHHHHHHH
6.2919608861
78AcetylationMKAYINKVEELKKKY
HHHHHHHHHHHHHHH
6.2919608861
80UbiquitinationAYINKVEELKKKYGI
HHHHHHHHHHHHHCC
69.7221890473
80AcetylationAYINKVEELKKKYGI
HHHHHHHHHHHHHCC
69.7219608861
80 (in isoform 2)Ubiquitination-69.7221890473
82AcetylationINKVEELKKKYGI--
HHHHHHHHHHHCC--
50.9625953088
82UbiquitinationINKVEELKKKYGI--
HHHHHHHHHHHCC--
50.96-
87UbiquitinationELKKKYGI-------
HHHHHHCC-------
4.6521890473
90 (in isoform 5)Phosphorylation-27642862
94UbiquitinationI--------------
C--------------
21890473
94 (in isoform 2)Ubiquitination-21890473
97Acetylation-----------------
-----------------
19608861
97Ubiquitination-----------------
-----------------
19608861
112 (in isoform 5)Phosphorylation-27251275
114Ubiquitination----------------------------------
----------------------------------
21890473
114Ubiquitination----------------------------------
----------------------------------
21890473
114 (in isoform 5)Ubiquitination--
116Acetylation------------------------------------
------------------------------------
19608861
116Ubiquitination------------------------------------
------------------------------------
19608861
116 (in isoform 5)Ubiquitination--
116Ubiquitination------------------------------------
------------------------------------
21890473
116Ubiquitination------------------------------------
------------------------------------
21890473
119Ubiquitination---------------------------------------
---------------------------------------
19608861
119Acetylation---------------------------------------
---------------------------------------
19608861
124Ubiquitination--------------------------------------------
--------------------------------------------
21890473
124 (in isoform 5)Ubiquitination--
124Ubiquitination--------------------------------------------
--------------------------------------------
21890473
138Ubiquitination----------------------------------------------------------
----------------------------------------------------------
19608861
138Ubiquitination----------------------------------------------------------
----------------------------------------------------------
21890473
138 (in isoform 5)Ubiquitination--
138Acetylation----------------------------------------------------------
----------------------------------------------------------
19608861
138Ubiquitination----------------------------------------------------------
----------------------------------------------------------
21890473

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CH10_HUMANHSPE1physical
26344197
LEG3_HUMANLGALS3physical
26344197
MFTC_HUMANSLC25A32physical
26344197

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"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.
Malonylation
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.
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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