dbPTM

ACBP5_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACBP5_ARATH
UniProt AC	Q8RWD9
Protein Name	Acyl-CoA-binding domain-containing protein 5
Gene Name	ACBP5
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	648
Subcellular Localization	Cytoplasm .
Protein Description	Binds medium- and long-chain acyl-CoA esters with very high affinity. Can interact in vitro with oleoyl-CoA, barely with palmitoyl-CoA, but not with arachidonyl-CoA. May function as an intracellular carrier of acyl-CoA esters (By similarity)..
Protein Sequence	MAHMVRASSGLSYPERFYAAASYVGLDGSQSSVKQLSSKFSNDTSLLLYTLHQQATLGPCSIPKPSAWNPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEADPGWYPRTSNSVLDPAVHVQINSTKAEPSFESGASFGETKTITSEDGRLTETQDKDVVLEDPDTVSVYNQWTAPRTSGQPPKARYQHGAAVIQDKMYMYGGNHNGRYLGDLHVLDLKNWTWSRVETKVVTGSQETSSPAKLTHCAGHSLIPWDNQLLSIGGHTKDPSESMPVMVFDLHCCSWSILKTYGKPPISRGGQSVTLVGKSLVIFGGQDAKRSLLNDLHILDLDTMTWEEIDAVGSPPTPRSDHAAAVHAERYLLIFGGGSHATCFDDLHVLDLQTMEWSRHTQQGDAPTPRAGHAGVTIGENWYIVGGGDNKSGASKTVVLNMSTLAWSVVTSVQEHVPLASEGLSLVVSSYNGEDIVVAFGGYNGHYNNEVNVLKPSHKSSLKSKIMGASAVPDSFSAVNNATTRDIESEIKVEGKADRIITTLKSEKEEVEASLNKEKIQTLQLKEELAEIDTRNTELYKELQSVRNQLAAEQSRCFKLEVEVAELRQKLQTMETLQKELELLQRQRAVASEQAATMNAKRQSSGGVWGWLAGTPPPKT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MAHMVRASSGLSYPE CCCCCCCCCCCCCCH	17.86	19880383
9	Phosphorylation	AHMVRASSGLSYPER CCCCCCCCCCCCCHH	42.65	23111157
12	Phosphorylation	VRASSGLSYPERFYA CCCCCCCCCCHHHHH	42.01	19376835
13	Phosphorylation	RASSGLSYPERFYAA CCCCCCCCCHHHHHH	17.73	23660473
133	Phosphorylation	KAEPSFESGASFGET CCCCCCCCCCCCCCC	37.33	22631563
136	Phosphorylation	PSFESGASFGETKTI CCCCCCCCCCCCEEE	36.99	19880383
140	Phosphorylation	SGASFGETKTITSED CCCCCCCCEEEECCC	33.59	19880383
144	Phosphorylation	FGETKTITSEDGRLT CCCCEEEECCCCCEE	31.15	25561503
145	Phosphorylation	GETKTITSEDGRLTE CCCEEEECCCCCEEC	29.82	25561503
517	Phosphorylation	ATTRDIESEIKVEGK CCCCCHHHHEEECCC	44.98	30291188

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 ACBP5_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACBP5_ARATH !!

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 ACBP5_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ACBP5_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ACBP5_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	19376835 [Abstract]