dbPTM

ACBP4_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACBP4_ARATH
UniProt AC	Q9MA55
Protein Name	Acyl-CoA-binding domain-containing protein 4
Gene Name	ACBP4
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	668
Subcellular Localization	Cytoplasm . Also to the periphery of the nucleus.
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. Plays a role in the biosynthesis of membrane lipids including galactolipids and phospholipids..
Protein Sequence	MAMPRATSGPAYPERFYAAASYVGLDGSDSSAKNVISKFPDDTALLLYALYQQATVGPCNTPKPSAWRPVEQSKWKSWQGLGTMPSIEAMRLFVKILEEDDPGWYSRASNDIPDPVVDVQINRAKDEPVVENGSTFSETKTISTENGRLAETQDKDVVSEDSNTVSVYNQWTAPQTSGQRPKARYEHGAAVIQDKMYIYGGNHNGRYLGDLHVLDLKSWTWSRVETKVATESQETSTPTLLAPCAGHSLIAWDNKLLSIGGHTKDPSESMQVKVFDPHTITWSMLKTYGKPPVSRGGQSVTMVGKTLVIFGGQDAKRSLLNDLHILDLDTMTWDEIDAVGVSPSPRSDHAAAVHAERFLLIFGGGSHATCFDDLHVLDLQTMEWSRPAQQGDAPTPRAGHAGVTIGENWFIVGGGDNKSGASESVVLNMSTLAWSVVASVQGRVPLASEGLSLVVSSYNGEDVLVAFGGYNGRYNNEINLLKPSHKSTLQTKTLEAPLPGSLSAVNNATTRDIESEVEVSQEGRVREIVMDNVNPGSKVEGNSERIIATIKSEKEELEASLNKERMQTLQLRQELGEAELRNTDLYKELQSVRGQLAAEQSRCFKLEVDVAELRQKLQTLETLQKELELLQRQKAASEQAAMNAKRQGSGGVWGWLAGSPQEKDDDSP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MAMPRATSGPAYPE -CCCCCCCCCCCCCH	35.18	23776212
8	Phosphorylation	MAMPRATSGPAYPER CCCCCCCCCCCCCHH	41.62	19880383
12	Phosphorylation	RATSGPAYPERFYAA CCCCCCCCCHHHHEE	14.57	23776212
134	Phosphorylation	EPVVENGSTFSETKT CCCEECCCCCCEEEE	37.55	23776212
135	Phosphorylation	PVVENGSTFSETKTI CCEECCCCCCEEEEE	32.36	23776212
137	Phosphorylation	VENGSTFSETKTIST EECCCCCCEEEEEEC	44.43	30291188
139	Phosphorylation	NGSTFSETKTISTEN CCCCCCEEEEEECCC	32.08	23776212
141	Phosphorylation	STFSETKTISTENGR CCCCEEEEEECCCCC	27.81	25561503
143	Phosphorylation	FSETKTISTENGRLA CCEEEEEECCCCCEE	34.59	25561503
144	Phosphorylation	SETKTISTENGRLAE CEEEEEECCCCCEEE	29.62	25561503
493	Phosphorylation	KSTLQTKTLEAPLPG CCCCCEEEECCCCCC	32.97	23776212
501	Phosphorylation	LEAPLPGSLSAVNNA ECCCCCCCHHHHCCC	19.74	30291188
503	Phosphorylation	APLPGSLSAVNNATT CCCCCCHHHHCCCCC	31.69	30291188
509	Phosphorylation	LSAVNNATTRDIESE HHHHCCCCCCCCCCC	25.20	30291188
510	Phosphorylation	SAVNNATTRDIESEV HHHCCCCCCCCCCCE	24.76	19880383
515	Phosphorylation	ATTRDIESEVEVSQE CCCCCCCCCEEECCC	47.48	30291188
520	Phosphorylation	IESEVEVSQEGRVRE CCCCEEECCCCCEEE	14.70	30291188
543	Phosphorylation	GSKVEGNSERIIATI CCCCCCCCCEEEEEE	38.82	30291188
637	Phosphorylation	LQRQKAASEQAAMNA HHHHHHHHHHHHHHH	34.79	25561503
649	Phosphorylation	MNAKRQGSGGVWGWL HHHHHHCCCCCCHHH	24.84	23776212
659	Phosphorylation	VWGWLAGSPQEKDDD CCHHHCCCCCCCCCC	20.15	23776212
667	Phosphorylation	PQEKDDDSP------ CCCCCCCCC------	39.23	24601666

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 ACBP4_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACBP4_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 ACBP4_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RAP23_ARATH	EBP	physical	18836139
CKL1_ARATH	CK1	physical	21798944

Drug and Disease Associations

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

Regulatory Network of ACBP4_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-501; SER-515 ANDSER-520, AND MASS SPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND MASSSPECTROMETRY.	19245862 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501; SER-503; SER-515AND SER-520, AND MASS SPECTROMETRY.	18433157 [Abstract]