ACLB2_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ACLB2_ARATH
• UniProt AC: Q9FGX1
• Protein Name: ATP-citrate synthase beta chain protein 2
• Gene Name: ACLB-2
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 608
• Subcellular Localization: Cytoplasm, cytosol .
• Protein Description: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. n contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains..
• Protein Sequence: MATGQLFSRTTQALFYNYKQLPVQRMLDFDFLCGRETPSVAGIINPGSEGFQKLFFGQEEIAIPVHAAIEAACAAHPTADVFINFASFRSAAASSMAALKQPTIKVVAIIAEGVPESDTKQLIAYARANNKVVIGPATVGGIQAGAFKIGDTAGTIDNIIQCKLYRPGSVGFVSKSGGMSNEMYNTVARVTDGIYEGIAIGGDVFPGSTLSDHILRFNNIPQIKMMVVLGELGGRDEYSLVEALKEGKVNKPVVAWVSGTCARLFKSEVQFGHAGAKSGGEMESAQAKNQALIDAGAIVPTSFEALESAIKETFEKLVEEGKVSPIKEVIPPQIPEDLNSAIKSGKVRAPTHIISTISDDRGEEPCYAGVPMSSIIEQGYGVGDVISLLWFKRSLPRYCTKFIEICIMLCADHGPCVSGAHNTIVTARAGKDLVSSLVSGLLTIGPRFGGAIDDAARYFKDACDRNLTPYEFVEGMKKKGIRVPGIGHRIKSRDNRDKRVELLQKFARSNFPSVKYMEYAVTVETYTLSKANNLVLNVDGAIGSLFLDLLAGSGMFTKQEIDEIVQIGYLNGLFVLARSIGLIGHTFDQKRLKQPLYRHPWEDVLYTK

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
152	Phosphorylation	GAFKIGDTAGTIDNI CCEECCCCCCCCCCE	23.05	25368622
155	Phosphorylation	KIGDTAGTIDNIIQC ECCCCCCCCCCEEEC	23.77	25368622
165	Phosphorylation	NIIQCKLYRPGSVGF CEEECEEECCCCEEE	10.56	25368622
169	Phosphorylation	CKLYRPGSVGFVSKS CEEECCCCEEEEECC	23.04	25368622
174	Phosphorylation	PGSVGFVSKSGGMSN CCCEEEEECCCCCCH	20.88	25368622
176	Phosphorylation	SVGFVSKSGGMSNEM CEEEEECCCCCCHHH	32.83	19880383
180	Phosphorylation	VSKSGGMSNEMYNTV EECCCCCCHHHHHHH	32.67	19880383
184	Phosphorylation	GGMSNEMYNTVARVT CCCCHHHHHHHHHHC	11.08	19880383
186	Phosphorylation	MSNEMYNTVARVTDG CCHHHHHHHHHHCCC	9.69	19880383
324	Phosphorylation	LVEEGKVSPIKEVIP HHHCCCCCCCCCCCC	25.13	25561503
527	Phosphorylation	AVTVETYTLSKANNL EEEEEEEECCCCCCE	31.79	19880383

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ACLB2_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ACLB2_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ACLB2_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of ACLB2_ARATH !!

Drug and Disease Associations

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