CINV1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CINV1_ARATH
• UniProt AC: Q9LQF2
• Protein Name: Alkaline/neutral invertase CINV1 {ECO:0000305}
• Gene Name: CINV1 {ECO:0000303|PubMed:17508130}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 551
• Subcellular Localization: Cytoplasm, cytosol . Nucleus . Detected in membrane and nucleus when associated with PIP5K9.
• Protein Description: Cytosolic invertase that specifically cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development including primary root elongation, root hair growth, leaf and silique development, and floral transition. Is involved in osmotic stress-induced inhibition on lateral root growth by controlling the concentration of hexose in cells. May regulate sugar-mediated root development by controlling sucrose catabolism in root cells..
• Protein Sequence: MEGVGLRAVGSHCSLSEMDDLDLTRALDKPRLKIERKRSFDERSMSELSTGYSRHDGIHDSPRGRSVLDTPLSSARNSFEPHPMMAEAWEALRRSMVFFRGQPVGTLAAVDNTTDEVLNYDQVFVRDFVPSALAFLMNGEPDIVKHFLLKTLQLQGWEKRVDRFKLGEGVMPASFKVLHDPIRETDNIVADFGESAIGRVAPVDSGFWWIILLRAYTKSTGDLTLSETPECQKGMKLILSLCLAEGFDTFPTLLCADGCSMIDRRMGVYGYPIEIQALFFMALRSALSMLKPDGDGREVIERIVKRLHALSFHMRNYFWLDHQNLNDIYRFKTEEYSHTAVNKFNVMPDSIPEWVFDFMPLRGGYFVGNVGPAHMDFRWFALGNCVSILSSLATPDQSMAIMDLLEHRWAELVGEMPLKICYPCLEGHEWRIVTGCDPKNTRWSYHNGGSWPVLLWQLTAACIKTGRPQIARRAVDLIESRLHRDCWPEYYDGKLGRYVGKQARKYQTWSIAGYLVAKMLLEDPSHIGMISLEEDKLMKPVIKRSASWPQL

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
1	Acetylation	-------MEGVGLRA -------CCCCCCEE		22223895
11	Phosphorylation	VGLRAVGSHCSLSEM CCCEECCCCCCHHHC		30291188
14	Phosphorylation	RAVGSHCSLSEMDDL EECCCCCCHHHCCCC		30291188
16	Phosphorylation	VGSHCSLSEMDDLDL CCCCCCHHHCCCCHH		24601666
24	Phosphorylation	EMDDLDLTRALDKPR HCCCCHHHHHHCCCC		23776212
39	Phosphorylation	LKIERKRSFDERSMS HHHEECCCCCHHHHH		23776212
44	Phosphorylation	KRSFDERSMSELSTG CCCCCHHHHHHHHCC		19880383
46	Phosphorylation	SFDERSMSELSTGYS CCCHHHHHHHHCCCC		19880383
49	Phosphorylation	ERSMSELSTGYSRHD HHHHHHHHCCCCCCC		19880383
50	Phosphorylation	RSMSELSTGYSRHDG HHHHHHHCCCCCCCC		19880383
52	Phosphorylation	MSELSTGYSRHDGIH HHHHHCCCCCCCCCC		23776212
53	Phosphorylation	SELSTGYSRHDGIHD HHHHCCCCCCCCCCC		23776212
61	Phosphorylation	RHDGIHDSPRGRSVL CCCCCCCCCCCCCCC		19880383
66	Phosphorylation	HDSPRGRSVLDTPLS CCCCCCCCCCCCCCH		30291188
70	Phosphorylation	RGRSVLDTPLSSARN CCCCCCCCCCHHCCC		30291188
73	Phosphorylation	SVLDTPLSSARNSFE CCCCCCCHHCCCCCC		30291188
74	Phosphorylation	VLDTPLSSARNSFEP CCCCCCHHCCCCCCC		19880383
545	Phosphorylation	MKPVIKRSASWPQL- HHHHHHHCCCCCCC-		23776212
547	Phosphorylation	PVIKRSASWPQL--- HHHHHCCCCCCC---		19880383

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

Oops, there are no upstream regulatory protein records of CINV1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
547	S	Phosphorylation	Phosphorylated at Ser-547 by CPK3 and CPK21.	18433157

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CINV1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PI5K9_ARATH	PIP5K9	physical	17220200
14337_ARATH	GRF7	physical	21798944
14333_ARATH	GRF3	physical	21798944
14310_ARATH	GRF10	physical	25256212
14338_ARATH	GRF8	physical	25256212
14336_ARATH	GRF6	physical	25256212
14337_ARATH	GRF7	physical	25256212
14335_ARATH	GRF5	physical	25256212
14334_ARATH	GF14 PHI	physical	25256212
14331_ARATH	GRF1	physical	25256212
14333_ARATH	GRF3	physical	25256212
14332_ARATH	GRF2	physical	25256212

Drug and Disease Associations

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