PIP24_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIP24_ARATH
• UniProt AC: Q9FF53
• Protein Name: Probable aquaporin PIP2-4
• Gene Name: PIP2-4
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 291
• Subcellular Localization: Cell membrane; Multi-pass membrane protein.
• Protein Description: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes..
• Protein Sequence: MAKDLDVNESGPPAARDYKDPPPAPFFDMEELRKWPLYRAVIAEFVATLLFLYVSILTVIGYKAQTDATAGGVDCGGVGILGIAWAFGGMIFVLVYCTAGISGGHINPAVTVGLFLARKVSLVRTVLYIVAQCLGAICGCGFVKAFQSSYYTRYGGGANELADGYNKGTGLGAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNNEKAWDDQWIFWVGPMIGAAAAAFYHQFILRAAAIKALGSFGSFGSFRSFA

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	-------MAKDLDVN -------CCCCCCCC	10.63	-
2	Acetylation	------MAKDLDVNE ------CCCCCCCCC	17.67	-
3	Methylation	-----MAKDLDVNES -----CCCCCCCCCC	58.48	-
280	Phosphorylation	AAIKALGSFGSFGSF HHHHHHHCCCCCCCC	27.55	30291188
283	Phosphorylation	KALGSFGSFGSFRSF HHHHCCCCCCCCCCC	25.15	30291188
286	Phosphorylation	GSFGSFGSFRSFA-- HCCCCCCCCCCCC--	18.57	30291188
289	Phosphorylation	GSFGSFRSFA----- CCCCCCCCCC-----	24.42	23111157

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

Oops, there are no upstream regulatory protein records of PIP24_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIP24_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 PIP24_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of PIP24_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-286, AND MASSSPECTROMETRY.
PubMed: 19245862