dbPTM

AQP4_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AQP4_RAT
UniProt AC	P47863
Protein Name	Aquaporin-4
Gene Name	Aqp4
Organism	Rattus norvegicus (Rat).
Sequence Length	323
Subcellular Localization	Membrane Multi-pass membrane protein.
Protein Description	Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system. It is expressed predominantly in the ependymal cell lining the aqueductal system and over the space of the brain in contact with the subarachnoid space, as cerebrospinal fluid fills these structures it may facilitate water balance between brain parenchyma and the fluid compartment. In the plasma membranes of the neurons of the paraventricular and supraoptic nuclei, it may mediate rapid changes in cell volume in response to local shifts in extracellular osmolarity..
Protein Sequence	MSDGAAARRWGKCGPPCSRESIMVAFKGVWTQAFWKAVTAEFLAMLIFVLLSVGSTINWGGSENPLPVDMVLISLCFGLSIATMVQCFGHISGGHINPAVTVAMVCTRKISIAKSVFYITAQCLGAIIGAGILYLVTPPSVVGGLGVTTVHGNLTAGHGLLVELIITFQLVFTIFASCDSKRTDVTGSVALAIGFSVAIGHLFAINYTGASMNPARSFGPAVIMGNWENHWIYWVGPIIGAVLAGALYEYVFCPDVELKRRLKEAFSKAAQQTKGSYMEVEDNRSQVETEDLILKPGVVHVIDIDRGDEKKGKDSSGEVLSSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	S-palmitoylation	AARRWGKCGPPCSRE HHHHCCCCCCCCCHH	9.73	18179769
17	S-palmitoylation	WGKCGPPCSRESIMV CCCCCCCCCHHHHHH	7.24	18179769
111	Phosphorylation	MVCTRKISIAKSVFY HHHCCCHHHHHHHHH	21.38	19297454
153	N-linked_Glycosylation	GVTTVHGNLTAGHGL CEEEECCCEECCCCH	21.24	-
180	Phosphorylation	TIFASCDSKRTDVTG HHHHCCCCCCCCCCH	28.50	19800950
263	Acetylation	VELKRRLKEAFSKAA HHHHHHHHHHHHHHH	45.22	22902405
263	Ubiquitination	VELKRRLKEAFSKAA HHHHHHHHHHHHHHH	45.22	-
268	Ubiquitination	RLKEAFSKAAQQTKG HHHHHHHHHHHHHCC	41.09	-
268	Acetylation	RLKEAFSKAAQQTKG HHHHHHHHHHHHHCC	41.09	22902405
273	Phosphorylation	FSKAAQQTKGSYMEV HHHHHHHHCCCCEEE	25.87	28551015
274	Ubiquitination	SKAAQQTKGSYMEVE HHHHHHHCCCCEEEC	41.33	-
276	Phosphorylation	AAQQTKGSYMEVEDN HHHHHCCCCEEECCC	23.90	17683130
277	Phosphorylation	AQQTKGSYMEVEDNR HHHHCCCCEEECCCC	13.13	27097102
285	Phosphorylation	MEVEDNRSQVETEDL EEECCCCHHEEHHHE	44.85	27097102
289	Phosphorylation	DNRSQVETEDLILKP CCCHHEEHHHEEECC	35.62	27097102
295	Ubiquitination	ETEDLILKPGVVHVI EHHHEEECCCEEEEE	32.50	-
295	Acetylation	ETEDLILKPGVVHVI EHHHEEECCCEEEEE	32.50	22902405
313	Ubiquitination	RGDEKKGKDSSGEVL CCCCCCCCCCCCCCC	64.42	-
315	Phosphorylation	DEKKGKDSSGEVLSS CCCCCCCCCCCCCCC	43.67	22108457
316	Phosphorylation	EKKGKDSSGEVLSSV CCCCCCCCCCCCCCC	49.45	25403869
321	Phosphorylation	DSSGEVLSSV----- CCCCCCCCCC-----	33.94	22108457
322	Phosphorylation	SSGEVLSSV------ CCCCCCCCC------	27.90	22108457

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
111	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
111	S	Phosphorylation	Kinase	PKG	-	Uniprot
180	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
180	S	Phosphorylation	Kinase	PKC	-	Uniprot
276	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
285	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
315	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
111	S	Phosphorylation	19800950
Phosphorylation by PKG at Ser-111 in response to glutamate increases conductance by 40% (By similarity).
180	S	Phosphorylation	19800950
Phosphorylation by PKC at Ser-180 promotes internalization from the cell membrane, reducing the conductance by 50%.

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 AQP4_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AQP4_RAT !!

Drug and Disease Associations

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

Regulatory Network of AQP4_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Vasopressin-dependent short-term regulation of aquaporin 4 expressedin Xenopus oocytes."; Moeller H.B., Fenton R.A., Zeuthen T., Macaulay N.; Neuroscience 164:1674-1684(2009). Cited for: PHOSPHORYLATION AT SER-180.	19800950 [Abstract]
"Identification of a molecular target for glutamate regulation ofastrocyte water permeability."; Gunnarson E., Zelenina M., Axehult G., Song Y., Bondar A., Krieger P.,Brismar H., Zelenin S., Aperia A.; Glia 56:587-596(2008). Cited for: PHOSPHORYLATION AT SER-111.	18286643 [Abstract]
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND MASSSPECTROMETRY.	16641100 [Abstract]
"A method for the comprehensive proteomic analysis of membraneproteins."; Wu C.C., MacCoss M.J., Howell K.E., Yates J.R. III; Nat. Biotechnol. 21:532-538(2003). Cited for: PHOSPHORYLATION AT SER-285.	12692561 [Abstract]