CESA7_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CESA7_ARATH
• UniProt AC: Q9SWW6
• Protein Name: Cellulose synthase A catalytic subunit 7 [UDP-forming]
• Gene Name: CESA7
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1026
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the secondary cell wall formation. Required for the xylem cell wall thickening..
• Protein Sequence: MEASAGLVAGSHNRNELVVIHNHEEPKPLKNLDGQFCEICGDQIGLTVEGDLFVACNECGFPACRPCYEYERREGTQNCPQCKTRYKRLRGSPRVEGDEDEEDIDDIEYEFNIEHEQDKHKHSAEAMLYGKMSYGRGPEDDENGRFPPVIAGGHSGEFPVGGGYGNGEHGLHKRVHPYPSSEAGSEGGWRERMDDWKLQHGNLGPEPDDDPEMGLIDEARQPLSRKVPIASSKINPYRMVIVARLVILAVFLRYRLLNPVHDALGLWLTSVICEIWFAVSWILDQFPKWFPIERETYLDRLSLRYEREGEPNMLAPVDVFVSTVDPLKEPPLVTSNTVLSILAMDYPVEKISCYVSDDGASMLTFESLSETAEFARKWVPFCKKFSIEPRAPEMYFTLKVDYLQDKVHPTFVKERRAMKREYEEFKVRINAQVAKASKVPLEGWIMQDGTPWPGNNTKDHPGMIQVFLGHSGGFDVEGHELPRLVYVSREKRPGFQHHKKAGAMNALVRVAGVLTNAPFMLNLDCDHYVNNSKAVREAMCFLMDPQIGKKVCYVQFPQRFDGIDTNDRYANRNTVFFDINMKGLDGIQGPVYVGTGCVFKRQALYGYEPPKGPKRPKMISCGCCPCFGRRRKNKKFSKNDMNGDVAALGGAEGDKEHLMSEMNFEKTFGQSSIFVTSTLMEEGGVPPSSSPAVLLKEAIHVISCGYEDKTEWGTELGWIYGSITEDILTGFKMHCRGWRSIYCMPKRPAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHSPLWYGYKGGKLKWLERFAYANTTIYPFTSIPLLAYCILPAICLLTDKFIMPPISTFASLFFISLFMSIIVTGILELRWSGVSIEEWWRNEQFWVIGGISAHLFAVVQGLLKILAGIDTNFTVTSKATDDDDFGELYAFKWTTLLIPPTTVLIINIVGVVAGISDAINNGYQSWGPLFGKLFFSFWVIVHLYPFLKGLMGRQNRTPTIVVIWSVLLASIFSLLWVRIDPFVLKTKGPDTSKCGINC

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	-------MEASAGLV -------CCCCCCCE	42.42	-
178	Phosphorylation	LHKRVHPYPSSEAGS CCCCCCCCCCCCCCC	10.81	25561503
180	Phosphorylation	KRVHPYPSSEAGSEG CCCCCCCCCCCCCCC	34.66	25561503
181	Phosphorylation	RVHPYPSSEAGSEGG CCCCCCCCCCCCCCC	27.28	30407730
185	Phosphorylation	YPSSEAGSEGGWRER CCCCCCCCCCCHHHC	39.87	30291188
621	S-palmitoylation	KRPKMISCGCCPCFG CCCCCEECCCCCCCC	3.15	27387950
623	S-palmitoylation	PKMISCGCCPCFGRR CCCEECCCCCCCCCC	2.48	27387950
624	S-palmitoylation	KMISCGCCPCFGRRR CCEECCCCCCCCCCC	1.67	27387950
626	S-palmitoylation	ISCGCCPCFGRRRKN EECCCCCCCCCCCCC	3.35	27387950
900	N-linked_Glycosylation	ILAGIDTNFTVTSKA HHHCCCCCEEEEECC	27.18	-
1022	S-palmitoylation	KGPDTSKCGINC--- CCCCCCCCCCCC---	7.10	27387950
1026	S-palmitoylation	TSKCGINC------- CCCCCCCC-------	5.80	27387950

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

Oops, there are no upstream regulatory protein records of CESA7_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CESA7_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 CESA7_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CESA7_ARATH	IRX3	physical	19056734
CESA4_ARATH	CESA4	physical	19056734
CESA8_ARATH	IRX1	physical	19056734
CESA4_ARATH	CESA4	physical	12538856
CESA8_ARATH	IRX1	physical	12538856
CESA1_ARATH	CESA1	physical	22926318
CESA3_ARATH	CEV1	physical	22926318
CESA4_ARATH	CESA4	physical	22926318
CESA6_ARATH	CESA6	physical	22926318
CESA8_ARATH	IRX1	physical	22926318
CNIH1_ARATH	AT3G12180	physical	24833385
CESA4_ARATH	CESA4	physical	19258017
CESA8_ARATH	IRX1	physical	19258017

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Identification of cellulose synthase AtCesA7 (IRX3) in vivophosphorylation sites -- a potential role in regulating proteindegradation.";
Taylor N.G.;
Plant Mol. Biol. 64:161-171(2007).
Cited for: PHOSPHORYLATION AT SER-185, AND MASS SPECTROMETRY.
PubMed: 17427041