CESA5_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CESA5_ARATH
• UniProt AC: Q8L778
• Protein Name: Cellulose synthase A catalytic subunit 5 [UDP-forming]
• Gene Name: CESA5
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1069
• 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..
• Protein Sequence: MNTGGRLIAGSHNRNEFVLINADESARIRSVEELSGQTCQICGDEIELSVDGESFVACNECAFPVCRPCYEYERREGNQSCPQCKTRYKRIKGSPRVEGDEEDDGIDDLDFEFDYSRSGLESETFSRRNSEFDLASAPPGSQIPLLTYGEEDVEISSDSHALIVSPSPGHIHRVHQPHFPDPAAHPRPMVPQKDLAVYGYGSVAWKDRMEEWKRKQNEKYQVVKHDGDSSLGDGDDADIPMMDEGRQPLSRKVPIKSSKINPYRMLIVLRLVILGLFFHYRILHPVNDAYALWLISVICEIWFAVSWVLDQFPKWYPIERETYLDRLSLRYEKEGKPSELAGVDVFVSTVDPMKEPPLITANTVLSILAVDYPVDRVACYVSDDGAAMLTFEALSETAEFARKWVPFCKKYTIEPRAPEWYFCHKMDYLKNKVHPAFVRERRAMKRDYEEFKVKINALVATAQKVPEEGWTMQDGTPWPGNNVRDHPGMIQVFLGNNGVRDVENNELPRLVYVSREKRPGFDHHKKAGAMNSLIRVSGVLSNAPYLLNVDCDHYINNSKALREAMCFMMDPQSGKKICYVQFPQRFDGIDKSDRYSNRNVVFFDINMKGLDGLQGPIYVGTGCVFRRQALYGFDAPKKKKTKRMTCNCWPKWCLFCCGLRKNRKSKTTDKKKKNREASKQIHALENIEEGTKGTNDAAKSPEAAQLKLEKKFGQSPVFVASAGMENGGLARNASPASLLREAIQVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHSHGWRSVYCTPKIPAFKGSAPINLSDRLHQVLRWALGSVEIFLSRHCPIWYGYGGGLKWLERLSYINSVVYPWTSIPLLVYCSLPAICLLTGKFIVPEISNYASILFMALFGSIAVTGILEMQWGKVGIDDWWRNEQFWVIGGVSAHLFALFQGLLKVLAGVETNFTVTSKAADDGEFSELYIFKWTSLLIPPTTLLIINVIGVIVGISDAISNGYDSWGPLFGRLFFAFWVILHLYPFLKGLLGKQDRMPTIILVWSILLASILTLLWVRVNPFVAKGGPILEICGLDCL

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	-------MNTGGRLI -------CCCCCCEE	43.72	-
11	Phosphorylation	GGRLIAGSHNRNEFV CCCEEECCCCCCCEE	14.47	25561503
118	Phosphorylation	FEFDYSRSGLESETF EEEECCCCCCCCCCC	41.61	25561503
122	Phosphorylation	YSRSGLESETFSRRN CCCCCCCCCCCCCCC	47.15	30407730
124	Phosphorylation	RSGLESETFSRRNSE CCCCCCCCCCCCCCC	35.87	30407730
126	Phosphorylation	GLESETFSRRNSEFD CCCCCCCCCCCCCCC	37.44	30407730
229	Phosphorylation	VVKHDGDSSLGDGDD EEECCCCCCCCCCCC	32.75	15308754
230	Phosphorylation	VKHDGDSSLGDGDDA EECCCCCCCCCCCCC	40.90	15308754
943	N-linked_Glycosylation	VLAGVETNFTVTSKA HHHCCCCCEEEEECC	19.65	-

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

Oops, there are no upstream regulatory protein records of CESA5_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CESA5_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 CESA5_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of CESA5_ARATH !!

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-229 AND SER-230, AND MASS SPECTROMETRY.
PubMed: 17427041

"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-230, ANDMASS SPECTROMETRY.
PubMed: 15308754