dbPTM

CESA1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CESA1_ARATH
UniProt AC	O48946
Protein Name	Cellulose synthase A catalytic subunit 1 [UDP-forming]
Gene Name	CESA1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1081
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 primary cell wall formation. Required during embryogenesis for cell elongation, orientation of cell expansion and complex cell wall formations, such as interdigitated pattern of epidermal pavement cells, stomatal guard cells and trichomes. Plays a role in lateral roots formation, but seems not necessary for the development of tip-growing cells such as root hairs. The presence of each protein CESA1 and CESA6 is critical for cell expansion after germination..
Protein Sequence	MEASAGLVAGSYRRNELVRIRHESDGGTKPLKNMNGQICQICGDDVGLAETGDVFVACNECAFPVCRPCYEYERKDGTQCCPQCKTRFRRHRGSPRVEGDEDEDDVDDIENEFNYAQGANKARHQRHGEEFSSSSRHESQPIPLLTHGHTVSGEIRTPDTQSVRTTSGPLGPSDRNAISSPYIDPRQPVPVRIVDPSKDLNSYGLGNVDWKERVEGWKLKQEKNMLQMTGKYHEGKGGEIEGTGSNGEELQMADDTRLPMSRVVPIPSSRLTPYRVVIILRLIILCFFLQYRTTHPVKNAYPLWLTSVICEIWFAFSWLLDQFPKWYPINRETYLDRLAIRYDRDGEPSQLVPVDVFVSTVDPLKEPPLVTANTVLSILSVDYPVDKVACYVSDDGSAMLTFESLSETAEFAKKWVPFCKKFNIEPRAPEFYFAQKIDYLKDKIQPSFVKERRAMKREYEEFKVRINALVAKAQKIPEEGWTMQDGTPWPGNNTRDHPGMIQVFLGHSGGLDTDGNELPRLIYVSREKRPGFQHHKKAGAMNALIRVSAVLTNGAYLLNVDCDHYFNNSKAIKEAMCFMMDPAIGKKCCYVQFPQRFDGIDLHDRYANRNIVFFDINMKGLDGIQGPVYVGTGCCFNRQALYGYDPVLTEEDLEPNIIVKSCCGSRKKGKSSKKYNYEKRRGINRSDSNAPLFNMEDIDEGFEGYDDERSILMSQRSVEKRFGQSPVFIAATFMEQGGIPPTTNPATLLKEAIHVISCGYEDKTEWGKEIGWIYGSVTEDILTGFKMHARGWISIYCNPPRPAFKGSAPINLSDRLNQVLRWALGSIEILLSRHCPIWYGYHGRLRLLERIAYINTIVYPITSIPLIAYCILPAFCLITDRFIIPEISNYASIWFILLFISIAVTGILELRWSGVSIEDWWRNEQFWVIGGTSAHLFAVFQGLLKVLAGIDTNFTVTSKATDEDGDFAELYIFKWTALLIPPTTVLLVNLIGIVAGVSYAVNSGYQSWGPLFGKLFFALWVIAHLYPFLKGLLGRQNRTPTIVIVWSVLLASIFSLLWVRINPFVDANPNANNFNGKGGVF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEASAGLV -------CCCCCCCE	42.42	22223895
11	Phosphorylation	SAGLVAGSYRRNELV CCCCEECCCCCCCEE	13.01	30589143
12	Phosphorylation	AGLVAGSYRRNELVR CCCEECCCCCCCEEE	16.81	25561503
24	Phosphorylation	LVRIRHESDGGTKPL EEEEEECCCCCCCCC	35.12	25561503
132	Phosphorylation	QRHGEEFSSSSRHES HHHCCCCCCCCCCCC	32.37	25561503
133	Phosphorylation	RHGEEFSSSSRHESQ HHCCCCCCCCCCCCC	37.34	25561503
134	Phosphorylation	HGEEFSSSSRHESQP HCCCCCCCCCCCCCC	30.14	29654922
135	Phosphorylation	GEEFSSSSRHESQPI CCCCCCCCCCCCCCC	39.34	25561503
139	Phosphorylation	SSSSRHESQPIPLLT CCCCCCCCCCCCEEE	34.82	27545962
146	Phosphorylation	SQPIPLLTHGHTVSG CCCCCEEECCEEEEC	33.23	27545962
150	Phosphorylation	PLLTHGHTVSGEIRT CEEECCEEEECEEEC	22.43	27545962
152	Phosphorylation	LTHGHTVSGEIRTPD EECCEEEECEEECCC	31.68	23111157
157	Phosphorylation	TVSGEIRTPDTQSVR EEECEEECCCCCCCE	31.04	25561503
160	Phosphorylation	GEIRTPDTQSVRTTS CEEECCCCCCCEECC	24.77	29654922
162	Phosphorylation	IRTPDTQSVRTTSGP EECCCCCCCEECCCC	18.69	15308754
165	Phosphorylation	PDTQSVRTTSGPLGP CCCCCCEECCCCCCC	24.13	23776212
166	Phosphorylation	DTQSVRTTSGPLGPS CCCCCEECCCCCCCC	22.56	23776212
167	Phosphorylation	TQSVRTTSGPLGPSD CCCCEECCCCCCCCC	37.49	19880383
173	Phosphorylation	TSGPLGPSDRNAISS CCCCCCCCCCCCCCC	47.61	23776212
179	Phosphorylation	PSDRNAISSPYIDPR CCCCCCCCCCCCCCC	23.89	27532006
180	Phosphorylation	SDRNAISSPYIDPRQ CCCCCCCCCCCCCCC	18.66	30291188
182	Phosphorylation	RNAISSPYIDPRQPV CCCCCCCCCCCCCCC	21.65	25561503
243	Phosphorylation	KGGEIEGTGSNGEEL CCCCEEECCCCCCEE	25.33	17317660
245	Phosphorylation	GEIEGTGSNGEELQM CCEEECCCCCCEEEE	41.31	29654922
256	Phosphorylation	ELQMADDTRLPMSRV EEEECCCCCCCCCCE	34.35	30407730
261	Phosphorylation	DDTRLPMSRVVPIPS CCCCCCCCCEEECCH	21.71	30407730
686	Phosphorylation	KRRGINRSDSNAPLF HHCCCCCCCCCCCCC	40.68	23776212
688	Phosphorylation	RGINRSDSNAPLFNM CCCCCCCCCCCCCCH	35.82	15308754
705	Phosphorylation	IDEGFEGYDDERSIL HCCCCCCCHHHHHHH	17.02	19376835
953	N-linked_Glycosylation	VLAGIDTNFTVTSKA HHHCCCCCEEEEECE	27.18	-

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
Oops, there are no upstream regulatory protein records of CESA1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CESA1_ARATH !!

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 CESA1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CESA6_ARATH	CESA6	physical	17878303
CESA3_ARATH	CEV1	physical	17878303
CESA1_ARATH	CESA1	physical	22926318
CESA3_ARATH	CEV1	physical	22926318
CESA4_ARATH	CESA4	physical	22926318
CESA6_ARATH	CESA6	physical	22926318
CESA7_ARATH	IRX3	physical	22926318
CESA8_ARATH	IRX1	physical	22926318
GUN25_ARATH	GH9A1	physical	25383767
CESA3_ARATH	CEV1	physical	25352273
CESA6_ARATH	CESA6	physical	25352273

Drug and Disease Associations

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

Regulatory Network of CESA1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167 AND SER-180, ANDMASS SPECTROMETRY.	19376835 [Abstract]
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASSSPECTROMETRY.	17317660 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165 AND SER-167, ANDMASS SPECTROMETRY.	14506206 [Abstract]