CESA3_ARATH - dbPTM
CESA3_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CESA3_ARATH
UniProt AC Q941L0
Protein Name Cellulose synthase A catalytic subunit 3 [UDP-forming]
Gene Name CESA3
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1065
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, especially in roots..
Protein Sequence MESEGETAGKPMKNIVPQTCQICSDNVGKTVDGDRFVACDICSFPVCRPCYEYERKDGNQSCPQCKTRYKRLKGSPAIPGDKDEDGLADEGTVEFNYPQKEKISERMLGWHLTRGKGEEMGEPQYDKEVSHNHLPRLTSRQDTSGEFSAASPERLSVSSTIAGGKRLPYSSDVNQSPNRRIVDPVGLGNVAWKERVDGWKMKQEKNTGPVSTQAASERGGVDIDASTDILADEALLNDEARQPLSRKVSIPSSRINPYRMVIMLRLVILCLFLHYRITNPVPNAFALWLVSVICEIWFALSWILDQFPKWFPVNRETYLDRLALRYDREGEPSQLAAVDIFVSTVDPLKEPPLVTANTVLSILAVDYPVDKVSCYVSDDGAAMLSFESLAETSEFARKWVPFCKKYSIEPRAPEWYFAAKIDYLKDKVQTSFVKDRRAMKREYEEFKIRINALVSKALKCPEEGWVMQDGTPWPGNNTRDHPGMIQVFLGQNGGLDAEGNELPRLVYVSREKRPGFQHHKKAGAMNALVRVSAVLTNGPFILNLDCDHYINNSKALREAMCFLMDPNLGKQVCYVQFPQRFDGIDKNDRYANRNTVFFDINLRGLDGIQGPVYVGTGCVFNRTALYGYEPPIKVKHKKPSLLSKLCGGSRKKNSKAKKESDKKKSGRHTDSTVPVFNLDDIEEGVEGAGFDDEKALLMSQMSLEKRFGQSAVFVASTLMENGGVPPSATPENLLKEAIHVISCGYEDKSDWGMEIGWIYGSVTEDILTGFKMHARGWRSIYCMPKLPAFKGSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGYNGRLKFLERFAYVNTTIYPITSIPLLMYCTLPAVCLFTNQFIIPQISNIASIWFLSLFLSIFATGILEMRWSGVGIDEWWRNEQFWVIGGVSAHLFAVFQGILKVLAGIDTNFTVTSKASDEDGDFAELYLFKWTTLLIPPTTLLIVNLVGVVAGVSYAINSGYQSWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVVWSVLLASIFSLLWVRIDPFTSRVTGPDILECGINC
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 Orthologous
Protein Cluster
3Phosphorylation-----MESEGETAGK
-----CCCCCCCCCC		63.8615308754
7Phosphorylation-MESEGETAGKPMKN
-CCCCCCCCCCCCCC		52.1225561503
130PhosphorylationPQYDKEVSHNHLPRL
CCCCCCCCCCCCCCC		21.4730589143
138PhosphorylationHNHLPRLTSRQDTSG
CCCCCCCCCCCCCCC		24.1229654922
139PhosphorylationNHLPRLTSRQDTSGE
CCCCCCCCCCCCCCC		32.3229654922
143PhosphorylationRLTSRQDTSGEFSAA
CCCCCCCCCCCCCCC		30.2323776212
144PhosphorylationLTSRQDTSGEFSAAS
CCCCCCCCCCCCCCC		44.6130291188
148PhosphorylationQDTSGEFSAASPERL
CCCCCCCCCCCHHHC		20.7223776212
151PhosphorylationSGEFSAASPERLSVS
CCCCCCCCHHHCCEE		27.3230291188
156PhosphorylationAASPERLSVSSTIAG
CCCHHHCCEEEEECC		26.6119376835
158PhosphorylationSPERLSVSSTIAGGK
CHHHCCEEEEECCCC		20.5619376835
159PhosphorylationPERLSVSSTIAGGKR
HHHCCEEEEECCCCC		22.9819376835
160PhosphorylationERLSVSSTIAGGKRL
HHCCEEEEECCCCCC		13.8219376835
169PhosphorylationAGGKRLPYSSDVNQS
CCCCCCCCCCCCCCC		25.9623820729
170PhosphorylationGGKRLPYSSDVNQSP
CCCCCCCCCCCCCCC		20.3729654922
171PhosphorylationGKRLPYSSDVNQSPN
CCCCCCCCCCCCCCC		39.4719880383
176PhosphorylationYSSDVNQSPNRRIVD
CCCCCCCCCCCCCCC		20.9530291188
207PhosphorylationKMKQEKNTGPVSTQA
CCCCCCCCCCCCHHH		54.6615308754
211PhosphorylationEKNTGPVSTQAASER
CCCCCCCCHHHHHHC		20.2419880383
212PhosphorylationKNTGPVSTQAASERG
CCCCCCCHHHHHHCC		23.5915308754
216PhosphorylationPVSTQAASERGGVDI
CCCHHHHHHCCCCCC		30.7319880383
226PhosphorylationGGVDIDASTDILADE
CCCCCCCCCCHHHCH		23.9015308754
227PhosphorylationGVDIDASTDILADEA
CCCCCCCCCHHHCHH		28.8715308754
249PhosphorylationQPLSRKVSIPSSRIN
CCCCCCCCCCHHHCC		31.6425561503
671PhosphorylationKSGRHTDSTVPVFNL
CCCCCCCCCCEECCH		32.2417317660
672PhosphorylationSGRHTDSTVPVFNLD
CCCCCCCCCEECCHH		31.4717317660
938N-linked_GlycosylationVLAGIDTNFTVTSKA
HHHCCCCCEEEEECC		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 CESA3_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CESA3_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 CESA3_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CESA6_ARATHCESA6physical
17878303
CESA1_ARATHCESA1physical
17878303
CESA1_ARATHCESA1physical
22926318
CESA3_ARATHCEV1physical
22926318
CESA4_ARATHCESA4physical
22926318
CESA6_ARATHCESA6physical
22926318
CESA7_ARATHIRX3physical
22926318
CESA8_ARATHIRX1physical
22926318
GUN25_ARATHGH9A1physical
25383767
CESA6_ARATHCESA6physical
25352273
CESA1_ARATHCESA1physical
25352273
GONS5_ARATHGONST5physical
24833385
PIP15_ARATHPIP1;5physical
24833385
UTR2_ARATHUTR2physical
24833385
MSBP1_ARATHMSBP1physical
24833385
HHP2_ARATHHHP2physical
24833385
LAG12_ARATHLOH2physical
24833385
UBC34_ARATHUBC34physical
24833385
ACBP6_ARATHACBP6physical
24833385
UTR3_ARATHUTR3physical
24833385
ARL_ARATHARLphysical
24833385
TRXH3_ARATHTRX3physical
24833385
LPAT2_ARATHLPAT2physical
24833385
CALX2_ARATHAT5G07340physical
24833385
SBP3_ARATHMAPR2physical
24833385
CP21D_ARATHAT3G66654physical
24833385
SPCS1_ARATHAT2G22425physical
24833385
PPA3_ARATHPAP3physical
24833385
RPKL_ARATHAT4G34220physical
24833385
BETL2_ARATHAT1G29060physical
24833385
TRXH7_ARATHTH7physical
24833385
CESA5_ARATHCESA5physical
25926481
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CESA3_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-143; SER-151; SER-176;SER-211 AND SER-216, AND MASS SPECTROMETRY.
"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-3; SER-151; SER-211 AND SER-216, AND MASSSPECTROMETRY.
"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-151, AND MASSSPECTROMETRY.
"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-3; SER-151; SER-211 ANDSER-216, AND MASS SPECTROMETRY.
"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 SER-211; THR-212 ANDSER-216, AND MASS SPECTROMETRY.

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