CESA4_ARATH - dbPTM
CESA4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CESA4_ARATH
UniProt AC Q84JA6
Protein Name Cellulose synthase A catalytic subunit 4 [UDP-forming]
Gene Name CESA4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1049
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 MEPNTMASFDDEHRHSSFSAKICKVCGDEVKDDDNGQTFVACHVCVYPVCKPCYEYERSNGNKCCPQCNTLYKRHKGSPKIAGDEENNGPDDSDDELNIKYRQDGSSIHQNFAYGSENGDYNSKQQWRPNGRAFSSTGSVLGKDFEAERDGYTDAEWKERVDKWKARQEKRGLVTKGEQTNEDKEDDEEEYLDAEARQPLWRKVPISSSKISPYRIVIVLRLVILVFFFRFRILTPAKDAYPLWLISVICEIWFALSWILDQFPKWFPINRETYLDRLSMRFERDGEKNKLAPVDVFVSTVDPLKEPPIITANTILSILAVDYPVNKVSCYVSDDGASMLLFDTLSETSEFARRWVPFCKKYNVEPRAPEFYFSEKIDYLKDKVQTTFVKDRRAMKREYEEFKVRINALVAKAQKKPEEGWVMQDGTPWPGNNTRDHPGMIQVYLGKEGAFDIDGNELPRLVYVSREKRPGYAHHKKAGAMNAMVRVSAVLTNAPFMLNLDCDHYINNSKAIRESMCFLMDPQLGKKLCYVQFPQRFDGIDLNDRYANRNIVFFDINMRGLDGIQGPVYVGTGCVFNRPALYGYEPPVSEKRKKMTCDCWPSWICCCCGGGNRNHKSDSSKKKSGIKSLFSKLKKKTKKKSDDKTMSSYSRKRSSTEAIFDLEDIEEGLEGYDELEKSSLMSQKNFEKRFGMSPVFIASTLMENGGLPEATNTSSLIKEAIHVISCGYEEKTEWGKEIGWIYGSVTEDILTGFRMHCRGWKSVYCMPKRPAFKGSAPINLSDRLHQVLRWALGSVEIFFSRHCPLWYAWGGKLKILERLAYINTIVYPFTSIPLLAYCTIPAVCLLTGKFIIPTINNFASIWFLALFLSIIATAILELRWSGVSINDLWRNEQFWVIGGVSAHLFAVFQGLLKVLFGVDTNFTVTSKGASDEADEFGDLYLFKWTTLLIPPTTLIILNMVGVVAGVSDAINNGYGSWGPLFGKLFFAFWVIVHLYPFLKGLMGRQNRTPTIVVLWSILLASIFSLVWVRIDPFLPKQTGPLLKQCGVDC
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
93PhosphorylationENNGPDDSDDELNIK
CCCCCCCCCCCCCEE
55.1030291188
114PhosphorylationSIHQNFAYGSENGDY
CHHCCEECCCCCCCC
19.6330407730
116PhosphorylationHQNFAYGSENGDYNS
HCCEECCCCCCCCCC
18.4030407730
135PhosphorylationRPNGRAFSSTGSVLG
CCCCCCCCCCCCCCC
26.4630291188
136PhosphorylationPNGRAFSSTGSVLGK
CCCCCCCCCCCCCCC
30.2730407730
137PhosphorylationNGRAFSSTGSVLGKD
CCCCCCCCCCCCCCC
32.0725561503
139PhosphorylationRAFSSTGSVLGKDFE
CCCCCCCCCCCCCCC
17.7930291188
374PhosphorylationRAPEFYFSEKIDYLK
CCCCCCHHHHHHHHH
26.9722074104
921N-linked_GlycosylationVLFGVDTNFTVTSKG
HHHCCCCCCEEECCC
26.57-

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 CESA4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CESA4_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 CESA4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CESA4_ARATHCESA4physical
19056734
CESA1_ARATHCESA1physical
22926318
CESA3_ARATHCEV1physical
22926318
CESA4_ARATHCESA4physical
22926318
CESA6_ARATHCESA6physical
22926318
CESA7_ARATHIRX3physical
22926318
CESA8_ARATHIRX1physical
22926318
GUN25_ARATHGH9A1physical
25383767
CESA4_ARATHCESA4physical
19258017
CESA8_ARATHIRX1physical
19258017

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CESA4_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-135, AND MASS SPECTROMETRY.

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