GUN25_ARATH - dbPTM
GUN25_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GUN25_ARATH
UniProt AC Q38890
Protein Name Endoglucanase 25
Gene Name KOR
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 621
Subcellular Localization Cell membrane
Single-pass type II membrane protein . Cell plate.
Protein Description Required for cellulose microfibrils formation. Involved in cell wall assembly during cell elongation and cell plate maturation in cytokinesis. Required for secondary cell wall formation in the developing xylem. May cycle through different intracellular compartments, including plasma membrane..
Protein Sequence MYGRDPWGGPLEINTADSATDDDRSRNLNDLDRAALSRPLDETQQSWLLGPTEQKKKKYVDLGCIIVSRKIFVWTVGTLVAAALLAGFITLIVKTVPRHHPKTPPPDNYTIALHKALKFFNAQKSGKLPKHNNVSWRGNSGLQDGKGETGSFYKDLVGGYYDAGDAIKFNFPMAYAMTMLSWSVIEYSAKYEAAGELTHVKELIKWGTDYFLKTFNSTADSIDDLVSQVGSGNTDDGNTDPNDHYCWMRPEDMDYKRPVTTCNGGCSDLAAEMAAALASASIVFKDNKEYSKKLVHGAKVVYQFGRTRRGRYSAGTAESSKFYNSSMYWDEFIWGGAWMYYATGNVTYLNLITQPTMAKHAGAFWGGPYYGVFSWDNKLAGAQLLLSRLRLFLSPGYPYEEILRTFHNQTSIVMCSYLPIFNKFNRTNGGLIELNHGAPQPLQYSVNAAFLATLYSDYLDAADTPGWYCGPNFYSTSVLRDFARSQIDYILGKNPRKMSYVVGFGTKYPRHVHHRGASIPKNKVKYNCKGGWKWRDSKKPNPNTIEGAMVAGPDKRDGYRDVRMNYNYTEPTLAGNAGLVAALVALSGEEEATGKIDKNTIFSAVPPLFPTPPPPPAPWKP
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
15PhosphorylationGGPLEINTADSATDD
CCCCEEECCCCCCCC
37.1915308754
18PhosphorylationLEINTADSATDDDRS
CEEECCCCCCCCHHH
30.5115308754
20PhosphorylationINTADSATDDDRSRN
EECCCCCCCCHHHCC
43.8615308754
25PhosphorylationSATDDDRSRNLNDLD
CCCCCHHHCCHHHHH
32.3030291188
37PhosphorylationDLDRAALSRPLDETQ
HHHHHHHCCCCCHHH
27.4217317660
43PhosphorylationLSRPLDETQQSWLLG
HCCCCCHHHHHHHCC
31.4119880383
46PhosphorylationPLDETQQSWLLGPTE
CCCHHHHHHHCCCCH
15.1830291188
108N-linked_GlycosylationPKTPPPDNYTIALHK
CCCCCCCCHHHHHHH
41.44-
133N-linked_GlycosylationGKLPKHNNVSWRGNS
CCCCCCCCCCCCCCC
28.99-
216N-linked_GlycosylationDYFLKTFNSTADSID
HHHHHHCCCCCCCHH
43.62-
324N-linked_GlycosylationAESSKFYNSSMYWDE
CCCCCCCCCCCCCEE
30.64-
345N-linked_GlycosylationWMYYATGNVTYLNLI
EEEEECCCEEEEEEE
20.71-
408N-linked_GlycosylationEILRTFHNQTSIVMC
HHHHHHCCCCCEEEE
42.51-
425N-linked_GlycosylationLPIFNKFNRTNGGLI
HHHHHCCCCCCCCCE
52.02-
567N-linked_GlycosylationRDVRMNYNYTEPTLA
EEEEECCCCCCCCCC
32.04-

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 GUN25_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GUN25_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 GUN25_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CESA4_ARATHCESA4physical
25383767
CESA8_ARATHIRX1physical
25383767
CESA1_ARATHCESA1physical
25383767
CESA3_ARATHCEV1physical
25383767
CESA6_ARATHCESA6physical
25383767
GUN25_ARATHGH9A1physical
25383767
CESA1_ARATHCESA1physical
24948829
CESA1_ARATHCESA1physical
24963054
CESA3_ARATHCEV1physical
24963054

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GUN25_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-18; THR-20 AND SER-25,AND MASS SPECTROMETRY.
"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 THR-20, AND MASSSPECTROMETRY.

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