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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
15 | Phosphorylation | GGPLEINTADSATDD CCCCEEECCCCCCCC | 37.19 | 15308754 | |
18 | Phosphorylation | LEINTADSATDDDRS CEEECCCCCCCCHHH | 30.51 | 15308754 | |
20 | Phosphorylation | INTADSATDDDRSRN EECCCCCCCCHHHCC | 43.86 | 15308754 | |
25 | Phosphorylation | SATDDDRSRNLNDLD CCCCCHHHCCHHHHH | 32.30 | 30291188 | |
37 | Phosphorylation | DLDRAALSRPLDETQ HHHHHHHCCCCCHHH | 27.42 | 17317660 | |
43 | Phosphorylation | LSRPLDETQQSWLLG HCCCCCHHHHHHHCC | 31.41 | 19880383 | |
46 | Phosphorylation | PLDETQQSWLLGPTE CCCHHHHHHHCCCCH | 15.18 | 30291188 | |
108 | N-linked_Glycosylation | PKTPPPDNYTIALHK CCCCCCCCHHHHHHH | 41.44 | - | |
133 | N-linked_Glycosylation | GKLPKHNNVSWRGNS CCCCCCCCCCCCCCC | 28.99 | - | |
216 | N-linked_Glycosylation | DYFLKTFNSTADSID HHHHHHCCCCCCCHH | 43.62 | - | |
324 | N-linked_Glycosylation | AESSKFYNSSMYWDE CCCCCCCCCCCCCEE | 30.64 | - | |
345 | N-linked_Glycosylation | WMYYATGNVTYLNLI EEEEECCCEEEEEEE | 20.71 | - | |
408 | N-linked_Glycosylation | EILRTFHNQTSIVMC HHHHHHCCCCCEEEE | 42.51 | - | |
425 | N-linked_Glycosylation | LPIFNKFNRTNGGLI HHHHHCCCCCCCCCE | 52.02 | - | |
567 | N-linked_Glycosylation | RDVRMNYNYTEPTLA EEEEECCCCCCCCCC | 32.04 | - |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GUN25_ARATH !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CESA4_ARATH | CESA4 | physical | 25383767 | |
CESA8_ARATH | IRX1 | physical | 25383767 | |
CESA1_ARATH | CESA1 | physical | 25383767 | |
CESA3_ARATH | CEV1 | physical | 25383767 | |
CESA6_ARATH | CESA6 | physical | 25383767 | |
GUN25_ARATH | GH9A1 | physical | 25383767 | |
CESA1_ARATH | CESA1 | physical | 24948829 | |
CESA1_ARATH | CESA1 | physical | 24963054 | |
CESA3_ARATH | CEV1 | physical | 24963054 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |