| UniProt ID | RTNLD_ARATH | |
|---|---|---|
| UniProt AC | Q9FFS0 | |
| Protein Name | Reticulon-like protein B4 | |
| Gene Name | RTNLB4 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 257 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Plays a role in the Agrobacterium-mediated plant transformation via its interaction with VirB2, the major component of the T-pilus.. | |
| Protein Sequence | MVEDHKHEESILEKIVEKIHGHGDSSSLSDSDDDKKSTSSSSSSFKSKIYRLFGREKPVHKVLGGGKPADIFLWRNKKVSGGVLGAVTASWVLFELFEYHLLAFLCHFAIFALAALFLWSNACTFIHKSTPHIPEVHIPEDPILQLVSGLRIEINRGLTLLRNIASGKDVKKFILVIAGLWVLSIIGSCYNFLTLFYTATVLLFTIPVLYEKYEDKVDAYGEKAMREIKKQYAVLDEKVLRKVISKIPRGALNKKKD | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 25 | Phosphorylation | KIHGHGDSSSLSDSD HHHCCCCCCCCCCCC | 26.81 | 23776212 | |
| 26 | Phosphorylation | IHGHGDSSSLSDSDD HHCCCCCCCCCCCCC | 39.78 | 23776212 | |
| 27 | Phosphorylation | HGHGDSSSLSDSDDD HCCCCCCCCCCCCCC | 35.53 | 15308754 | |
| 29 | Phosphorylation | HGDSSSLSDSDDDKK CCCCCCCCCCCCCCC | 36.70 | 19880383 | |
| 31 | Phosphorylation | DSSSLSDSDDDKKST CCCCCCCCCCCCCCC | 39.29 | 19880383 | |
| 37 | Phosphorylation | DSDDDKKSTSSSSSS CCCCCCCCCCCCCHH | 38.98 | 25368622 | |
| 38 | Phosphorylation | SDDDKKSTSSSSSSF CCCCCCCCCCCCHHH | 41.32 | 25561503 | |
| 39 | Phosphorylation | DDDKKSTSSSSSSFK CCCCCCCCCCCHHHH | 35.00 | 19880383 | |
| 40 | Phosphorylation | DDKKSTSSSSSSFKS CCCCCCCCCCHHHHH | 34.04 | 25561503 | |
| 42 | Phosphorylation | KKSTSSSSSSFKSKI CCCCCCCCHHHHHHH | 31.76 | 25561503 | |
| 43 | Phosphorylation | KSTSSSSSSFKSKIY CCCCCCCHHHHHHHH | 41.56 | 25561503 | |
| 44 | Phosphorylation | STSSSSSSFKSKIYR CCCCCCHHHHHHHHH | 38.35 | 25561503 | |
| 245 | Phosphorylation | KVLRKVISKIPRGAL HHHHHHHHHCCCCHH | 27.76 | 19376835 |
| 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 RTNLD_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RTNLD_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 RTNLD_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RTNLA_ARATH | BTI1 | physical | 15494553 | |
| RTNLB_ARATH | BTI2 | physical | 15494553 | |
| RAE1A_ARATH | RAB8 | physical | 15494553 | |
| RTNLD_ARATH | BTI3 | physical | 21798944 | |
| CYB5E_ARATH | CB5-E | physical | 21798944 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| 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-245, 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-31, AND MASSSPECTROMETRY. | |
| "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-26; SER-27; SER-29 ANDSER-31, AND MASS SPECTROMETRY. | |