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 | ||
* 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. |