UniProt ID | RTNLA_ARATH | |
---|---|---|
UniProt AC | Q9SUR3 | |
Protein Name | Reticulon-like protein B1 | |
Gene Name | RTNLB1 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 275 | |
Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Cell 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 | MAEEHKHDESVIAPEPAVEVVERESLMDKISEKIHHGGDSSSSSSSSDDEDEKKKTKKPSSPSSSMKSKVYRLFGREQPVHKVLGGGKPADIFMWKNKKMSGGVLGGATAAWVVFELMEYHLLTLLCHVMIVVLAVLFLWSNATMFINKSPPKIPEVHIPEEPILQLASGLRIEINRGFSSLREIASGRDLKKFLIAIAGLWVLSILGGCFNFLTLAYIALVLLFTVPLAYDKYEDKVDPLGEKAMIELKKQYAVLDEKVLSKIPLGPLKNKKKD | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAEEHKHDE ------CCCCCCCCC | 30.77 | - | |
6 | Acetylation | --MAEEHKHDESVIA --CCCCCCCCCCCCC | 56.91 | 21311031 | |
10 | Phosphorylation | EEHKHDESVIAPEPA CCCCCCCCCCCCCCC | 25.53 | 25368622 | |
31 | Phosphorylation | ESLMDKISEKIHHGG HHHHHHHHHHHCCCC | 38.28 | 30291188 | |
40 | Phosphorylation | KIHHGGDSSSSSSSS HHCCCCCCCCCCCCC | 35.08 | 19376835 | |
41 | Phosphorylation | IHHGGDSSSSSSSSD HCCCCCCCCCCCCCC | 38.69 | 19376835 | |
42 | Phosphorylation | HHGGDSSSSSSSSDD CCCCCCCCCCCCCCC | 37.89 | 19376835 | |
43 | Phosphorylation | HGGDSSSSSSSSDDE CCCCCCCCCCCCCCH | 35.87 | 19376835 | |
44 | Phosphorylation | GGDSSSSSSSSDDED CCCCCCCCCCCCCHH | 35.87 | 27531888 | |
45 | Phosphorylation | GDSSSSSSSSDDEDE CCCCCCCCCCCCHHH | 35.49 | 19376835 | |
46 | Phosphorylation | DSSSSSSSSDDEDEK CCCCCCCCCCCHHHH | 39.47 | 27531888 | |
47 | Phosphorylation | SSSSSSSSDDEDEKK CCCCCCCCCCHHHHH | 51.53 | 19376835 | |
56 | Phosphorylation | DEDEKKKTKKPSSPS CHHHHHHCCCCCCCC | 53.86 | 19376835 | |
60 | Phosphorylation | KKKTKKPSSPSSSMK HHHCCCCCCCCHHHH | 64.85 | 23776212 | |
61 | Phosphorylation | KKTKKPSSPSSSMKS HHCCCCCCCCHHHHH | 37.01 | 19880383 | |
63 | Phosphorylation | TKKPSSPSSSMKSKV CCCCCCCCHHHHHHH | 36.67 | 23776212 | |
64 | Phosphorylation | KKPSSPSSSMKSKVY CCCCCCCHHHHHHHH | 37.52 | 23776212 | |
65 | Phosphorylation | KPSSPSSSMKSKVYR CCCCCCHHHHHHHHH | 34.27 | 23776212 |
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 RTNLA_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RTNLA_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 RTNLA_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RTNLB_ARATH | BTI2 | physical | 15494553 | |
RTNLD_ARATH | BTI3 | physical | 15494553 | |
RAE1A_ARATH | RAB8 | physical | 15494553 | |
RTNLA_ARATH | BTI1 | physical | 15494553 | |
RTNLA_ARATH | BTI1 | physical | 20424177 | |
RTNLC_ARATH | RTNLB3 | physical | 20424177 | |
RTNLD_ARATH | BTI3 | physical | 20424177 | |
FLS2_ARATH | FLS2 | physical | 21949153 |
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-61, AND MASSSPECTROMETRY. |