UniProt ID | SERK5_ARATH | |
---|---|---|
UniProt AC | Q8LPS5 | |
Protein Name | Somatic embryogenesis receptor kinase 5 | |
Gene Name | SERK5 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 601 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Serine/threonine-kinase of unknown function.. | |
Protein Sequence | MEHGSSRGFIWLILFLDFVSRVTGKTQVDALIALRSSLSSGDHTNNILQSWNATHVTPCSWFHVTCNTENSVTRLDLGSANLSGELVPQLAQLPNLQYLELFNNNITGEIPEELGDLMELVSLDLFANNISGPIPSSLGKLGKLRFLRLYNNSLSGEIPRSLTALPLDVLDISNNRLSGDIPVNGSFSQFTSMSFANNKLRPRPASPSPSPSGTSAAIVVGVAAGAALLFALAWWLRRKLQGHFLDVPAEEDPEVYLGQFKRFSLRELLVATEKFSKRNVLGKGRFGILYKGRLADDTLVAVKRLNEERTKGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPEGNPALDWPKRKHIALGSARGLAYLHDHCDQKIIHLDVKAANILLDEEFEAVVGDFGLAKLMNYNDSHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGVMLLELITGQKAFDLARLANDDDIMLLDWVKEVLKEKKLESLVDAELEGKYVETEVEQLIQMALLCTQSSAMERPKMSEVVRMLEGDGLAERWEEWQKEEMPIHDFNYQAYPHAGTDWLIPYSNSLIENDYPSGPR | |
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 |
---|---|---|---|---|---|
52 | N-linked_Glycosylation | NNILQSWNATHVTPC HCHHHHCCCCCCCCC | 39.96 | - | |
81 | N-linked_Glycosylation | RLDLGSANLSGELVP EEECCCCCCCCCHHH | 36.12 | - | |
105 | N-linked_Glycosylation | YLELFNNNITGEIPE EHHHHCCCCCCCCCH | 34.01 | - | |
129 | N-linked_Glycosylation | SLDLFANNISGPIPS HHHHHHCCCCCCCCC | 26.77 | - | |
151 | N-linked_Glycosylation | LRFLRLYNNSLSGEI HHHHCCCCCCCCCCC | 35.88 | - | |
184 | N-linked_Glycosylation | LSGDIPVNGSFSQFT CCCCCCCCCCHHHHH | 34.73 | - | |
272 | Phosphorylation | LRELLVATEKFSKRN HHHHHHHHHHHHCCC | 32.03 | - | |
298 | Phosphorylation | KGRLADDTLVAVKRL CCCCCCCEEEEEEEC | 24.55 | - | |
319 | Phosphorylation | GGELQFQTEVEMISM CCEEEEHHHHHHHHH | 43.20 | 24243849 | |
325 | Phosphorylation | QTEVEMISMAVHRNL HHHHHHHHHHHHHHH | 10.20 | 24243849 | |
356 | Phosphorylation | YPYMANGSVASCLRE EHHCCCCCHHHHHHC | 17.83 | 24243849 | |
359 | Phosphorylation | MANGSVASCLRERPE CCCCCHHHHHHCCCC | 16.13 | - | |
432 | Phosphorylation | KLMNYNDSHVTTAVR HHCCCCCCCCHHHHH | 19.07 | 23111157 | |
435 | Phosphorylation | NYNDSHVTTAVRGTI CCCCCCCHHHHHHHH | 12.01 | 23111157 | |
436 | Phosphorylation | YNDSHVTTAVRGTIG CCCCCCHHHHHHHHC | 23.28 | 23111157 | |
441 | Phosphorylation | VTTAVRGTIGHIAPE CHHHHHHHHCCCCHH | 17.14 | 18694562 | |
449 | Phosphorylation | IGHIAPEYLSTGKSS HCCCCHHHHHCCCCC | 12.61 | 25561503 | |
451 | Phosphorylation | HIAPEYLSTGKSSEK CCCHHHHHCCCCCCC | 33.92 | 19880383 | |
452 | Phosphorylation | IAPEYLSTGKSSEKT CCHHHHHCCCCCCCC | 46.14 | 25561503 | |
456 | Phosphorylation | YLSTGKSSEKTDVFG HHHCCCCCCCCCCCH | 46.74 | 24243849 | |
506 | Phosphorylation | LKEKKLESLVDAELE HHHHCHHHHHCHHHC | 44.09 | 19880383 | |
532 | Phosphorylation | IQMALLCTQSSAMER HHHHHHHCCCCHHCC | 31.30 | - |
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 SERK5_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SERK5_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 SERK5_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SERK5_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Identification of in vitro phosphorylation sites in the Arabidopsisthaliana somatic embryogenesis receptor-like kinases."; Karlova R., Boeren S., van Dongen W., Kwaaitaal M., Aker J.,Vervoort J., de Vries S.C.; Proteomics 9:368-379(2009). Cited for: AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT THR-441 AND SER-506. |