SERK5_ARATH - dbPTM
SERK5_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
52N-linked_GlycosylationNNILQSWNATHVTPC
HCHHHHCCCCCCCCC
39.96-
81N-linked_GlycosylationRLDLGSANLSGELVP
EEECCCCCCCCCHHH
36.12-
105N-linked_GlycosylationYLELFNNNITGEIPE
EHHHHCCCCCCCCCH
34.01-
129N-linked_GlycosylationSLDLFANNISGPIPS
HHHHHHCCCCCCCCC
26.77-
151N-linked_GlycosylationLRFLRLYNNSLSGEI
HHHHCCCCCCCCCCC
35.88-
184N-linked_GlycosylationLSGDIPVNGSFSQFT
CCCCCCCCCCHHHHH
34.73-
272PhosphorylationLRELLVATEKFSKRN
HHHHHHHHHHHHCCC
32.03-
298PhosphorylationKGRLADDTLVAVKRL
CCCCCCCEEEEEEEC
24.55-
319PhosphorylationGGELQFQTEVEMISM
CCEEEEHHHHHHHHH
43.2024243849
325PhosphorylationQTEVEMISMAVHRNL
HHHHHHHHHHHHHHH
10.2024243849
356PhosphorylationYPYMANGSVASCLRE
EHHCCCCCHHHHHHC
17.8324243849
359PhosphorylationMANGSVASCLRERPE
CCCCCHHHHHHCCCC
16.13-
432PhosphorylationKLMNYNDSHVTTAVR
HHCCCCCCCCHHHHH
19.0723111157
435PhosphorylationNYNDSHVTTAVRGTI
CCCCCCCHHHHHHHH
12.0123111157
436PhosphorylationYNDSHVTTAVRGTIG
CCCCCCHHHHHHHHC
23.2823111157
441PhosphorylationVTTAVRGTIGHIAPE
CHHHHHHHHCCCCHH
17.1418694562
449PhosphorylationIGHIAPEYLSTGKSS
HCCCCHHHHHCCCCC
12.6125561503
451PhosphorylationHIAPEYLSTGKSSEK
CCCHHHHHCCCCCCC
33.9219880383
452PhosphorylationIAPEYLSTGKSSEKT
CCHHHHHCCCCCCCC
46.1425561503
456PhosphorylationYLSTGKSSEKTDVFG
HHHCCCCCCCCCCCH
46.7424243849
506PhosphorylationLKEKKLESLVDAELE
HHHHCHHHHHCHHHC
44.0919880383
532PhosphorylationIQMALLCTQSSAMER
HHHHHHHCCCCHHCC
31.30-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERK5_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SERK5_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERK5_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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