SERK2_ARATH - dbPTM
SERK2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERK2_ARATH
UniProt AC Q9XIC7
Protein Name Somatic embryogenesis receptor kinase 2
Gene Name SERK2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 628
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Serine/threonine-kinase involved in brassinosteroid-dependent and -independent signaling pathways. Acts redundantly with SERK1 as a control point for sporophytic development controlling male gametophyte production..
Protein Sequence MGRKKFEAFGFVCLISLLLLFNSLWLASSNMEGDALHSLRANLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNADLSGQLVPQLGQLKNLQYLELYSNNITGPVPSDLGNLTNLVSLDLYLNSFTGPIPDSLGKLFKLRFLRLNNNSLTGPIPMSLTNIMTLQVLDLSNNRLSGSVPDNGSFSLFTPISFANNLDLCGPVTSRPCPGSPPFSPPPPFIPPPIVPTPGGYSATGAIAGGVAAGAALLFAAPALAFAWWRRRKPQEFFFDVPAEEDPEVHLGQLKRFSLRELQVATDSFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPPSQLPLAWSIRQQIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLARLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEMLVDPDLQSNYTEAEVEQLIQVALLCTQSSPMERPKMSEVVRMLEGDGLAEKWDEWQKVEVLRQEVELSSHPTSDWILDSTDNLHAMELSGPR
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
107N-linked_GlycosylationYLELYSNNITGPVPS
EEEHHHCCCCCCCCC		27.53-
118N-linked_GlycosylationPVPSDLGNLTNLVSL
CCCCCCCHHHHHHHH		51.49-
153N-linked_GlycosylationLRFLRLNNNSLTGPI
EEEEECCCCCCCCCC		44.0226308901
187N-linked_GlycosylationLSGSVPDNGSFSLFT
CCCCCCCCCCEECCC		41.7726308901
294PhosphorylationLGQLKRFSLRELQVA
HHHHCCCCHHHHEHH		30.4624243849
302PhosphorylationLRELQVATDSFSNKN
HHHHEHHHHCCCCCC		33.0624243849
328PhosphorylationKGRLADGTLVAVKRL
CCEECCCCEEEEEEH		20.7118694562
340PhosphorylationKRLKEERTPGGELQF
EEHHHCCCCCCCEEE		29.5724243849
349PhosphorylationGGELQFQTEVEMISM
CCCEEEEEHHHHHHH		43.2024243849
355PhosphorylationQTEVEMISMAVHRNL
EEHHHHHHHHHHHHH		10.2024243849
386PhosphorylationYPYMANGSVASCLRE
ECCCCCCCHHHHHHC		17.8324243849
389PhosphorylationMANGSVASCLRERPP
CCCCCHHHHHHCCCH		16.13-
418PhosphorylationLGSARGLSYLHDHCD
HHCCCCHHHHHHCCC		28.5924243849
459PhosphorylationGLARLMDYKDTHVTT
HHHHHHCCCCCCCHH		9.2215308754
462PhosphorylationRLMDYKDTHVTTAVR
HHHCCCCCCCHHHHH		17.6915308754
465PhosphorylationDYKDTHVTTAVRGTI
CCCCCCCHHHHHCCC		11.0530291188
466PhosphorylationYKDTHVTTAVRGTIG
CCCCCCHHHHHCCCC		23.2830291188
471PhosphorylationVTTAVRGTIGHIAPE
CHHHHHCCCCCCCHH		17.1418694562
479PhosphorylationIGHIAPEYLSTGKSS
CCCCCHHHHHCCCCC		12.6125561503
481PhosphorylationHIAPEYLSTGKSSEK
CCCHHHHHCCCCCCC		33.9219880383
482PhosphorylationIAPEYLSTGKSSEKT
CCHHHHHCCCCCCCC		46.1425561503
486PhosphorylationYLSTGKSSEKTDVFG
HHHCCCCCCCCCCCH		46.7424243849
562PhosphorylationIQVALLCTQSSPMER
HHHHHHHCCCCCCCC		31.30-
604PhosphorylationLRQEVELSSHPTSDW
HHHHCHHCCCCCCCC		17.0719105183
616PhosphorylationSDWILDSTDNLHAME
CCCEECCCCCCEECC		28.6819105183
625PhosphorylationNLHAMELSGPR----
CCEECCCCCCC----		33.1819105183
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 SERK2_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERK2_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 SERK2_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SERK2_ARATHSERK2physical
16284305
WAXS6_ARATHAT5G55330physical
21423366
Y5838_ARATHBIR1physical
21423366
PXC3_ARATHAT2G41820physical
21423366
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERK2_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-302; THR-462; THR-465;THR-466; SER-604; THR-616 AND SER-625.
"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 THR-462; THR-465 ANDTHR-466, AND MASS SPECTROMETRY.

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