SERK1_ARATH - dbPTM
SERK1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERK1_ARATH
UniProt AC Q94AG2
Protein Name Somatic embryogenesis receptor kinase 1
Gene Name SERK1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 625
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Endoplasmic reticulum membrane
Single-pass type I membrane protein.
Protein Description Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway..
Protein Sequence MESSYVVFILLSLILLPNHSLWLASANLEGDALHTLRVTLVDPNNVLQSWDPTLVNPCTWFHVTCNNENSVIRVDLGNAELSGHLVPELGVLKNLQYLELYSNNITGPIPSNLGNLTNLVSLDLYLNSFSGPIPESLGKLSKLRFLRLNNNSLTGSIPMSLTNITTLQVLDLSNNRLSGSVPDNGSFSLFTPISFANNLDLCGPVTSHPCPGSPPFSPPPPFIQPPPVSTPSGYGITGAIAGGVAAGAALLFAAPAIAFAWWRRRKPLDIFFDVPAEEDPEVHLGQLKRFSLRELQVASDGFSNKNILGRGGFGKVYKGRLADGTLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASCLRERPPSQPPLDWPTRKRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEEFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKLEMLVDPDLQTNYEERELEQVIQVALLCTQGSPMERPKMSEVVRMLEGDGLAEKWDEWQKVEILREEIDLSPNPNSDWILDSTYNLHAVELSGPR
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
104N-linked_GlycosylationYLELYSNNITGPIPS
EEEHHHCCCCCCCCC		27.5323929946
115N-linked_GlycosylationPIPSNLGNLTNLVSL
CCCCCCCHHHHHHHH		47.02-
150N-linked_GlycosylationLRFLRLNNNSLTGSI
CEEEEECCCCCCCCC		44.0223929946
163N-linked_GlycosylationSIPMSLTNITTLQVL
CCCCCCCCCEEEEEE		34.6023929946
184N-linked_GlycosylationLSGSVPDNGSFSLFT
CCCCCCCCCCEECCC		41.7723929946
291PhosphorylationLGQLKRFSLRELQVA
HHHCCCCCCCCEEEC		30.4624243849
299PhosphorylationLRELQVASDGFSNKN
CCCEEECCCCCCCCC		39.1324243849
303PhosphorylationQVASDGFSNKNILGR
EECCCCCCCCCCCCC		53.0424243849
325PhosphorylationKGRLADGTLVAVKRL
CCEECCCCEEEEEEH		20.7118694562
337PhosphorylationKRLKEERTPGGELQF
EEHHHCCCCCCEEEE		29.5724243849
346PhosphorylationGGELQFQTEVEMISM
CCEEEEEEHHHHHHH		43.2024243849
352PhosphorylationQTEVEMISMAVHRNL
EEHHHHHHHHHHHHH		10.2024243849
383PhosphorylationYPYMANGSVASCLRE
ECCCCCCCHHHHHCC		17.8324243849
386PhosphorylationMANGSVASCLRERPP
CCCCCHHHHHCCCCC		16.13-
394PhosphorylationCLRERPPSQPPLDWP
HHCCCCCCCCCCCCC		58.9819105183
402PhosphorylationQPPLDWPTRKRIALG
CCCCCCCCHHHHHHC		44.5624243849
415PhosphorylationLGSARGLSYLHDHCD
HCCCCCHHHHHHCCC		28.5924243849
456PhosphorylationGLAKLMDYKDTHVTT
HHHHHHCCCCCCCHH		9.2215308754
459PhosphorylationKLMDYKDTHVTTAVR
HHHCCCCCCCHHHHH		17.6930291188
462PhosphorylationDYKDTHVTTAVRGTI
CCCCCCCHHHHHCCC		11.0530291188
463PhosphorylationYKDTHVTTAVRGTIG
CCCCCCHHHHHCCCC		23.2830291188
468PhosphorylationVTTAVRGTIGHIAPE
CHHHHHCCCCCCCHH		17.1418694562
476PhosphorylationIGHIAPEYLSTGKSS
CCCCCHHHHHCCCCC		12.6125561503
478PhosphorylationHIAPEYLSTGKSSEK
CCCHHHHHCCCCCCC		33.9219880383
479PhosphorylationIAPEYLSTGKSSEKT
CCHHHHHCCCCCCCC		46.1425561503
483PhosphorylationYLSTGKSSEKTDVFG
HHHCCCCCCCCCCCH		46.7424243849
541PhosphorylationLVDPDLQTNYEEREL
HCCCCCCCCCCHHHH		47.2524243849
543PhosphorylationDPDLQTNYEERELEQ
CCCCCCCCCHHHHHH		23.6624243849
559PhosphorylationIQVALLCTQGSPMER
HHHHHHHCCCCCCCC		35.6124243849
606PhosphorylationDLSPNPNSDWILDST
CCCCCCCCCCCCCCC		35.2619105183
612PhosphorylationNSDWILDSTYNLHAV
CCCCCCCCCEEEEEE		29.3719105183
613PhosphorylationSDWILDSTYNLHAVE
CCCCCCCCEEEEEEE		18.9819105183
614PhosphorylationDWILDSTYNLHAVEL
CCCCCCCEEEEEEEC		21.4819105183
622PhosphorylationNLHAVELSGPR----
EEEEEECCCCC----		32.9911509554
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 SERK1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
299SPhosphorylation

19105183
462TPhosphorylation

11509554
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 SERK1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
14336_ARATHGRF6physical
15592873
CD48A_ARATHCDC48physical
15592873
BRI1_ARATHBRI1physical
19105183
P2C70_ARATHKAPPphysical
12101128
SERK2_ARATHSERK2physical
16284305
SERK1_ARATHSERK1physical
16284305
BAK1_ARATHBAK1physical
16473966
BRI1_ARATHBRI1physical
16473966
P2C70_ARATHKAPPphysical
16473966
CD48A_ARATHCDC48physical
16473966
14337_ARATHGRF7physical
16473966
AGL15_ARATHAGL15physical
16473966
COL14_ARATHAT2G33500physical
16473966
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERK1_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: MUTAGENESIS OF THR-541; SER-562 AND SER-570, AND PHOSPHORYLATION ATSER-291; SER-299; SER-303; THR-325; THR-337; THR-346; SER-352;SER-383; SER-394; THR-402; SER-415; TYR-456; THR-459; THR-462;THR-463; THR-468; TYR-476; SER-478; THR-479; SER-483; THR-541;TYR-543; THR-559; SER-606; SER-612; THR-613; TYR-614 AND SER-622.

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