CERK1_ARATH - dbPTM
CERK1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CERK1_ARATH
UniProt AC A8R7E6
Protein Name Chitin elicitor receptor kinase 1
Gene Name CERK1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 617
Subcellular Localization Cell membrane
Single-pass membrane protein .
Protein Description Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI). Mediates chitin-induced phosphorylation of PBL27. [PubMed: 24750441]
Protein Sequence MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATDNFNLSFKIGQGGFGAVYYAELRGEKAAIKKMDMEASKQFLAELKVLTRVHHVNLVRLIGYCVEGSLFLVYEYVENGNLGQHLHGSGREPLPWTKRVQIALDSARGLEYIHEHTVPVYVHRDIKSANILIDQKFRAKVADFGLTKLTEVGGSATRGAMGTFGYMAPETVYGEVSAKVDVYAFGVVLYELISAKGAVVKMTEAVGEFRGLVGVFEESFKETDKEEALRKIIDPRLGDSYPFDSVYKMAELGKACTQENAQLRPSMRYIVVALSTLFSSTGNWDVGNFQNEDLVSLMSGR
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
40N-linked_GlycosylationLASYYLENGTTLSVI
HHHHHHHCCCEEEEE
22654057
52N-linked_GlycosylationSVINQNLNSSIAPYD
EEEECCCCCCCCCHH
22654057
102N-linked_GlycosylationPGDFLGHNFSYSVRQ
CCCCCCCCCEEEEEC
22654057
123N-linked_GlycosylationVAISNYANLTTMESL
EEEECCCCCCHHHHH
22654057
152N-linked_GlycosylationATLNVLVNCSCGDES
EEEEEEEECCCCCCC
22654057
185PhosphorylationLSSIARSSGVSADIL
HHHHHHHCCCCHHHH
29797451
266PhosphorylationKNKSKGDSFSSSIPL
HCCCCCCCCCCCCCC
20610395
268PhosphorylationKSKGDSFSSSIPLST
CCCCCCCCCCCCCCC
20610395
270PhosphorylationKGDSFSSSIPLSTKA
CCCCCCCCCCCCCCC
22654057
274PhosphorylationFSSSIPLSTKADHAS
CCCCCCCCCCCCCCC
20610395
281PhosphorylationSTKADHASSTSLQSG
CCCCCCCCCCCCCCC
27288362
282PhosphorylationTKADHASSTSLQSGG
CCCCCCCCCCCCCCC
27288362
283PhosphorylationKADHASSTSLQSGGL
CCCCCCCCCCCCCCC
27288362
284PhosphorylationADHASSTSLQSGGLG
CCCCCCCCCCCCCCC
27288362
287PhosphorylationASSTSLQSGGLGGAG
CCCCCCCCCCCCCCC
17317660
296PhosphorylationGLGGAGVSPGIAAIS
CCCCCCCCCCEEEEE
27288362
303PhosphorylationSPGIAAISVDKSVEF
CCCEEEEECCCCCEE
27288362
390PhosphorylationEGSLFLVYEYVENGN
HCEEEEEEEEHHCCC
-
466PhosphorylationDFGLTKLTEVGGSAT
HCCCEEEEEECCCCC
19880383
479PhosphorylationATRGAMGTFGYMAPE
CCCCCCCCCCCCCCC
-
519PhosphorylationKGAVVKMTEAVGEFR
CCCEEEHHHHHHHHH
24750441

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 CERK1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CERK1_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 CERK1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CERK1_ARATHCERK1physical
25070640
APX1_ARATHAPX1physical
25036661
SODC1_ARATHCSD1physical
25036661
TRXH4_ARATHATTRX4physical
25036661
FNRL2_ARATHFNR2physical
25036661
IF5A2_ARATHFBR12physical
25036661
ACBP6_ARATHACBP6physical
25036661
G3PB_ARATHGAPBphysical
25036661
ERF82_ARATHERF3physical
25036661
BGL18_ARATHBGLU18physical
25036661
FER2_ARATHFED Aphysical
25036661
KCS10_ARATHKCS10physical
25036661
CID7_ARATHCID7physical
25036661
SODC2_ARATHCSD2physical
25036661
PP14_ARATHTOPP4physical
25036661
SPCS2_ARATHAT2G39960physical
25036661
IQD14_ARATHIQD14physical
25036661
SPL3_ARATHSPL3physical
25036661
NLTP6_ARATHLTP6physical
25036661
CML36_ARATHAT3G10190physical
25036661
PSA5B_ARATHPAE2physical
25036661
Y3148_ARATHAT3G14840physical
25036661
Y3684_ARATHAT3G26840physical
25036661
NACA2_ARATHNACA2physical
25036661
SUT31_ARATHSULTR3;1physical
25036661
CAB6_ARATHLHCA1physical
25036661
MED21_ARATHMED21physical
25036661
PIP27_ARATHPIP3physical
25036661
AGP18_ARATHAGP18physical
25036661
UBQ3_ARATHUBQ3physical
25036661
GRP17_ARATHGRP17physical
25036661
KIN1_ARATHKIN1physical
25036661
EF1B2_ARATHAT5G19510physical
25036661
PIST_ARATHPIphysical
25036661
GRXC4_ARATHAT5G20500physical
25036661
VSP2_ARATHVSP2physical
25036661
DIRL1_ARATHDIR1physical
25036661
RH35_ARATHAT5G51280physical
25036661
CIPK7_ARATHCIPK7physical
24833385
AKT6_ARATHSPIKphysical
24833385
WNK8_ARATHWNK8physical
24833385
ANXD1_ARATHANNAT1physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
CHX28_ARATHchx28physical
24833385
LYK5_ARATHAT2G33580physical
25340959
CERK1_ARATHCERK1physical
25340959

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CERK1_ARATH

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Related Literatures of Post-Translational Modification

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