FLS2_ARATH - dbPTM
FLS2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FLS2_ARATH
UniProt AC Q9FL28
Protein Name LRR receptor-like serine/threonine-protein kinase FLS2
Gene Name FLS2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1173
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Endosome membrane
Single-pass type I membrane protein . Internalization by endocytosis. Accumulates at the plasma membrane, in an ACD6-dependent manner, in response to salicylic acid (SA) signal
Protein Description Constitutes the pattern-recognition receptor (PPR) that determines the specific perception of flagellin (flg22), a potent elicitor of the defense response to pathogen-associated molecular patterns (PAMPs). Flagellin-binding to the receptor is the first step to initiate the innate immune MAP kinase signaling cascade (MEKK1, MKK4/MKK5 and MPK3/MPK6), resulting in enhanced resistance against pathogens. Binding to the effector AvrPto1 or to the phosphatase hopD2 from Pseudomonas syringae blocks the downstream plant immune response..
Protein Sequence MKLLSKTFLILTLTFFFFGIALAKQSFEPEIEALKSFKNGISNDPLGVLSDWTIIGSLRHCNWTGITCDSTGHVVSVSLLEKQLEGVLSPAIANLTYLQVLDLTSNSFTGKIPAEIGKLTELNQLILYLNYFSGSIPSGIWELKNIFYLDLRNNLLSGDVPEEICKTSSLVLIGFDYNNLTGKIPECLGDLVHLQMFVAAGNHLTGSIPVSIGTLANLTDLDLSGNQLTGKIPRDFGNLLNLQSLVLTENLLEGDIPAEIGNCSSLVQLELYDNQLTGKIPAELGNLVQLQALRIYKNKLTSSIPSSLFRLTQLTHLGLSENHLVGPISEEIGFLESLEVLTLHSNNFTGEFPQSITNLRNLTVLTVGFNNISGELPADLGLLTNLRNLSAHDNLLTGPIPSSISNCTGLKLLDLSHNQMTGEIPRGFGRMNLTFISIGRNHFTGEIPDDIFNCSNLETLSVADNNLTGTLKPLIGKLQKLRILQVSYNSLTGPIPREIGNLKDLNILYLHSNGFTGRIPREMSNLTLLQGLRMYSNDLEGPIPEEMFDMKLLSVLDLSNNKFSGQIPALFSKLESLTYLSLQGNKFNGSIPASLKSLSLLNTFDISDNLLTGTIPGELLASLKNMQLYLNFSNNLLTGTIPKELGKLEMVQEIDLSNNLFSGSIPRSLQACKNVFTLDFSQNNLSGHIPDEVFQGMDMIISLNLSRNSFSGEIPQSFGNMTHLVSLDLSSNNLTGEIPESLANLSTLKHLKLASNNLKGHVPESGVFKNINASDLMGNTDLCGSKKPLKPCTIKQKSSHFSKRTRVILIILGSAAALLLVLLLVLILTCCKKKEKKIENSSESSLPDLDSALKLKRFEPKELEQATDSFNSANIIGSSSLSTVYKGQLEDGTVIAVKVLNLKEFSAESDKWFYTEAKTLSQLKHRNLVKILGFAWESGKTKALVLPFMENGNLEDTIHGSAAPIGSLLEKIDLCVHIASGIDYLHSGYGFPIVHCDLKPANILLDSDRVAHVSDFGTARILGFREDGSTTASTSAFEGTIGYLAPEFAYMRKVTTKADVFSFGIIMMELMTKQRPTSLNDEDSQDMTLRQLVEKSIGNGRKGMVRVLDMELGDSIVSLKQEEAIEDFLKLCLFCTSSRPEDRPDMNEILTHLMKLRGKANSFREDRNEDREV
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
62N-linked_GlycosylationIGSLRHCNWTGITCD
EECCCCCCCCCEEEC		32.97-
94N-linked_GlycosylationVLSPAIANLTYLQVL
CCCHHHHHCCEEEEE		27.1424114786
179N-linked_GlycosylationLIGFDYNNLTGKIPE
EEEECCCCCCCCCCH		32.52-
217N-linked_GlycosylationVSIGTLANLTDLDLS
EEHHHHCCCCCEECC		46.7324114786
262N-linked_GlycosylationDIPAEIGNCSSLVQL
CCCCCCCCCCCEEEE		28.3224114786
347N-linked_GlycosylationVLTLHSNNFTGEFPQ
EEEEECCCCCCCCCH		38.58-
361N-linked_GlycosylationQSITNLRNLTVLTVG
HHHCCCCCCEEEEEE		43.1424114786
371N-linked_GlycosylationVLTVGFNNISGELPA
EEEEECCCCCCCCCC		27.7824114786
388N-linked_GlycosylationGLLTNLRNLSAHDNL
HHHHHCCCCCCCCCC		41.3224114786
406N-linked_GlycosylationPIPSSISNCTGLKLL
CCCCHHHCCCCCEEE		26.2124114786
432N-linked_GlycosylationPRGFGRMNLTFISIG
CCCCCCCCEEEEEEC		34.2724114786
453N-linked_GlycosylationEIPDDIFNCSNLETL
CCCCCCCCCCCCCEE		28.74-
466N-linked_GlycosylationTLSVADNNLTGTLKP
EEEECCCCCCCCCHH		39.26-
525N-linked_GlycosylationRIPREMSNLTLLQGL
CCCHHHCCHHHHHHH		35.42-
588N-linked_GlycosylationSLQGNKFNGSIPASL
EECCCCCCCCCCCHH		44.9324114786
631N-linked_GlycosylationKNMQLYLNFSNNLLT
CCCEEEEECCCCCCC		25.4124114786
684N-linked_GlycosylationTLDFSQNNLSGHIPD
EEECCCCCCCCCCCH		28.13-
704N-linked_GlycosylationMDMIISLNLSRNSFS
CEEEEEEECCCCCCC		29.2224114786
720N-linked_GlycosylationEIPQSFGNMTHLVSL
CCCCCCCCCEEEEEE		30.12-
733N-linked_GlycosylationSLDLSSNNLTGEIPE
EEECCCCCCCCCCCH		40.71-
744N-linked_GlycosylationEIPESLANLSTLKHL
CCCHHHHCHHHHHHH		39.56-
772N-linked_GlycosylationSGVFKNINASDLMGN
CCCCCCCCHHHHCCC		42.67-
830S-palmitoylationLLVLILTCCKKKEKK
HHHHHHHHCHHHHHH		2.6127493678
831S-palmitoylationLVLILTCCKKKEKKI
HHHHHHHCHHHHHHC		6.4527493678
841PhosphorylationKEKKIENSSESSLPD
HHHHCCCCCCCCCCC		23.7724894044
867PhosphorylationPKELEQATDSFNSAN
HHHHHHHHHCCCCCC		31.6920103591
869PhosphorylationELEQATDSFNSANII
HHHHHHHCCCCCCEE		23.2124104392
906PhosphorylationVLNLKEFSAESDKWF
EECHHHCCCCCCCCC		32.0224104392
938PhosphorylationILGFAWESGKTKALV
HHHEEECCCCCEEEE		34.5824104392
941PhosphorylationFAWESGKTKALVLPF
EEECCCCCEEEEEEE		25.6924104392
961PhosphorylationLEDTIHGSAAPIGSL
CCCEECCCCCCHHHH		13.7024104392
984PhosphorylationHIASGIDYLHSGYGF
HHHCCCHHHHCCCCC		12.37-
1035PhosphorylationGSTTASTSAFEGTIG
CCCCCCCHHHCCCHH		28.59-
1043PhosphorylationAFEGTIGYLAPEFAY
HHCCCHHCCCHHHHH		8.88-
1050PhosphorylationYLAPEFAYMRKVTTK
CCCHHHHHHCCCCCH		11.63-
1084PhosphorylationTSLNDEDSQDMTLRQ
CCCCCCCHHCCHHHH		26.4924104392
1115PhosphorylationLDMELGDSIVSLKQE
EECCCCCEEEECCHH		24.0824104392
1162PhosphorylationKLRGKANSFREDRNE
HHHCCHHHHHCCCCC		30.4625561503
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
869SPhosphorylationKinaseBAK1Q94F62
Uniprot
906SPhosphorylationKinaseBAK1Q94F62
Uniprot
961SPhosphorylationKinaseBAK1Q94F62
Uniprot
1115SPhosphorylationKinaseBAK1Q94F62
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FLS2_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 FLS2_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P2C70_ARATHKAPPphysical
11340188
BAK1_ARATHBAK1physical
21593986
PUB13_ARATHPUB13physical
21680842
Y5126_ARATHAT5G41260physical
21726371
RPM1_ARATHRPM1physical
21726371
RIN4_ARATHRIN4physical
21726371
FLS2_ARATHFLS2physical
22388452
ACA8_ARATHACA8physical
22535420
Y4523_ARATHBSK1physical
23532072
FLS2_ARATHFLS2physical
23637603
BAK1_ARATHBAK1physical
24114786
BAK1_ARATHBAK1physical
21464298
BAK1_ARATHBAK1physical
25070640
BAK1_ARATHBAK1physical
24372399
LRK62_ARATHLECRKA4.1physical
24844677
BAK1_ARATHBAK1physical
24844677
BAK1_ARATHBAK1physical
24130196
CNIH1_ARATHAT3G12180physical
24833385
BETL2_ARATHAT1G29060physical
24833385
BIK1_ARATHBIK1physical
20018686
FLS2_ARATHFLS2physical
20018686
UBQ3_ARATHUBQ3physical
25873653
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FLS2_ARATH

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Related Literatures of Post-Translational Modification

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