ERL2_ARATH - dbPTM
ERL2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERL2_ARATH
UniProt AC Q6XAT2
Protein Name LRR receptor-like serine/threonine-protein kinase ERL2
Gene Name ERL2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 967
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description Receptor kinase that regulates inflorescence architecture and organ shape as well as stomatal patterning, including density and clustering, together with ERL1 and ER..
Protein Sequence MRRIETMKGLFFCLGMVVFMLLGSVSPMNNEGKALMAIKASFSNVANMLLDWDDVHNHDFCSWRGVFCDNVSLNVVSLNLSNLNLGGEISSALGDLMNLQSIDLQGNKLGGQIPDEIGNCVSLAYVDFSTNLLFGDIPFSISKLKQLEFLNLKNNQLTGPIPATLTQIPNLKTLDLARNQLTGEIPRLLYWNEVLQYLGLRGNMLTGTLSPDMCQLTGLWYFDVRGNNLTGTIPESIGNCTSFEILDVSYNQITGVIPYNIGFLQVATLSLQGNKLTGRIPEVIGLMQALAVLDLSDNELTGPIPPILGNLSFTGKLYLHGNKLTGQIPPELGNMSRLSYLQLNDNELVGKIPPELGKLEQLFELNLANNNLVGLIPSNISSCAALNQFNVHGNFLSGAVPLEFRNLGSLTYLNLSSNSFKGKIPAELGHIINLDTLDLSGNNFSGSIPLTLGDLEHLLILNLSRNHLNGTLPAEFGNLRSIQIIDVSFNFLAGVIPTELGQLQNINSLILNNNKIHGKIPDQLTNCFSLANLNISFNNLSGIIPPMKNFTRFSPASFFGNPFLCGNWVGSICGPSLPKSQVFTRVAVICMVLGFITLICMIFIAVYKSKQQKPVLKGSSKQPEGSTKLVILHMDMAIHTFDDIMRVTENLDEKYIIGYGASSTVYKCTSKTSRPIAIKRIYNQYPSNFREFETELETIGSIRHRNIVSLHGYALSPFGNLLFYDYMENGSLWDLLHGPGKKVKLDWETRLKIAVGAAQGLAYLHHDCTPRIIHRDIKSSNILLDGNFEARLSDFGIAKSIPATKTYASTYVLGTIGYIDPEYARTSRLNEKSDIYSFGIVLLELLTGKKAVDNEANLHQMILSKADDNTVMEAVDAEVSVTCMDSGHIKKTFQLALLCTKRNPLERPTMQEVSRVLLSLVPSPPPKKLPSPAKVQEGEERRESHSSDTTTPQWFVQFREDISKSSL
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
70N-linked_GlycosylationWRGVFCDNVSLNVVS
CCCEEECCEEEEEEE
26.85-
79N-linked_GlycosylationSLNVVSLNLSNLNLG
EEEEEEEECCCCCCC
33.64-
228N-linked_GlycosylationYFDVRGNNLTGTIPE
EEEECCCCCEECCCC
41.63-
239N-linked_GlycosylationTIPESIGNCTSFEIL
CCCCCCCCCCEEEEE
24.99-
310N-linked_GlycosylationPIPPILGNLSFTGKL
CCCCCCCEEEECCEE
29.12-
334N-linked_GlycosylationQIPPELGNMSRLSYL
CCCHHHCCCCCEEEE
37.57-
379N-linked_GlycosylationLVGLIPSNISSCAAL
CEEEECCCHHHHHHH
32.57-
414N-linked_GlycosylationLGSLTYLNLSSNSFK
CCCCEEEECCCCCCC
27.71-
443N-linked_GlycosylationTLDLSGNNFSGSIPL
EEECCCCCCCCCCCE
35.67-
462N-linked_GlycosylationLEHLLILNLSRNHLN
HHHHHHHCCCCCCCC
29.04-
469N-linked_GlycosylationNLSRNHLNGTLPAEF
CCCCCCCCCCCCHHH
33.58-
534N-linked_GlycosylationCFSLANLNISFNNLS
CCHHHCCEEEECCCC
27.89-
539N-linked_GlycosylationNLNISFNNLSGIIPP
CCEEEECCCCCCCCC
33.31-
549N-linked_GlycosylationGIIPPMKNFTRFSPA
CCCCCCCCCCCCCCH
36.95-
640PhosphorylationHMDMAIHTFDDIMRV
EEEHHHHCHHHHHHH
23.73-
648PhosphorylationFDDIMRVTENLDEKY
HHHHHHHHCCCCCCE
14.59-
724PhosphorylationPFGNLLFYDYMENGS
CCCCEEEEEECCCCC
13.21-
763PhosphorylationGAAQGLAYLHHDCTP
HHHHHHHHHCCCCCC
16.18-
818PhosphorylationYVLGTIGYIDPEYAR
EEECHHCCCCHHHHH
9.78-
826PhosphorylationIDPEYARTSRLNEKS
CCHHHHHHCCCCCCC
15.27-

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 ERL2_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERL2_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 ERL2_ARATH !!

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

Oops, there are no PPI records of ERL2_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERL2_ARATH

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Related Literatures of Post-Translational Modification

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