dbPTM

FERON_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FERON_ARATH
UniProt AC	Q9SCZ4
Protein Name	Receptor-like protein kinase FERONIA
Gene Name	FER
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	895
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Accumulates asymmetrically in the female gametophyte synergid membrane at the filiform apparatus.
Protein Description	Receptor-like protein kinase that mediates the female control of male gamete delivery during fertilization, including growth cessation of compatible pollen tubes ensuring a reproductive isolation barriers, by regulating MLO7 subcellular polarization upon pollen tube perception in the female gametophyte synergids. Required for cell elongation during vegetative growth, mostly in a brassinosteroids- (BR-) independent manner. Acts as an upstream regulator for the Rac/Rop-signaling pathway that controls ROS-mediated root hair development. Seems to regulate a cross-talk between brassinosteroids and ethylene signaling pathways during hypocotyl elongation. Negative regulator of brassinosteroid response in light-grown hypocotyls, but required for brassinosteroid response in etiolated seedlings. Mediates sensitivity to powdery mildew (e.g. Golovinomyces orontii). Positive regulator of auxin-promoted growth that represses the abscisic acid (ABA) signaling via the activation of ABI2 phosphatase. Required for RALF1-mediated extracellular alkalinization in a signaling pathway preventing cell expansion..
Protein Sequence	MKITEGRFRLSLLLLLLLISAATLISAADYSPTEKILLNCGGGASNLTDTDNRIWISDVKSKFLSSSSEDSKTSPALTQDPSVPEVPYMTARVFRSPFTYTFPVASGRKFVRLYFYPNSYDGLNATNSLFSVSFGPYTLLKNFSASQTAEALTYAFIIKEFVVNVEGGTLNMTFTPESAPSNAYAFVNGIEVTSMPDMYSSTDGTLTMVGSSGSVTIDNSTALENVYRLNVGGNDISPSADTGLYRSWYDDQPYIFGAGLGIPETADPNMTIKYPTGTPTYVAPVDVYSTARSMGPTAQINLNYNLTWIFSIDSGFTYLVRLHFCEVSSNITKINQRVFTIYLNNQTAEPEADVIAWTSSNGVPFHKDYVVNPPEGNGQQDLWLALHPNPVNKPEYYDSLLNGVEIFKMNTSDGNLAGTNPIPGPQVTADPSKVLRPTTRKSKSNTAIIAGAASGAVVLALIIGFCVFGAYRRRKRGDYQPASDATSGWLPLSLYGNSHSAGSAKTNTTGSYASSLPSNLCRHFSFAEIKAATKNFDESRVLGVGGFGKVYRGEIDGGTTKVAIKRGNPMSEQGVHEFQTEIEMLSKLRHRHLVSLIGYCEENCEMILVYDYMAHGTMREHLYKTQNPSLPWKQRLEICIGAARGLHYLHTGAKHTIIHRDVKTTNILLDEKWVAKVSDFGLSKTGPTLDHTHVSTVVKGSFGYLDPEYFRRQQLTEKSDVYSFGVVLFEALCARPALNPTLAKEQVSLAEWAPYCYKKGMLDQIVDPYLKGKITPECFKKFAETAMKCVLDQGIERPSMGDVLWNLEFALQLQESAEENGKGVCGDMDMDEIKYDDGNCKGKNDKSSDVYEGNVTDSRSSGIDMSIGGRSLASEDSDGLTPSAVFSQIMNPKGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	N-linked_Glycosylation	NCGGGASNLTDTDNR CCCCCHHCCCCCCCC	46.56	-
57	Phosphorylation	TDNRIWISDVKSKFL CCCCEEEEHHHHHHC	22.73	19880383
124	N-linked_Glycosylation	PNSYDGLNATNSLFS CCCCCCCCCCCCEEE	50.69	-
142	N-linked_Glycosylation	GPYTLLKNFSASQTA CHHHHHCCCCHHHHH	35.75	-
171	N-linked_Glycosylation	NVEGGTLNMTFTPES EEECCEEEEEECCCC	27.56	-
219	N-linked_Glycosylation	SGSVTIDNSTALENV CCEEEECCCCHHHEE	37.09	-
269	N-linked_Glycosylation	IPETADPNMTIKYPT CCCCCCCCCEEECCC	40.55	-
305	N-linked_Glycosylation	AQINLNYNLTWIFSI EEEECCEEEEEEEEE	29.89	-
330	N-linked_Glycosylation	HFCEVSSNITKINQR EEEEECCCCEEECCE	38.14	-
345	N-linked_Glycosylation	VFTIYLNNQTAEPEA EEEEEECCCCCCCCC	37.67	-
410	N-linked_Glycosylation	GVEIFKMNTSDGNLA CEEEEEEECCCCCCC	36.70	-
518	Phosphorylation	SYASSLPSNLCRHFS CCHHCCCCHHHHHCC	47.96	17317660
525	Phosphorylation	SNLCRHFSFAEIKAA CHHHHHCCHHHHHHH	19.88	25561503
692	Phosphorylation	TGPTLDHTHVSTVVK CCCCCCCCCHHHEEE	24.52	25561503
695	Phosphorylation	TLDHTHVSTVVKGSF CCCCCCHHHEEECCC	14.10	17317660
696	Phosphorylation	LDHTHVSTVVKGSFG CCCCCHHHEEECCCC	28.38	15308754
701	Phosphorylation	VSTVVKGSFGYLDPE HHHEEECCCCCCCHH	15.13	17317660
704	Phosphorylation	VVKGSFGYLDPEYFR EEECCCCCCCHHHHH	13.11	30407730
858	Phosphorylation	YEGNVTDSRSSGIDM EECCCCCCCCCCCCE	25.38	24458638
860	Phosphorylation	GNVTDSRSSGIDMSI CCCCCCCCCCCCEEE	36.55	15308754
861	Phosphorylation	NVTDSRSSGIDMSIG CCCCCCCCCCCEEEC	38.36	17317660
866	Phosphorylation	RSSGIDMSIGGRSLA CCCCCCEEECCCCCC	17.84	15308754
871	Phosphorylation	DMSIGGRSLASEDSD CEEECCCCCCCCCCC	31.40	24458638
874	Phosphorylation	IGGRSLASEDSDGLT ECCCCCCCCCCCCCC	47.43	24458638
877	Phosphorylation	RSLASEDSDGLTPSA CCCCCCCCCCCCHHH	29.53	30407730
881	Phosphorylation	SEDSDGLTPSAVFSQ CCCCCCCCHHHHHHH	22.26	30407730
883	Phosphorylation	DSDGLTPSAVFSQIM CCCCCCHHHHHHHHC	31.65	30407730
887	Phosphorylation	LTPSAVFSQIMNPKG CCHHHHHHHHCCCCC	16.52	30407730

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 FERON_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
858	S	Phosphorylation	24458638
Phosphorylated at Ser-858, Ser-871 and Ser-874 upon activation by RALF1.
871	S	Phosphorylation	24458638
Phosphorylated at Ser-858, Ser-871 and Ser-874 upon activation by RALF1.
874	S	Phosphorylation	24458638
Phosphorylated at Ser-858, Ser-871 and Ser-874 upon activation by RALF1.

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 FERON_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ROGF1_ARATH	ROPGEF1	physical	20876100
RLF1_ARATH	RALF1	physical	24458638
METK1_ARATH	SAM1	physical	25988356
METK2_ARATH	SAM-2	physical	25988356

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of FERON_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION AT SER-518; SER-695 AND SER-861, IDENTIFICATION BYMASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.	17317660 [Abstract]
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND THR-696, ANDMASS SPECTROMETRY.	15308754 [Abstract]
"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 SER-866, AND MASSSPECTROMETRY.	14506206 [Abstract]

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