dbPTM

BIK1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BIK1_ARATH
UniProt AC	O48814
Protein Name	Serine/threonine-protein kinase BIK1 {ECO:0000305}
Gene Name	BIK1 {ECO:0000303\|PubMed:16339855}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	395
Subcellular Localization	Cell membrane Lipid-anchor .
Protein Description	Plays a central role in immune responses. [PubMed: 20413097 Required to activate the resistance responses to necrotrophic pathogens]
Protein Sequence	MGSCFSSRVKADIFHNGKSSDLYGLSLSSRKSSSTVAAAQKTEGEILSSTPVKSFTFNELKLATRNFRPDSVIGEGGFGCVFKGWLDESTLTPTKPGTGLVIAVKKLNQEGFQGHREWLTEINYLGQLSHPNLVKLIGYCLEDEHRLLVYEFMQKGSLENHLFRRGAYFKPLPWFLRVNVALDAAKGLAFLHSDPVKVIYRDIKASNILLDADYNAKLSDFGLARDGPMGDLSYVSTRVMGTYGYAAPEYMSSGHLNARSDVYSFGVLLLEILSGKRALDHNRPAKEENLVDWARPYLTSKRKVLLIVDNRLDTQYLPEEAVRMASVAVQCLSFEPKSRPTMDQVVRALQQLQDNLGKPSQTNPVKDTKKLGFKTGTTKSSEKRFTQKPFGRHLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGSCFSSRV ------CCCCCCCCE	32.87	26021844
4	S-palmitoylation	----MGSCFSSRVKA ----CCCCCCCCEEE	2.96	-
26	Phosphorylation	SSDLYGLSLSSRKSS CCCEECEECCCCCCC	23.11	30407730
28	Phosphorylation	DLYGLSLSSRKSSST CEECEECCCCCCCCC	25.40	30407730
29	Phosphorylation	LYGLSLSSRKSSSTV EECEECCCCCCCCCH	49.36	30407730
48	Phosphorylation	KTEGEILSSTPVKSF HCCCCHHCCCCCCEE	37.52	24104392
54	Phosphorylation	LSSTPVKSFTFNELK HCCCCCCEEEHHHHH	29.74	24104392
56	Phosphorylation	STPVKSFTFNELKLA CCCCCEEEHHHHHHH	32.42	24104392
71	Phosphorylation	TRNFRPDSVIGEGGF HCCCCCCCCCCCCCC	20.51	17317660
89	Phosphorylation	FKGWLDESTLTPTKP EECEECCCCCCCCCC	28.52	29649442
90	Phosphorylation	KGWLDESTLTPTKPG ECEECCCCCCCCCCC	32.38	29649442
120	Phosphorylation	QGHREWLTEINYLGQ CCHHHHHHHCHHHHH	35.57	29649442
129	Phosphorylation	INYLGQLSHPNLVKL CHHHHHCCCCCHHHH	29.07	29649442
150	Phosphorylation	DEHRLLVYEFMQKGS HHHHHHHHHHHHCCC	11.92	24532660
168	Phosphorylation	HLFRRGAYFKPLPWF CHHHCCCCCCCCCHH	18.24	24104392
206	Phosphorylation	IYRDIKASNILLDAD EECCCCHHHEEECCC	21.28	24104392
214	Phosphorylation	NILLDADYNAKLSDF HEEECCCCCCCHHHH	20.81	24104392
233	Phosphorylation	DGPMGDLSYVSTRVM CCCCCCCHHHHCCCC	28.38	23431184
236	UMPylation	MGDLSYVSTRVMGTY CCCCHHHHCCCCCCC	11.41	22504181
236	Phosphorylation	MGDLSYVSTRVMGTY CCCCHHHHCCCCCCC	11.41	24104392
237	UMPylation	GDLSYVSTRVMGTYG CCCHHHHCCCCCCCC	19.76	22504181
237	Phosphorylation	GDLSYVSTRVMGTYG CCCHHHHCCCCCCCC	19.76	24104392
242	Phosphorylation	VSTRVMGTYGYAAPE HHCCCCCCCCCCCCH	8.83	24104392
243	Phosphorylation	STRVMGTYGYAAPEY HCCCCCCCCCCCCHH	11.47	24532660
250	Phosphorylation	YGYAAPEYMSSGHLN CCCCCCHHHCCCCCC	10.96	24104392
252	Phosphorylation	YAAPEYMSSGHLNAR CCCCHHHCCCCCCCC	32.06	24104392
253	Phosphorylation	AAPEYMSSGHLNARS CCCHHHCCCCCCCCC	17.44	24104392
314	Phosphorylation	IVDNRLDTQYLPEEA EECCCCCCCCCCHHH	24.57	24104392
360	Phosphorylation	QDNLGKPSQTNPVKD HHHCCCCCCCCCCCC	53.79	24104392
362	Phosphorylation	NLGKPSQTNPVKDTK HCCCCCCCCCCCCCC	45.91	24104392
368	Phosphorylation	QTNPVKDTKKLGFKT CCCCCCCCCCCCCCC	25.10	24104392
377	Phosphorylation	KLGFKTGTTKSSEKR CCCCCCCCCCCCCCC	35.96	19880383

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
48	S	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
71	S	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
89	S	Phosphorylation	Kinase	EFR	C0LGT6	Uniprot
90	T	Phosphorylation	Kinase	EFR	C0LGT6	Uniprot
120	T	Phosphorylation	Kinase	EFR	C0LGT6	Uniprot
129	S	Phosphorylation	Kinase	EFR	C0LGT6	Uniprot
206	S	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
236	S	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
237	T	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
242	T	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
360	S	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
362	T	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot
368	T	Phosphorylation	Kinase	BAK1	Q94F62	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
89	S	Phosphorylation	29649442
Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to the microbe-associated molecular pattern (MAMP) flg22.19).
90	T	Phosphorylation	29649442
Phosphorylated, especially by EFR at Ser-89 and Thr-90, in response to the microbe-associated molecular pattern (MAMP) flg22.19).
233	S	Phosphorylation	23431184
Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1.
236	S	Phosphorylation	20413097
Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1.
237	T	Phosphorylation	20404519
Phosphorylated at Ser-233, Ser-236 and THR-237 by PEPR1.

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 BIK1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLS2_ARATH	FLS2	physical	20413097
PEPR1_ARATH	PEPR1	physical	23431184
BRI1_ARATH	BRI1	physical	23818580
FLS2_ARATH	FLS2	physical	23637603
RBOHD_ARATH	RBOHD	physical	24630626
BAK1_ARATH	BAK1	physical	20018686
FLS2_ARATH	FLS2	physical	20018686
BIK1_ARATH	BIK1	physical	20018686
PEPR1_ARATH	PEPR1	physical	25188390

Drug and Disease Associations

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

Regulatory Network of BIK1_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 [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.	17317660 [Abstract]
"Phosphorylation of receptor-like cytoplasmic kinases by bacterialflagellin."; Lu D., Wu S., He P., Shan L.; Plant Signal. Behav. 5:598-600(2010). Cited for: FUNCTION, INTERACTION WITH FLS2 AND BAK1, AUTOPHOSPHORYLATION, ANDPHOSPHORYLATION AT THR-237.	20404519 [Abstract]

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