dbPTM

ABI5_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ABI5_ARATH
UniProt AC	Q9SJN0
Protein Name	Protein ABSCISIC ACID-INSENSITIVE 5
Gene Name	ABI5
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	442
Subcellular Localization	Nucleus .
Protein Description	Participates in ABA-regulated gene expression during seed development and subsequent vegetative stage by acting as the major mediator of ABA repression of growth. Binds to the embryo specification element and the ABA-responsive element (ABRE) of the Dc3 gene promoter and to the ABRE of the Em1 and Em6 genes promoters. Can also trans-activate its own promoter, suggesting that it is autoregulated. Plays a role in sugar-mediated senescence..
Protein Sequence	MVTRETKLTSEREVESSMAQARHNGGGGGENHPFTSLGRQSSIYSLTLDEFQHALCENGKNFGSMNMDEFLVSIWNAEENNNNQQQAAAAAGSHSVPANHNGFNNNNNNGGEGGVGVFSGGSRGNEDANNKRGIANESSLPRQGSLTLPAPLCRKTVDEVWSEIHRGGGSGNGGDSNGRSSSSNGQNNAQNGGETAARQPTFGEMTLEDFLVKAGVVREHPTNPKPNPNPNQNQNPSSVIPAAAQQQLYGVFQGTGDPSFPGQAMGVGDPSGYAKRTGGGGYQQAPPVQAGVCYGGGVGFGAGGQQMGMVGPLSPVSSDGLGHGQVDNIGGQYGVDMGGLRGRKRVVDGPVEKVVERRQRRMIKNRESAARSRARKQAYTVELEAELNQLKEENAQLKHALAELERKRKQQYFESLKSRAQPKLPKSNGRLRTLMRNPSCPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	Phosphorylation	TSLGRQSSIYSLTLD CCCCCCCEEEEEEHH	19.73	-
64	Phosphorylation	ENGKNFGSMNMDEFL HCCCCCCCCCHHHHH	11.66	-
138	Phosphorylation	KRGIANESSLPRQGS CCCCCCCCCCCCCCC	36.66	27288362
139	Phosphorylation	RGIANESSLPRQGSL CCCCCCCCCCCCCCC	35.89	27288362
145	Phosphorylation	SSLPRQGSLTLPAPL CCCCCCCCCCCCHHH	15.16	25561503
147	Phosphorylation	LPRQGSLTLPAPLCR CCCCCCCCCCHHHCC	32.18	25561503
201	Phosphorylation	ETAARQPTFGEMTLE CCCCCCCCCCCCCHH	35.61	-
391	Sumoylation	EAELNQLKEENAQLK HHHHHHHHHHHHHHH	53.90	-
391	Sumoylation	EAELNQLKEENAQLK HHHHHHHHHHHHHHH	53.90	19276109

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
-	K	Ubiquitination	E3 ubiquitin ligase	DWA2	Q6NPN9	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	KEG	Q9FY48	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	THO6	Q8L4M1	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
391	K	Sumoylation		19276109
Sumoylated at Lys-391 by SIZ1.

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 ABI5_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1A110_ARATH	ACS10	physical	12569131
ABI3_ARATH	ABI3	physical	11489176
CUL4_ARATH	CUL4	physical	20525848
AI5L3_ARATH	EEL	physical	21279647
ARR4_ARATH	ARR4	physical	21699589
ARR5_ARATH	RR5	physical	21699589
ARR6_ARATH	ARR6	physical	21699589
MED25_ARATH	PFT1	physical	22822206
SUMO1_ARATH	SUMO1	physical	19276109
FYPP3_ARATH	FYPP3	physical	23404889
FYPP1_ARATH	AT1G50370	physical	23404889
GAI_ARATH	GAI	physical	24326588
TAP46_ARATH	TAP46	physical	24357600
PP2A5_ARATH	PP2A	physical	24357600
AFP2_ARATH	AFP2	physical	24823379
ABI5_ARATH	ABI5	physical	24823379
AFP4_ARATH	TMAC2	physical	24823379
CADH5_ARATH	CAD5	physical	24823379
NADB_ARATH	AO	physical	24823379
RVE2_ARATH	RVE2	physical	24823379
P2C78_ARATH	HAI1	physical	24823379
FCA_ARATH	FCA	physical	25266977
SRK2D_ARATH	SNRK2.2	physical	23007729
SRK2I_ARATH	SNRK2.3	physical	23007729
P2C75_ARATH	AHG1	physical	23007729
AI5L4_ARATH	ABF1	physical	23007729
ABI5_ARATH	ABI5	physical	23007729
AI5L6_ARATH	ABF3	physical	23007729
CDPKB_ARATH	CDPK2	physical	23007729
P2C37_ARATH	PP2CA	physical	23007729
CIPKB_ARATH	SIP4	physical	25858916

Drug and Disease Associations

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

Regulatory Network of ABI5_ARATH

Related Literatures of Post-Translational Modification

Sumoylation
Reference	PubMed
"Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negativelyregulates abscisic acid signaling."; Miura K., Lee J., Jin J.B., Yoo C.Y., Miura T., Hasegawa P.M.; Proc. Natl. Acad. Sci. U.S.A. 106:5418-5423(2009). Cited for: SUMOYLATION AT LYS-391, AND MUTAGENESIS OF LYS-391.	19276109 [Abstract]