dbPTM

ICE1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ICE1_ARATH
UniProt AC	Q9LSE2
Protein Name	Transcription factor ICE1
Gene Name	SCRM
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	494
Subcellular Localization	Nucleus .
Protein Description	Transcriptional activator that regulates the cold-induced transcription of CBF/DREB1 genes. Binds specifically to the MYC recognition sites (5'-CANNTG-3') found in the CBF3/DREB1A promoter. Mediates stomatal differentiation in the epidermis probably by controlling successive roles of SPCH, MUTE, and FAMA..
Protein Sequence	MGLDGNNGGGVWLNGGGGEREENEEGSWGRNQEDGSSQFKPMLEGDWFSSNQPHPQDLQMLQNQPDFRYFGGFPFNPNDNLLLQHSIDSSSSCSPSQAFSLDPSQQNQFLSTNNNKGCLLNVPSSANPFDNAFEFGSESGFLNQIHAPISMGFGSLTQLGNRDLSSVPDFLSARSLLAPESNNNNTMLCGGFTAPLELEGFGSPANGGFVGNRAKVLKPLEVLASSGAQPTLFQKRAAMRQSSGSKMGNSESSGMRRFSDDGDMDETGIEVSGLNYESDEINESGKAAESVQIGGGGKGKKKGMPAKNLMAERRRRKKLNDRLYMLRSVVPKISKMDRASILGDAIDYLKELLQRINDLHNELESTPPGSLPPTSSSFHPLTPTPQTLSCRVKEELCPSSLPSPKGQQARVEVRLREGRAVNIHMFCGRRPGLLLATMKALDNLGLDVQQAVISCFNGFALDVFRAEQCQEGQEILPDQIKAVLFDTAGYAGMI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
393	Sumoylation	QTLSCRVKEELCPSS CCEEEEECHHHCCCC	26.56	-
393	Sumoylation	QTLSCRVKEELCPSS CCEEEEECHHHCCCC	26.56	-
403	Phosphorylation	LCPSSLPSPKGQQAR HCCCCCCCCCCCCEE	44.53	27531888

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	HOS1	Q84JU6	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
393	K	Sumoylation		16702557
Sumoylated at Lys-393 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 ICE1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HOS1_ARATH	HOS1	physical	22960247
TI10A_ARATH	JAZ1	physical	23933884
TIF6B_ARATH	JAZ3	physical	23933884
TIF6A_ARATH	JAZ4	physical	23933884
TIF7_ARATH	TIFY7	physical	23933884
TIF3A_ARATH	JAZ11	physical	23933884
UBQ3_ARATH	UBQ3	physical	24220632
SUMO3_ARATH	SUMO3	physical	20855607
SRK2E_ARATH	OST1	physical	25669882
SRK2I_ARATH	SNRK2.3	physical	25669882
BH095_ARATH	RGE1	physical	24553285
SCRM2_ARATH	SCRM2	genetic	26311645

Drug and Disease Associations

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

Regulatory Network of ICE1_ARATH

Related Literatures of Post-Translational Modification

Sumoylation
Reference	PubMed
"SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression andfreezing tolerance in Arabidopsis."; Miura K., Jin J.B., Lee J., Yoo C.Y., Stirm V., Miura T.,Ashworth E.N., Bressan R.A., Yun D.J., Hasegawa P.M.; Plant Cell 19:1403-1414(2007). Cited for: FUNCTION, SUMOYLATION AT LYS-393, AND MUTAGENESIS OF LYS-393.	17416732 [Abstract]