SIZ1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIZ1_ARATH
• UniProt AC: Q680Q4
• Protein Name: E3 SUMO-protein ligase SIZ1 {ECO:0000303|PubMed:15894620}
• Gene Name: SIZ1 {ECO:0000303|PubMed:15894620}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 884
• Subcellular Localization: Nucleus speckle .
• Protein Description: E3 SUMO protein ligase involved in regulation processes. Mediates SUMO/ attachment to PHR1, a MYB transcriptional activator controlling the phosphate deficiency responses. [PubMed: 15894620 Functions as an upstream negative regulator of salicylic acid (SA) accumulation and subsequent SA-mediated systemic acquired resistance (SAR) signaling. Probably not involved in jasmonic acid (JA)-mediated defense response. Participates in abiotic stress-induced sumoylation. Controls heat shock-induced SUMO1 and SUMO2 conjugation and facilitates basal thermotolerance. Involved in freezing tolerance by mediating sumoylation of ICE1, a transcription activator of the cold signaling regulator CBF3/DREB1A. Acts as positive regulator of drought stress tolerance. Acts as floral repressor that promotes FLC expression by repressing FLD activity through sumoylation. Acts as negative regulator of abscisic acid (ABA) signaling through ABI5 sumoylation. Mediates sumoylation of SCE1, GTE3 and GTE5.]
• Protein Sequence: MDLEANCKEKLSYFRIKELKDVLTQLGLSKQGKKQELVDRILTLLSDEQAARLLSKKNTVAKEAVAKLVDDTYRKMQVSGASDLASKGQVSSDTSNLKVKGEPEDPFQPEIKVRCVCGNSLETDSMIQCEDPRCHVWQHVGCVILPDKPMDGNPPLPESFYCEICRLTRADPFWVTVAHPLSPVRLTATTIPNDGASTMQSVERTFQITRADKDLLAKPEYDVQAWCMLLNDKVLFRMQWPQYADLQVNGVPVRAINRPGGQLLGVNGRDDGPIITSCIRDGVNRISLSGGDVRIFCFGVRLVKRRTLQQVLNLIPEEGKGETFEDALARVRRCIGGGGGDDNADSDSDIEVVADFFGVNLRCPMSGSRIKVAGRFLPCVHMGCFDLDVFVELNQRSRKWQCPICLKNYSVEHVIVDPYFNRITSKMKHCDEEVTEIEVKPDGSWRVKFKRESERRELGELSQWHAPDGSLCPSAVDIKRKMEMLPVKQEGYSDGPAPLKLGIRKNRNGIWEVSKPNTNGLSSSNRQEKVGYQEKNIIPMSSSATGSGRDGDDASVNQDAIGTFDFVANGMELDSISMNVDSGYNFPDRNQSGEGGNNEVIVLSDSDDENDLVITPGPAYSGCQTDGGLTFPLNPPGIINSYNEDPHSIAGGSSGLGLFNDDDEFDTPLWSFPSETPEAPGFQLFRSDADVSGGLVGLHHHSPLNCSPEINGGYTMAPETSMASVPVVPGSTGRSEANDGLVDNPLAFGRDDPSLQIFLPTKPDASAQSGFKNQADMSNGLRSEDWISLRLGDSASGNHGDPATTNGINSSHQMSTREGSMDTTTETASLLLGMNDSRQDKAKKQRSDNPFSFPRQKRSNNEQDHQTRHRSLNKICIILCAGKN

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
79	Phosphorylation	TYRKMQVSGASDLAS HHHHHHHCCHHHHHH	16.26	19880383
86	Phosphorylation	SGASDLASKGQVSSD CCHHHHHHCCCCCCC	44.61	19880383
91	Phosphorylation	LASKGQVSSDTSNLK HHHCCCCCCCCCCCE	18.01	23776212
92	Phosphorylation	ASKGQVSSDTSNLKV HHCCCCCCCCCCCEE	46.15	23776212
94	Phosphorylation	KGQVSSDTSNLKVKG CCCCCCCCCCCEECC	22.82	23776212
95	Phosphorylation	GQVSSDTSNLKVKGE CCCCCCCCCCEECCC	45.19	23776212
100	Sumoylation	DTSNLKVKGEPEDPF CCCCCEECCCCCCCC	56.84	-
100	Sumoylation	DTSNLKVKGEPEDPF CCCCCEECCCCCCCC	56.84	-
346	Phosphorylation	GGDDNADSDSDIEVV CCCCCCCCCCCCCCE	36.28	23572148
348	Phosphorylation	DDNADSDSDIEVVAD CCCCCCCCCCCCEEH	44.43	23572148
479	Sumoylation	CPSAVDIKRKMEMLP CCCHHHHHHHHHCCC	41.31	-
488	Sumoylation	KMEMLPVKQEGYSDG HHHCCCCCCCCCCCC	40.46	-
488	Sumoylation	KMEMLPVKQEGYSDG HHHCCCCCCCCCCCC	40.46	-
492	Phosphorylation	LPVKQEGYSDGPAPL CCCCCCCCCCCCCCC	11.66	25561503
493	Phosphorylation	PVKQEGYSDGPAPLK CCCCCCCCCCCCCCE	47.12	19880383
542	Phosphorylation	KNIIPMSSSATGSGR CCEECCCCCCCCCCC	20.10	29654922
547	Phosphorylation	MSSSATGSGRDGDDA CCCCCCCCCCCCCCC	26.71	29654922
820	Phosphorylation	QMSTREGSMDTTTET CCCCCCCCCCCHHHH	14.56	23776212
823	Phosphorylation	TREGSMDTTTETASL CCCCCCCCHHHHHHH	27.29	23776212
824	Phosphorylation	REGSMDTTTETASLL CCCCCCCHHHHHHHH	20.54	23776212
870 (in isoform 3)	Phosphorylation	-	39.28	23776212
870 (in isoform 4)	Phosphorylation	-	39.28	23776212
872 (in isoform 3)	Phosphorylation	-	8.36	23776212
872 (in isoform 4)	Phosphorylation	-	8.36	23776212

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SIZ1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
100	K	Sumoylation	Autosumoylated at Lys-100 and Lys-488.	18502747
488	K	Sumoylation	Autosumoylated at Lys-100 and Lys-488.	18502747

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SIZ1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NIA1_ARATH	NIA1	physical	21772271
NIA2_ARATH	NIA2	physical	21772271
ABI5_ARATH	ABI5	physical	19276109
FLC_ARATH	FLC	physical	24218331
CMT3_ARATH	CMT3	physical	26398805
ICE1_ARATH	ICE1	physical	17416732
SUMO1_ARATH	SUMO1	physical	17416732
SIZ1_ARATH	SIZ1	physical	18502747
SUMO1_ARATH	SUMO1	physical	18502747
GTE3_ARATH	GTE3	physical	18502747
SCE1_ARATH	SCE1	physical	18502747
GTE5_ARATH	AT1G17790	physical	18502747
COP1_ARATH	COP1	physical	27128446
GID2_ARATH	SLY1	physical	26008766

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Sumoylation

"The PHD domain of plant PIAS proteins mediates sumoylation ofbromodomain GTE proteins.";
Garcia-Dominguez M., March-Diaz R., Reyes J.C.;
J. Biol. Chem. 283:21469-21477(2008).
Cited for: FUNCTION, AUTOSUMOYLATION AT LYS-100 AND LYS-488, INTERACTION WITHSCE1; GTE3 AND GTE5, DOMAIN, AND MUTAGENESIS OF LYS-100 AND LYS-488.
PubMed: 18502747