dbPTM

SAE2_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SAE2_ARATH
UniProt AC	Q9SJT1
Protein Name	SUMO-activating enzyme subunit 2
Gene Name	SAE2
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	700
Subcellular Localization	Nucleus.
Protein Description	The dimeric enzyme acts as an E1 ligase for SUMO1 and SUMO2. It mediates ATP-dependent activation of SUMO proteins and formation of a thioester with a conserved cysteine residue on SAE2..
Protein Sequence	MATQQQQSAIKGAKVLMVGAGGIGCELLKTLALSGFEDIHIIDMDTIEVSNLNRQFLFRRSHVGQSKAKVARDAVLRFRPNINIRSYHANVKNPEFDVDFFKQFDVVLNGLDNLDARRHVNRLCLAADVPLVESGTTGFLGQVTVHIKGKTECYECQTKPAPKTYPVCTITSTPTKFVHCIVWAKDLLFAKLFGDKNQDNDLNVRSNNSASSSKETEDVFERSEDEDIEQYGRKIYDHVFGSNIEAALSNEETWKNRRRPRPIYSKDVLPESLTQQNGSTQNCSVTDGDLMVSAMPSLGLKNPQELWGLTQNSLVFIEALKLFFAKRKKEIGHLTFDKDDQLAVEFVTAAANIRAESFGIPLHSLFEAKGIAGNIVHAVATTNAIIAGLIVIEAIKVLKKDVDKFRMTYCLEHPSKKLLLMPIEPYEPNPACYVCSETPLVLEINTRKSKLRDLVDKIVKTKLGMNLPLIMHGNSLLYEVGDDLDDIMVANYNANLEKYLSELPSPILNGSILTVEDLQQELSCKINVKHRFFSEILNPVLNSVWFLIILPSTFPKLFHFTESRNQDGLSLDIILGFSNVTIRRVLTMFETGRRLTHPLLILFCHREEFDEEKEPEGMVLSGWTPSPATNGESASTSNNENPVDVTESSSGSEPASKKRRLSETEASNHKKETENVESEDDDIMEVENPMMVSKKKIRVE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATQQQQSA ------CCHHHHHHH	17.70	22223895
223	Phosphorylation	TEDVFERSEDEDIEQ HHCHHHCCCCHHHHH	42.05	30407730
673	Phosphorylation	ASNHKKETENVESED HHCCHHHHCCCCCCC	41.56	23776212
678	Phosphorylation	KETENVESEDDDIME HHHCCCCCCCCCCEE	41.88	12482876
693	Phosphorylation	VENPMMVSKKKIRVE CCCCEEECCCCCCCC	22.36	23776212

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 SAE2_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SAE2_ARATH !!

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 SAE2_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAI_ARATH	GAI	physical	24434138
RGA_ARATH	RGA1	physical	24434138
SCE1_ARATH	SCE1	physical	24434138

Drug and Disease Associations

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

Regulatory Network of SAE2_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-673 AND SER-678, ANDMASS SPECTROMETRY.	19376835 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASSSPECTROMETRY.	18433157 [Abstract]