TPS5_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TPS5_ARATH
• UniProt AC: O23617
• Protein Name: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 5
• Gene Name: TPS5
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 862
• Protein Sequence: MVSRSYSNLLDLASGNFHSFSREKKRFPRVATVTGVLSELDDDNNSNSVCSDAPSSVTQDRIIIVGNQLPIKSHRNSAGKLSFSWDNDSLLLQLKDGMREDMEVVYIGCLKEQIDTVEQDDVSQRLLENFKCVPAYIPPELFTKYYHGFCKQHLWPLFHYMLPLTPDLGGRFDRSLWQAYLSVNKIFADKVMEVISPDDDFVWVHDYHLMVLPTFLRKRFNRVKLGFFLHSPFPSSEIYRTLPVRNELLRALLNADLIGFHTFDYARHFLSCCSRMLGLSYQSKRGTIGLEYYGRTVSIKILPVGIHISQLQSILNLPETQTKVAELRDQFLDQKVLLGVDDMDIFKGISLKLLAMEQLLTQHPEKRGRVVLVQIANPARGRGKDVQEVQSETEATVKRINEMFGRPGYQPVVLIDTPLQFFERIAYYVIAECCLVTAVRDGMNLIPYEYIICRQGNPKLNETIGLDPSAAKKSMLVVSEFIGCSPSLSGAIRVNPWNIDAVTEAMDYALIVSEAEKQMRHEKHHKYVSTHDVAYWARSFIQDLERACGDHVRKRCWGIGFGLGFRVVALDPSFKKLSIEHIVSAYKRTKNRAILLDYDGTMVQPGSIRTTPTRETIEILNNLSSDPKNIVYLVSGKDRRTLTEWFSSCDDLGLGAEHGYFIRPNDGTDWETSSLVSGFEWKQIAEPVMRLYTETTDGSTIETKETALVWNYQFADPDFGSCQAKELMEHLESVLTNDPVSVKTGQQLVEVKPQGVNKGLVAERLLTTMQEKGKLLDFILCVGDDRSDEDMFEVIMSAKDGPALSPVAEIFACTVGQKPSKAKYYLDDTAEIIRMLDGLAATNTTISDQTDSTATVPTKDLF

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
5	Phosphorylation	---MVSRSYSNLLDL ---CCCCCHHHHHHH	25.96	19880383
6	Phosphorylation	--MVSRSYSNLLDLA --CCCCCHHHHHHHH	10.64	23172892
7	Phosphorylation	-MVSRSYSNLLDLAS -CCCCCHHHHHHHHC	23.42	23172892
14	Phosphorylation	SNLLDLASGNFHSFS HHHHHHHCCCCCCCC	41.38	19376835
19	Phosphorylation	LASGNFHSFSREKKR HHCCCCCCCCCCCCC	22.30	23172892
21	Phosphorylation	SGNFHSFSREKKRFP CCCCCCCCCCCCCCC	42.41	19376835
32	Phosphorylation	KRFPRVATVTGVLSE CCCCCEEEEEHHHHC	18.75	30291188
34	Phosphorylation	FPRVATVTGVLSELD CCCEEEEEHHHHCCC	19.74	30407730
38	Phosphorylation	ATVTGVLSELDDDNN EEEEHHHHCCCCCCC	33.44	30407730
46	Phosphorylation	ELDDDNNSNSVCSDA CCCCCCCCCCCCCCC	36.41	30407730
48	Phosphorylation	DDDNNSNSVCSDAPS CCCCCCCCCCCCCCC	25.07	30407730
51	Phosphorylation	NNSNSVCSDAPSSVT CCCCCCCCCCCCCCC	34.35	30407730
55	Phosphorylation	SVCSDAPSSVTQDRI CCCCCCCCCCCCCEE	38.88	27531888
56	Phosphorylation	VCSDAPSSVTQDRII CCCCCCCCCCCCEEE	28.29	27531888
287	Phosphorylation	SYQSKRGTIGLEYYG CCCCCCCEEEEEEEC	18.86	25368622
573	Phosphorylation	RVVALDPSFKKLSIE EEEEECCCHHHCCHH	49.73	25561503
695	Phosphorylation	VMRLYTETTDGSTIE HHHHEEECCCCCEEE	23.53	28295753

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

Oops, there are no upstream regulatory protein records of TPS5_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
5	S	Phosphorylation	Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3.	16771775
32	T	Phosphorylation	Both Ser-5 and Thr-32 must be phosphorylated for binding to GRF/14-3-3.	16771775

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TPS5_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of TPS5_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphatesynthase 5 in response to 2-deoxyglucose.";
Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J.,Wong B.H.C., Mackintosh C.;
Plant J. 47:211-223(2006).
Cited for: PHOSPHORYLATION AT SER-5 AND THR-32, MUTAGENESIS OF SER-5 AND THR-32,INTERACTION WITH GRF/14-3-3, AND MASS SPECTROMETRY.
PubMed: 16771775