dbPTM

AGD3_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AGD3_ARATH
UniProt AC	Q5W7F2
Protein Name	ADP-ribosylation factor GTPase-activating protein AGD3
Gene Name	AGD3
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	827
Subcellular Localization	Golgi apparatus, trans-Golgi network . BAR and PH domains are essential for the proper localization. Localization seems to be regulated by CVP2 and CVL1 activity as the phosphatidylinositol 4-monophosphate (PIP)-binding by the PH domain is required f
Protein Description	GTPase-activating protein (GAP) for ADP ribosylation factor (ARF). Involved in the spatial control of provascular differentiation. Required for the formation of the normal pattern of continuous secondary veins. Involved in auxin signaling but not in polar auxin transport or in auxin responses. Required for PIN1 internalization in roots..
Protein Sequence	MHFTKLDDSPMFRKQLQSMEESAEILRERSLKFYKGCRKYTEGLGEAYDGDIAFASALETFGGGHNDPISVAFGGPVMTKFTIALREIGTYKEVLRSQVEHILNDRLLQFANMDLHEVKEARKRFDKASLTYDQAREKFLSLRKGTKSDVAAALEQELHTSRSMFEQARFNLVTALSNVEAKKRFEFLEAVSGTMDAHLRYFKQGYELLHQMEPYINQVLTYAQQSRERSNYEQAALNEKMQEYKRQVDRESRWGSNGSNGSPNGDGIQAIGRSSHKMIDAVMQSAARGKVQTIRQGYLSKRSSNLRGDWKRRFFVLDSRGMLYYYRKQCSKPSGSGSQLSGQRNSSELGSGLLSRWLSSNNHGHGGVHDEKSVARHTVNLLTSTIKVDADQSDLRFCFRIISPTKNYTLQAESALDQMDWIEKITGVIASLLSSQVPEQRLPGSPMGSGHHRSASESSSYESSEYDHPTTEEFVCERSFLGYNERPSRSFQPQRSIRKGEKPIDALRKVCGNDKCADCGAPEPDWASLNLGVLVCIECSGVHRNLGVHISKVRSLTLDVKVWEPSVISLFQALGNTFANTVWEELLHSRSAIHFDPGLTVSDKSRVMVTGKPSYADMISIKEKYIQAKYAEKLFVRRSRDSDFPQSAAQQMWDAVSGNDKKAVYRLIVNGDADVNYVYDQTSSSSLTLSRVILVPERPKREDVLLRLRNELLDRTGSSSNISPEGSGGSSLLHCACEKADLGMVELLLQYGANVNASDSSGQTPLHCCLLRGKVTIARLLLTRGADPEAMNREGKTALDIAAESNFTDPEVLALLSDTNGYNHRQC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
256	Phosphorylation	DRESRWGSNGSNGSP HCHHHCCCCCCCCCC	30.93	19880383
259	Phosphorylation	SRWGSNGSNGSPNGD HHCCCCCCCCCCCCC	42.12	19880383
262	Phosphorylation	GSNGSNGSPNGDGIQ CCCCCCCCCCCCCCH	21.31	30291188
346	Phosphorylation	QLSGQRNSSELGSGL HCCCCCCHHHHCHHH	27.64	23111157
347	Phosphorylation	LSGQRNSSELGSGLL CCCCCCHHHHCHHHH	40.15	25561503
351	Phosphorylation	RNSSELGSGLLSRWL CCHHHHCHHHHHHHH	38.60	25561503
445	Phosphorylation	PEQRLPGSPMGSGHH CCCCCCCCCCCCCCC	15.13	19363154
454	Phosphorylation	MGSGHHRSASESSSY CCCCCCCCCCCCCCC	31.61	23328941
456	Phosphorylation	SGHHRSASESSSYES CCCCCCCCCCCCCCC	38.98	23328941
716	Phosphorylation	RNELLDRTGSSSNIS HHHHHHCCCCCCCCC	40.87	23776212
718	Phosphorylation	ELLDRTGSSSNISPE HHHHCCCCCCCCCCC	29.94	23776212
719	Phosphorylation	LLDRTGSSSNISPEG HHHCCCCCCCCCCCC	28.84	23776212
720	Phosphorylation	LDRTGSSSNISPEGS HHCCCCCCCCCCCCC	39.62	23776212
723	Phosphorylation	TGSSSNISPEGSGGS CCCCCCCCCCCCCCC	22.58	23776212
727	Phosphorylation	SNISPEGSGGSSLLH CCCCCCCCCCCCHHH	38.02	23776212
730	Phosphorylation	SPEGSGGSSLLHCAC CCCCCCCCCHHHHHH	22.72	23776212
731	Phosphorylation	PEGSGGSSLLHCACE CCCCCCCCHHHHHHC	37.92	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 AGD3_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AGD3_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 AGD3_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DRP1A_ARATH	DL1	physical	15923323
IP5P6_ARATH	CVP2	physical	19363154

Drug and Disease Associations

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

Regulatory Network of AGD3_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-445, AND MASSSPECTROMETRY.	18433157 [Abstract]