dbPTM

P4KB1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	P4KB1_ARATH
UniProt AC	Q9FMJ0
Protein Name	Phosphatidylinositol 4-kinase beta 1
Gene Name	PI4KB1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1121
Subcellular Localization	Cell membrane . Golgi apparatus, trans-Golgi network . Cytoplasmic vesicle membrane Peripheral membrane protein Cytoplasmic side . Associated to tip-localized membranes in growing root hairs.
Protein Description	Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5-trisphosphate. Necessary for proper organization of the trans-Golgi network (TGN) and post-Golgi secretion in root hairs. Together with PI4KB2, required during polarized root hair expansion and pollen tube elongation. Functions redundantly with PI4KB2 upstream of the cold response phosphoinositide-dependent phospholipase C (PI-PLC) pathway..
Protein Sequence	MPMGRFLSLVRGDSAESPREITSQSNIIGDTGSNGWLIRFFDSAFFCEWIAVSYLYKHPHAGVRDYLCNRMYTLPLSGIESYLFQICYMMVHKPSPSLDKFVIDICGKSLKIALKVHWFLLAELEDADDNEGISRIQEKCQIAATLMGEWSPLMRPQNEVSTPGSKNQVLNRLLSSKQKLFSLKLSPPTQKSLSFSPSPGTNVQDDGSQLPAEDNKIFKKLIPSPKVRDALMFRKSADKDDEESEKEGFFKRLLRDSKGEGDEPIPNSEGFFKRLLKDNKSEDEDITNSSEGFFKRLLSSKGESEELTSSSDGLFKRLLRDNKGDEEELGANSDSFFKRLLRESKNEDEESNPNSEGFFKKLFRDSKPEDDKVPKEVDDEDKDGFLKKLFREKNDDKRHGSEKNEANGTVYADKKSGEEDEREGFFKKFFKEKSDDKKDIVKVDDGNESEGDESPEFSLFKRLFRIHPEDAKPTSENENSSNGLVESSPGTENFFRKLFRDRDQSVEDSELFGSKKHKEKRPGSPKQRDDTPSGKPPLPNNTASQFRKGAYHESLEFVQALCETSYGLVDIFPIEDRKIGLRESLAEINFHLSEAEITGGICFPMGRGVFRVVHIPEDECILLNSREKAPYMISVEVLKAETPSAKESSNSQKLSKGGIPLANGDAFLQKPPPWAYPLWTTQEVYRNSADRMSLSTAQAIDQAMTPKSEVKVKLVNVSLSVEDRTSALESFGDPIDDVLGEAPRTGLNNDLEWVRVVVTADPGLRMESIPDPSVPRKKEHRRVPSTVAMEEVRAAAAKGEAPPGLPLKGAGQDSSDAQPRANGGMLKEGDALSGELWEGKRDRIRKASIYGKLPGWDLRSIIVKSGDDCRQEHLAVQLISHFYDIFQEAGLPLWLRPYEVLVTSSYTALIETIPDTASIHSIKSRYPNITSLRDFFVAKYKENSPSFKLAQRNFVESMAGYSLVCYLLQVKDRHNGNLLLDEEGHIIHIDFGFMLSNSPGGVNFESAPFKLTRELLEVMDSDADGVPSEFFDYFKVLCIQGFLTCRKHAERIILLVEMLQDSGFPCFKGGPRTIQNLRKRFHLSLTEEQCVSLVLSLISSSLDAWRTRQYDYYQRVLNGIL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPMGRFLSLVRGDSA CCCCCHHHHHCCCCC	23.31	29654922
299	Phosphorylation	GFFKRLLSSKGESEE HHHHHHHCCCCCCCC	34.30	30589143
344	Phosphorylation	FKRLLRESKNEDEES HHHHHHHHCCCCCCC	34.05	23776212
351	Phosphorylation	SKNEDEESNPNSEGF HCCCCCCCCCCCHHH	56.38	23776212
355	Phosphorylation	DEESNPNSEGFFKKL CCCCCCCCHHHHHHH	40.11	23776212
449	Phosphorylation	KVDDGNESEGDESPE ECCCCCCCCCCCCCC	51.37	19880383
454	Phosphorylation	NESEGDESPEFSLFK CCCCCCCCCCCHHHH	34.17	23776212
458	Phosphorylation	GDESPEFSLFKRLFR CCCCCCCHHHHHHHC	31.10	23776212
509	Phosphorylation	RDQSVEDSELFGSKK CCCCHHHHHHHCCCC	23.77	25561503
514	Phosphorylation	EDSELFGSKKHKEKR HHHHHHCCCCCCCCC	31.06	30291188
785	Phosphorylation	KEHRRVPSTVAMEEV CCCCCCCCCHHHHHH	32.43	23111157
786	Phosphorylation	EHRRVPSTVAMEEVR CCCCCCCCHHHHHHH	13.25	23111157

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 P4KB1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of P4KB1_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 P4KB1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of P4KB1_ARATH !!

Drug and Disease Associations

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

Regulatory Network of P4KB1_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 SER-449, AND MASSSPECTROMETRY.	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-449 AND SER-454,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	18433157 [Abstract]