PATL4_ARATH - dbPTM
PATL4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PATL4_ARATH
UniProt AC Q94C59
Protein Name Patellin-4
Gene Name PATL4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 540
Subcellular Localization Membrane
Peripheral membrane protein. Cytoplasm. Mainly membrane-associated. Also cytoplasmic (By similarity)..
Protein Description Carrier protein that may be involved in membrane-trafficking events associated with cell plate formation during cytokinesis. Binds to some hydrophobic molecules such as phosphoinositides and promotes their transfer between the different cellular sites (By similarity)..
Protein Sequence MTAEVKVEEKQVESEVVIAPAVVPEETTVKAVVEETKVEEDESKPEGVEKSASFKEESDFFADLKESEKKALSDLKSKLEEAIVDNTLLKTKKKESSPMKEKKEEVVKPEAEVEKKKEEAAEEKVEEEKKSEAVVTEEAPKAETVEAVVTEEIIPKEEVTTVVEKVEEETKEEEKKTEDVVTEEVKAETIEVEDEDESVDKDIELWGVPLLPSKGAESTDVILLKFLRARDFKVNEAFEMLKKTLKWRKQNKIDSILGEEFGEDLATAAYMNGVDRESHPVCYNVHSEELYQTIGSEKNREKFLRWRFQLMEKGIQKLNLKPGGVTSLLQIHDLKNAPGVSRTEIWVGIKKVIETLQDNYPEFVSRNIFINVPFWFYAMRAVLSPFLTQRTKSKFVVARPAKVRETLLKYIPADELPVQYGGFKTVDDTEFSNETVSEVVVKPGSSETIEIPAPETEGTLVWDIAVLGWEVNYKEEFVPTEEGAYTVIVQKVKKMGANEGPIRNSFKNSQAGKIVLTVDNVSGKKKKVLYRYRTKTESSS
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 Orthologous
Protein Cluster
51PhosphorylationKPEGVEKSASFKEES
CCCCCCCCHHHCHHH
18.6823776212
53PhosphorylationEGVEKSASFKEESDF
CCCCCCHHHCHHHCC
43.9024601666
58PhosphorylationSASFKEESDFFADLK
CHHHCHHHCCCHHHH
40.5923776212
96PhosphorylationLKTKKKESSPMKEKK
HHCCCCCCCCCHHHH
48.9325561503
97PhosphorylationKTKKKESSPMKEKKE
HCCCCCCCCCHHHHH
30.0625561503
182PhosphorylationKKTEDVVTEEVKAET
HCCCCCCCHHHEEEE
26.6919880383
505PhosphorylationNEGPIRNSFKNSQAG
CCCCCCHHCCCCCCC
27.9625561503

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 PATL4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PATL4_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 PATL4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO3_ARATHSUMO3physical
20855607
SUMO1_ARATHSUMO1physical
20855607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PATL4_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-53, AND MASSSPECTROMETRY.
"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-53, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis.";
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.;
Mol. Cell. Proteomics 6:1198-1214(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, AND MASSSPECTROMETRY.

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