PATL2_ARATH - dbPTM
PATL2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PATL2_ARATH
UniProt AC Q56ZI2
Protein Name Patellin-2
Gene Name PATL2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 683
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 MAQEEIQKPTASVPVVKEETPAPVKEVEVPVTTEKAVAAPAPEATEEKVVSEVAVPETEVTAVKEEEVATGKEILQSESFKEEGYLASELQEAEKNALAELKELVREALNKREFTAPPPPPAPVKEEKVEEKKTEETEEKKEEVKTEEKSLEAETKEEEKSAAPATVETKKEEILAAPAPIVAETKKEETPVAPAPVETKPAAPVVAETKKEEILPAAPVTTETKVEEKVVPVETTPAAPVTTETKEEEKAAPVTTETKEEEKAAPGETKKEEKATASTQVKRASKFIKDIFVSVTTSEKKKEEEKPAVVTIEKAFAADQEEETKTVEAVEESIVSITLPETAAYVEPEEVSIWGIPLLEDERSDVILLKFLRARDFKVKEAFTMLKNTVQWRKENKIDDLVSEDLEGSEFEKLVFTHGVDKQGHVVIYSSYGEFQNKEIFSDKEKLSKFLKWRIQFQEKCVRSLDFSPEAKSSFVFVSDFRNAPGLGQRALWQFIKRAVKQFEDNYPEFVAKELFINVPWWYIPYYKTFGSIITSPRTRSKMVLSGPSKSAETIFKYVAPEVVPVKYGGLSKDSPFTVEDGVTEAVVKSTSKYTIDLPATEGSTLSWELRVLGADVSYGAQFEPSNEASYTVIVSKNRKVGLTDEPVITDSFKASEAGKVVITIDNQTFKKKKVLYRSKTQA
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
2Acetylation------MAQEEIQKP
------CCHHHHCCC		26.0322223895
45PhosphorylationAAPAPEATEEKVVSE
ECCCCCCCCCCCCEE		42.9127545962
51PhosphorylationATEEKVVSEVAVPET
CCCCCCCEEEECCCC		29.3723111157
58PhosphorylationSEVAVPETEVTAVKE
EEEECCCCEEEEEEH		29.6830407730
61PhosphorylationAVPETEVTAVKEEEV
ECCCCEEEEEEHHHH		21.3627545962
70PhosphorylationVKEEEVATGKEILQS
EEHHHHHCCHHHHHC		54.7027545962
77PhosphorylationTGKEILQSESFKEEG
CCHHHHHCCCHHHCC		31.5924601666
79PhosphorylationKEILQSESFKEEGYL
HHHHHCCCHHHCCCH		47.0330291188
85PhosphorylationESFKEEGYLASELQE
CCHHHCCCHHHHHHH		11.4523776212
88PhosphorylationKEEGYLASELQEAEK
HHCCCHHHHHHHHHH		35.9223776212
115PhosphorylationALNKREFTAPPPPPA
HHHCCCCCCCCCCCC		33.2419880383
150PhosphorylationEVKTEEKSLEAETKE
HHHHHHHHHHHHCHH		34.4223111157
221PhosphorylationILPAAPVTTETKVEE
HCCCCCCCCCCEEEE		20.1823111157
242PhosphorylationTTPAAPVTTETKEEE
CCCCCCCCCCCHHHH		20.1823111157
255PhosphorylationEEKAAPVTTETKEEE
HHHCCCCCCCCHHHH		20.1823111157
297PhosphorylationDIFVSVTTSEKKKEE
HHEEEECCCHHHHCC		32.5030589143
298PhosphorylationIFVSVTTSEKKKEEE
HEEEECCCHHHHCCC		37.7423572148
403PhosphorylationNKIDDLVSEDLEGSE
CCHHHHHHCCCCCCC		32.4630291188
409PhosphorylationVSEDLEGSEFEKLVF
HHCCCCCCCCEEEEE		29.7230291188
474PhosphorylationFSPEAKSSFVFVSDF
CCHHHHCCEEEEECC		25.4029654922
532PhosphorylationPYYKTFGSIITSPRT
CHHHHHCHHHCCCCC		13.4623776212
535PhosphorylationKTFGSIITSPRTRSK
HHHCHHHCCCCCCCC		30.8923776212
536PhosphorylationTFGSIITSPRTRSKM
HHCHHHCCCCCCCCE		11.2830291188
568PhosphorylationPEVVPVKYGGLSKDS
CCCEEEEECCCCCCC		19.3617586839
572PhosphorylationPVKYGGLSKDSPFTV
EEEECCCCCCCCCEE		37.3817586839
575PhosphorylationYGGLSKDSPFTVEDG
ECCCCCCCCCEECCC		26.1617586839
578PhosphorylationLSKDSPFTVEDGVTE
CCCCCCCEECCCCEE		26.7717586839
664PhosphorylationEAGKVVITIDNQTFK
CCCCEEEEECCCEEC		15.6319880383
669PhosphorylationVITIDNQTFKKKKVL
EEEECCCEECEEEEE		43.6119880383
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 PATL2_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PATL2_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 PATL2_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PATL2_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PATL2_ARATH

loading...

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-79, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory