DRP2A_ARATH - dbPTM
DRP2A_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DRP2A_ARATH
UniProt AC Q9SE83
Protein Name Dynamin-2A
Gene Name DRP2A
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 914
Subcellular Localization Cytoplasm, cytosol. Golgi apparatus membrane
Peripheral membrane protein. Cytoplasm, cytoskeleton, phragmoplast. Cytoplasmic vesicle, clathrin-coated vesicle . Localized in the forming cell plate during cytokinesis.
Protein Description Microtubule-associated force-producing protein involved in clathrin-mediated vesicle trafficking from the trans-Golgi network to the central vacuole. Able to bind and hydrolyze GTP. Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P)..
Protein Sequence MEAIDELSQLSDSMKQAASLLADEDPDETSSSKRPATFLNVVALGNVGAGKSAVLNSLIGHPVLPTGENGATRAPIIIELSRESSLSSKAIILQIDNKSQQVSASALRHSLQDRLSKGASGKNRDEINLKLRTSTAPPLKLVDLPGLDQRIVDESMIAEYAQHNDAILLVIVPASQASEISSSRALKIAKEYDPESTRTIGIIGKIDQAAENSKALAAVQALLSNQGPPKTTDIPWVAVIGQSVSIASAQSGSGENSLETAWRAESESLKSILTGAPQSKLGRIALVDTLASQIRSRMKLRLPSVLSGLQGKSQIVQDELARLGEQLVNSAEGTRAIALELCREFEDKFLLHLAGGEGSGWKVVASFEGNFPNRIKQLPLDRHFDLNNVKRVVLEADGYQPYLISPEKGLRSLIKIVLELAKDPARLCVDEVHRVLVDIVSASANATPGLGRYPPFKREVVAIASAALDGFKNEAKKMVVALVDMERAFVPPQHFIRLVQRRMERQRREEELKGRSSKKGQDAEQSLLSRATSPQPDGPTAGGSLKSMKDKPSPQDKETPEVSGLKTAGPEGEITAGYLMKKSAKTNGWSRRWFVLNEKTGKLGYTKKQEERNFRGTITLEECTIEEIPEDEVEKSKSSKDKKANGPDSKGPGLVFKITCKVPYKTVLKAHNALVLKAESVVDKNEWINKLQKVIQARGGQVGSVSMRQSLSEGSLDKMVRKPIDPEEELRWMSQEVRGYVEAVLNSLAANVPKAVVLCQVEKAKEDMLNQLYSSISAIGNERIESLIQEDQNVKRRRERYQKQSSLLSKLTRQLSIHDNRAAAASSYSDNSGTESSPRASGGSSGDDWMNAFNSAANGPSDSLSKYGSGGHSRRYSDPAQNGDAASPGSGSNRRTTPNRLPPAPPPTGSAYRY
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
1Acetylation-------MEAIDELS
-------CHHHHHHH		7.6722223895
8PhosphorylationMEAIDELSQLSDSMK
CHHHHHHHHHCHHHH		27.3323820729
13PhosphorylationELSQLSDSMKQAASL
HHHHHCHHHHHHHHH		25.2219880383
84PhosphorylationIIELSRESSLSSKAI
EEEECCCCCCCCCEE		35.1529797451
268PhosphorylationAWRAESESLKSILTG
HHHHCHHHHHHHHHC		50.8319880383
271PhosphorylationAESESLKSILTGAPQ
HCHHHHHHHHHCCCH		28.2919880383
274PhosphorylationESLKSILTGAPQSKL
HHHHHHHHCCCHHHH		29.6319880383
307PhosphorylationLRLPSVLSGLQGKSQ
CCCHHHHHHCCCCHH		34.9925561503
359PhosphorylationHLAGGEGSGWKVVAS
HHCCCCCCCCEEEEE		36.8619880383
526PhosphorylationKGQDAEQSLLSRATS
CCCHHHHHHHHHCCC		23.8425561503
529PhosphorylationDAEQSLLSRATSPQP
HHHHHHHHHCCCCCC		25.7630291188
532PhosphorylationQSLLSRATSPQPDGP
HHHHHHCCCCCCCCC		39.5719880383
533PhosphorylationSLLSRATSPQPDGPT
HHHHHCCCCCCCCCC		22.1319880383
540PhosphorylationSPQPDGPTAGGSLKS
CCCCCCCCCCCCCCC		43.3923776212
544PhosphorylationDGPTAGGSLKSMKDK
CCCCCCCCCCCCCCC		31.5423776212
547PhosphorylationTAGGSLKSMKDKPSP
CCCCCCCCCCCCCCC		36.0419376835
567PhosphorylationPEVSGLKTAGPEGEI
CCCCCCCCCCCCCEE		41.7219880383
704PhosphorylationARGGQVGSVSMRQSL
HCCCCCCCHHHCCCC		16.5025561503
706PhosphorylationGGQVGSVSMRQSLSE
CCCCCCHHHCCCCCC		15.2229654922
710PhosphorylationGSVSMRQSLSEGSLD
CCHHHCCCCCCCCHH		24.4123776212
712PhosphorylationVSMRQSLSEGSLDKM
HHHCCCCCCCCHHHH		45.2030291188
715PhosphorylationRQSLSEGSLDKMVRK
CCCCCCCCHHHHHCC		29.3723776212
805PhosphorylationRERYQKQSSLLSKLT
HHHHHHHHHHHHHHH		29.9530407730
806PhosphorylationERYQKQSSLLSKLTR
HHHHHHHHHHHHHHH		30.7327531888
809PhosphorylationQKQSSLLSKLTRQLS
HHHHHHHHHHHHHHC		30.8030407730
816PhosphorylationSKLTRQLSIHDNRAA
HHHHHHHCCCCCCHH		15.0019880383
826PhosphorylationDNRAAAASSYSDNSG
CCCHHHHHCCCCCCC		25.6923776212
827PhosphorylationNRAAAASSYSDNSGT
CCHHHHHCCCCCCCC		24.7523776212
828PhosphorylationRAAAASSYSDNSGTE
CHHHHHCCCCCCCCC		19.9723776212
829PhosphorylationAAAASSYSDNSGTES
HHHHHCCCCCCCCCC		32.0623776212
832PhosphorylationASSYSDNSGTESSPR
HHCCCCCCCCCCCCC		52.6723776212
834PhosphorylationSYSDNSGTESSPRAS
CCCCCCCCCCCCCCC		32.3023776212
836PhosphorylationSDNSGTESSPRASGG
CCCCCCCCCCCCCCC		45.5423776212
837PhosphorylationDNSGTESSPRASGGS
CCCCCCCCCCCCCCC		16.5127532006
873PhosphorylationKYGSGGHSRRYSDPA
CCCCCCCCCCCCCCC		23.0229654922
876PhosphorylationSGGHSRRYSDPAQNG
CCCCCCCCCCCCCCC		19.1319376835
877PhosphorylationGGHSRRYSDPAQNGD
CCCCCCCCCCCCCCC		34.9919376835
887PhosphorylationAQNGDAASPGSGSNR
CCCCCCCCCCCCCCC		31.3617317660
890PhosphorylationGDAASPGSGSNRRTT
CCCCCCCCCCCCCCC		42.2919376835
892PhosphorylationAASPGSGSNRRTTPN
CCCCCCCCCCCCCCC		28.9419376835
896PhosphorylationGSGSNRRTTPNRLPP
CCCCCCCCCCCCCCC		43.2819376835
897PhosphorylationSGSNRRTTPNRLPPA
CCCCCCCCCCCCCCC		19.4319376835
908PhosphorylationLPPAPPPTGSAYRY-
CCCCCCCCCCCCCC-		49.9319376835
910PhosphorylationPAPPPTGSAYRY---
CCCCCCCCCCCC---		25.3019376835
912PhosphorylationPPPTGSAYRY-----
CCCCCCCCCC-----		16.4919376835
914PhosphorylationPTGSAYRY-------
CCCCCCCC-------		15.3819376835
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 DRP2A_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DRP2A_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 DRP2A_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP1G1_ARATHGAMMA-ADAPTIN 1physical
12207647
DRP2A_ARATHADL6physical
12105222
DRP2A_ARATHADL6physical
25462567
DRP2B_ARATHDL3physical
25462567
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DRP2A_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-533, AND MASSSPECTROMETRY.

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