DRP2B_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DRP2B_ARATH
• UniProt AC: Q9LQ55
• Protein Name: Dynamin-2B
• Gene Name: DRP2B
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 920
• Subcellular Localization: Cytoplasm, cytoskeleton .
• Protein Description: Putative microtubule-associated force-producing protein, able to bind and hydrolyze GTP..
• Protein Sequence: MEAIDELSQLSDSMRQAASLLADEDPDETSSSRRPATSLNVVALGNVGAGKSAVLNSLIGHPVLPTGENGATRAPIIIDLSREESLSSKAIILQIDNKNQQVSASALRHSLQDRLSKGASGRGRDEIYLKLRTSTAPPLKLIDLPGLDQRIVDDSMIGEHAQHNDAILLVVVPASQASEISSSRALKIAKEYDPESTRTVGIISKIDQAAENPKSLAAVQALLSNQGPPKTTDIPWVALIGQSVSIASAQSGGSENSLETAWRAESESLKSILTGAPQSKLGRIALVDTLASQIRSRMKLRLPNILTGLQGKSQIVQDELARLGEQLVSSAEGTRAIALELCREFEDKFLLHLAGGEGSGWKVVASFEGNFPNRIKKLPLDRHFDLNNVKRIVLEADGYQPYLISPEKGLRSLIKTVLELAKDPARLCVDEVHRVLVDIVSASANATPGLGRYPPFKREVVAIASAALDGFKNEAKKMVVALVDMERAFVPPQHFIRLVQRRMERQRREEELKGRSSKKGQDAEQSLLNRATSPQPDGPSSTGGSLKSLRDKLMPQDKDKDKEKETPEVSGLKTAGPEGEITAGYLMKKSAKTNGWSRRWFVLNEKTGKLGYTKKQEERNFRGTVTLEECSIEEISDDEGEKSKSSKDKKSNGPDSKGPGLVFKITCRVPYKTVLKAHNALVLKAESMVDKNEWINKLQKVIQARGGQVGSASMRQSLSEGSLDKMVRKPVDPEEELRWMSQEVRGYVEAVLNSLAANVPKAVVLCQVEKSKEDMLNQLYSSISAIGNERIESLIQEDQNVKRRRDRYQKQSSLLSKLTRQLSIHDNRAAAASSWSDNSGTESSPRTNGGSSGEDWMNAFNAAASGPDSLKRYGSGGHSRRYSDPAQNGEDSSGSGGSSRRTTPNRLPPAPPQSGSSYRY

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
1	Acetylation	-------MEAIDELS -------CHHHHHHH	7.67	22223895
135	Phosphorylation	YLKLRTSTAPPLKLI EEEEECCCCCCEEEE	42.44	19880383
268	Phosphorylation	AWRAESESLKSILTG HHHHCHHHHHHHHHC	50.83	19880383
271	Phosphorylation	AESESLKSILTGAPQ HCHHHHHHHHHCCCH	28.29	19880383
274	Phosphorylation	ESLKSILTGAPQSKL HHHHHHHHCCCHHHH	29.63	19880383
359	Phosphorylation	HLAGGEGSGWKVVAS HHCCCCCCCCEEEEE	36.86	19880383
532	Phosphorylation	QSLLNRATSPQPDGP HHHHHHCCCCCCCCC	37.39	19880383
533	Phosphorylation	SLLNRATSPQPDGPS HHHHHCCCCCCCCCC	22.13	19880383
540	Phosphorylation	SPQPDGPSSTGGSLK CCCCCCCCCCCHHHH	46.17	23776212
541	Phosphorylation	PQPDGPSSTGGSLKS CCCCCCCCCCHHHHH	33.92	19376835
542	Phosphorylation	QPDGPSSTGGSLKSL CCCCCCCCCHHHHHH	50.31	19376835
545	Phosphorylation	GPSSTGGSLKSLRDK CCCCCCHHHHHHHHH	33.69	23776212
548	Phosphorylation	STGGSLKSLRDKLMP CCCHHHHHHHHHHCC	33.65	19376835
574	Phosphorylation	PEVSGLKTAGPEGEI CCCCCCCCCCCCCEE	41.72	19880383
636	Phosphorylation	ECSIEEISDDEGEKS ECEEEECCCCCCCCC	42.14	23111157
717	Phosphorylation	GSASMRQSLSEGSLD CCHHHHHHCCCCCHH	24.41	23776212
719	Phosphorylation	ASMRQSLSEGSLDKM HHHHHHCCCCCHHHH	45.20	30291188
722	Phosphorylation	RQSLSEGSLDKMVRK HHHCCCCCHHHHHCC	29.37	23776212
812	Phosphorylation	RDRYQKQSSLLSKLT HHHHHHHHHHHHHHH	29.95	30407730
813	Phosphorylation	DRYQKQSSLLSKLTR HHHHHHHHHHHHHHH	30.73	27531888
816	Phosphorylation	QKQSSLLSKLTRQLS HHHHHHHHHHHHHHC	30.80	30407730
823	Phosphorylation	SKLTRQLSIHDNRAA HHHHHHHCCCCCCHH	15.00	19880383
833	Phosphorylation	DNRAAAASSWSDNSG CCCHHHHHCCCCCCC	27.84	19376835
834	Phosphorylation	NRAAAASSWSDNSGT CCHHHHHCCCCCCCC	26.35	19376835
836	Phosphorylation	AAAASSWSDNSGTES HHHHHCCCCCCCCCC	28.94	19376835
839	Phosphorylation	ASSWSDNSGTESSPR HHCCCCCCCCCCCCC	52.67	23776212
841	Phosphorylation	SWSDNSGTESSPRTN CCCCCCCCCCCCCCC	32.30	23776212
843	Phosphorylation	SDNSGTESSPRTNGG CCCCCCCCCCCCCCC	45.54	19880383
844	Phosphorylation	DNSGTESSPRTNGGS CCCCCCCCCCCCCCC	16.51	30291188
879	Phosphorylation	RYGSGGHSRRYSDPA HCCCCCCCCCCCCCC	23.02	25561503
882	Phosphorylation	SGGHSRRYSDPAQNG CCCCCCCCCCCCCCC	19.13	23776212
883	Phosphorylation	GGHSRRYSDPAQNGE CCCCCCCCCCCCCCC	34.99	23776212
892	Phosphorylation	PAQNGEDSSGSGGSS CCCCCCCCCCCCCCC	32.09	23776212
893	Phosphorylation	AQNGEDSSGSGGSSR CCCCCCCCCCCCCCC	49.66	23776212
895	Phosphorylation	NGEDSSGSGGSSRRT CCCCCCCCCCCCCCC	41.76	23776212
898	Phosphorylation	DSSGSGGSSRRTTPN CCCCCCCCCCCCCCC	24.97	23776212
899	Phosphorylation	SSGSGGSSRRTTPNR CCCCCCCCCCCCCCC	29.11	23776212
902	Phosphorylation	SGGSSRRTTPNRLPP CCCCCCCCCCCCCCC	45.56	25561503
903	Phosphorylation	GGSSRRTTPNRLPPA CCCCCCCCCCCCCCC	19.43	29654922

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DRP2B_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DRP2B_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DRP2B_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DRP1A_ARATH	DL1	physical	20231465
DRP2B_ARATH	DL3	physical	25462567
DRP2A_ARATH	ADL6	physical	25462567

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-883, ANDMASS SPECTROMETRY.
PubMed: 19376835

"Quantitative phosphoproteomic analysis of plasma membrane proteinsreveals regulatory mechanisms of plant innate immune responses.";
Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C.;
Plant J. 51:931-940(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND MASSSPECTROMETRY.
PubMed: 17651370

"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-844, AND MASSSPECTROMETRY.
PubMed: 17317660